diff --git a/test_files/PTM_id_file.txt b/test_files/PTM_id_file.txt
new file mode 100644
index 0000000..1a5cee8
--- /dev/null
+++ b/test_files/PTM_id_file.txt
@@ -0,0 +1,9258 @@
+P12688	YKL126W	YPK1	57	Phosphothreonine
+P12688	YKL126W	YPK1	61	Phosphoserine
+P12688	YKL126W	YPK1	64	Phosphoserine
+P12688	YKL126W	YPK1	71	Phosphoserine
+P12688	YKL126W	YPK1	170	Phosphoserine
+P12688	YKL126W	YPK1	502	Phosphothreonine
+P12688	YKL126W	YPK1	504	Phosphothreonine%3B
+P12688	YKL126W	YPK1	644	Phosphoserine
+P12688	YKL126W	YPK1	653	Phosphoserine
+P12688	YKL126W	YPK1	662	Phosphothreonine%3B
+P12688	YKL126W	YPK1	671	Phosphoserine
+P25491	YNL064C	YDJ1	406	Cysteine
+P25491	YNL064C	YDJ1	406	S-farnesyl
+P25491	YNL064C	YDJ1	198	Glycyl
+P16521	YLR249W	YEF3	2	N-acetylserine
+P16521	YLR249W	YEF3	187	N6%2CN6%2CN6-trimethyllysine
+P16521	YLR249W	YEF3	196	N6%2CN6%2CN6-trimethyllysine
+P16521	YLR249W	YEF3	642	Phosphoserine
+P16521	YLR249W	YEF3	789	N6%2CN6%2CN6-trimethyllysine
+P16521	YLR249W	YEF3	972	Phosphothreonine
+P16521	YLR249W	YEF3	974	Phosphoserine
+P16521	YLR249W	YEF3	1039	Phosphoserine
+P16521	YLR249W	YEF3	1040	Phosphoserine
+P16521	YLR249W	YEF3	350	Glycyl
+P16521	YLR249W	YEF3	636	Glycyl
+P11484	YDL229W	SSB1	2	N-acetylalanine
+P11484	YDL229W	SSB1	47	Phosphothreonine
+P11484	YDL229W	SSB1	431	Phosphothreonine
+P39940	YER125W	RSP5	258	Glycyl
+Q06224	YLR277C	YSH1	517	Phosphoserine%3B
+P02829	YPL240C	HSP82	657	Phosphoserine
+P10591	YAL005C	SSA1	2	N-acetylserine
+P10591	YAL005C	SSA1	62	Phosphoserine
+P10591	YAL005C	SSA1	551	Phosphoserine
+P10591	YAL005C	SSA1	603	Phosphoserine
+P10591	YAL005C	SSA1	556	Glycyl
+P41800	YLL006W	MMM1	6	N-linked
+P41800	YLL006W	MMM1	50	N-linked
+P41800	YLL006W	MMM1	55	N-linked
+P41800	YLL006W	MMM1	59	N-linked
+P00546	YBR160W	CDC28	2	N-acetylserine
+P00546	YBR160W	CDC28	19	Phosphotyrosine
+P00546	YBR160W	CDC28	169	Phosphothreonine
+P15108	YMR186W	HSC82	653	Phosphoserine
+P31539	YLL026W	HSP104	1	N-acetylmethionine
+P31539	YLL026W	HSP104	206	Phosphoserine
+P31539	YLL026W	HSP104	306	Phosphoserine
+P31539	YLL026W	HSP104	499	Phosphothreonine
+P31539	YLL026W	HSP104	535	Phosphoserine
+P31539	YLL026W	HSP104	442	Glycyl
+P31539	YLL026W	HSP104	620	Glycyl
+P25623	YCR030C	SYP1	264	Phosphoserine
+P25623	YCR030C	SYP1	331	Phosphoserine
+P25623	YCR030C	SYP1	416	Phosphothreonine
+P25623	YCR030C	SYP1	496	Phosphoserine
+P25623	YCR030C	SYP1	500	Phosphoserine
+P25623	YCR030C	SYP1	577	Phosphothreonine
+P25623	YCR030C	SYP1	256	Glycyl
+P08539	YHR005C	GPA1	2	N-myristoyl
+P08539	YHR005C	GPA1	3	S-palmitoyl
+P08539	YHR005C	GPA1	165	Glycyl
+P15442	YDR283C	GCN2	761	Phosphoserine
+P15442	YDR283C	GCN2	882	Phosphothreonine%3B
+P15442	YDR283C	GCN2	887	Phosphothreonine%3B
+P10592	YLL024C	SSA2	2	N-acetylserine
+P10592	YLL024C	SSA2	20	Phosphoserine
+P10592	YLL024C	SSA2	551	Phosphoserine
+P10592	YLL024C	SSA2	603	Phosphoserine
+P10592	YLL024C	SSA2	556	Glycyl
+P06782	YDR477W	SNF1	210	Phosphothreonine%3B
+P06782	YDR477W	SNF1	413	Phosphoserine
+P06782	YDR477W	SNF1	487	Phosphoserine
+P06782	YDR477W	SNF1	632	Phosphoserine
+P06782	YDR477W	SNF1	461	Glycyl
+P06782	YDR477W	SNF1	549	Glycyl
+P22147	YGL173C	XRN1	1506	Phosphothreonine
+P22147	YGL173C	XRN1	1510	Phosphoserine
+P32598	YER133W	GLC7	1	N-acetylmethionine
+P32598	YER133W	GLC7	22	Glycyl
+P32598	YER133W	GLC7	47	Glycyl
+P35202	YOR143C	THI80	2	N-acetylserine
+P16120	YCR053W	THR4	124	N6-(pyridoxal
+P16120	YCR053W	THR4	467	Phosphoserine
+P40328	YPL074W	YTA6	255	Phosphoserine
+P39077	YJL014W	CCT3	1	N-acetylmethionine
+P39077	YJL014W	CCT3	257	Phosphoserine
+P35691	YKL056C	TMA19	9	Phosphoserine
+P35691	YKL056C	TMA19	15	Phosphoserine
+P29056	YGR246C	BRF1	381	Phosphoserine
+P29056	YGR246C	BRF1	384	Phosphoserine
+P32318	YGR144W	THI4	205	2%2C3-didehydroalanine
+Q08144	YOL018C	TLG2	109	Phosphoserine
+P07273	YGL043W	DST1	116	Phosphoserine
+P00927	YER086W	ILV1	109	N6-(pyridoxal
+P41338	YPL028W	ERG10	2	N-acetylserine
+O74700	YEL020W-A	TIM9	1	N-acetylmethionine
+Q12218	YOR009W	TIR4	465	GPI-anchor
+Q12218	YOR009W	TIR4	327	N-linked
+Q12218	YOR009W	TIR4	348	N-linked
+Q12218	YOR009W	TIR4	368	N-linked
+Q12218	YOR009W	TIR4	403	N-linked
+Q12218	YOR009W	TIR4	404	N-linked
+Q05998	YLR237W	THI7	560	Phosphoserine
+P40040	YER063W	THO1	22	Phosphoserine
+P40040	YER063W	THO1	58	Phosphoserine
+P40040	YER063W	THO1	68	Phosphoserine
+P27654	YBR067C	TIP1	186	GPI-anchor
+P10863	YER011W	TIR1	233	GPI-anchor
+P32802	YLR083C	EMP70	61	N-linked
+P32802	YLR083C	EMP70	282	N-linked
+Q03290	YDR460W	TFB3	157	Phosphoserine
+Q03290	YDR460W	TFB3	258	Phosphothreonine
+P46678	YNL039W	BDP1	49	Phosphoserine
+P46678	YNL039W	BDP1	178	Phosphoserine
+Q12415	YOR110W	TFC7	365	Phosphoserine
+P42883	YNL332W	THI12	62	N6-(pyridoxal
+P40340	YGR270W	YTA7	2	N-acetylalanine
+P40340	YGR270W	YTA7	11	Phosphoserine
+P40340	YGR270W	YTA7	17	Phosphoserine
+P40340	YGR270W	YTA7	94	Phosphoserine
+P40340	YGR270W	YTA7	212	Phosphothreonine
+P40340	YGR270W	YTA7	229	Phosphothreonine
+P40340	YGR270W	YTA7	241	Phosphoserine
+P40340	YGR270W	YTA7	259	Phosphoserine
+P40340	YGR270W	YTA7	285	Phosphoserine
+P40340	YGR270W	YTA7	367	Phosphoserine
+P40340	YGR270W	YTA7	369	Phosphoserine
+P40340	YGR270W	YTA7	370	Phosphoserine
+P40340	YGR270W	YTA7	735	Phosphoserine
+P40340	YGR270W	YTA7	1142	Phosphoserine
+P40340	YGR270W	YTA7	1256	Phosphoserine
+Q08921	YPL180W	TCO89	52	Phosphothreonine
+Q08921	YPL180W	TCO89	82	Phosphothreonine
+Q08921	YPL180W	TCO89	84	Phosphoserine
+Q08921	YPL180W	TCO89	104	Phosphoserine
+Q08921	YPL180W	TCO89	107	Phosphoserine
+Q08921	YPL180W	TCO89	115	Phosphoserine
+Q08921	YPL180W	TCO89	144	Phosphoserine
+Q08921	YPL180W	TCO89	203	Phosphoserine
+Q08921	YPL180W	TCO89	215	Phosphoserine
+Q08921	YPL180W	TCO89	290	Phosphoserine
+Q08921	YPL180W	TCO89	397	Phosphoserine
+Q08921	YPL180W	TCO89	575	Phosphoserine
+Q08921	YPL180W	TCO89	707	Phosphoserine
+P32776	YDR311W	TFB1	150	Phosphothreonine
+P33339	YGR047C	TFC4	311	Phosphoserine
+Q08686	YOR251C	TUM1	201	Phosphoserine
+Q08686	YOR251C	TUM1	264	Phosphoserine
+P33315	YBR117C	TKL2	286	Phosphoserine
+P33315	YBR117C	TKL2	648	Glycyl
+P36165	YKR089C	TGL4	55	Phosphoserine
+P36165	YKR089C	TGL4	737	Phosphoserine
+P36165	YKR089C	TGL4	749	Phosphoserine
+P36165	YKR089C	TGL4	751	Phosphoserine
+P36165	YKR089C	TGL4	836	Phosphoserine
+P47183	YJR156C	THI11	62	N6-(pyridoxal
+P43534	YFL058W	THI5	62	N6-(pyridoxal
+P89886	YER007C-A	TMA20	1	N-acetylmethionine
+Q12049	YPR045C	THP3	1	N-acetylmethionine
+P40462	YIL137C	TMA108	2	N-acetylserine
+Q12513	YDL110C	TMA17	24	Phosphoserine
+Q12513	YDL110C	TMA17	68	Phosphoserine
+P53840	YNL273W	TOF1	626	Phosphoserine
+P53840	YNL273W	TOF1	654	Phosphoserine
+P53840	YNL273W	TOF1	1056	Phosphoserine
+P53840	YNL273W	TOF1	1058	Phosphoserine
+P53840	YNL273W	TOF1	1213	Phosphoserine
+P40310	YJL093C	TOK1	119	Phosphoserine
+Q03280	YDR457W	TOM1	1890	Phosphoserine
+Q03280	YDR457W	TOM1	2096	Phosphothreonine
+Q03280	YDR457W	TOM1	2119	Phosphoserine
+Q03280	YDR457W	TOM1	2376	Phosphoserine
+Q03280	YDR457W	TOM1	2406	Phosphoserine
+Q03280	YDR457W	TOM1	2418	Phosphoserine
+P35180	YGR082W	TOM20	172	Phosphoserine
+P38825	YHR117W	TOM71	55	Phosphoserine
+P32830	YBR091C	TIM12	2	N-acetylserine
+P33890	YOR010C	TIR2	231	GPI-anchor
+Q08422	YOR052C	TMC1	2	N-acetylserine
+Q08422	YOR052C	TMC1	43	Phosphoserine
+Q08422	YOR052C	TMC1	54	Phosphoserine
+P04786	YOL006C	TOP1	14	Phosphoserine
+P04786	YOL006C	TOP1	15	Phosphoserine
+P04786	YOL006C	TOP1	24	Phosphoserine
+P04786	YOL006C	TOP1	49	Phosphoserine
+P04786	YOL006C	TOP1	76	Phosphoserine
+P06786	YNL088W	TOP2	1086	Phosphothreonine%3B
+P06786	YNL088W	TOP2	1087	Phosphoserine%3B
+P06786	YNL088W	TOP2	1252	Phosphoserine
+P06786	YNL088W	TOP2	1258	Phosphothreonine%3B
+P06786	YNL088W	TOP2	1266	Phosphoserine%3B
+P06786	YNL088W	TOP2	1269	Phosphoserine%3B
+P06786	YNL088W	TOP2	1272	Phosphoserine%3B
+P06786	YNL088W	TOP2	1353	Phosphoserine%3B
+P06786	YNL088W	TOP2	1356	Phosphoserine%3B
+P06786	YNL088W	TOP2	1408	Phosphoserine%3B
+P06786	YNL088W	TOP2	1423	Phosphoserine%3B
+Q06177	YLR327C	TMA10	28	Phosphoserine
+Q06177	YLR327C	TMA10	79	Phosphoserine
+P49334	YNL131W	TOM22	44	Phosphoserine
+P49334	YNL131W	TOM22	46	Phosphoserine
+P38288	YBR162C	TOS1	236	N-linked
+P38288	YBR162C	TOS1	417	N-linked
+P12685	YJL129C	TRK1	15	Phosphoserine
+P12685	YJL129C	TRK1	414	Phosphoserine
+P12685	YJL129C	TRK1	534	Phosphoserine
+P12685	YJL129C	TRK1	100	N-linked
+P12685	YJL129C	TRK1	169	N-linked
+P12685	YJL129C	TRK1	222	N-linked
+P12685	YJL129C	TRK1	227	N-linked
+P12685	YJL129C	TRK1	251	N-linked
+P12685	YJL129C	TRK1	369	N-linked
+P12685	YJL129C	TRK1	383	N-linked
+P12685	YJL129C	TRK1	497	N-linked
+P12685	YJL129C	TRK1	501	N-linked
+P12685	YJL129C	TRK1	532	N-linked
+P12685	YJL129C	TRK1	580	N-linked
+P12685	YJL129C	TRK1	677	N-linked
+P12685	YJL129C	TRK1	919	N-linked
+P12685	YJL129C	TRK1	1030	N-linked
+P12685	YJL129C	TRK1	1135	N-linked
+Q12400	YOL093W	TRM10	16	Phosphothreonine
+Q12400	YOL093W	TRM10	283	Phosphoserine
+Q02648	YPL030W	TRM44	107	Phosphoserine
+P32643	YER175C	TMT1	2	N-acetylserine
+P32600	YKL203C	TOR2	10	Phosphothreonine
+P17536	YNL079C	TPM1	195	Phosphoserine
+P17536	YNL079C	TPM1	39	Glycyl
+P17536	YNL079C	TPM1	59	Glycyl
+P17536	YNL079C	TPM1	187	Glycyl
+P53283	YGR138C	TPO2	50	Phosphoserine
+Q12256	YOR273C	TPO4	589	Phosphothreonine
+Q12256	YOR273C	TPO4	606	Phosphothreonine
+Q12256	YOR273C	TPO4	608	Phosphothreonine
+Q12256	YOR273C	TPO4	633	Phosphoserine
+Q12256	YOR273C	TPO4	646	Phosphoserine
+Q05024	YMR233W	TRI1	113	Phosphoserine
+Q05024	YMR233W	TRI1	225	Phosphoserine
+Q05024	YMR233W	TRI1	201	Glycyl
+Q05024	YMR233W	TRI1	215	Glycyl
+P33753	YKR056W	TRM2	92	Phosphoserine
+P33753	YKR056W	TRM2	93	Phosphoserine
+P22217	YLR043C	TRX1	54	Glycyl
+P22217	YLR043C	TRX1	66	Glycyl
+P22217	YLR043C	TRX1	96	Glycyl
+P34760	YML028W	TSA1	174	Phosphothreonine
+P34760	YML028W	TSA1	14	Glycyl
+P34760	YML028W	TSA1	89	Glycyl
+P34760	YML028W	TSA1	132	Glycyl
+P40061	YER093C	TSC11	19	Phosphoserine
+P40061	YER093C	TSC11	81	Phosphoserine
+P40061	YER093C	TSC11	84	Phosphoserine
+P40061	YER093C	TSC11	87	Phosphoserine
+P40061	YER093C	TSC11	141	Phosphoserine
+P40552	YIL011W	TIR3	245	GPI-anchor
+P40552	YIL011W	TIR3	234	N-linked
+Q12000	YOR091W	TMA46	301	Phosphoserine
+Q06266	YLR183C	TOS4	40	Phosphoserine
+Q06266	YLR183C	TOS4	100	Phosphoserine
+Q07824	YLL028W	TPO1	19	Phosphoserine%3B
+Q07824	YLL028W	TPO1	52	Phosphothreonine%3B
+Q07824	YLL028W	TPO1	72	Phosphoserine
+Q07824	YLL028W	TPO1	76	Phosphoserine
+Q07824	YLL028W	TPO1	89	Phosphothreonine
+Q07824	YLL028W	TPO1	91	Phosphoserine
+Q07824	YLL028W	TPO1	342	Phosphoserine%3B
+Q12199	YPR040W	TIP41	55	Phosphothreonine
+P23254	YPR074C	TKL1	286	Phosphoserine
+P23254	YPR074C	TKL1	335	Phosphoserine
+P23254	YPR074C	TKL1	402	Phosphoserine
+P23254	YPR074C	TKL1	492	Phosphoserine
+P23254	YPR074C	TKL1	647	Glycyl
+Q03322	YDR468C	TLG1	31	Phosphothreonine%3B
+Q03322	YDR468C	TLG1	205	S-palmitoyl
+Q03322	YDR468C	TLG1	206	S-palmitoyl
+Q03322	YDR468C	TLG1	183	Glycyl
+P53322	YGR260W	TNA1	27	Phosphoserine
+P53322	YGR260W	TNA1	283	Glycyl
+Q08919	YPL176C	TRE1	139	N-linked
+Q08919	YPL176C	TRE1	213	N-linked
+Q08919	YPL176C	TRE1	529	N-linked
+Q03774	YDR165W	TRM82	93	Phosphoserine
+P32893	YGR166W	TRS65	393	Phosphoserine
+P32893	YGR166W	TRS65	398	Phosphoserine
+Q02208	YKR010C	TOF2	397	Phosphoserine
+Q02208	YKR010C	TOF2	405	Phosphothreonine
+P07213	YNL121C	TOM70	174	Phosphoserine
+P48560	YNL300W	TOS6	80	GPI-anchor
+P48560	YNL300W	TOS6	69	N-linked
+P00942	YDR050C	TPI1	4	Phosphothreonine
+P00942	YDR050C	TPI1	71	Phosphoserine
+P00942	YDR050C	TPI1	215	Phosphoserine
+P00942	YDR050C	TPI1	223	Glycyl
+P40414	YIL138C	TPM2	55	Phosphoserine
+P40414	YIL138C	TPM2	116	Phosphoserine
+P40414	YIL138C	TPM2	157	Phosphoserine
+Q06451	YPR156C	TPO3	55	Phosphoserine
+Q06451	YPR156C	TPO3	98	Phosphothreonine
+Q06451	YPR156C	TPO3	101	Phosphoserine
+Q06451	YPR156C	TPO3	132	Phosphoserine
+P36029	YKL174C	TPO5	569	Phosphoserine
+Q04183	YDR407C	TRS120	379	Phosphoserine
+Q04183	YDR407C	TRS120	387	Phosphoserine
+P38427	YML100W	TSL1	49	Phosphoserine
+P38427	YML100W	TSL1	53	Phosphoserine
+P38427	YML100W	TSL1	56	Phosphoserine
+P38427	YML100W	TSL1	71	Phosphoserine
+P38427	YML100W	TSL1	77	Phosphoserine
+P38427	YML100W	TSL1	135	Phosphoserine
+P38427	YML100W	TSL1	147	Phosphoserine
+P38427	YML100W	TSL1	161	Phosphoserine
+P38427	YML100W	TSL1	229	Phosphoserine
+P38427	YML100W	TSL1	251	Phosphothreonine
+P38427	YML100W	TSL1	303	Phosphoserine
+P38427	YML100W	TSL1	815	Phosphothreonine
+P35172	YBR001C	NTH2	52	Phosphoserine
+P35172	YBR001C	NTH2	53	Phosphoserine
+P35172	YBR001C	NTH2	88	Phosphothreonine
+P35172	YBR001C	NTH2	112	Phosphoserine
+P34219	YBL054W	TOD6	280	Phosphoserine
+P34219	YBL054W	TOD6	333	Phosphoserine
+P34219	YBL054W	TOD6	341	Phosphoserine
+P34219	YBL054W	TOD6	366	Phosphoserine
+P33448	YOR045W	TOM6	1	N-acetylmethionine
+P38811	YHR099W	TRA1	2	N-acetylserine
+P38811	YHR099W	TRA1	172	Phosphoserine
+P38811	YHR099W	TRA1	542	Phosphoserine
+Q08693	YOR256C	TRE2	228	N-linked
+Q08693	YOR256C	TRE2	669	N-linked
+Q08693	YOR256C	TRE2	736	N-linked
+P48561	YNL299W	TRF5	596	Phosphoserine
+P48561	YNL299W	TRF5	602	Phosphoserine
+P28584	YKR050W	TRK2	216	N-linked
+P28584	YKR050W	TRK2	233	N-linked
+P28584	YKR050W	TRK2	265	N-linked
+P33122	YOR344C	TYE7	104	Phosphoserine
+P33122	YOR344C	TYE7	237	Phosphothreonine
+P21734	YDR177W	UBC1	93	Glycyl
+P33296	YER100W	UBC6	139	Phosphoserine
+P33296	YER100W	UBC6	178	Phosphothreonine
+P32571	YDR069C	DOA4	443	Phosphoserine
+P19812	YGR184C	UBR1	296	Phosphoserine
+P19812	YGR184C	UBR1	300	Phosphoserine
+P19812	YGR184C	UBR1	1938	Phosphoserine
+Q07963	YLR024C	UBR2	1218	Phosphoserine
+Q07963	YLR024C	UBR2	1222	Phosphoserine
+Q07963	YLR024C	UBR2	709	Glycyl
+Q06682	YDR330W	UBX5	139	Phosphoserine
+P29509	YDR353W	TRR1	303	Phosphoserine
+P38962	YDR084C	TVP23	63	N-linked
+P38962	YDR084C	TVP23	86	N-linked
+P38962	YDR084C	TVP23	185	N-linked
+P22803	YGR209C	TRX2	62	Phosphoserine
+P22803	YGR209C	TRX2	67	Glycyl
+P22803	YGR209C	TRX2	97	Glycyl
+Q12094	YOR006C	TSR3	286	Phosphoserine
+Q12094	YOR006C	TSR3	289	Phosphoserine
+Q08747	YOR295W	UAF30	218	Phosphoserine
+Q08747	YOR295W	UAF30	220	Phosphoserine
+Q08747	YOR295W	UAF30	223	Phosphoserine
+P14682	YDR054C	CDC34	186	Phosphoserine
+P14682	YDR054C	CDC34	282	Phosphoserine
+P14682	YDR054C	CDC34	292	Phosphoserine
+P40032	YER049W	TPA1	607	Phosphoserine
+P38426	YMR261C	TPS3	148	Phosphoserine
+P38426	YMR261C	TPS3	150	Phosphoserine
+P38426	YMR261C	TPS3	181	Phosphoserine
+P38426	YMR261C	TPS3	265	Phosphothreonine
+P38426	YMR261C	TPS3	267	Phosphoserine
+P38426	YMR261C	TPS3	273	Phosphoserine
+P38426	YMR261C	TPS3	960	Phosphoserine
+P46959	YJL125C	GCD14	302	Phosphoserine
+Q12009	YDL201W	TRM8	7	Phosphoserine%3B
+Q12009	YDL201W	TRM8	59	Phosphoserine
+P53250	YGR080W	TWF1	167	Phosphoserine
+P53250	YGR080W	TWF1	172	Phosphoserine
+P00899	YER090W	TRP2	81	Phosphoserine
+P00899	YER090W	TRP2	223	Phosphothreonine
+P00937	YKL211C	TRP3	2	Phosphoserine
+P00931	YGL026C	TRP5	384	N6-(pyridoxal
+P00931	YGL026C	TRP5	540	Phosphoserine
+P00931	YGL026C	TRP5	683	Phosphoserine
+Q04767	YMR071C	TVP18	146	Phosphothreonine
+Q04767	YMR071C	TVP18	153	Phosphothreonine
+Q04767	YMR071C	TVP18	22	N-linked
+Q99394	YOR115C	TRS33	2	N-acetylserine
+Q04120	YDR453C	TSA2	174	Phosphothreonine
+Q04120	YDR453C	TSA2	14	Glycyl
+Q04120	YDR453C	TSA2	89	Glycyl
+Q04120	YDR453C	TSA2	132	Glycyl
+P36097	YKL033W	TTI1	817	Phosphoserine
+P16649	YCR084C	TUP1	439	Phosphoserine
+P32356	YDR001C	NTH1	2	N-acetylserine
+P32356	YDR001C	NTH1	20	Phosphoserine
+P32356	YDR001C	NTH1	21	Phosphoserine
+P32356	YDR001C	NTH1	23	Phosphoserine
+P32356	YDR001C	NTH1	58	Phosphothreonine
+P32356	YDR001C	NTH1	60	Phosphoserine
+P32356	YDR001C	NTH1	66	Phosphoserine
+P32356	YDR001C	NTH1	83	Phosphoserine
+P53044	YGR048W	UFD1	354	Phosphoserine
+P33202	YKL010C	UFD4	87	Phosphothreonine
+P33202	YKL010C	UFD4	349	Glycyl
+Q02724	YPL020C	ULP1	2	N-acetylserine
+Q02724	YPL020C	ULP1	21	Phosphoserine
+Q02724	YPL020C	ULP1	25	Phosphoserine
+Q02724	YPL020C	ULP1	179	Phosphothreonine
+Q02724	YPL020C	ULP1	264	Phosphoserine
+P28274	YBL039C	URA7	422	Glycyl
+P40362	YJL069C	UTP18	182	Phosphoserine
+P40362	YJL069C	UTP18	184	Phosphoserine
+P40498	YIL091C	UTP25	53	Phosphoserine
+P40498	YIL091C	UTP25	63	Phosphoserine
+P40498	YIL091C	UTP25	196	Phosphoserine
+P16140	YBR127C	VMA2	4	Phosphoserine
+P16140	YBR127C	VMA2	137	Phosphoserine
+P16140	YBR127C	VMA2	503	Phosphoserine
+P16140	YBR127C	VMA2	504	Phosphoserine
+P16140	YBR127C	VMA2	511	Phosphoserine%3B
+P16140	YBR127C	VMA2	515	Phosphoserine
+P16140	YBR127C	VMA2	14	Glycyl
+P16140	YBR127C	VMA2	508	Glycyl
+P38358	YBR293W	VBA2	420	N-linked
+Q04602	YDR119W	VBA4	62	Phosphoserine
+Q04602	YDR119W	VBA4	99	Phosphoserine
+Q04602	YDR119W	VBA4	106	Phosphoserine
+Q04602	YDR119W	VBA4	160	Phosphoserine
+Q04602	YDR119W	VBA4	192	Phosphoserine
+Q04602	YDR119W	VBA4	480	N-linked
+Q04602	YDR119W	VBA4	553	N-linked
+P39538	YJL197W	UBP12	84	Phosphoserine
+P39538	YJL197W	UBP12	1160	Phosphoserine
+P47049	YJL048C	UBX6	369	Phosphoserine
+P40554	YIL008W	URM1	99	1-thioglycine
+P40554	YIL008W	URM1	99	Glycyl
+Q04500	YML093W	UTP14	34	Phosphoserine
+Q04500	YML093W	UTP14	35	Phosphoserine
+Q04500	YML093W	UTP14	151	Phosphoserine
+Q04500	YML093W	UTP14	423	Phosphoserine
+Q04500	YML093W	UTP14	424	Phosphoserine
+Q04500	YML093W	UTP14	488	Phosphoserine
+Q04500	YML093W	UTP14	500	Phosphoserine
+Q04500	YML093W	UTP14	562	Phosphoserine
+Q04500	YML093W	UTP14	668	Phosphoserine
+Q04500	YML093W	UTP14	738	Phosphoserine
+Q12339	YOR004W	UTP23	182	Phosphoserine
+P43123	YDL103C	QRI1	218	Phosphoserine
+P43123	YDL103C	QRI1	461	Phosphoserine
+P52490	YDR092W	UBC13	92	Glycyl
+Q02159	YMR022W	UBC7	89	Glycyl
+Q08562	YOR191W	ULS1	121	Phosphoserine
+P25386	YDL058W	USO1	1770	Phosphoserine
+P42945	YJL109C	UTP10	2	N-acetylserine
+Q06078	YLR409C	UTP21	2	N-acetylserine
+Q06078	YLR409C	UTP21	772	Phosphoserine
+P53254	YGR090W	UTP22	10	Phosphoserine
+P53254	YGR090W	UTP22	58	Phosphoserine
+P53254	YGR090W	UTP22	60	Phosphothreonine
+P53254	YGR090W	UTP22	64	Phosphoserine
+P53276	YGR128C	UTP8	95	Phosphothreonine
+P53276	YGR128C	UTP8	148	Phosphoserine
+P53276	YGR128C	UTP8	150	Phosphoserine
+P21373	YJR049C	UTR1	499	Phosphoserine
+P21373	YJR049C	UTR1	503	Phosphoserine
+Q01476	YOR124C	UBP2	907	Phosphoserine
+P43593	YFR010W	UBP6	389	Phosphothreonine
+P43593	YFR010W	UBP6	470	Phosphoserine
+P38882	YHR196W	UTP9	547	Phosphoserine
+P38882	YHR196W	UTP9	564	Phosphoserine
+P25591	YCL063W	VAC17	2	N-acetylalanine
+P25591	YCL063W	VAC17	119	Phosphoserine
+P25591	YCL063W	VAC17	149	Phosphothreonine
+P25591	YCL063W	VAC17	178	Phosphoserine
+P25591	YCL063W	VAC17	248	Phosphothreonine
+P25591	YCL063W	VAC17	269	Phosphoserine
+P17255	YDL185W	VMA1	2	N-acetylalanine
+P17255	YDL185W	VMA1	131	Phosphothreonine
+P17255	YDL185W	VMA1	858	Phosphoserine
+P17255	YDL185W	VMA1	928	Phosphoserine
+P06104	YGL058W	RAD6	120	Phosphoserine%3B
+P38349	YBR273C	UBX7	388	Phosphoserine
+P38349	YBR273C	UBX7	19	Glycyl
+P53177	YGL050W	TYW3	26	Phosphoserine
+P53177	YGL050W	TYW3	238	Phosphoserine
+P22515	YKL210W	UBA1	2	N-acetylserine
+P22515	YKL210W	UBA1	265	Phosphoserine
+P22515	YKL210W	UBA1	914	Phosphoserine
+P22515	YKL210W	UBA1	595	Glycyl
+P22515	YKL210W	UBA1	608	Glycyl
+P52491	YLR306W	UBC12	1	N-acetylmethionine
+P15732	YDR059C	UBC5	12	Phosphoserine
+P15732	YDR059C	UBC5	91	Glycyl
+P38187	YBL067C	UBP13	198	Phosphoserine
+P25037	YDL122W	UBP1	530	Phosphoserine
+P25037	YDL122W	UBP1	531	Phosphoserine
+P25037	YDL122W	UBP1	555	Phosphoserine
+P25037	YDL122W	UBP1	618	Phosphoserine
+P25037	YDL122W	UBP1	638	Phosphoserine
+P25037	YDL122W	UBP1	652	Phosphothreonine
+P25037	YDL122W	UBP1	653	Phosphoserine
+P25037	YDL122W	UBP1	654	Phosphoserine
+P25037	YDL122W	UBP1	670	Phosphoserine
+P25037	YDL122W	UBP1	755	Phosphoserine
+P32861	YKL035W	UGP1	2	N-acetylserine
+P32861	YKL035W	UGP1	17	Phosphoserine
+P32861	YKL035W	UGP1	19	Phosphothreonine
+P32861	YKL035W	UGP1	21	Phosphoserine
+P32861	YKL035W	UGP1	79	Phosphoserine
+P32861	YKL035W	UGP1	369	Omega-N-methylarginine
+Q08960	YPL207W	TYW1	496	Glycyl
+P38820	YHR111W	UBA4	1	N-acetylmethionine
+P38820	YHR111W	UBA4	326	Phosphoserine
+P15731	YBR082C	UBC4	12	Phosphoserine
+P15731	YBR082C	UBC4	91	Glycyl
+P34223	YBL058W	SHP1	128	Phosphoserine
+P34223	YBL058W	SHP1	210	Phosphoserine
+P34223	YBL058W	SHP1	224	Phosphoserine
+P34223	YBL058W	SHP1	315	Phosphoserine
+P34223	YBL058W	SHP1	321	Phosphoserine
+P34223	YBL058W	SHP1	322	Phosphoserine
+P34223	YBL058W	SHP1	331	Phosphothreonine
+P34223	YBL058W	SHP1	241	Glycyl
+Q04511	YML088W	UFO1	511	Phosphoserine
+Q04511	YML088W	UFO1	514	Phosphothreonine
+P40537	YIL031W	ULP2	788	Phosphoserine
+P40537	YIL031W	ULP2	903	Phosphoserine
+P40537	YIL031W	ULP2	983	Phosphoserine
+P40537	YIL031W	ULP2	984	Phosphoserine
+Q12151	YDR213W	UPC2	122	Phosphothreonine
+Q12151	YDR213W	UPC2	519	Phosphoserine
+P50623	YDL064W	UBC9	2	N-acetylserine
+P0CG63	YLL039C	UBI4	76	Glycyl
+Q03327	YDR470C	UGO1	1	N-acetylmethionine
+P39547	YAR027W	UIP3	11	Glycyl
+P39547	YAR027W	UIP3	218	Glycyl
+P18562	YHR128W	FUR1	82	Phosphoserine
+P27515	YNR012W	URK1	17	Phosphoserine
+P27515	YNR012W	URK1	276	Phosphoserine
+P32366	YLR447C	VMA6	1	N-acetylmethionine
+Q06708	YLR386W	VAC14	767	Phosphoserine
+Q06708	YLR386W	VAC14	805	Phosphoserine
+Q06708	YLR386W	VAC14	867	Phosphoserine
+Q99385	YDL128W	VCX1	1	N-acetylmethionine
+Q99385	YDL128W	VCX1	13	Phosphoserine
+P53058	YGL258W	VEL1	26	N-linked
+P53058	YGL258W	VEL1	48	N-linked
+P53058	YGL258W	VEL1	91	N-linked
+P53058	YGL258W	VEL1	139	N-linked
+P53058	YGL258W	VEL1	152	N-linked
+Q08926	YPL186C	UIP4	140	Phosphoserine
+Q08926	YPL186C	UIP4	185	Phosphoserine
+Q08926	YPL186C	UIP4	205	Phosphoserine
+P39001	YDR207C	UME6	114	Phosphoserine
+P39001	YDR207C	UME6	141	Phosphoserine
+P39001	YDR207C	UME6	150	Phosphoserine
+P39001	YDR207C	UME6	228	Phosphoserine
+P39001	YDR207C	UME6	316	Phosphoserine
+P39001	YDR207C	UME6	318	Phosphoserine
+P39001	YDR207C	UME6	645	Phosphoserine
+P23202	YNL229C	URE2	2	N-acetylmethionine
+Q03714	YML029W	USA1	374	Phosphoserine
+Q03714	YML029W	USA1	376	Phosphoserine
+Q03714	YML029W	USA1	379	Phosphoserine
+P36172	YKR105C	VBA5	70	N-linked
+P36172	YKR105C	VBA5	423	N-linked
+P04840	YNL055C	POR1	109	Phosphoserine
+P04840	YNL055C	POR1	117	Phosphothreonine
+P40157	YNL212W	VID27	170	Phosphoserine
+P40157	YNL212W	VID27	195	Phosphoserine
+P40157	YNL212W	VID27	196	Phosphoserine
+P40157	YNL212W	VID27	222	Phosphoserine
+P40157	YNL212W	VID27	486	Phosphothreonine
+Q06685	YLR410W	VIP1	31	Phosphoserine
+Q06685	YLR410W	VIP1	54	Phosphoserine
+Q06685	YLR410W	VIP1	77	Phosphoserine
+Q06685	YLR410W	VIP1	895	Phosphoserine
+Q06685	YLR410W	VIP1	1107	Phosphoserine
+P39968	YEL013W	VAC8	11	Phosphoserine
+P39968	YEL013W	VAC8	16	Phosphoserine
+P39968	YEL013W	VAC8	2	N-myristoyl
+P39968	YEL013W	VAC8	4	S-palmitoyl
+P39968	YEL013W	VAC8	5	S-palmitoyl
+P39968	YEL013W	VAC8	7	S-palmitoyl
+P39968	YEL013W	VAC8	77	Glycyl
+P39968	YEL013W	VAC8	515	Glycyl
+Q05934	YLR373C	VID22	21	N-linked
+Q05934	YLR373C	VID22	242	N-linked
+Q05934	YLR373C	VID22	291	N-linked
+Q05934	YLR373C	VID22	540	N-linked
+Q05934	YLR373C	VID22	645	N-linked
+Q05934	YLR373C	VID22	649	N-linked
+Q05934	YLR373C	VID22	652	N-linked
+Q05934	YLR373C	VID22	662	N-linked
+Q05934	YLR373C	VID22	669	N-linked
+Q05934	YLR373C	VID22	673	N-linked
+Q05934	YLR373C	VID22	688	N-linked
+Q05934	YLR373C	VID22	722	N-linked
+P23642	YML115C	VAN1	25	Phosphoserine
+P23642	YML115C	VAN1	215	N-linked
+P23642	YML115C	VAN1	251	N-linked
+P48836	YHR039C-A	VMA10	2	N-acetylserine
+P32319	YBL017C	PEP1	96	N-linked
+P32319	YBL017C	PEP1	170	N-linked
+P32319	YBL017C	PEP1	447	N-linked
+P32319	YBL017C	PEP1	793	N-linked
+P32319	YBL017C	PEP1	1010	N-linked
+P32319	YBL017C	PEP1	1303	N-linked
+P32913	YOR132W	VPS17	544	Phosphoserine
+Q04272	YMR077C	VPS20	2	N-myristoyl
+P39702	YAL002W	VPS8	1	N-acetylmethionine
+P38329	YBR235W	VHC1	34	Phosphoserine
+P38329	YBR235W	VHC1	654	Phosphoserine
+P38329	YBR235W	VHC1	915	Phosphoserine
+P38329	YBR235W	VHC1	918	Phosphoserine
+P40522	YIL056W	VHR1	409	Phosphoserine
+Q08438	YOR054C	VHS3	90	Phosphothreonine
+P53285	YGR141W	VPS62	74	N-linked
+P53285	YGR141W	VPS62	145	N-linked
+Q06525	YPR152C	URN1	150	Phosphoserine
+Q12132	YPL230W	USV1	162	Phosphoserine
+Q12132	YPL230W	USV1	163	Phosphoserine
+P53950	YNL054W	VAC7	164	Phosphoserine
+P53950	YNL054W	VAC7	1020	N-linked
+P53950	YNL054W	VAC7	1099	N-linked
+P47161	YJR126C	VPS70	55	N-linked
+P47161	YJR126C	VPS70	237	N-linked
+P47161	YJR126C	VPS70	568	N-linked
+P47161	YJR126C	VPS70	599	N-linked
+P47161	YJR126C	VPS70	670	N-linked
+P37370	YLR337C	VRP1	519	Phosphoserine
+P37370	YLR337C	VRP1	762	Phosphoserine
+P37370	YLR337C	VRP1	109	N-linked
+P37370	YLR337C	VRP1	212	N-linked
+P37370	YLR337C	VRP1	337	N-linked
+P37370	YLR337C	VRP1	383	N-linked
+P37370	YLR337C	VRP1	784	N-linked
+P37370	YLR337C	VRP1	796	N-linked
+Q03631	YML076C	WAR1	128	Phosphothreonine
+P31412	YKL080W	VMA5	2	N-acetylalanine
+P22203	YOR332W	VMA4	2	N-acetylserine
+Q04301	YMR088C	VBA1	123	N-linked
+Q04301	YMR088C	VBA1	324	N-linked
+Q04301	YMR088C	VBA1	504	N-linked
+P25594	YCL069W	VBA3	195	N-linked
+P53262	YGR106C	VOA1	69	N-linked
+P53262	YGR106C	VOA1	104	N-linked
+P53262	YGR106C	VOA1	172	N-linked
+P32563	YOR270C	VPH1	2	N-acetylalanine
+P38959	YDR080W	VPS41	26	Phosphoserine
+P38959	YDR080W	VPS41	53	Phosphoserine
+Q12071	YDR027C	VPS54	69	Phosphoserine
+Q12071	YDR027C	VPS54	72	Phosphoserine
+Q12071	YDR027C	VPS54	74	Phosphothreonine
+P47111	YJR044C	VPS55	137	Phosphoserine
+Q12016	YOL129W	VPS68	1	N-acetylmethionine
+Q12016	YOL129W	VPS68	8	Phosphoserine
+Q12016	YOL129W	VPS68	52	N-linked
+Q06385	YDR372C	VPS74	14	Phosphoserine
+Q06385	YDR372C	VPS74	19	Phosphoserine
+Q07655	YDL224C	WHI4	22	Phosphoserine
+Q07655	YDL224C	WHI4	206	Phosphoserine
+Q07655	YDL224C	WHI4	258	Phosphoserine
+Q07655	YDL224C	WHI4	283	Phosphoserine
+P42839	YNL321W	VNX1	26	Phosphothreonine
+P42839	YNL321W	VNX1	32	Phosphoserine
+P42839	YNL321W	VNX1	33	Phosphothreonine
+P42839	YNL321W	VNX1	110	Phosphoserine
+P42839	YNL321W	VNX1	118	Phosphothreonine
+P42839	YNL321W	VNX1	121	Phosphoserine
+P42839	YNL321W	VNX1	361	N-linked
+P39904	YDR484W	VPS52	602	Phosphoserine
+P54787	YML097C	VPS9	375	Phosphoserine
+Q06263	YLR181C	VTA1	183	Phosphoserine
+Q06263	YLR181C	VTA1	195	Phosphothreonine
+Q06263	YLR181C	VTA1	233	Phosphoserine
+P47165	YJR133W	XPT1	79	Phosphoserine
+P53076	YGL227W	VID30	2	N-acetylserine
+P53076	YGL227W	VID30	147	Phosphoserine
+P53076	YGL227W	VID30	246	Phosphoserine
+P53076	YGL227W	VID30	248	Phosphoserine
+P53076	YGL227W	VID30	277	Phosphoserine
+P22219	YBR097W	VPS15	2	N-myristoyl
+P21576	YKR001C	VPS1	579	Phosphoserine
+P21576	YKR001C	VPS1	599	Phosphoserine
+Q04338	YMR197C	VTI1	2	N-acetylserine
+Q04338	YMR197C	VTI1	110	Phosphoserine
+Q04338	YMR197C	VTI1	149	Phosphoserine
+P40438	YIL173W	VTH1	479	N-linked
+P40438	YIL173W	VTH1	769	N-linked
+P40438	YIL173W	VTH1	986	N-linked
+P40890	YJL222W	VTH2	479	N-linked
+P40890	YJL222W	VTH2	769	N-linked
+P40890	YJL222W	VTH2	986	N-linked
+P34761	YNL197C	WHI3	231	Phosphoserine
+P40463	YIL135C	VHS2	53	Phosphoserine
+P40463	YIL135C	VHS2	61	Phosphoserine
+P40463	YIL135C	VHS2	102	Phosphoserine
+P40463	YIL135C	VHS2	172	Phosphoserine
+P40463	YIL135C	VHS2	299	Phosphoserine
+P40463	YIL135C	VHS2	301	Phosphoserine
+P40463	YIL135C	VHS2	303	Phosphoserine
+P40463	YIL135C	VHS2	325	Phosphoserine
+Q07878	YLL040C	VPS13	1364	Phosphoserine
+Q07878	YLL040C	VPS13	1382	Phosphoserine
+Q07878	YLL040C	VPS13	1715	Phosphoserine
+Q07878	YLL040C	VPS13	1729	Phosphoserine
+Q07878	YLL040C	VPS13	1731	Phosphoserine
+Q03390	YDR486C	VPS60	12	Phosphoserine
+P53853	YNL246W	VPS75	3	Phosphoserine
+Q12215	YOL105C	WSC3	84	N-linked
+Q12215	YOL105C	WSC3	367	N-linked
+Q12215	YOL105C	WSC3	370	N-linked
+P38739	YHL028W	WSC4	340	N-linked
+P38739	YHL028W	WSC4	386	N-linked
+P38739	YHL028W	WSC4	389	N-linked
+P38739	YHL028W	WSC4	398	N-linked
+P38739	YHL028W	WSC4	479	N-linked
+P38739	YHL028W	WSC4	553	N-linked
+P38739	YHL028W	WSC4	583	N-linked
+P43582	YFL010C	WWM1	75	Phosphoserine
+P43582	YFL010C	WWM1	78	Phosphothreonine
+P43582	YFL010C	WWM1	50	Glycyl
+P43582	YFL010C	WWM1	60	Glycyl
+P53241	YGR065C	VHT1	32	Phosphoserine
+P53241	YGR065C	VHT1	33	Phosphoserine
+P53241	YGR065C	VHT1	43	Phosphoserine
+P40547	YIL017C	VID28	226	Phosphoserine
+P38735	YHL035C	VMR1	11	N-linked
+P38735	YHL035C	VMR1	370	N-linked
+P20795	YLR396C	VPS33	626	Phosphoserine
+P34110	YJL154C	VPS35	846	Phosphoserine
+P34110	YJL154C	VPS35	848	Phosphoserine
+P34110	YJL154C	VPS35	868	Phosphoserine
+Q02725	YPL019C	VTC3	43	Phosphoserine
+Q02725	YPL019C	VTC3	45	Phosphoserine
+Q02725	YPL019C	VTC3	50	Phosphoserine
+Q02725	YPL019C	VTC3	183	Phosphothreonine
+Q02725	YPL019C	VTC3	195	Phosphoserine
+Q02725	YPL019C	VTC3	198	Phosphoserine
+Q02725	YPL019C	VTC3	270	Phosphoserine
+Q02725	YPL019C	VTC3	274	Phosphoserine
+Q02725	YPL019C	VTC3	589	Phosphoserine
+Q02725	YPL019C	VTC3	592	Phosphoserine
+Q02725	YPL019C	VTC3	621	Phosphoserine
+Q02725	YPL019C	VTC3	622	Phosphoserine
+P47075	YJL012C	VTC4	75	Glycyl
+Q12416	YOR083W	WHI5	47	Phosphothreonine
+Q12416	YOR083W	WHI5	57	Phosphothreonine
+Q12416	YOR083W	WHI5	59	Phosphoserine
+Q12416	YOR083W	WHI5	62	Phosphoserine
+Q12416	YOR083W	WHI5	88	Phosphoserine
+Q12416	YOR083W	WHI5	113	Phosphoserine
+Q12416	YOR083W	WHI5	115	Phosphoserine
+Q12416	YOR083W	WHI5	154	Phosphoserine
+Q12416	YOR083W	WHI5	156	Phosphoserine
+Q12416	YOR083W	WHI5	161	Phosphoserine
+Q12416	YOR083W	WHI5	262	Phosphoserine
+Q12416	YOR083W	WHI5	288	Phosphoserine
+Q12416	YOR083W	WHI5	290	Phosphothreonine
+Q12363	YOR230W	WTM1	187	Phosphothreonine
+Q12363	YOR230W	WTM1	200	Phosphoserine
+Q12363	YOR230W	WTM1	370	Phosphothreonine
+Q12363	YOR230W	WTM1	406	Phosphothreonine
+P36095	YKL041W	VPS24	203	Glycyl
+P40343	YNR006W	VPS27	157	Phosphoserine
+P40343	YNR006W	VPS27	495	Phosphoserine
+P40343	YNR006W	VPS27	613	Phosphoserine
+P40343	YNR006W	VPS27	294	Glycyl
+P36116	YKR020W	VPS51	2	N-acetylalanine
+Q03388	YDR485C	VPS72	425	Phosphoserine
+P40046	YER072W	VTC1	2	N-acetylserine
+P43585	YFL004W	VTC2	182	Phosphoserine
+P43585	YFL004W	VTC2	187	Phosphoserine
+P43585	YFL004W	VTC2	196	Phosphoserine
+P43585	YFL004W	VTC2	264	Phosphoserine
+P43585	YFL004W	VTC2	583	Phosphoserine
+P43585	YFL004W	VTC2	615	Phosphoserine
+P43585	YFL004W	VTC2	616	Phosphoserine
+P43585	YFL004W	VTC2	620	Phosphothreonine
+P43585	YFL004W	VTC2	626	Phosphoserine
+P43585	YFL004W	VTC2	657	Phosphoserine
+P53832	YNL283C	WSC2	402	Phosphothreonine
+P53832	YNL283C	WSC2	455	Phosphoserine
+P53832	YNL283C	WSC2	458	Phosphoserine
+P42826	YGR194C	XKS1	244	Phosphoserine
+P33301	YDR369C	XRS2	349	Phosphoserine
+P33301	YDR369C	XRS2	533	Phosphoserine
+P33301	YDR369C	XRS2	534	Phosphoserine
+P33301	YDR369C	XRS2	553	Phosphoserine
+P33301	YDR369C	XRS2	555	Phosphothreonine
+Q02792	YOR048C	RAT1	574	Phosphoserine
+P30822	YGR218W	CRM1	1080	Phosphoserine
+P36017	YOR089C	VPS21	188	Phosphoserine
+P36017	YOR089C	VPS21	210	Cysteine
+P36017	YOR089C	VPS21	208	S-geranylgeranyl
+P36017	YOR089C	VPS21	210	S-geranylgeranyl
+Q03897	YDR128W	MTC5	759	Phosphoserine
+P32386	YLL048C	YBT1	936	Phosphoserine
+P32386	YLL048C	YBT1	940	Phosphoserine
+P32386	YLL048C	YBT1	955	Phosphoserine
+P32386	YLL048C	YBT1	6	N-linked
+P32386	YLL048C	YBT1	97	N-linked
+P25349	YCR004C	YCP4	244	Cysteine
+P25349	YCR004C	YCP4	243	S-palmitoyl
+P25349	YCR004C	YCP4	244	S-farnesyl
+P34225	YBL060W	YEL1	290	Phosphothreonine
+P34225	YBL060W	YEL1	293	Phosphoserine
+P34225	YBL060W	YEL1	299	Phosphoserine
+Q92393	YOR142W-B	TY1B-OR	416	Phosphoserine
+P53049	YGR281W	YOR1	10	Phosphoserine
+P53049	YGR281W	YOR1	24	Phosphoserine
+P53049	YGR281W	YOR1	53	Phosphothreonine
+P53049	YGR281W	YOR1	661	N-linked
+P53049	YGR281W	YOR1	759	N-linked
+P53049	YGR281W	YOR1	799	N-linked
+P18961	YMR104C	YPK2	63	Phosphothreonine
+P18961	YMR104C	YPK2	66	Phosphothreonine
+P18961	YMR104C	YPK2	72	Phosphoserine
+P18961	YMR104C	YPK2	499	Phosphothreonine
+P18961	YMR104C	YPK2	501	Phosphothreonine%3B
+P18961	YMR104C	YPK2	641	Phosphoserine%3B
+P18961	YMR104C	YPK2	650	Phosphoserine
+P18961	YMR104C	YPK2	659	Phosphothreonine%3B
+P18961	YMR104C	YPK2	669	Phosphoserine
+P32939	YML001W	YPT7	208	Cysteine
+P32939	YML001W	YPT7	206	S-geranylgeranyl
+P32939	YML001W	YPT7	208	S-geranylgeranyl
+P32939	YML001W	YPT7	147	Glycyl
+P36036	YKL214C	YRA2	1	N-acetylmethionine
+P38079	YBR054W	YRO2	293	Phosphoserine
+P38079	YBR054W	YRO2	341	Phosphothreonine
+P38079	YBR054W	YRO2	343	Phosphoserine
+P38079	YBR054W	YRO2	286	Glycyl
+P39109	YDR135C	YCF1	251	Phosphoserine
+P39109	YDR135C	YCF1	873	Phosphoserine
+P39109	YDR135C	YCF1	903	Phosphoserine
+P39109	YDR135C	YCF1	908	Phosphoserine
+P39109	YDR135C	YCF1	911	Phosphothreonine
+P39109	YDR135C	YCF1	914	Phosphoserine
+Q12316	YGR161C-D	TY1B-GR3	416	Phosphoserine
+Q12222	YOL128C	YGK3	211	Phosphoserine
+Q99219	YIL082W	TY3A-I	2	N-acetylserine
+P53845	YNL263C	YIF1	2	N-acetylserine
+P47098	YJR027W	TY1B-JR1	416	Phosphoserine
+P36015	YKL196C	YKT6	158	Phosphothreonine
+P36015	YKL196C	YKT6	197	Cysteine
+P36015	YKL196C	YKT6	196	S-palmitoyl
+P36015	YKL196C	YKT6	197	S-farnesyl
+Q06328	YDR352W	YPQ2	136	Phosphoserine
+P40583	YIR039C	YPS6	515	GPI-anchor
+P40583	YIR039C	YPS6	57	N-linked
+P40583	YIR039C	YPS6	149	N-linked
+P40583	YIR039C	YPS6	156	N-linked
+P40583	YIR039C	YPS6	161	N-linked
+P40583	YIR039C	YPS6	183	N-linked
+P40583	YIR039C	YPS6	195	N-linked
+P40583	YIR039C	YPS6	311	N-linked
+P40583	YIR039C	YPS6	363	N-linked
+P40583	YIR039C	YPS6	375	N-linked
+P40583	YIR039C	YPS6	379	N-linked
+P40583	YIR039C	YPS6	472	N-linked
+P48559	YNL304W	YPT11	415	S-geranylgeranyl
+P48559	YNL304W	YPT11	416	S-geranylgeranyl
+P51996	YGL210W	YPT32	2	N-acetylserine
+P51996	YGL210W	YPT32	221	S-geranylgeranyl
+P51996	YGL210W	YPT32	222	S-geranylgeranyl
+P40517	YIL063C	YRB2	31	Phosphothreonine
+P40517	YIL063C	YRB2	179	Phosphoserine
+P50111	YMR273C	ZDS1	229	Phosphoserine
+P0CX65	YDR316W-A	TY1A-DR5	416	Phosphoserine
+Q99315	YGR109W-B	TY3B-G	2	N-acetylserine
+P47100	YJR029W	TY1B-JR2	416	Phosphoserine
+P0CX68	YLR035C-B	TY1A-LR1	416	Phosphoserine
+P0CX59	YOR142W-A	TY1A-OR	416	Phosphoserine
+P0C2I9	YPR137C-B	TY1B-PR1	416	Phosphoserine
+P0C2J1	YPR158C-D	TY1B-PR3	416	Phosphoserine
+P43587	YFR003C	YPI1	2	N-acetylserine
+P43587	YFR003C	YPI1	22	Phosphoserine
+P43587	YFR003C	YPI1	133	Phosphoserine
+P36019	YNL093W	YPT53	220	Cysteine
+P36019	YNL093W	YPT53	218	S-geranylgeranyl
+P36019	YNL093W	YPT53	220	S-geranylgeranyl
+P0CX57	YAR010C	TY1A-A	416	Phosphoserine
+P38749	YHL009C	YAP3	135	Phosphoserine
+Q12217	YBR012W-A	TY1A-BR	416	Phosphoserine
+Q12193	YBR012W-B	TY1B-BR	416	Phosphoserine
+Q12235	YLL055W	YCT1	500	Phosphoserine
+Q12235	YLL055W	YCT1	501	Phosphoserine
+Q12235	YLL055W	YCT1	146	N-linked
+Q03855	YDR098C-B	TY1B-DR1	416	Phosphoserine
+P0CX66	YER159C-A	TY1A-ER2	416	Phosphoserine
+P40028	YER041W	YEN1	730	Phosphoserine
+P40028	YER041W	YEN1	731	Phosphoserine
+Q12141	YGR027W-B	TY1B-GR1	416	Phosphoserine
+P0CX72	YLR157C-A	TY1A-LR2	416	Phosphoserine
+Q12441	YDR210C-C	TY1A-DR3	416	Phosphoserine
+Q99231	YDR210C-D	TY1B-DR3	416	Phosphoserine
+P0CX71	YER137C-A	TY1A-ER1	416	Phosphoserine
+P0C2I7	YLR256W-B/YLR256W-C	TY1B-LR4	416	Phosphoserine
+Q12402	YPR028W	YOP1	2	N-acetylserine
+Q6Q5H1	YPR158C-C	TY1A-PR3	416	Phosphoserine
+Q07688	YDL235C	YPD1	64	Phosphohistidine
+Q04116	YDR451C	YHP1	315	Phosphoserine
+P40017	YER024W	YAT2	2	N-acetylserine
+P40017	YER024W	YAT2	783	Phosphoserine
+P42937	YGR203W	YCH1	1	N-acetylmethionine
+P0CX67	YGR161C-C	TY1A-GR3	416	Phosphoserine
+P0CX74	YJR026W	TY1A-JR1	416	Phosphoserine
+P40544	YIL023C	YKE4	184	N-linked
+P40544	YIL023C	YKE4	274	N-linked
+P40544	YIL023C	YKE4	285	N-linked
+P0C2I3	YDR365W-B	TY1B-DR6	416	Phosphoserine
+Q12085	YGR027W-A	TY1A-GR1	416	Phosphoserine
+Q12485	YGR038C-A	TY1A-GR2	416	Phosphoserine
+Q12269	YGR038C-B	TY1B-GR2	416	Phosphoserine
+P0C2I6	YLR227W-B	TY1B-LR3	416	Phosphoserine
+P0CX76	YML040W	TY1A-ML2	416	Phosphoserine
+P38806	YHR090C	YNG2	183	Phosphoserine
+P38806	YHR090C	YNG2	185	Phosphothreonine
+P38806	YHR090C	YNG2	188	Phosphoserine
+P0CX73	YPL257W-A	TY1A-PL	416	Phosphoserine
+P0CX58	YPR137C-A	TY1A-PR1	416	Phosphoserine
+Q07950	YLR020C	YEH2	73	Phosphoserine
+Q07950	YLR020C	YEH2	107	Phosphoserine
+P25637	YCR059C	YIH1	187	Glycyl
+P53108	YGL161C	YIP5	60	Phosphoserine
+Q03434	YML039W	TY1B-ML2	416	Phosphoserine
+P38070	YBR028C	YPK3	90	Phosphoserine
+P38070	YBR028C	YPK3	105	Phosphoserine
+P38070	YBR028C	YPK3	107	Phosphothreonine
+P38070	YBR028C	YPK3	321	Phosphoserine%3B
+P38070	YBR028C	YPK3	490	Phosphothreonine%3B
+P38070	YBR028C	YPK3	513	Phosphoserine%3B
+P53057	YGL259W	YPS5	57	N-linked
+P38815	YHR105W	YPT35	65	Phosphoserine
+P38815	YHR105W	YPT35	66	Phosphoserine
+Q99260	YLR262C	YPT6	215	Cysteine
+Q99260	YLR262C	YPT6	213	S-geranylgeranyl
+Q99260	YLR262C	YPT6	215	S-geranylgeranyl
+P31111	YDR285W	ZIP1	481	Phosphoserine
+P40021	YER033C	ZRG8	275	Phosphoserine
+P40021	YER033C	ZRG8	354	Phosphoserine
+P40021	YER033C	ZRG8	403	Phosphoserine
+P40021	YER033C	ZRG8	407	Phosphoserine
+P40021	YER033C	ZRG8	632	Phosphoserine
+P40021	YER033C	ZRG8	676	Phosphoserine
+Q12512	YOL154W	ZPS1	28	N-linked
+Q12512	YOL154W	ZPS1	57	N-linked
+Q12512	YOL154W	ZPS1	98	N-linked
+Q12512	YOL154W	ZPS1	217	N-linked
+Q06325	YDR349C	YPS7	26	N-linked
+Q06325	YDR349C	YPS7	59	N-linked
+Q06325	YDR349C	YPS7	106	N-linked
+Q06325	YDR349C	YPS7	131	N-linked
+Q06325	YDR349C	YPS7	140	N-linked
+Q06325	YDR349C	YPS7	143	N-linked
+Q06325	YDR349C	YPS7	148	N-linked
+Q06325	YDR349C	YPS7	175	N-linked
+Q06325	YDR349C	YPS7	308	N-linked
+Q06325	YDR349C	YPS7	391	N-linked
+Q06325	YDR349C	YPS7	455	N-linked
+Q06325	YDR349C	YPS7	478	N-linked
+Q06325	YDR349C	YPS7	484	N-linked
+Q06325	YDR349C	YPS7	549	N-linked
+Q06325	YDR349C	YPS7	552	N-linked
+P38146	YBR264C	YPT10	199	Cysteine
+P38146	YBR264C	YPT10	197	S-geranylgeranyl
+P38146	YBR264C	YPT10	199	S-geranylgeranyl
+P38555	YER031C	YPT31	2	N-acetylserine
+P38555	YER031C	YPT31	222	S-geranylgeranyl
+P38555	YER031C	YPT31	223	S-geranylgeranyl
+P36018	YKR014C	YPT52	139	Phosphoserine
+P36018	YKR014C	YPT52	142	Phosphoserine
+P36018	YKR014C	YPT52	232	S-geranylgeranyl
+P36018	YKR014C	YPT52	233	S-geranylgeranyl
+P36018	YKR014C	YPT52	151	Glycyl
+P38280	YBR148W	YSW1	159	Phosphoserine
+P38280	YBR148W	YSW1	160	Phosphoserine
+Q12324	YOR087W	YVC1	636	Phosphothreonine
+P53303	YGR211W	ZPR1	23	Phosphoserine
+P53303	YGR211W	ZPR1	407	Phosphothreonine
+P0C2I5	YLR157C-B	TY1B-LR2	416	Phosphoserine
+Q04670	YMR050C	TY1B-MR2	416	Phosphoserine
+Q12470	YNL054W-A	TY1A-NL2	416	Phosphoserine
+Q92392	YOL103W-A	TY1A-OL	416	Phosphoserine
+P0CX60	YPR158W-A	TY1A-PR2	416	Phosphoserine
+Q12159	YDR381W	YRA1	2	N-acetylserine
+Q12159	YDR381W	YRA1	8	Phosphoserine
+Q12159	YDR381W	YRA1	100	Phosphoserine
+P53107	YGL164C	YRB30	272	Phosphothreonine
+Q12436	YLR130C	ZRT2	148	Phosphoserine
+Q12436	YLR130C	ZRT2	149	Phosphoserine
+Q12436	YLR130C	ZRT2	162	Phosphoserine
+Q12436	YLR130C	ZRT2	170	Phosphoserine
+Q12436	YLR130C	ZRT2	188	Phosphothreonine
+P32527	YGR285C	ZUO1	50	Phosphoserine
+P0CX75	YLR227W-A	TY1A-LR3	416	Phosphoserine
+Q04706	YML045W-A	TY1A-ML1	416	Phosphoserine
+P0CX69	YMR051C	TY1A-MR2	416	Phosphoserine
+Q03697	YML038C	YMD8	209	Phosphoserine
+Q03697	YML038C	YMD8	99	N-linked
+Q12273	YOL103W-B	TY1B-OL	416	Phosphoserine
+Q12697	YOR291W	YPK9	1	N-acetylmethionine
+Q12697	YOR291W	YPK9	95	Phosphothreonine
+Q12697	YOR291W	YPK9	108	Phosphoserine
+Q12697	YOR291W	YPK9	1117	Phosphoserine
+Q12697	YOR291W	YPK9	1120	Phosphoserine
+Q12303	YLR121C	YPS3	483	GPI-anchor
+Q12303	YLR121C	YPS3	75	N-linked
+Q12303	YLR121C	YPS3	120	N-linked
+Q12303	YLR121C	YPS3	160	N-linked
+Q12303	YLR121C	YPS3	163	N-linked
+Q12303	YLR121C	YPS3	275	N-linked
+Q12303	YLR121C	YPS3	309	N-linked
+Q12303	YLR121C	YPS3	328	N-linked
+Q12303	YLR121C	YPS3	367	N-linked
+Q12303	YLR121C	YPS3	422	N-linked
+Q12303	YLR121C	YPS3	445	N-linked
+Q12303	YLR121C	YPS3	462	N-linked
+P41920	YDR002W	YRB1	60	Phosphoserine
+Q08245	YOL109W	ZEO1	2	N-acetylserine
+Q08245	YOL109W	ZEO1	2	Phosphoserine
+Q08245	YOL109W	ZEO1	25	Phosphoserine
+Q08245	YOL109W	ZEO1	40	Phosphoserine
+Q08245	YOL109W	ZEO1	49	Phosphothreonine
+Q08245	YOL109W	ZEO1	18	Glycyl
+Q08245	YOL109W	ZEO1	23	Glycyl
+Q08245	YOL109W	ZEO1	29	Glycyl
+Q08245	YOL109W	ZEO1	34	Glycyl
+Q08245	YOL109W	ZEO1	45	Glycyl
+Q08245	YOL109W	ZEO1	57	Glycyl
+Q08245	YOL109W	ZEO1	82	Glycyl
+P32329	YLR120C	YPS1	548	GPI-anchor
+P32329	YLR120C	YPS1	95	N-linked
+P32329	YLR120C	YPS1	203	N-linked
+P32329	YLR120C	YPS1	232	N-linked
+P32329	YLR120C	YPS1	242	N-linked
+P32329	YLR120C	YPS1	245	N-linked
+P32329	YLR120C	YPS1	299	N-linked
+P32329	YLR120C	YPS1	358	N-linked
+P32329	YLR120C	YPS1	480	N-linked
+P32329	YLR120C	YPS1	522	N-linked
+P32329	YLR120C	YPS1	532	N-linked
+P01123	YFL038C	YPT1	1	N-acetylmethionine
+P01123	YFL038C	YPT1	172	Phosphoserine
+P01123	YFL038C	YPT1	174	Phosphoserine
+P01123	YFL038C	YPT1	23	S-palmitoyl
+P01123	YFL038C	YPT1	123	S-palmitoyl
+P01123	YFL038C	YPT1	205	S-geranylgeranyl
+P01123	YFL038C	YPT1	206	S-geranylgeranyl
+P01123	YFL038C	YPT1	144	Glycyl
+P47043	YJL056C	ZAP1	156	Phosphoserine
+P47043	YJL056C	ZAP1	166	Phosphoserine
+P47043	YJL056C	ZAP1	515	Phosphoserine
+P54786	YML109W	ZDS2	50	Phosphoserine
+P35723	YKL065C	YET1	190	Glycyl
+Q12173	YGR109W-A	TY3A-G	2	N-acetylserine
+P38616	YNL160W	YGP1	40	N-linked
+P38616	YNL160W	YGP1	50	N-linked
+P38616	YNL160W	YGP1	53	N-linked
+P38616	YNL160W	YGP1	58	N-linked
+P38616	YNL160W	YGP1	61	N-linked
+P38616	YNL160W	YGP1	65	N-linked
+P38616	YNL160W	YGP1	87	N-linked
+P38616	YNL160W	YGP1	94	N-linked
+P38616	YNL160W	YGP1	100	N-linked
+P38616	YNL160W	YGP1	106	N-linked
+P38616	YNL160W	YGP1	118	N-linked
+P38616	YNL160W	YGP1	172	N-linked
+P38616	YNL160W	YGP1	239	N-linked
+P38616	YNL160W	YGP1	286	N-linked
+P47099	YJR028W	TY1A-JR2	416	Phosphoserine
+P0C2I8	YLR256W-A	TY1A-LR4	416	Phosphoserine
+Q12414	YPL257W-B	TY1B-PL	416	Phosphoserine
+Q12010	YOL092W	YPQ1	9	N-linked
+Q12010	YOL092W	YPQ1	189	N-linked
+Q12010	YOL092W	YPQ1	275	N-linked
+P32793	YHR016C	YSC84	301	Phosphoserine
+P32793	YHR016C	YSC84	311	Phosphoserine
+P26725	YJL139C	YUR1	77	N-linked
+P26725	YJL139C	YUR1	82	N-linked
+P26725	YJL139C	YUR1	92	N-linked
+P26725	YJL139C	YUR1	167	N-linked
+P26725	YJL139C	YUR1	414	N-linked
+P53735	YNR039C	ZRG17	16	Phosphoserine
+P53735	YNR039C	ZRG17	131	Phosphoserine
+P53735	YNR039C	ZRG17	498	Phosphoserine
+P20107	YMR243C	ZRC1	387	Phosphoserine
+P20107	YMR243C	ZRC1	393	Phosphoserine
+P20107	YMR243C	ZRC1	397	Phosphoserine
+P20107	YMR243C	ZRC1	357	Glycyl
+P34240	YKL175W	ZRT3	178	Phosphoserine
+P34240	YKL175W	ZRT3	188	Phosphoserine
+Q06681	YDR326C	YSP2	13	Phosphoserine
+Q06681	YDR326C	YSP2	411	Phosphoserine
+Q06681	YDR326C	YSP2	596	Phosphoserine
+Q06681	YDR326C	YSP2	1032	Phosphoserine
+Q06681	YDR326C	YSP2	1306	N-linked
+Q06681	YDR326C	YSP2	1373	N-linked
+Q06681	YDR326C	YSP2	1430	N-linked
+P15891	YCR088W	ABP1	2	N-acetylalanine
+P15891	YCR088W	ABP1	165	Phosphothreonine
+P15891	YCR088W	ABP1	167	Phosphoserine
+P15891	YCR088W	ABP1	169	Phosphoserine
+P15891	YCR088W	ABP1	181	Phosphothreonine
+P15891	YCR088W	ABP1	183	Phosphoserine
+P15891	YCR088W	ABP1	313	Phosphoserine
+P15891	YCR088W	ABP1	365	Phosphoserine
+P15891	YCR088W	ABP1	389	Phosphoserine
+P15891	YCR088W	ABP1	458	Phosphoserine
+P15891	YCR088W	ABP1	481	Phosphoserine
+P15891	YCR088W	ABP1	464	Glycyl
+P32316	YBL015W	ACH1	2	N-acetylthreonine
+P32316	YBL015W	ACH1	350	Phosphoserine
+Q00362	YGL190C	CDC55	124	Phosphoserine
+P47096	YJR025C	BNA1	176	Phosphoserine
+P32357	YBL074C	AAR2	253	Phosphoserine
+P32357	YBL074C	AAR2	274	Phosphothreonine
+P32357	YBL074C	AAR2	328	Phosphotyrosine
+P32357	YBL074C	AAR2	331	Phosphoserine
+P32357	YBL074C	AAR2	345	Phosphothreonine
+P07248	YDR216W	ADR1	54	Phosphoserine
+P07248	YDR216W	ADR1	188	Phosphothreonine
+P07248	YDR216W	ADR1	193	Phosphothreonine
+P07248	YDR216W	ADR1	230	Phosphoserine%3B
+P07248	YDR216W	ADR1	258	Phosphoserine
+P07248	YDR216W	ADR1	259	Phosphothreonine
+P07248	YDR216W	ADR1	299	Phosphoserine
+P07248	YDR216W	ADR1	323	Phosphoserine
+P07248	YDR216W	ADR1	325	Phosphoserine
+P07248	YDR216W	ADR1	327	Phosphothreonine
+P38903	YOR014W	RTS1	242	Phosphothreonine
+P38903	YOR014W	RTS1	257	Phosphothreonine
+P47129	YJR083C	ACF4	44	Phosphoserine
+P47129	YJR083C	ACF4	71	Phosphoserine
+P47129	YJR083C	ACF4	74	Phosphoserine
+P47129	YJR083C	ACF4	78	Phosphoserine
+P47129	YJR083C	ACF4	165	Phosphoserine
+P47129	YJR083C	ACF4	288	Phosphoserine
+P14164	YKL112W	ABF1	189	Phosphothreonine
+P14164	YKL112W	ABF1	193	Phosphoserine
+P14164	YKL112W	ABF1	467	Phosphoserine
+P14164	YKL112W	ABF1	554	Phosphoserine
+P14164	YKL112W	ABF1	618	Phosphoserine
+P14164	YKL112W	ABF1	624	Phosphoserine%3B
+P14164	YKL112W	ABF1	720	Phosphoserine%3B
+P14164	YKL112W	ABF1	18	Glycyl
+P40535	YIL036W	CST6	171	Phosphoserine
+P40535	YIL036W	CST6	179	Phosphoserine
+P40535	YIL036W	CST6	399	Phosphoserine
+P40535	YIL036W	CST6	557	Phosphoserine
+P40535	YIL036W	CST6	559	Phosphothreonine
+P31787	YGR037C	ACB1	51	Glycyl
+P31787	YGR037C	ACB1	72	Glycyl
+P32323	YNR044W	AGA1	699	GPI-anchor
+Q12471	YOL136C	PFK27	55	Glycyl
+P23542	YLR027C	AAT2	2	N-acetylserine
+P23542	YLR027C	AAT2	255	N6-(pyridoxal
+P23542	YLR027C	AAT2	389	Phosphoserine
+Q07622	YDL203C	ACK1	184	Glycyl
+Q07622	YDL203C	ACK1	191	Glycyl
+Q03771	YDR161W	ACL4	2	N-acetylserine
+P21192	YLR131C	ACE2	80	Phosphoserine
+P21192	YLR131C	ACE2	122	Phosphoserine
+P21192	YLR131C	ACE2	247	Phosphoserine
+P21192	YLR131C	ACE2	249	Phosphoserine
+P21192	YLR131C	ACE2	253	Phosphoserine
+P21192	YLR131C	ACE2	259	Phosphothreonine
+P21192	YLR131C	ACE2	385	Phosphoserine
+P21192	YLR131C	ACE2	392	Phosphoserine
+P21192	YLR131C	ACE2	483	Phosphoserine
+P21192	YLR131C	ACE2	486	Phosphothreonine
+P21192	YLR131C	ACE2	501	Phosphothreonine
+P21192	YLR131C	ACE2	564	Phosphoserine
+P21192	YLR131C	ACE2	709	Phosphoserine
+P21192	YLR131C	ACE2	714	Phosphoserine
+P28240	YER065C	ICL1	53	Phosphothreonine
+P38720	YHR183W	GND1	50	Phosphoserine
+Q01802	YKL106W	AAT1	286	N6-(pyridoxal
+Q08641	YOR239W	ABP140	93	Phosphoserine
+Q08641	YOR239W	ABP140	150	Phosphothreonine
+Q08641	YOR239W	ABP140	321	Phosphoserine
+Q08641	YOR239W	ABP140	326	Phosphoserine
+Q08641	YOR239W	ABP140	347	Phosphothreonine
+P40433	YIL107C	PFK26	92	Phosphoserine
+P40433	YIL107C	PFK26	157	Phosphothreonine
+P40433	YIL107C	PFK26	644	Phosphoserine
+P40433	YIL107C	PFK26	652	Phosphoserine
+P40433	YIL107C	PFK26	659	Phosphoserine
+P40433	YIL107C	PFK26	667	Phosphoserine
+Q00955	YNR016C	ACC1	2	N-acetylserine
+Q00955	YNR016C	ACC1	2	Phosphoserine
+Q00955	YNR016C	ACC1	735	N6-biotinyllysine
+Q00955	YNR016C	ACC1	790	Phosphoserine
+Q00955	YNR016C	ACC1	1148	Phosphoserine
+Q00955	YNR016C	ACC1	1157	Phosphoserine
+Q00955	YNR016C	ACC1	1162	Phosphoserine
+P40529	YIL044C	AGE2	2	N-acetylserine
+P40529	YIL044C	AGE2	180	Phosphoserine
+P40529	YIL044C	AGE2	183	Phosphoserine
+P40529	YIL044C	AGE2	207	Phosphoserine
+P46680	YMR092C	AIP1	2	N-acetylserine
+P52893	YLR089C	ALT1	77	Phosphoserine
+P52893	YLR089C	ALT1	412	N6-(pyridoxal
+P38065	YBL037W	APL3	727	Phosphothreonine
+P38065	YBL037W	APL3	733	Phosphoserine
+P53886	YNL172W	APC1	1462	Phosphoserine
+P36154	YKR074W	AIM29	78	Phosphoserine
+P46367	YOR374W	ALD4	96	Phosphoserine
+P46367	YOR374W	ALD4	216	Phosphothreonine
+P46367	YOR374W	ALD4	500	Phosphoserine
+P40350	YPL227C	ALG5	83	N-linked
+P40350	YPL227C	ALG5	119	N-linked
+P43633	YGL021W	ALK1	76	Phosphoserine
+P43633	YGL021W	ALK1	79	Phosphoserine
+Q08269	YOL130W	ALR1	2	N-acetylserine
+Q08269	YOL130W	ALR1	77	Phosphotyrosine
+Q08269	YOL130W	ALR1	85	Phosphoserine
+Q08269	YOL130W	ALR1	185	Phosphoserine
+Q08269	YOL130W	ALR1	188	Phosphoserine
+Q08269	YOL130W	ALR1	220	Phosphoserine
+Q08269	YOL130W	ALR1	221	Phosphoserine
+Q08269	YOL130W	ALR1	236	Phosphoserine
+Q08269	YOL130W	ALR1	242	Phosphothreonine
+Q08269	YOL130W	ALR1	850	Phosphoserine
+P14904	YKL103C	APE1	356	Phosphoserine
+P14904	YKL103C	APE1	107	N-linked
+P14904	YKL103C	APE1	110	N-linked
+P14904	YKL103C	APE1	448	N-linked
+P60010	YFL039C	ACT1	1	N-acetylmethionine
+P60010	YFL039C	ACT1	191	Glycyl
+P25371	YCR011C	ADP1	659	Phosphoserine
+P25371	YCR011C	ADP1	702	Phosphoserine
+P25371	YCR011C	ADP1	50	N-linked
+P25371	YCR011C	ADP1	114	N-linked
+P25371	YCR011C	ADP1	165	N-linked
+P25371	YCR011C	ADP1	221	N-linked
+P25371	YCR011C	ADP1	935	N-linked
+P33304	YDR085C	AFR1	472	Phosphoserine
+P33304	YDR085C	AFR1	526	Phosphoserine
+P43636	YGL065C	ALG2	170	N-linked
+P43636	YGL065C	ALG2	303	N-linked
+P43636	YGL065C	ALG2	371	N-linked
+P43636	YGL065C	ALG2	400	N-linked
+P47029	YJL084C	ALY2	155	Phosphoserine
+P47029	YJL084C	ALY2	162	Phosphoserine
+P47029	YJL084C	ALY2	213	Phosphoserine
+P47029	YJL084C	ALY2	586	Phosphoserine
+P47029	YJL084C	ALY2	826	Phosphoserine
+P47029	YJL084C	ALY2	838	Phosphoserine
+P47029	YJL084C	ALY2	900	Phosphoserine
+P47029	YJL084C	ALY2	1022	Phosphoserine
+P47029	YJL084C	ALY2	1023	Phosphoserine
+P40502	YIL087C	AIM19	2	N-acetylserine
+P40563	YIR003W	AIM21	18	Phosphothreonine
+P40563	YIR003W	AIM21	36	Phosphoserine
+P40563	YIR003W	AIM21	58	Phosphothreonine
+P40563	YIR003W	AIM21	70	Phosphoserine
+P40563	YIR003W	AIM21	85	Phosphothreonine
+P40563	YIR003W	AIM21	104	Phosphoserine
+P40563	YIR003W	AIM21	183	Phosphoserine
+P40563	YIR003W	AIM21	206	Phosphoserine
+P40563	YIR003W	AIM21	231	Phosphoserine
+P40563	YIR003W	AIM21	277	Phosphothreonine
+P40563	YIR003W	AIM21	284	Phosphoserine
+P40563	YIR003W	AIM21	324	Phosphoserine
+P40563	YIR003W	AIM21	552	Phosphothreonine
+P40563	YIR003W	AIM21	576	Phosphoserine
+P40563	YIR003W	AIM21	620	Phosphoserine
+P40563	YIR003W	AIM21	623	Phosphoserine
+P40563	YIR003W	AIM21	625	Phosphoserine
+P40563	YIR003W	AIM21	627	Phosphoserine
+P40563	YIR003W	AIM21	667	Phosphoserine
+P40563	YIR003W	AIM21	671	Phosphoserine
+P40563	YIR003W	AIM21	675	Phosphoserine
+P40563	YIR003W	AIM21	678	Phosphoserine
+P16550	YCL050C	APA1	60	Phosphothreonine
+P00330	YOL086C	ADH1	2	N-acetylserine
+P00330	YOL086C	ADH1	213	Phosphoserine
+P00330	YOL086C	ADH1	223	Phosphothreonine
+P00330	YOL086C	ADH1	279	Phosphoserine
+P00330	YOL086C	ADH1	316	Phosphoserine
+P00330	YOL086C	ADH1	226	Glycyl
+P00330	YOL086C	ADH1	234	Glycyl
+P00330	YOL086C	ADH1	287	Glycyl
+P00330	YOL086C	ADH1	319	Glycyl
+P00331	YMR303C	ADH2	2	N-acetylserine
+P00331	YMR303C	ADH2	213	Phosphoserine
+P00331	YMR303C	ADH2	223	Phosphothreonine
+P00331	YMR303C	ADH2	279	Phosphoserine
+P00331	YMR303C	ADH2	316	Phosphoserine
+P00331	YMR303C	ADH2	226	Glycyl
+P00331	YMR303C	ADH2	234	Glycyl
+P00331	YMR303C	ADH2	287	Glycyl
+P00331	YMR303C	ADH2	319	Glycyl
+Q04894	YMR318C	ADH6	131	Phosphoserine
+Q04894	YMR318C	ADH6	315	Phosphoserine
+Q04894	YMR318C	ADH6	359	Phosphoserine
+P38266	YBR108W	AIM3	57	Phosphoserine
+P38266	YBR108W	AIM3	58	Phosphoserine
+P38266	YBR108W	AIM3	64	Phosphoserine
+P38266	YBR108W	AIM3	476	Phosphoserine
+P38266	YBR108W	AIM3	729	Phosphothreonine
+P38266	YBR108W	AIM3	861	Phosphothreonine
+Q99299	YPL158C	AIM44	25	Phosphoserine
+P53954	YNL048W	ALG11	262	N-linked
+P53954	YNL048W	ALG11	393	N-linked
+P53954	YNL048W	ALG11	480	N-linked
+P53954	YNL048W	ALG11	490	N-linked
+P38313	YBR211C	AME1	41	Phosphoserine
+P38313	YBR211C	AME1	45	Phosphoserine
+P38313	YBR211C	AME1	53	Phosphoserine
+P38313	YBR211C	AME1	59	Phosphoserine
+P38313	YBR211C	AME1	101	Phosphoserine
+P52910	YLR153C	ACS2	679	Phosphoserine
+P52910	YLR153C	ACS2	506	Glycyl
+P25376	YCL025C	AGP1	6	Phosphoserine
+P25376	YCL025C	AGP1	633	S-palmitoyl
+P25376	YCL025C	AGP1	11	Glycyl
+P10869	YER052C	HOM3	333	Phosphothreonine
+Q08548	YOR175C	ALE1	513	Phosphoserine
+Q08548	YOR175C	ALE1	605	Phosphoserine
+Q08548	YOR175C	ALE1	610	Phosphoserine
+Q08548	YOR175C	ALE1	615	Phosphoserine
+P36117	YKR021W	ALY1	220	Phosphoserine
+P38113	YBR145W	ADH5	226	Phosphothreonine
+P38113	YBR145W	ADH5	282	Phosphoserine
+P38113	YBR145W	ADH5	319	Phosphoserine
+P38113	YBR145W	ADH5	229	Glycyl
+P38113	YBR145W	ADH5	237	Glycyl
+P38113	YBR145W	ADH5	290	Glycyl
+Q12013	YOR034C	AKR2	534	N-linked
+P52892	YDR111C	ALT2	327	N6-(pyridoxal
+P14540	YKL060C	FBA1	11	Phosphothreonine
+P14540	YKL060C	FBA1	56	Phosphoserine
+P14540	YKL060C	FBA1	63	Phosphoserine
+P14540	YKL060C	FBA1	76	Phosphoserine
+P14540	YKL060C	FBA1	83	Phosphoserine
+P14540	YKL060C	FBA1	96	Phosphoserine
+P14540	YKL060C	FBA1	147	Phosphoserine
+P14540	YKL060C	FBA1	150	Phosphothreonine
+P14540	YKL060C	FBA1	179	Phosphothreonine
+P14540	YKL060C	FBA1	268	Phosphoserine
+P14540	YKL060C	FBA1	290	Phosphothreonine
+P14540	YKL060C	FBA1	310	Phosphotyrosine
+P14540	YKL060C	FBA1	313	Phosphoserine
+P14540	YKL060C	FBA1	27	Glycyl
+P14540	YKL060C	FBA1	73	Glycyl
+P14540	YKL060C	FBA1	85	Glycyl
+P14540	YKL060C	FBA1	308	Glycyl
+P50076	YGR227W	DIE2	31	N-linked
+P50076	YGR227W	DIE2	278	N-linked
+P50076	YGR227W	DIE2	372	N-linked
+P32375	YIR027C	DAL1	157	N6-carboxylysine
+P54783	YML086C	ALO1	56	Pros-8alpha-FAD
+P38971	YNL270C	ALP1	39	Phosphothreonine
+Q08981	YPL267W	ACM1	48	Phosphoserine
+Q08981	YPL267W	ACM1	161	Phosphothreonine
+Q08981	YPL267W	ACM1	202	Phosphoserine
+P32463	YKL192C	ACP1	82	O-(pantetheine
+P25377	YCR105W	ADH7	132	Phosphoserine
+P25377	YCR105W	ADH7	316	Phosphoserine
+P32781	YGL032C	AGA2	22	O-linked
+P32781	YGL032C	AGA2	30	O-linked
+P32781	YGL032C	AGA2	32	O-linked
+P32781	YGL032C	AGA2	39	O-linked
+P32781	YGL032C	AGA2	63	O-linked
+P32781	YGL032C	AGA2	66	O-linked
+P32781	YGL032C	AGA2	75	O-linked
+P38628	YEL058W	PCM1	67	Phosphoserine
+P43567	YFL030W	AGX1	201	N6-(pyridoxal
+Q12476	YDL175C	AIR2	31	Phosphoserine
+Q12476	YDL175C	AIR2	49	Phosphoserine
+P19414	YLR304C	ACO1	391	Phosphoserine
+P19414	YLR304C	ACO1	409	Phosphothreonine
+P19414	YLR304C	ACO1	556	Phosphoserine
+Q03233	YMR184W	ADD37	79	Phosphoserine
+Q12433	YOR023C	AHC1	282	Phosphoserine
+Q12433	YOR023C	AHC1	505	Phosphoserine
+P38013	YLR109W	AHP1	2	N-acetylserine
+P38013	YLR109W	AHP1	28	Phosphoserine
+P38013	YLR109W	AHP1	59	Phosphoserine
+P38013	YLR109W	AHP1	116	Phosphoserine
+P38013	YLR109W	AHP1	32	Glycyl
+P38013	YLR109W	AHP1	48	Glycyl
+P38013	YLR109W	AHP1	113	Glycyl
+Q12156	YDR063W	AIM7	2	N-acetylserine
+Q12156	YDR063W	AIM7	137	Phosphoserine
+P40507	YIL079C	AIR1	37	Phosphoserine
+P39010	YDR264C	AKR1	51	Phosphoserine
+P39010	YDR264C	AKR1	57	Phosphoserine
+P38840	YHR137W	ARO9	90	Phosphoserine
+P38840	YHR137W	ARO9	92	Phosphoserine
+P80428	YJL081C	ARP4	349	Phosphoserine
+P40467	YIL130W	ASG1	166	Phosphoserine%3B
+P40467	YIL130W	ASG1	186	Phosphoserine
+P40467	YIL130W	ASG1	963	Phosphoserine
+P34233	YKL185W	ASH1	56	Phosphoserine
+P34233	YKL185W	ASH1	465	Phosphoserine
+P49435	YML022W	APT1	68	Phosphoserine
+P18544	YOL140W	ARG8	276	N6-(pyridoxal
+P53974	YNL020C	ARK1	478	Phosphoserine
+P53974	YNL020C	ARK1	522	Phosphoserine
+P53974	YNL020C	ARK1	535	Phosphoserine
+P38116	YBR164C	ARL1	2	N-myristoyl
+P40994	YOR094W	ARF3	2	N-myristoyl
+P53090	YGL202W	ARO8	100	Phosphoserine
+P32449	YBR249C	ARO4	2	N-acetylserine
+P53946	YNL059C	ARP5	7	Phosphoserine
+P53946	YNL059C	ARP5	24	Phosphothreonine
+P53946	YNL059C	ARP5	383	Phosphoserine
+P53946	YNL059C	ARP5	12	Glycyl
+Q12386	YOR141C	ARP8	65	Phosphoserine
+Q12386	YOR141C	ARP8	70	Phosphoserine
+P53731	YNR035C	ARC35	155	Phosphothreonine
+P53731	YNR035C	ARC35	324	Phosphoserine
+P38986	YDR321W	ASP1	350	Phosphoserine
+P40024	YER036C	ARB1	43	Phosphoserine
+P40024	YER036C	ARB1	65	Phosphoserine
+P40024	YER036C	ARB1	196	Phosphoserine
+P40024	YER036C	ARB1	446	Phosphothreonine
+P11076	YDL192W	ARF1	2	N-myristoyl
+P11076	YDL192W	ARF1	127	Glycyl
+P00812	YPL111W	CAR1	1	N-acetylmethionine
+P00812	YPL111W	CAR1	16	Phosphoserine
+P00812	YPL111W	CAR1	77	Phosphothreonine
+P00812	YPL111W	CAR1	270	Phosphothreonine
+P15274	YML035C	AMD1	19	Phosphoserine
+P15274	YML035C	AMD1	58	Phosphoserine
+P15274	YML035C	AMD1	61	Phosphoserine
+P15274	YML035C	AMD1	138	Phosphoserine
+Q08951	YPL195W	APL5	2	N-acetylthreonine
+Q08951	YPL195W	APL5	700	Phosphoserine
+Q08951	YPL195W	APL5	727	Phosphoserine
+Q08951	YPL195W	APL5	767	Phosphothreonine
+Q08951	YPL195W	APL5	770	Phosphoserine
+Q08951	YPL195W	APL5	773	Phosphoserine
+Q08951	YPL195W	APL5	798	Phosphoserine
+Q08951	YPL195W	APL5	888	Phosphoserine
+Q08951	YPL195W	APL5	918	Phosphoserine
+P36973	YDR441C	APT2	2	N-acetylserine
+P25628	YCR048W	ARE1	21	Phosphoserine
+P25628	YCR048W	ARE1	45	Phosphoserine
+P36090	YKL047W	ANR2	511	S-palmitoyl
+P36090	YKL047W	ANR2	516	S-palmitoyl
+P46682	YGR261C	APL6	693	Phosphoserine
+P46682	YGR261C	APL6	698	Phosphoserine
+P46682	YGR261C	APL6	724	Phosphoserine
+P46682	YGR261C	APL6	726	Phosphoserine
+P04076	YHR018C	ARG4	27	Phosphoserine
+P38832	YHR126C	ANS1	137	GPI-anchor
+P37302	YBR286W	APE3	85	N-linked
+P37302	YBR286W	APE3	96	N-linked
+P37302	YBR286W	APE3	115	N-linked
+P37302	YBR286W	APE3	150	N-linked
+P37302	YBR286W	APE3	162	N-linked
+P37302	YBR286W	APE3	371	N-linked
+P37302	YBR286W	APE3	427	N-linked
+P37302	YBR286W	APE3	480	N-linked
+P22936	YKL114C	APN1	356	Phosphoserine
+Q06408	YDR380W	ARO10	588	Glycyl
+P38080	YBR059C	AKL1	2	N-acetylserine
+P38080	YBR059C	AKL1	10	Phosphoserine
+P38080	YBR059C	AKL1	407	Phosphoserine
+P38080	YBR059C	AKL1	471	Phosphothreonine
+P38080	YBR059C	AKL1	504	Phosphoserine
+P38080	YBR059C	AKL1	541	Phosphoserine
+P38080	YBR059C	AKL1	574	Phosphoserine
+P38080	YBR059C	AKL1	801	Phosphoserine
+P38080	YBR059C	AKL1	846	Phosphoserine
+P38080	YBR059C	AKL1	953	Phosphoserine
+P38080	YBR059C	AKL1	960	Phosphoserine
+P38080	YBR059C	AKL1	1048	Phosphoserine
+P38080	YBR059C	AKL1	1072	Phosphoserine
+P38080	YBR059C	AKL1	1008	Glycyl
+P38080	YBR059C	AKL1	1046	Glycyl
+P54115	YPL061W	ALD6	3	Glycyl
+P54115	YPL061W	ALD6	142	Glycyl
+P54115	YPL061W	ALD6	196	Glycyl
+P16661	YBR110W	ALG1	88	N-linked
+P16661	YBR110W	ALG1	199	N-linked
+P16661	YBR110W	ALG1	425	N-linked
+P19880	YML007W	YAP1	9	Phosphoserine
+P19880	YML007W	YAP1	14	Phosphoserine
+P19880	YML007W	YAP1	17	Phosphoserine
+P19880	YML007W	YAP1	165	Phosphothreonine
+P19880	YML007W	YAP1	204	Phosphoserine
+P19880	YML007W	YAP1	372	Phosphoserine
+P19880	YML007W	YAP1	528	Phosphoserine
+P27351	YJR005W	APL1	649	Phosphoserine
+P27351	YJR005W	APL1	652	Phosphothreonine
+P27351	YJR005W	APL1	683	Phosphoserine
+Q99186	YOL062C	APM4	179	Phosphoserine
+Q99186	YOL062C	APM4	180	Phosphoserine
+Q99186	YOL062C	APM4	181	Phosphoserine
+P38115	YBR149W	ARA1	151	Phosphothreonine
+P53309	YGR241C	YAP1802	449	Phosphothreonine
+P53309	YGR241C	YAP1802	282	Glycyl
+P13586	YGL167C	PMR1	2	N-acetylserine
+P13586	YGL167C	PMR1	227	Phosphoserine
+Q12675	YDR093W	DNF2	70	Phosphothreonine
+Q12675	YDR093W	DNF2	85	Phosphoserine
+Q12675	YDR093W	DNF2	389	Phosphoserine
+Q12675	YDR093W	DNF2	392	Phosphoserine
+Q12675	YDR093W	DNF2	396	Phosphoserine
+Q12675	YDR093W	DNF2	403	Phosphoserine
+Q12675	YDR093W	DNF2	406	Phosphotyrosine
+Q12675	YDR093W	DNF2	782	Phosphothreonine
+Q12675	YDR093W	DNF2	1542	Phosphoserine
+Q12675	YDR093W	DNF2	1592	Phosphoserine
+Q12675	YDR093W	DNF2	938	Glycyl
+P40527	YIL048W	NEO1	102	Phosphoserine
+P40527	YIL048W	NEO1	551	Phosphoserine
+P38316	YBR217W	ATG12	186	Glycyl
+Q06628	YPR185W	ATG13	344	Phosphoserine%3B
+Q06628	YPR185W	ATG13	348	Phosphoserine%3B
+Q06628	YPR185W	ATG13	355	Phosphoserine
+Q06628	YPR185W	ATG13	437	Phosphoserine%3B
+Q06628	YPR185W	ATG13	438	Phosphoserine%3B
+Q06628	YPR185W	ATG13	461	Phosphoserine
+Q06628	YPR185W	ATG13	496	Phosphoserine%3B
+Q06628	YPR185W	ATG13	535	Phosphoserine%3B
+Q06628	YPR185W	ATG13	541	Phosphoserine%3B
+Q06628	YPR185W	ATG13	554	Phosphoserine
+Q06628	YPR185W	ATG13	581	Phosphoserine%3B
+Q06628	YPR185W	ATG13	646	Phosphoserine%3B
+Q06628	YPR185W	ATG13	649	Phosphoserine%3B
+P21306	YPL271W	ATP15	52	Phosphothreonine
+P00830	YJR121W	ATP2	112	Phosphothreonine
+P00830	YJR121W	ATP2	237	Phosphothreonine
+P00830	YJR121W	ATP2	373	Phosphoserine
+P05626	YPL078C	ATP4	144	Phosphoserine
+Q07528	YDL113C	ATG20	2	N-acetylserine
+Q07528	YDL113C	ATG20	361	Phosphoserine
+Q07528	YDL113C	ATG20	363	Phosphoserine
+P48016	YPR026W	ATH1	28	N-linked
+P48016	YPR026W	ATH1	32	N-linked
+P48016	YPR026W	ATH1	98	N-linked
+P48016	YPR026W	ATH1	207	N-linked
+P48016	YPR026W	ATH1	238	N-linked
+P48016	YPR026W	ATH1	247	N-linked
+P48016	YPR026W	ATH1	255	N-linked
+P48016	YPR026W	ATH1	259	N-linked
+P48016	YPR026W	ATH1	325	N-linked
+P48016	YPR026W	ATH1	370	N-linked
+P48016	YPR026W	ATH1	376	N-linked
+P48016	YPR026W	ATH1	488	N-linked
+P48016	YPR026W	ATH1	539	N-linked
+P48016	YPR026W	ATH1	568	N-linked
+P48016	YPR026W	ATH1	628	N-linked
+P48016	YPR026W	ATH1	638	N-linked
+P48016	YPR026W	ATH1	696	N-linked
+P48016	YPR026W	ATH1	705	N-linked
+P48016	YPR026W	ATH1	879	N-linked
+P48016	YPR026W	ATH1	897	N-linked
+P48016	YPR026W	ATH1	910	N-linked
+P48016	YPR026W	ATH1	972	N-linked
+P48016	YPR026W	ATH1	990	N-linked
+P48016	YPR026W	ATH1	1031	N-linked
+P48016	YPR026W	ATH1	1049	N-linked
+P48016	YPR026W	ATH1	1064	N-linked
+P48016	YPR026W	ATH1	1147	N-linked
+P48016	YPR026W	ATH1	1157	N-linked
+Q12233	YPR020W	ATP20	1	N-acetylmethionine
+Q12233	YPR020W	ATP20	3	Phosphoserine
+Q12233	YPR020W	ATP20	62	Phosphoserine
+Q12500	YLR114C	AVL9	519	Phosphoserine
+Q12500	YLR114C	AVL9	524	Phosphoserine
+Q05933	YLR370C	ARC18	29	Glycyl
+P0CX79	YLR160C	ASP3-4	29	N-linked
+P0CX79	YLR160C	ASP3-4	93	N-linked
+P0CX79	YLR160C	ASP3-4	239	N-linked
+P25641	YCR068W	ATG15	173	N-linked
+P25641	YCR068W	ATG15	202	N-linked
+P25641	YCR068W	ATG15	208	N-linked
+P35193	YOL082W	ATG19	136	Phosphoserine
+P35193	YOL082W	ATG19	141	Phosphoserine
+P35193	YOL082W	ATG19	243	Phosphoserine
+P35193	YOL082W	ATG19	213	Glycyl
+P35193	YOL082W	ATG19	216	Glycyl
+P53104	YGL180W	ATG1	34	Phosphoserine
+P53104	YGL180W	ATG1	129	Phosphothreonine
+P53104	YGL180W	ATG1	226	Phosphothreonine%3B
+P53104	YGL180W	ATG1	304	Phosphoserine
+P53104	YGL180W	ATG1	365	Phosphoserine
+P53104	YGL180W	ATG1	390	Phosphoserine
+P53104	YGL180W	ATG1	508	Phosphoserine%3B
+P53104	YGL180W	ATG1	515	Phosphoserine%3B
+P53104	YGL180W	ATG1	533	Phosphoserine
+P53104	YGL180W	ATG1	551	Phosphoserine
+P53104	YGL180W	ATG1	552	Phosphoserine
+P53104	YGL180W	ATG1	590	Phosphothreonine
+P53104	YGL180W	ATG1	621	Phosphoserine
+P53104	YGL180W	ATG1	635	Phosphoserine
+P53104	YGL180W	ATG1	638	Phosphoserine
+P53104	YGL180W	ATG1	647	Phosphoserine
+P53104	YGL180W	ATG1	677	Phosphoserine
+P53104	YGL180W	ATG1	680	Phosphoserine
+P53104	YGL180W	ATG1	683	Phosphoserine
+P53104	YGL180W	ATG1	769	Phosphoserine
+P53104	YGL180W	ATG1	783	Phosphoserine
+P53867	YNL223W	ATG4	488	Phosphoserine
+Q12380	YPL149W	ATG5	149	Glycyl
+Q12092	YPL166W	ATG29	106	Phosphoserine
+Q12092	YPL166W	ATG29	187	Phosphoserine
+Q12092	YPL166W	ATG29	188	Phosphoserine
+P40458	YIL146C	ATG32	114	Phosphoserine
+P40458	YIL146C	ATG32	119	Phosphoserine
+P38182	YBL078C	ATG8	116	Phosphatidylethanolamine
+P32453	YNL315C	ATP11	109	Phosphoserine
+P40851	YPR122W	AXL1	262	Phosphoserine
+Q06541	YLR242C	ARV1	296	N-linked
+P46993	YJL170C	ASG7	121	Phosphoserine
+P46993	YJL170C	ASG7	123	Phosphoserine
+P46993	YJL170C	ASG7	125	Phosphoserine
+P46993	YJL170C	ASG7	153	Phosphothreonine
+P54074	YMR119W	ASI1	2	N-linked
+P54074	YMR119W	ASI1	19	N-linked
+P54074	YMR119W	ASI1	29	N-linked
+P48361	YGR097W	ASK10	344	Phosphoserine
+P48361	YGR097W	ASK10	793	Phosphoserine
+P48361	YGR097W	ASK10	808	Phosphothreonine
+P48361	YGR097W	ASK10	944	Phosphoserine
+P48361	YGR097W	ASK10	969	Phosphoserine
+P48361	YGR097W	ASK10	1017	Phosphothreonine
+P48361	YGR097W	ASK10	1070	Phosphoserine
+P48361	YGR097W	ASK10	1095	Phosphoserine
+P48361	YGR097W	ASK10	1098	Phosphoserine
+P32660	YER166W	DNF1	53	Phosphoserine
+P32660	YER166W	DNF1	70	Phosphothreonine
+P32660	YER166W	DNF1	81	Phosphoserine
+P32660	YER166W	DNF1	85	Phosphothreonine
+P32660	YER166W	DNF1	92	Phosphoserine
+P32660	YER166W	DNF1	94	Phosphothreonine
+P32660	YER166W	DNF1	104	Phosphoserine
+P32660	YER166W	DNF1	109	Phosphothreonine
+P32660	YER166W	DNF1	351	Phosphoserine
+P32660	YER166W	DNF1	354	Phosphoserine
+P32660	YER166W	DNF1	358	Phosphoserine
+P32660	YER166W	DNF1	365	Phosphoserine
+P32660	YER166W	DNF1	368	Phosphotyrosine
+P32660	YER166W	DNF1	1506	Phosphoserine
+P32660	YER166W	DNF1	1551	Phosphothreonine
+P32660	YER166W	DNF1	1552	Phosphoserine
+P32660	YER166W	DNF1	1563	Phosphoserine
+P32660	YER166W	DNF1	895	Glycyl
+Q12674	YMR162C	DNF3	627	Phosphoserine
+P30902	YKL016C	ATP7	2	N-acetylserine
+P40518	YIL062C	ARC15	142	Phosphothreonine
+Q06598	YPR201W	ARR3	201	N-linked
+Q06598	YPR201W	ARR3	365	N-linked
+P35734	YKL052C	ASK1	26	Phosphoserine
+P35734	YKL052C	ASK1	118	Phosphoserine
+P35734	YKL052C	ASK1	134	Phosphoserine
+P35734	YKL052C	ASK1	140	Phosphothreonine
+P35734	YKL052C	ASK1	155	Phosphoserine
+P35734	YKL052C	ASK1	156	Phosphoserine
+P35734	YKL052C	ASK1	200	Phosphoserine%3B
+P35734	YKL052C	ASK1	216	Phosphoserine
+P35734	YKL052C	ASK1	250	Phosphoserine%3B
+P53855	YNL242W	ATG2	236	Phosphoserine
+Q05789	YLR211C	ATG38	2	N-acetylserine
+P36107	YKL004W	AUR1	392	Phosphoserine
+P36107	YKL004W	AUR1	395	Phosphoserine
+P36107	YKL004W	AUR1	132	N-linked
+P36062	YKL146W	AVT3	59	Phosphoserine
+P36062	YKL146W	AVT3	119	Phosphoserine
+P36062	YKL146W	AVT3	121	Phosphoserine
+P36062	YKL146W	AVT3	165	Phosphoserine
+P53629	YNR019W	ARE2	175	Phosphoserine
+P53629	YNR019W	ARE2	176	Phosphoserine
+P19146	YDL137W	ARF2	2	N-myristoyl
+P19146	YDL137W	ARF2	127	Glycyl
+P49089	YPR145W	ASN1	265	Phosphoserine
+P49089	YPR145W	ASN1	509	Phosphoserine
+P43601	YFR021W	ATG18	354	Phosphoserine
+Q02887	YPL100W	ATG21	213	Phosphothreonine
+Q02887	YPL100W	ATG21	237	Phosphoserine
+P25568	YCL038C	ATG22	278	Phosphoserine
+Q06485	YLR356W	ATG33	127	Phosphoserine
+Q06485	YLR356W	ATG33	129	Phosphoserine
+P40344	YNR007C	ATG3	19	N6-acetyllysine%3B
+P40344	YNR007C	ATG3	48	N6-acetyllysine%3B
+P32907	YNR002C	ATO2	2	N-acetylserine
+P32907	YNR002C	ATO2	2	Phosphoserine
+P32907	YNR002C	ATO2	7	Phosphoserine
+P32907	YNR002C	ATO2	21	Phosphoserine
+P32907	YNR002C	ATO2	22	Phosphoserine
+P32907	YNR002C	ATO2	28	Phosphoserine
+P32907	YNR002C	ATO2	40	Phosphoserine
+P32454	YKL157W	APE2	381	N-linked
+P32454	YKL157W	APE2	713	N-linked
+P32381	YDL029W	ARP2	1	N-acetylmethionine
+P53244	YGR068C	ART5	364	Glycyl
+P53983	YNL008C	ASI3	24	N-linked
+P53983	YNL008C	ASI3	34	N-linked
+P53983	YNL008C	ASI3	46	N-linked
+P53983	YNL008C	ASI3	66	N-linked
+P0CZ17	YLR155C	ASP3-1	29	N-linked
+P0CZ17	YLR155C	ASP3-1	93	N-linked
+P0CZ17	YLR155C	ASP3-1	239	N-linked
+P39524	YAL026C	DRS2	102	Phosphoserine
+P39986	YEL031W	SPF1	324	Phosphoserine
+P39986	YEL031W	SPF1	936	Phosphoserine
+Q01217	YER069W	ARG5,6	359	Phosphoserine
+Q02804	YPL051W	ARL3	1	N-acetylmethionine
+Q02804	YPL051W	ARL3	50	Glycyl
+P28777	YGL148W	ARO2	2	N-acetylserine
+P18634	YLR392C	ART10	118	Glycyl
+P50275	YOR058C	ASE1	17	Phosphoserine
+P0CX77	YLR157C	ASP3-2	29	N-linked
+P0CX77	YLR157C	ASP3-2	93	N-linked
+P0CX77	YLR157C	ASP3-2	239	N-linked
+P0CX78	YLR158C	ASP3-3	29	N-linked
+P0CX78	YLR158C	ASP3-3	93	N-linked
+P0CX78	YLR158C	ASP3-3	239	N-linked
+Q06321	YLR189C	ATG26	76	Phosphoserine
+Q06321	YLR189C	ATG26	693	Phosphoserine
+Q12142	YDL149W	ATG9	143	Phosphoserine
+Q12142	YDL149W	ATG9	144	Phosphoserine
+Q12142	YDL149W	ATG9	787	Phosphoserine
+Q12359	YDR384C	ATO3	4	Phosphoserine
+P61829	Q0130	OLI1	1	N-formylmethionine
+P35817	YLR399C	BDF1	270	Phosphoserine
+P35817	YLR399C	BDF1	429	Phosphoserine
+P35817	YLR399C	BDF1	615	Phosphoserine
+P35817	YLR399C	BDF1	659	Phosphoserine
+P39714	YAL060W	BDH1	63	Phosphoserine
+P07251	YBL099W	ATP1	57	Phosphoserine
+P07251	YBL099W	ATP1	178	Phosphoserine
+P13090	YML116W	ATR1	394	N-linked
+P13090	YML116W	ATR1	471	N-linked
+Q01389	YJL095W	BCK1	407	Phosphothreonine
+Q01389	YJL095W	BCK1	411	Phosphoserine
+Q01389	YJL095W	BCK1	491	Phosphoserine
+Q01389	YJL095W	BCK1	747	Phosphoserine
+Q01389	YJL095W	BCK1	816	Phosphoserine
+Q01389	YJL095W	BCK1	1058	Phosphoserine
+Q01389	YJL095W	BCK1	1061	Phosphoserine
+Q01389	YJL095W	BCK1	1134	Phosphoserine%3B
+P39713	YAL061W	BDH2	63	Phosphoserine
+Q08347	YOL164W	BDS1	1	N-acetylmethionine
+P81449	YDR322C-A	TIM11	2	N-acetylserine
+P41815	YDR046C	BAP3	14	Phosphoserine
+P41815	YDR046C	BAP3	79	Phosphoserine
+P47068	YJL020C	BBC1	103	Phosphoserine
+P47068	YJL020C	BBC1	158	Phosphoserine
+P47068	YJL020C	BBC1	166	Phosphoserine
+P47068	YJL020C	BBC1	565	Phosphoserine
+P47068	YJL020C	BBC1	621	Phosphoserine
+P47068	YJL020C	BBC1	631	Phosphoserine
+P47068	YJL020C	BBC1	634	Phosphoserine
+P47068	YJL020C	BBC1	636	Phosphothreonine
+P47068	YJL020C	BBC1	638	Phosphoserine
+P47068	YJL020C	BBC1	647	Phosphoserine
+P47068	YJL020C	BBC1	850	Phosphothreonine
+P47068	YJL020C	BBC1	889	Phosphoserine
+P47068	YJL020C	BBC1	894	Phosphothreonine
+P47068	YJL020C	BBC1	895	Phosphothreonine
+P47068	YJL020C	BBC1	1012	Glycyl
+Q08236	YOL078W	AVO1	1	N-acetylmethionine
+Q08236	YOL078W	AVO1	140	Phosphoserine
+Q08236	YOL078W	AVO1	144	Phosphoserine
+Q08236	YOL078W	AVO1	400	Phosphoserine
+Q08236	YOL078W	AVO1	509	Phosphoserine
+Q08236	YOL078W	AVO1	510	Phosphothreonine
+Q08236	YOL078W	AVO1	552	Phosphoserine
+P47082	YJR001W	AVT1	8	Phosphoserine
+P47082	YJR001W	AVT1	15	Phosphoserine
+P47082	YJR001W	AVT1	35	Phosphoserine
+P47082	YJR001W	AVT1	181	Phosphothreonine
+P47082	YJR001W	AVT1	187	Phosphoserine
+P38084	YBR068C	BAP2	3	Phosphoserine
+P38084	YBR068C	BAP2	15	Phosphothreonine
+P38084	YBR068C	BAP2	16	Phosphoserine
+P38084	YBR068C	BAP2	19	Phosphoserine
+P38084	YBR068C	BAP2	21	Phosphoserine
+P38084	YBR068C	BAP2	24	Phosphoserine
+P38084	YBR068C	BAP2	76	Phosphoserine
+P38084	YBR068C	BAP2	84	Phosphoserine
+P39960	YER155C	BEM2	129	Phosphoserine
+P39960	YER155C	BEM2	283	Phosphoserine
+P39960	YER155C	BEM2	1012	Phosphoserine
+P39960	YER155C	BEM2	1016	Phosphoserine
+P39960	YER155C	BEM2	1038	Phosphothreonine
+P39960	YER155C	BEM2	1046	Phosphoserine
+P39960	YER155C	BEM2	1054	Phosphoserine
+P39960	YER155C	BEM2	1128	Phosphoserine
+P39960	YER155C	BEM2	27	Glycyl
+P36149	YKR068C	BET3	80	S-palmitoyl
+P47134	YJR089W	BIR1	477	Phosphoserine
+P47134	YJR089W	BIR1	508	Phosphoserine
+P47134	YJR089W	BIR1	552	Phosphoserine
+P47134	YJR089W	BIR1	587	Phosphoserine
+P47134	YJR089W	BIR1	751	Phosphoserine
+P47134	YJR089W	BIR1	765	Phosphoserine
+P47041	YJL058C	BIT61	58	Phosphotyrosine
+P47041	YJL058C	BIT61	59	Phosphoserine
+P47041	YJL058C	BIT61	139	Phosphoserine
+P47041	YJL058C	BIT61	144	Phosphoserine
+Q08235	YOL077C	BRX1	285	Phosphoserine
+Q05611	YDR275W	BSC2	177	Phosphoserine
+Q08280	YOL137W	BSC6	37	Phosphoserine
+Q08280	YOL137W	BSC6	41	Phosphoserine
+Q08280	YOL137W	BSC6	49	N-linked
+P47176	YJR148W	BAT2	202	N6-(pyridoxal
+P15703	YGR282C	BGL2	202	N-linked
+P15703	YGR282C	BGL2	284	N-linked
+P50277	YNR058W	BIO3	314	N6-(pyridoxal
+Q08965	YPL217C	BMS1	438	Phosphoserine
+Q08965	YPL217C	BMS1	478	Phosphoserine
+Q08965	YPL217C	BMS1	492	Phosphoserine
+Q08965	YPL217C	BMS1	504	Phosphothreonine
+Q08965	YPL217C	BMS1	516	Phosphothreonine
+Q08965	YPL217C	BMS1	518	Phosphoserine
+Q08965	YPL217C	BMS1	523	Phosphoserine
+Q08965	YPL217C	BMS1	574	Phosphoserine
+Q08965	YPL217C	BMS1	578	Phosphoserine
+P47039	YJL060W	BNA3	271	N6-(pyridoxal
+P40450	YIL159W	BNR1	621	Phosphoserine
+P40450	YIL159W	BNR1	751	Phosphoserine
+Q07660	YDL231C	BRE4	830	N-linked
+P53755	YNR069C	BSC5	111	Phosphoserine
+P53755	YNR069C	BSC5	350	Phosphoserine
+Q06604	YPR171W	BSP1	46	Phosphoserine
+Q06604	YPR171W	BSP1	79	Phosphoserine
+Q06604	YPR171W	BSP1	88	Phosphoserine
+Q06604	YPR171W	BSP1	185	Phosphoserine
+Q06604	YPR171W	BSP1	220	Phosphoserine
+Q06604	YPR171W	BSP1	309	Phosphoserine
+Q06604	YPR171W	BSP1	320	Phosphoserine
+P50944	YNL101W	AVT4	88	Phosphoserine
+P50944	YNL101W	AVT4	130	Phosphoserine
+P50944	YNL101W	AVT4	165	Phosphoserine
+P41696	YOR113W	AZF1	61	Phosphoserine
+P41696	YOR113W	AZF1	286	Phosphoserine
+P41696	YOR113W	AZF1	325	Phosphoserine
+Q12365	YPL255W	BBP1	29	Phosphoserine
+Q12365	YPL255W	BBP1	73	Phosphoserine
+Q12365	YPL255W	BBP1	115	Phosphoserine
+P38928	YIL140W	AXL2	642	Phosphoserine
+P38928	YIL140W	AXL2	673	Phosphoserine
+P38928	YIL140W	AXL2	676	Phosphoserine
+P38928	YIL140W	AXL2	41	N-linked
+P38928	YIL140W	AXL2	50	N-linked
+P38928	YIL140W	AXL2	96	N-linked
+P38928	YIL140W	AXL2	117	N-linked
+P38928	YIL140W	AXL2	163	N-linked
+P38928	YIL140W	AXL2	260	N-linked
+P38928	YIL140W	AXL2	266	N-linked
+P38928	YIL140W	AXL2	304	N-linked
+P38928	YIL140W	AXL2	324	N-linked
+P38928	YIL140W	AXL2	359	N-linked
+P38928	YIL140W	AXL2	382	N-linked
+P38928	YIL140W	AXL2	389	N-linked
+P38928	YIL140W	AXL2	403	N-linked
+P38928	YIL140W	AXL2	447	N-linked
+P38928	YIL140W	AXL2	451	N-linked
+P38928	YIL140W	AXL2	495	N-linked
+P33306	YER167W	BCK2	334	Phosphoserine
+P33306	YER167W	BCK2	757	Phosphoserine
+P33306	YER167W	BCK2	761	Phosphoserine
+Q07442	YDL070W	BDF2	264	Phosphoserine
+P53858	YNL233W	BNI4	43	Phosphoserine
+P53858	YNL233W	BNI4	133	Phosphoserine
+P53858	YNL233W	BNI4	281	Phosphoserine
+P53858	YNL233W	BNI4	364	Phosphoserine
+P53858	YNL233W	BNI4	394	Phosphoserine
+P53858	YNL233W	BNI4	410	Phosphothreonine
+P53858	YNL233W	BNI4	476	Phosphoserine
+P53858	YNL233W	BNI4	500	Phosphoserine
+P53858	YNL233W	BNI4	503	Phosphoserine
+P53858	YNL233W	BNI4	618	Phosphoserine
+P53858	YNL233W	BNI4	703	Phosphothreonine
+P53858	YNL233W	BNI4	746	Phosphoserine
+P53858	YNL233W	BNI4	825	Phosphoserine
+Q06338	YDR361C	BCP1	205	Phosphothreonine
+Q06338	YDR361C	BCP1	209	Phosphothreonine
+P47113	YJR053W	BFA1	317	Phosphoserine
+P40013	YER016W	BIM1	2	N-acetylserine
+P40013	YER016W	BIM1	157	Phosphoserine
+P29366	YBR200W	BEM1	1	N-acetylmethionine
+P29366	YBR200W	BEM1	47	Phosphoserine
+P29366	YBR200W	BEM1	255	Phosphoserine
+P29366	YBR200W	BEM1	258	Phosphoserine
+P29366	YBR200W	BEM1	458	Phosphoserine
+P29366	YBR200W	BEM1	461	Phosphoserine
+P38813	YHR101C	BIG1	24	N-linked
+P38813	YHR101C	BIG1	144	N-linked
+P43583	YFL007W	BLM10	11	Phosphoserine
+P43583	YFL007W	BLM10	29	Phosphoserine
+P43583	YFL007W	BLM10	56	Phosphoserine
+P43583	YFL007W	BLM10	62	Phosphoserine
+P43583	YFL007W	BLM10	64	Phosphothreonine
+P43583	YFL007W	BLM10	66	Phosphothreonine
+P43583	YFL007W	BLM10	1041	Phosphoserine
+Q04347	YMR014W	BUD22	257	Phosphothreonine
+Q04347	YMR014W	BUD22	367	Phosphoserine
+Q04347	YMR014W	BUD22	371	Phosphothreonine
+Q04347	YMR014W	BUD22	375	Phosphoserine
+P33314	YKL092C	BUD2	2	N-acetylserine
+P33314	YKL092C	BUD2	854	Phosphoserine
+P47136	YJR092W	BUD4	10	Phosphoserine
+P47136	YJR092W	BUD4	78	Phosphoserine
+P47136	YJR092W	BUD4	81	Phosphoserine
+P47136	YJR092W	BUD4	91	Phosphoserine
+P47136	YJR092W	BUD4	96	Phosphoserine
+P47136	YJR092W	BUD4	167	Phosphoserine
+P47136	YJR092W	BUD4	365	Phosphothreonine
+P47136	YJR092W	BUD4	367	Phosphoserine
+P47136	YJR092W	BUD4	511	Phosphoserine
+P47136	YJR092W	BUD4	616	Phosphoserine
+P47136	YJR092W	BUD4	805	Phosphoserine
+P47136	YJR092W	BUD4	811	Phosphoserine
+P41697	YLR319C	BUD6	12	Phosphothreonine
+P41697	YLR319C	BUD6	233	Phosphoserine
+P41697	YLR319C	BUD6	327	Phosphoserine
+P41697	YLR319C	BUD6	342	Phosphoserine
+P38822	YHR114W	BZZ1	327	Phosphoserine
+P38822	YHR114W	BZZ1	463	Phosphoserine
+P38822	YHR114W	BZZ1	472	Phosphoserine
+P38822	YHR114W	BZZ1	476	Phosphoserine
+Q04749	YMR068W	AVO2	315	Phosphoserine
+Q04749	YMR068W	AVO2	350	Phosphoserine
+P40074	YER119C	AVT6	344	Phosphoserine
+P12630	YIL015W	BAR1	84	N-linked
+P12630	YIL015W	BAR1	90	N-linked
+P12630	YIL015W	BAR1	268	N-linked
+P12630	YIL015W	BAR1	308	N-linked
+P12630	YIL015W	BAR1	366	N-linked
+P12630	YIL015W	BAR1	398	N-linked
+P12630	YIL015W	BAR1	468	N-linked
+P12630	YIL015W	BAR1	503	N-linked
+P12630	YIL015W	BAR1	551	N-linked
+Q12186	YLR116W	MSL5	93	Phosphoserine
+Q12186	YLR116W	MSL5	95	Phosphoserine
+Q12186	YLR116W	MSL5	100	Phosphotyrosine
+Q12186	YLR116W	MSL5	382	Phosphoserine
+P38891	YHR208W	BAT1	219	N6-(pyridoxal
+P38891	YHR208W	BAT1	315	Phosphothreonine
+P38772	YHR040W	BCD1	330	Phosphoserine
+P32873	YPL115C	BEM3	254	Phosphoserine
+Q06631	YDR299W	BFR2	41	Phosphoserine
+Q06631	YDR299W	BFR2	44	Phosphoserine
+Q06631	YDR299W	BFR2	366	Phosphoserine
+Q06631	YDR299W	BFR2	372	Phosphoserine
+Q06631	YDR299W	BFR2	379	Phosphoserine
+P11709	YCL029C	BIK1	95	Phosphoserine
+P11709	YCL029C	BIK1	110	Phosphoserine
+Q08492	YOR078W	BUD21	16	Phosphoserine
+Q08492	YOR078W	BUD21	45	Phosphoserine
+Q08492	YOR078W	BUD21	65	Phosphoserine
+Q08492	YOR078W	BUD21	144	Phosphoserine
+Q05949	YLR226W	BUR2	24	Phosphoserine
+P27614	YJL172W	CPS1	88	N-linked
+P27614	YJL172W	CPS1	176	N-linked
+P27614	YJL172W	CPS1	228	N-linked
+P27614	YJL172W	CPS1	381	N-linked
+P27614	YJL172W	CPS1	525	N-linked
+P27614	YJL172W	CPS1	8	Glycyl
+P00729	YMR297W	PRC1	124	N-linked
+P00729	YMR297W	PRC1	198	N-linked
+P00729	YMR297W	PRC1	279	N-linked
+P00729	YMR297W	PRC1	479	N-linked
+P34730	YDR099W	BMH2	2	N-acetylserine
+P38041	YBL085W	BOI1	104	Phosphoserine
+P38041	YBL085W	BOI1	106	Phosphoserine
+P38041	YBL085W	BOI1	128	Phosphoserine
+P38041	YBL085W	BOI1	151	Phosphothreonine
+P38041	YBL085W	BOI1	158	Phosphothreonine
+P38041	YBL085W	BOI1	209	Phosphoserine
+P38041	YBL085W	BOI1	393	Phosphoserine
+P38041	YBL085W	BOI1	412	Phosphoserine
+P38041	YBL085W	BOI1	525	Phosphoserine
+P38041	YBL085W	BOI1	528	Phosphoserine
+P38041	YBL085W	BOI1	589	Phosphoserine
+P38041	YBL085W	BOI1	590	Phosphoserine
+P38041	YBL085W	BOI1	593	Phosphoserine
+P38041	YBL085W	BOI1	644	Phosphoserine
+P38041	YBL085W	BOI1	655	Phosphoserine
+P38041	YBL085W	BOI1	735	Phosphoserine
+P38041	YBL085W	BOI1	919	Phosphothreonine
+P53836	YNL278W	CAF120	491	Phosphoserine
+P53836	YNL278W	CAF120	510	Phosphoserine
+P53836	YNL278W	CAF120	518	Phosphoserine
+P53836	YNL278W	CAF120	538	Phosphoserine
+P53836	YNL278W	CAF120	556	Phosphoserine
+P53836	YNL278W	CAF120	871	Phosphoserine
+P53836	YNL278W	CAF120	885	Phosphoserine
+P39101	YER048C	CAJ1	132	Glycyl
+P17555	YNL138W	SRV2	454	Phosphoserine
+P06787	YBR109C	CMD1	82	Phosphoserine
+P06787	YBR109C	CMD1	102	Phosphoserine
+P27825	YAL058W	CNE1	25	N-linked
+P27825	YAL058W	CNE1	104	N-linked
+P27825	YAL058W	CNE1	296	N-linked
+P27825	YAL058W	CNE1	416	N-linked
+P27825	YAL058W	CNE1	425	N-linked
+P04817	YEL063C	CAN1	54	Phosphoserine
+P04817	YEL063C	CAN1	66	Phosphoserine
+P28495	YKL007W	CAP1	2	N-acetylserine
+P28495	YKL007W	CAP1	17	Phosphoserine
+P34237	YKL179C	COY1	364	Phosphoserine
+P34237	YKL179C	COY1	450	Phosphoserine
+P34237	YKL179C	COY1	453	Phosphoserine
+P34237	YKL179C	COY1	555	Phosphoserine
+P15202	YDR256C	CTA1	2	N-acetylserine
+Q06071	YLR408C	BLS1	33	Phosphoserine
+P29311	YER177W	BMH1	2	N-acetylserine
+P29311	YER177W	BMH1	89	Phosphoserine
+P29311	YER177W	BMH1	76	Glycyl
+P48582	YPL084W	BRO1	740	Phosphoserine
+P32639	YER172C	BRR2	403	Phosphoserine
+P25558	YCL014W	BUD3	766	Phosphoserine
+P25558	YCL014W	BUD3	1045	Phosphothreonine
+P25558	YCL014W	BUD3	1063	Phosphoserine
+P25558	YCL014W	BUD3	1075	Phosphoserine
+P25558	YCL014W	BUD3	1134	Phosphoserine
+P25558	YCL014W	BUD3	1149	Phosphoserine
+P25558	YCL014W	BUD3	1157	Phosphothreonine
+P25558	YCL014W	BUD3	1160	Phosphoserine
+P25558	YCL014W	BUD3	1228	Phosphoserine
+P25558	YCL014W	BUD3	1254	Phosphoserine
+P25558	YCL014W	BUD3	1257	Phosphoserine
+P25558	YCL014W	BUD3	1390	Phosphoserine
+P25558	YCL014W	BUD3	1412	Phosphoserine
+P25558	YCL014W	BUD3	1429	Phosphothreonine
+P25558	YCL014W	BUD3	1440	Phosphothreonine
+P25558	YCL014W	BUD3	1443	Phosphoserine
+P25558	YCL014W	BUD3	1501	Phosphoserine
+P25558	YCL014W	BUD3	1549	Phosphoserine
+P25558	YCL014W	BUD3	1589	Phosphoserine
+P25558	YCL014W	BUD3	1614	Phosphoserine
+P25558	YCL014W	BUD3	792	Glycyl
+P25558	YCL014W	BUD3	963	Glycyl
+Q12191	YDL099W	BUG1	2	N-acetylserine
+Q12191	YDL099W	BUG1	87	Phosphoserine
+Q12191	YDL099W	BUG1	170	Phosphoserine
+Q12191	YDL099W	BUG1	292	Phosphothreonine
+Q03758	YML111W	BUL2	22	Phosphothreonine
+Q03758	YML111W	BUL2	557	Phosphoserine
+P12962	YOR276W	CAF20	78	Phosphoserine
+P12962	YOR276W	CAF20	91	Phosphoserine
+P12962	YOR276W	CAF20	99	Phosphothreonine
+P12962	YOR276W	CAF20	101	Phosphothreonine
+P12962	YOR276W	CAF20	102	Phosphothreonine
+P12962	YOR276W	CAF20	154	Phosphoserine
+P53890	YNL166C	BNI5	70	Phosphoserine
+P53890	YNL166C	BNI5	179	Phosphoserine
+P53890	YNL166C	BNI5	194	Phosphoserine
+P53890	YNL166C	BNI5	257	Phosphothreonine
+P53890	YNL166C	BNI5	270	Phosphoserine
+P53890	YNL166C	BNI5	273	Phosphoserine
+P53890	YNL166C	BNI5	274	Phosphothreonine
+P53890	YNL166C	BNI5	332	Phosphoserine
+P53890	YNL166C	BNI5	340	Phosphoserine
+P53890	YNL166C	BNI5	344	Phosphotyrosine
+P53890	YNL166C	BNI5	346	Phosphoserine
+P53890	YNL166C	BNI5	350	Phosphoserine
+P39969	YER114C	BOI2	18	Phosphoserine
+P39969	YER114C	BOI2	24	Phosphoserine
+P39969	YER114C	BOI2	28	Phosphoserine
+P39969	YER114C	BOI2	450	Phosphoserine
+P39969	YER114C	BOI2	519	Phosphoserine
+P39969	YER114C	BOI2	523	Phosphoserine
+P39969	YER114C	BOI2	546	Phosphoserine
+P39969	YER114C	BOI2	652	Phosphoserine
+P43132	YLR015W	BRE2	227	Phosphoserine
+P38356	YBR290W	BSD2	312	Glycyl
+P43573	YFL023W	BUD27	580	Phosphoserine
+P53323	YGR262C	BUD32	187	Phosphoserine%3B
+P53323	YGR262C	BUD32	189	Phosphoserine%3B
+P41698	YLR353W	BUD8	92	N-linked
+P41698	YLR353W	BUD8	110	N-linked
+P41698	YLR353W	BUD8	211	N-linked
+P41698	YLR353W	BUD8	240	N-linked
+P41698	YLR353W	BUD8	271	N-linked
+P41698	YLR353W	BUD8	333	N-linked
+P41698	YLR353W	BUD8	396	N-linked
+P41698	YLR353W	BUD8	423	N-linked
+P53226	YGR041W	BUD9	112	Phosphoserine
+P53226	YGR041W	BUD9	189	Phosphoserine
+P53226	YGR041W	BUD9	83	N-linked
+P53226	YGR041W	BUD9	139	N-linked
+P53226	YGR041W	BUD9	142	N-linked
+P53226	YGR041W	BUD9	221	N-linked
+P53226	YGR041W	BUD9	259	N-linked
+P53226	YGR041W	BUD9	263	N-linked
+P53226	YGR041W	BUD9	289	N-linked
+P53226	YGR041W	BUD9	299	N-linked
+P53226	YGR041W	BUD9	340	N-linked
+P48524	YMR275C	BUL1	58	Phosphoserine
+P48524	YMR275C	BUL1	70	Phosphoserine
+P07245	YGR204W	ADE3	176	Phosphoserine
+P07245	YGR204W	ADE3	318	Phosphothreonine
+P07245	YGR204W	ADE3	322	Phosphoserine
+P36076	YKL088W	CAB3	42	Phosphoserine
+P36076	YKL088W	CAB3	116	Phosphoserine
+P36076	YKL088W	CAB3	121	Phosphoserine
+P36076	YKL088W	CAB3	124	Phosphoserine
+P36076	YKL088W	CAB3	264	Phosphoserine
+P13517	YIL034C	CAP2	2	N-acetylserine
+P13517	YIL034C	CAP2	85	Phosphoserine
+P13517	YIL034C	CAP2	92	Phosphoserine
+Q02948	YPL120W	VPS30	142	Phosphothreonine
+P38934	YOR198C	BFR1	260	Phosphoserine
+P38934	YOR198C	BFR1	336	Phosphothreonine
+P38934	YOR198C	BFR1	369	Phosphoserine
+Q06150	YLR267W	BOP2	383	Phosphoserine
+P53741	YNR051C	BRE5	187	Phosphoserine
+P53741	YNR051C	BRE5	282	Phosphoserine
+P53741	YNR051C	BRE5	336	Phosphothreonine
+P53741	YNR051C	BRE5	340	Phosphoserine
+P53741	YNR051C	BRE5	398	Phosphoserine
+P43571	YFL025C	BST1	19	N-linked
+P43571	YFL025C	BST1	295	N-linked
+P43571	YFL025C	BST1	302	N-linked
+P43571	YFL025C	BST1	447	N-linked
+P43571	YFL025C	BST1	456	N-linked
+P43571	YFL025C	BST1	485	N-linked
+P43571	YFL025C	BST1	565	N-linked
+P43571	YFL025C	BST1	651	N-linked
+P43571	YFL025C	BST1	668	N-linked
+P43571	YFL025C	BST1	694	N-linked
+P43571	YFL025C	BST1	918	N-linked
+P41832	YNL271C	BNI1	311	Phosphoserine
+P41832	YNL271C	BNI1	325	Phosphoserine
+P41832	YNL271C	BNI1	1085	Phosphoserine
+P41832	YNL271C	BNI1	1170	Phosphoserine
+P41832	YNL271C	BNI1	1338	Phosphoserine
+P41832	YNL271C	BNI1	1344	Phosphoserine
+P41832	YNL271C	BNI1	1918	Phosphothreonine
+P25385	YLR078C	BOS1	1	N-acetylmethionine
+P14772	YLL015W	BPT1	645	Phosphoserine
+P14772	YLL015W	BPT1	885	Phosphoserine
+P14772	YLL015W	BPT1	889	Phosphothreonine
+P14772	YLL015W	BPT1	893	Phosphoserine
+P14772	YLL015W	BPT1	895	Phosphoserine
+P14772	YLL015W	BPT1	916	Phosphothreonine
+P14772	YLL015W	BPT1	927	Phosphoserine
+P14772	YLL015W	BPT1	931	Phosphoserine
+P14772	YLL015W	BPT1	934	Phosphothreonine
+P14772	YLL015W	BPT1	1011	N-linked
+P23293	YPR161C	SGV1	240	Phosphothreonine%3B
+P23293	YPR161C	SGV1	400	Phosphoserine
+P23293	YPR161C	SGV1	405	Phosphothreonine
+P23293	YPR161C	SGV1	417	Phosphoserine
+P23293	YPR161C	SGV1	634	Phosphoserine
+P36106	YKL005C	BYE1	177	Phosphoserine
+P32797	YDL220C	CDC13	306	Phosphoserine
+P32797	YDL220C	CDC13	308	Phosphothreonine
+P32797	YDL220C	CDC13	333	Phosphoserine
+P25656	YCR094W	CDC50	199	N-linked
+P25656	YCR094W	CDC50	216	N-linked
+P25656	YCR094W	CDC50	237	N-linked
+P25656	YCR094W	CDC50	288	N-linked
+P25656	YCR094W	CDC50	329	N-linked
+P09119	YJL194W	CDC6	368	Phosphothreonine
+P53197	YGL003C	CDH1	213	Phosphoserine
+Q12453	YOR112W	CEX1	754	Phosphoserine
+P07267	YPL154C	PEP4	144	N-linked
+P07267	YPL154C	PEP4	345	N-linked
+P32582	YGR155W	CYS4	53	N6-(pyridoxal
+P32582	YGR155W	CYS4	134	Phosphoserine
+P32582	YGR155W	CYS4	350	Phosphoserine
+P32582	YGR155W	CYS4	424	Phosphoserine
+Q06703	YLR308W	CDA2	142	N-linked
+Q06703	YLR308W	CDA2	181	N-linked
+Q06703	YLR308W	CDA2	199	N-linked
+Q06703	YLR308W	CDA2	246	N-linked
+Q06703	YLR308W	CDA2	263	N-linked
+P27636	YAR019C	CDC15	561	Phosphoserine
+P27636	YAR019C	CDC15	567	Phosphoserine
+P27636	YAR019C	CDC15	870	Phosphothreonine
+P04821	YLR310C	CDC25	151	Phosphoserine
+P04821	YLR310C	CDC25	154	Phosphoserine
+P04821	YLR310C	CDC25	423	Phosphoserine
+P04821	YLR310C	CDC25	580	Phosphoserine
+P04821	YLR310C	CDC25	596	Phosphoserine
+P04821	YLR310C	CDC25	632	Phosphoserine
+P04821	YLR310C	CDC25	635	Phosphothreonine
+P04821	YLR310C	CDC25	649	Phosphoserine
+P25694	YDL126C	CDC48	472	Phosphoserine
+P25694	YDL126C	CDC48	519	Phosphoserine
+P25694	YDL126C	CDC48	735	Phosphothreonine
+P25694	YDL126C	CDC48	770	Phosphoserine
+P25694	YDL126C	CDC48	305	Glycyl
+P25694	YDL126C	CDC48	322	Glycyl
+P25694	YDL126C	CDC48	346	Glycyl
+P25694	YDL126C	CDC48	522	Glycyl
+P25694	YDL126C	CDC48	539	Glycyl
+P25694	YDL126C	CDC48	594	Glycyl
+P25694	YDL126C	CDC48	673	Glycyl
+P40969	YMR168C	CEP3	575	Phosphoserine
+P53894	YNL161W	CBK1	109	Phosphothreonine
+P24869	YPR119W	CLB2	2	N-acetylserine
+P80235	YAR035W	YAT1	517	Phosphoserine
+P25296	YKL190W	CNB1	2	N-myristoyl
+P07253	YBR120C	CBP6	2	N-acetylserine
+P07253	YBR120C	CBP6	97	Phosphothreonine
+P31384	YAL021C	CCR4	33	Phosphothreonine
+P31384	YAL021C	CCR4	278	Phosphoserine
+P31384	YAL021C	CCR4	285	Phosphothreonine
+Q12127	YLR110C	CCW12	112	GPI-anchor
+Q12127	YLR110C	CCW12	21	N-linked
+Q12127	YLR110C	CCW12	23	O-linked
+Q12127	YLR110C	CCW12	24	O-linked
+Q12127	YLR110C	CCW12	26	O-linked
+Q12127	YLR110C	CCW12	28	O-linked
+Q12127	YLR110C	CCW12	31	O-linked
+Q12127	YLR110C	CCW12	32	O-linked
+Q12127	YLR110C	CCW12	33	O-linked
+Q12127	YLR110C	CCW12	36	O-linked
+Q12127	YLR110C	CCW12	38	O-linked
+Q12127	YLR110C	CCW12	39	O-linked
+Q12127	YLR110C	CCW12	46	O-linked
+Q12127	YLR110C	CCW12	48	O-linked
+Q12127	YLR110C	CCW12	81	N-linked
+Q12127	YLR110C	CCW12	97	N-linked
+Q12127	YLR110C	CCW12	80	Glycyl
+P32457	YLR314C	CDC3	2	N-acetylserine
+P32457	YLR314C	CDC3	2	Phosphoserine
+P32457	YLR314C	CDC3	9	Phosphoserine
+P32457	YLR314C	CDC3	47	Phosphothreonine
+P32457	YLR314C	CDC3	60	Phosphoserine
+P32457	YLR314C	CDC3	77	Phosphoserine
+P32457	YLR314C	CDC3	175	Phosphoserine
+P32457	YLR314C	CDC3	468	Phosphothreonine
+P32457	YLR314C	CDC3	509	Phosphoserine
+P32457	YLR314C	CDC3	4	Glycyl
+P32457	YLR314C	CDC3	11	Glycyl
+P32457	YLR314C	CDC3	30	Glycyl
+P32457	YLR314C	CDC3	63	Glycyl
+P32457	YLR314C	CDC3	287	Glycyl
+Q06697	YLR418C	CDC73	114	Phosphoserine
+Q06697	YLR418C	CDC73	150	Phosphoserine
+P17106	YJR060W	CBF1	1	N-acetylmethionine
+P17106	YJR060W	CBF1	45	Phosphoserine%3B
+P17106	YJR060W	CBF1	48	Phosphoserine
+P17106	YJR060W	CBF1	84	Phosphoserine
+P17106	YJR060W	CBF1	138	Phosphothreonine
+Q06702	YLR307W	CDA1	26	N-linked
+Q06702	YLR307W	CDA1	50	N-linked
+Q06702	YLR307W	CDA1	68	N-linked
+Q06702	YLR307W	CDA1	189	N-linked
+P25342	YCR002C	CDC10	1	N-acetylmethionine
+P25342	YCR002C	CDC10	216	Phosphothreonine
+P32468	YHR107C	CDC12	2	N-acetylserine
+P16522	YHR166C	CDC23	59	Phosphoserine%3B
+P06704	YOR257W	CDC31	130	Phosphothreonine
+P25356	YCR032W	BPH1	1667	Glycyl
+P27637	YAR014C	BUD14	2	N-acetylserine
+P27637	YAR014C	BUD14	159	Phosphotyrosine
+P27637	YAR014C	BUD14	160	Phosphoserine
+P27637	YAR014C	BUD14	162	Phosphoserine
+P27637	YAR014C	BUD14	177	Phosphothreonine
+P27637	YAR014C	BUD14	212	Phosphoserine
+P27637	YAR014C	BUD14	222	Phosphoserine
+P27637	YAR014C	BUD14	376	Phosphoserine
+P27637	YAR014C	BUD14	378	Phosphoserine
+P27637	YAR014C	BUD14	401	Phosphoserine
+P27637	YAR014C	BUD14	507	Phosphoserine
+P27637	YAR014C	BUD14	655	Phosphoserine
+P27637	YAR014C	BUD14	658	Phosphoserine
+P27637	YAR014C	BUD14	670	Phosphoserine
+P32504	YGR140W	CBF2	566	Phosphoserine
+P32504	YGR140W	CBF2	706	Phosphotyrosine
+P33322	YLR175W	CBF5	47	Phosphoserine
+P33322	YLR175W	CBF5	378	Phosphothreonine
+P33322	YLR175W	CBF5	9	Glycyl
+P33322	YLR175W	CBF5	267	Glycyl
+P50077	YGR217W	CCH1	284	Phosphoserine
+P00431	YKR066C	CCP1	220	Phosphotyrosine
+Q7LHD1	YDR134C	CCW22	115	GPI-anchor
+Q7LHD1	YDR134C	CCW22	21	N-linked
+Q7LHD1	YDR134C	CCW22	82	N-linked
+P19073	YLR229C	CDC42	188	Cysteine
+P19073	YLR229C	CDC42	188	S-geranylgeranyl
+P32458	YJR076C	CDC11	2	N-acetylserine
+P32458	YJR076C	CDC11	2	Phosphoserine
+P32458	YJR076C	CDC11	305	Phosphoserine
+P32458	YJR076C	CDC11	327	Phosphothreonine
+P32458	YJR076C	CDC11	412	Glycyl
+P14724	YFR036W	CDC26	12	Phosphoserine
+P06101	YDR168W	CDC37	14	Phosphoserine
+P06101	YDR168W	CDC37	17	Phosphoserine
+P06101	YDR168W	CDC37	367	Phosphoserine
+P06101	YDR168W	CDC37	466	Phosphoserine
+P06101	YDR168W	CDC37	484	Phosphoserine
+Q12018	YDL132W	CDC53	760	Glycyl
+P38910	YOR020C	HSP10	2	N-acetylserine
+P38910	YOR020C	HSP10	31	Phosphoserine
+P47818	YLR220W	CCC1	29	Phosphoserine
+P47818	YLR220W	CCC1	53	Phosphoserine
+P47818	YLR220W	CCC1	68	Phosphoserine
+P47818	YLR220W	CCC1	71	Phosphoserine
+P47818	YLR220W	CCC1	83	Phosphoserine
+O13547	YLR390W-A	CCW14	217	GPI-anchor
+O13547	YLR390W-A	CCW14	87	N-linked
+O13547	YLR390W-A	CCW14	161	Glycyl
+Q00684	YFR028C	CDC14	467	Phosphoserine
+O13297	YPL228W	CET1	2	N-acetylserine
+O13297	YPL228W	CET1	15	Phosphoserine
+O13297	YPL228W	CET1	124	Phosphoserine
+P29029	YLR286C	CTS1	553	N-linked
+Q12114	YLR330W	CHS5	305	Phosphothreonine
+Q12114	YLR330W	CHS5	338	Phosphoserine
+Q12114	YLR330W	CHS5	362	Phosphoserine
+Q12114	YLR330W	CHS5	365	Phosphoserine
+Q12114	YLR330W	CHS5	383	Phosphoserine
+Q12114	YLR330W	CHS5	384	Phosphoserine
+Q12114	YLR330W	CHS5	573	Phosphoserine
+Q12114	YLR330W	CHS5	579	Phosphoserine
+Q12114	YLR330W	CHS5	590	Phosphoserine
+Q12114	YLR330W	CHS5	584	Glycyl
+P43634	YLR098C	CHA4	164	Phosphoserine
+P43634	YLR098C	CHA4	166	Phosphoserine
+P22516	YPL008W	CHL1	86	Phosphoserine
+P22516	YPL008W	CHL1	172	Phosphoserine
+Q08032	YLR103C	CDC45	453	Phosphothreonine
+P07834	YFL009W	CDC4	104	Phosphoserine
+P32562	YMR001C	CDC5	23	Phosphothreonine
+P32562	YMR001C	CDC5	419	Phosphoserine
+P40558	YIL003W	CFD1	291	Phosphoserine
+P53280	YGR134W	CAF130	1042	Phosphoserine
+P08004	YNL192W	CHS1	34	Phosphoserine
+P08004	YNL192W	CHS1	35	Phosphoserine
+P08004	YNL192W	CHS1	270	Phosphoserine
+P08004	YNL192W	CHS1	299	Phosphoserine
+P08004	YNL192W	CHS1	318	Phosphoserine
+P08004	YNL192W	CHS1	328	Phosphothreonine
+P08004	YNL192W	CHS1	358	Phosphoserine
+P14180	YBR038W	CHS2	40	Phosphoserine
+P14180	YBR038W	CHS2	82	Phosphoserine
+P14180	YBR038W	CHS2	86	Phosphoserine
+P14180	YBR038W	CHS2	100	Phosphoserine
+P14180	YBR038W	CHS2	133	Phosphoserine
+P14180	YBR038W	CHS2	217	Phosphoserine
+P14180	YBR038W	CHS2	22	N-linked
+P14180	YBR038W	CHS2	197	N-linked
+P14180	YBR038W	CHS2	447	N-linked
+P32657	YER164W	CHD1	36	Phosphoserine
+P32657	YER164W	CHD1	72	Phosphoserine
+P32657	YER164W	CHD1	987	Phosphoserine
+P32657	YER164W	CHD1	989	Phosphoserine
+P32657	YER164W	CHD1	1336	Phosphoserine
+P32657	YER164W	CHD1	1364	Phosphoserine
+P32657	YER164W	CHD1	1372	Phosphoserine
+P32657	YER164W	CHD1	1144	Glycyl
+Q06350	YDR371W	CTS2	147	N-linked
+Q06350	YDR371W	CTS2	228	N-linked
+Q06350	YDR371W	CTS2	456	N-linked
+Q06350	YDR371W	CTS2	472	N-linked
+P05374	YGR157W	CHO2	2	N-acetylserine
+P29465	YBR023C	CHS3	537	Phosphoserine
+P29465	YBR023C	CHS3	538	Phosphothreonine
+P29465	YBR023C	CHS3	82	N-linked
+P29465	YBR023C	CHS3	114	N-linked
+P29465	YBR023C	CHS3	152	N-linked
+P29465	YBR023C	CHS3	163	N-linked
+P29465	YBR023C	CHS3	303	N-linked
+P29465	YBR023C	CHS3	332	N-linked
+P29465	YBR023C	CHS3	371	N-linked
+P29465	YBR023C	CHS3	136	Glycyl
+P40019	YER030W	CHZ1	2	N-acetylserine
+P40019	YER030W	CHZ1	68	Phosphoserine
+P40019	YER030W	CHZ1	70	Phosphoserine
+Q07897	YLR003C	CMS1	59	Phosphoserine
+P27895	YEL061C	CIN8	972	Phosphoserine
+P48562	YNL298W	CLA4	29	Phosphoserine
+P48562	YNL298W	CLA4	46	Phosphoserine
+P48562	YNL298W	CLA4	351	Phosphoserine
+P48562	YNL298W	CLA4	367	Phosphoserine
+P48562	YNL298W	CLA4	425	Phosphoserine
+P22137	YGL206C	CHC1	1107	Glycyl
+Q06156	YLR272C	YCS4	464	Phosphoserine
+Q06156	YLR272C	YCS4	475	Phosphoserine
+P53079	YGL223C	COG1	1	N-acetylmethionine
+P53079	YGL223C	COG1	305	Phosphoserine
+Q12510	YDL156W	CMR1	64	Phosphoserine
+Q12510	YDL156W	CMR1	69	Phosphothreonine
+Q12510	YDL156W	CMR1	224	Phosphoserine
+Q06680	YDR325W	YCG1	198	Phosphoserine
+Q06680	YDR325W	YCG1	933	Phosphoserine
+Q06680	YDR325W	YCG1	981	Phosphoserine
+Q06680	YDR325W	YCG1	1008	Phosphoserine
+P47001	YJL158C	CIS3	68	O-linked
+P47001	YJL158C	CIS3	78	O-linked
+P47001	YJL158C	CIS3	105	O-linked
+P47001	YJL158C	CIS3	106	O-linked
+P47001	YJL158C	CIS3	107	O-linked
+P47001	YJL158C	CIS3	109	O-linked
+P47001	YJL158C	CIS3	111	O-linked
+P47001	YJL158C	CIS3	112	O-linked
+P47001	YJL158C	CIS3	113	O-linked
+P47001	YJL158C	CIS3	114	N-linked
+P47001	YJL158C	CIS3	116	O-linked
+P47001	YJL158C	CIS3	117	O-linked
+P47001	YJL158C	CIS3	118	O-linked
+Q03690	YMR012W	CLU1	1247	Phosphoserine
+P53865	YNL225C	CNM67	17	Phosphoserine
+P53865	YNL225C	CNM67	20	Phosphoserine
+P53865	YNL225C	CNM67	72	Phosphoserine
+P53865	YNL225C	CNM67	85	Phosphoserine
+P53865	YNL225C	CNM67	89	Phosphoserine
+P53865	YNL225C	CNM67	151	Phosphoserine
+P41810	YDR238C	SEC26	181	Phosphoserine
+P41810	YDR238C	SEC26	540	Phosphoserine
+Q01519	YLR038C	COX12	82	Phosphoserine
+Q03048	YLL050C	COF1	4	Phosphoserine
+P00401	Q0045	COX1	245	1'-histidyl-3'-tyrosine
+P38287	YBR161W	CSH1	354	Phosphoserine
+P43639	YGL019W	CKB1	2	N-acetylserine
+P43639	YGL019W	CKB1	2	Phosphoserine
+P46946	YGL175C	SAE2	143	Phosphoserine
+P46946	YGL175C	SAE2	267	Phosphoserine%3B
+P32074	YNL287W	SEC21	638	Phosphothreonine
+P32074	YNL287W	SEC21	643	Phosphoserine
+P32074	YNL287W	SEC21	653	Phosphoserine
+P32074	YNL287W	SEC21	647	Glycyl
+P32798	YOR316C	COT1	225	Phosphoserine
+P32798	YOR316C	COT1	301	Glycyl
+P04037	YGL187C	COX4	55	Phosphothreonine
+P10614	YHR007C	ERG11	458	Phosphoserine
+P10614	YHR007C	ERG11	116	Glycyl
+P10614	YHR007C	ERG11	353	Glycyl
+P10614	YHR007C	ERG11	454	Glycyl
+P08679	YCR005C	CIT2	21	Phosphoserine
+P08679	YCR005C	CIT2	218	Glycyl
+P08679	YCR005C	CIT2	239	Glycyl
+P08679	YCR005C	CIT2	354	Glycyl
+P08679	YCR005C	CIT2	385	Glycyl
+P17891	YGR167W	CLC1	49	Phosphothreonine
+P17891	YGR167W	CLC1	52	Phosphoserine
+P41811	YGL137W	SEC27	326	Phosphoserine
+P38170	YBL097W	BRN1	245	Phosphoserine
+P38170	YBL097W	BRN1	548	Phosphoserine
+P43621	YFR051C	RET2	277	Phosphothreonine
+Q06705	YLR380W	CSR1	2	N-acetylserine
+Q06705	YLR380W	CSR1	2	Phosphoserine
+Q03957	YKL139W	CTK1	14	Phosphoserine%3B
+Q03957	YKL139W	CTK1	338	Phosphothreonine
+P40094	YER157W	COG3	507	Phosphoserine
+P40094	YER157W	COG3	647	Phosphoserine
+Q06440	YLR429W	CRN1	441	Phosphoserine
+Q06440	YLR429W	CRN1	454	Phosphoserine
+Q06440	YLR429W	CRN1	456	Phosphoserine
+Q06440	YLR429W	CRN1	517	Phosphothreonine
+Q06440	YLR429W	CRN1	529	Phosphothreonine
+Q06440	YLR429W	CRN1	573	Phosphoserine
+Q06440	YLR429W	CRN1	579	Phosphoserine
+Q12150	YLR087C	CSF1	82	N-linked
+Q12150	YLR087C	CSF1	117	N-linked
+Q12150	YLR087C	CSF1	144	N-linked
+Q12150	YLR087C	CSF1	271	N-linked
+Q12150	YLR087C	CSF1	478	N-linked
+Q12150	YLR087C	CSF1	530	N-linked
+Q12150	YLR087C	CSF1	816	N-linked
+Q12150	YLR087C	CSF1	821	N-linked
+Q12150	YLR087C	CSF1	839	N-linked
+Q12150	YLR087C	CSF1	892	N-linked
+Q12150	YLR087C	CSF1	1309	N-linked
+Q12150	YLR087C	CSF1	1368	N-linked
+Q12150	YLR087C	CSF1	1453	N-linked
+Q12150	YLR087C	CSF1	1785	N-linked
+Q12150	YLR087C	CSF1	1921	N-linked
+Q12150	YLR087C	CSF1	2130	N-linked
+Q12150	YLR087C	CSF1	2146	N-linked
+Q12150	YLR087C	CSF1	2280	N-linked
+Q12150	YLR087C	CSF1	2337	N-linked
+Q12150	YLR087C	CSF1	2520	N-linked
+Q12150	YLR087C	CSF1	2578	N-linked
+Q12150	YLR087C	CSF1	2719	N-linked
+Q12150	YLR087C	CSF1	2869	N-linked
+Q12748	YLR381W	CTF3	2	N-acetylserine
+Q08923	YPL181W	CTI6	174	Phosphothreonine
+Q08923	YPL181W	CTI6	175	Phosphoserine
+Q08923	YPL181W	CTI6	177	Phosphothreonine
+Q08923	YPL181W	CTI6	216	Phosphoserine
+Q08923	YPL181W	CTI6	267	Phosphoserine
+Q12734	YPR030W	CSR2	23	Phosphoserine
+Q12734	YPR030W	CSR2	46	Phosphoserine
+Q12734	YPR030W	CSR2	127	Phosphoserine
+Q12734	YPR030W	CSR2	327	Phosphoserine
+Q12734	YPR030W	CSR2	987	Phosphoserine
+Q12734	YPR030W	CSR2	841	Glycyl
+P25618	YCR017C	CWH43	419	N-linked
+P25618	YCR017C	CWH43	490	N-linked
+P25618	YCR017C	CWH43	767	N-linked
+P25618	YCR017C	CWH43	792	N-linked
+P25618	YCR017C	CWH43	825	N-linked
+Q04632	YML071C	COG8	410	Phosphoserine
+P38845	YHR146W	CRP1	153	Phosphoserine
+P38845	YHR146W	CRP1	156	Phosphoserine
+P38845	YHR146W	CRP1	182	Phosphothreonine
+P38845	YHR146W	CRP1	271	Phosphoserine
+P38845	YHR146W	CRP1	295	Phosphothreonine
+P38845	YHR146W	CRP1	319	Phosphoserine
+P38845	YHR146W	CRP1	343	Phosphoserine
+P38845	YHR146W	CRP1	366	Phosphothreonine
+P38845	YHR146W	CRP1	394	Phosphoserine
+P38845	YHR146W	CRP1	440	Phosphoserine
+P43497	YKL096W-A	CWP2	71	GPI-anchor
+P53968	YNL027W	CRZ1	170	Phosphothreonine
+P53968	YNL027W	CRZ1	175	Phosphoserine
+P53968	YNL027W	CRZ1	245	Phosphoserine
+P53968	YNL027W	CRZ1	385	Phosphoserine
+P14306	YLR178C	TFS1	1	N-acetylmethionine
+P53301	YGR189C	CRH1	482	GPI-anchor
+P53301	YGR189C	CRH1	117	N-linked
+P53301	YGR189C	CRH1	177	N-linked
+P53301	YGR189C	CRH1	201	N-linked
+Q06538	YLR241W	CSC1	171	N-linked
+P35206	YBR036C	CSG2	35	N-linked
+P35206	YBR036C	CSG2	49	N-linked
+P25355	YCR054C	CTR86	433	Phosphothreonine
+P25355	YCR054C	CTR86	559	Phosphoserine
+P53923	YNL119W	NCS2	489	Phosphoserine
+P53830	YNL286W	CUS2	163	Phosphoserine
+P00044	YJR048W	CYC1	78	N6%2CN6%2CN6-trimethyllysine%3B
+P00044	YJR048W	CYC1	79	N6%2CN6%2CN6-trimethyllysine
+P32898	YDR430C	CYM1	920	Phosphoserine
+P32623	YEL040W	UTR2	445	GPI-anchor
+P32623	YEL040W	UTR2	28	N-linked
+P32623	YEL040W	UTR2	96	N-linked
+P32623	YEL040W	UTR2	190	N-linked
+P32623	YEL040W	UTR2	196	N-linked
+P32623	YEL040W	UTR2	233	N-linked
+P32623	YEL040W	UTR2	237	N-linked
+P32623	YEL040W	UTR2	261	N-linked
+P32623	YEL040W	UTR2	297	N-linked
+P32623	YEL040W	UTR2	310	N-linked
+P49573	YPR124W	CTR1	344	Phosphoserine
+P49573	YPR124W	CTR1	349	Phosphoserine
+P49573	YPR124W	CTR1	356	Phosphothreonine
+P49573	YPR124W	CTR1	369	Phosphoserine
+P49573	YPR124W	CTR1	113	N-linked
+P49573	YPR124W	CTR1	148	N-linked
+P49573	YPR124W	CTR1	345	Glycyl
+P89105	YOL145C	CTR9	1015	Phosphoserine
+P89105	YOL145C	CTR9	1017	Phosphoserine
+Q04201	YML101C	CUE4	48	Phosphoserine
+Q04201	YML101C	CUE4	37	Glycyl
+Q08412	YOR042W	CUE5	21	Phosphoserine
+Q08412	YOR042W	CUE5	36	Phosphoserine
+Q08412	YOR042W	CUE5	70	Phosphothreonine
+Q08412	YOR042W	CUE5	91	Phosphoserine
+Q08412	YOR042W	CUE5	167	Phosphothreonine
+Q08412	YOR042W	CUE5	220	Phosphoserine
+Q08412	YOR042W	CUE5	309	Phosphoserine
+Q08412	YOR042W	CUE5	318	Phosphoserine
+Q08412	YOR042W	CUE5	346	Phosphothreonine
+Q08412	YOR042W	CUE5	348	Phosphoserine
+Q08412	YOR042W	CUE5	352	Phosphothreonine
+Q08412	YOR042W	CUE5	364	Phosphothreonine
+Q08412	YOR042W	CUE5	367	Phosphothreonine
+Q08412	YOR042W	CUE5	407	Phosphoserine
+Q08412	YOR042W	CUE5	15	Glycyl
+Q08412	YOR042W	CUE5	59	Glycyl
+Q08412	YOR042W	CUE5	76	Glycyl
+Q08412	YOR042W	CUE5	156	Glycyl
+Q08412	YOR042W	CUE5	354	Glycyl
+Q08412	YOR042W	CUE5	396	Glycyl
+P47050	YJL047C	RTT101	791	Glycyl
+P53854	YNL245C	CWC25	129	Phosphoserine
+Q12046	YDL209C	CWC2	335	Phosphoserine
+Q12046	YDL209C	CWC2	336	Phosphoserine
+P53008	YGL027C	CWH41	42	N-linked
+P53008	YGL027C	CWH41	122	N-linked
+P53008	YGL027C	CWH41	135	N-linked
+P53008	YGL027C	CWH41	787	N-linked
+P28319	YKL096W	CWP1	217	GPI-anchor
+Q08226	YOL063C	CRT10	704	Phosphoserine
+P53859	YNL232W	CSL4	94	Phosphoserine
+P21657	YIR023W	DAL81	833	Phosphoserine
+P47179	YJR151C	DAN4	1137	GPI-anchor
+P22204	YGR092W	DBF2	17	Phosphoserine
+P22204	YGR092W	DBF2	20	Phosphoserine
+P22204	YGR092W	DBF2	74	Phosphoserine
+P22204	YGR092W	DBF2	374	Phosphoserine%3B
+P22204	YGR092W	DBF2	544	Phosphothreonine%3B
+P24309	YKL149C	DBR1	269	Phosphoserine
+P36091	YKL046C	DCW1	428	GPI-anchor
+P36091	YKL046C	DCW1	34	N-linked
+P36091	YKL046C	DCW1	84	N-linked
+P36091	YKL046C	DCW1	109	N-linked
+P36091	YKL046C	DCW1	133	N-linked
+P36091	YKL046C	DCW1	203	N-linked
+P36091	YKL046C	DCW1	225	N-linked
+P36091	YKL046C	DCW1	240	N-linked
+P36091	YKL046C	DCW1	265	N-linked
+P36091	YKL046C	DCW1	281	N-linked
+P36091	YKL046C	DCW1	337	N-linked
+P36091	YKL046C	DCW1	362	N-linked
+P36091	YKL046C	DCW1	420	N-linked
+P53899	YNL155W	CUZ1	273	Phosphoserine
+P08678	YJL005W	CYR1	2	N-acetylserine
+P08678	YJL005W	CYR1	376	Phosphothreonine
+P08678	YJL005W	CYR1	389	Phosphothreonine
+P08678	YJL005W	CYR1	433	Phosphoserine
+P08678	YJL005W	CYR1	487	Phosphoserine
+P08678	YJL005W	CYR1	497	Phosphoserine
+P08678	YJL005W	CYR1	562	Phosphoserine
+P47178	YJR150C	DAN1	275	GPI-anchor
+P18962	YHR028C	DAP2	63	N-linked
+P18962	YHR028C	DAP2	79	N-linked
+P18962	YHR028C	DAP2	110	N-linked
+P18962	YHR028C	DAP2	139	N-linked
+P18962	YHR028C	DAP2	372	N-linked
+P18962	YHR028C	DAP2	392	N-linked
+P18962	YHR028C	DAP2	421	N-linked
+P18962	YHR028C	DAP2	738	N-linked
+Q12123	YOR173W	DCS2	341	Phosphoserine
+P46963	YML112W	CTK3	35	Phosphothreonine
+P53137	YGL110C	CUE3	377	Phosphoserine
+Q12389	YDL031W	DBP10	101	Phosphoserine
+Q12389	YDL031W	DBP10	398	Phosphoserine
+Q12389	YDL031W	DBP10	400	Phosphoserine
+P24783	YNL112W	DBP2	88	Phosphoserine
+P24783	YNL112W	DBP2	90	Phosphoserine
+P24783	YNL112W	DBP2	474	Glycyl
+P20449	YOR046C	DBP5	86	Phosphoserine
+P20449	YOR046C	DBP5	93	Phosphoserine
+P20449	YOR046C	DBP5	162	Phosphoserine
+P53734	YNR038W	DBP6	73	Phosphoserine
+P53734	YNR038W	DBP6	77	Phosphoserine
+P53734	YNR038W	DBP6	78	Phosphoserine
+P21182	YOL052C	SPE2	88	Pyruvic
+P08432	YKL184W	SPE1	116	N6-(pyridoxal
+P06634	YOR204W	DED1	2	N-acetylalanine
+P06634	YOR204W	DED1	62	Dimethylated
+P06634	YOR204W	DED1	215	Phosphoserine
+P06634	YOR204W	DED1	218	Phosphoserine
+P06634	YOR204W	DED1	263	Phosphoserine
+P06634	YOR204W	DED1	535	Phosphoserine
+P06634	YOR204W	DED1	539	Phosphoserine
+P06634	YOR204W	DED1	543	Phosphoserine
+P06634	YOR204W	DED1	572	Phosphoserine
+P06634	YOR204W	DED1	576	Phosphoserine
+P06634	YOR204W	DED1	598	Phosphoserine
+P06634	YOR204W	DED1	158	Glycyl
+P38307	YBR201W	DER1	1	N-acetylmethionine
+Q01454	YPR135W	CTF4	377	Phosphoserine
+Q01454	YPR135W	CTF4	379	Phosphoserine
+Q01454	YPR135W	CTF4	398	Phosphoserine
+Q01454	YPR135W	CTF4	401	Phosphothreonine
+Q01454	YPR135W	CTF4	411	Phosphothreonine
+Q01454	YPR135W	CTF4	463	Phosphoserine
+P53769	YLR323C	CWC24	33	Phosphoserine
+P53769	YLR323C	CWC24	105	Phosphoserine
+P35176	YDR304C	CPR5	139	N-linked
+P14832	YDR155C	CPR1	2	N-acetylserine
+P14832	YDR155C	CPR1	71	Phosphothreonine
+P14832	YDR155C	CPR1	142	Phosphoserine
+P14832	YDR155C	CPR1	145	Phosphoserine
+P14832	YDR155C	CPR1	29	Glycyl
+P14832	YDR155C	CPR1	42	Glycyl
+P14832	YDR155C	CPR1	123	Glycyl
+P14832	YDR155C	CPR1	139	Glycyl
+P14832	YDR155C	CPR1	151	Glycyl
+P14832	YDR155C	CPR1	158	Glycyl
+P31373	YAL012W	CYS3	204	N6-(pyridoxal
+P31373	YAL012W	CYS3	362	Phosphoserine
+Q12248	YDR016C	DAD1	91	Phosphoserine
+P25334	YCR069W	CPR4	166	N-linked
+P06106	YLR303W	MET17	44	Phosphoserine
+P06106	YLR303W	MET17	209	N6-(pyridoxal
+P06106	YLR303W	MET17	160	Glycyl
+Q99288	YDR051C	DET1	248	Phosphoserine
+Q05080	YMR032W	HOF1	337	Phosphoserine
+Q05080	YMR032W	HOF1	366	Phosphoserine
+Q05080	YMR032W	HOF1	421	Phosphoserine
+P20448	YJL033W	HCA4	692	Phosphoserine
+P20448	YJL033W	HCA4	710	Phosphoserine
+P20448	YJL033W	HCA4	714	Phosphoserine
+P20448	YJL033W	HCA4	743	Phosphoserine
+P40087	YER143W	DDI1	171	Glycyl
+P40087	YER143W	DDI1	257	Glycyl
+P69851	YDR320C-A	DAD4	1	N-acetylmethionine
+P32328	YPR111W	DBF20	17	Phosphoserine
+P32328	YPR111W	DBF20	366	Phosphoserine
+P32328	YPR111W	DBF20	536	Phosphothreonine
+P53550	YNL118C	DCP2	116	Phosphoserine
+P53550	YNL118C	DCP2	439	Phosphoserine
+P53550	YNL118C	DCP2	677	Phosphothreonine
+P53550	YNL118C	DCP2	679	Phosphoserine
+P53550	YNL118C	DCP2	682	Phosphoserine
+P53550	YNL118C	DCP2	751	Phosphoserine
+P53550	YNL118C	DCP2	771	Phosphoserine
+P53550	YNL118C	DCP2	773	Phosphoserine
+P53550	YNL118C	DCP2	778	Phosphoserine
+P18899	YMR173W	DDR48	183	Phosphoserine
+P18899	YMR173W	DDR48	191	Phosphoserine
+P18899	YMR173W	DDR48	314	Phosphoserine
+P18899	YMR173W	DDR48	322	Phosphoserine
+P31385	YAL013W	DEP1	56	Phosphoserine
+P31385	YAL013W	DEP1	120	Phosphoserine
+P31385	YAL013W	DEP1	370	Phosphoserine
+P14922	YBR112C	CYC8	429	Phosphoserine
+P14922	YBR112C	CYC8	475	Phosphothreonine
+P14922	YBR112C	CYC8	710	Phosphoserine
+P14922	YBR112C	CYC8	741	Phosphoserine
+P14922	YBR112C	CYC8	768	Phosphoserine
+P14922	YBR112C	CYC8	815	Phosphoserine
+P14922	YBR112C	CYC8	817	Phosphoserine
+P14922	YBR112C	CYC8	866	Phosphoserine
+P14922	YBR112C	CYC8	943	Phosphoserine
+Q07533	YDL117W	CYK3	209	Phosphoserine
+Q07533	YDL117W	CYK3	292	Phosphoserine
+Q07533	YDL117W	CYK3	313	Phosphoserine
+Q07533	YDL117W	CYK3	354	Phosphoserine
+Q07533	YDL117W	CYK3	391	Phosphothreonine
+P36162	YKR083C	DAD2	1	N-acetylmethionine
+P53267	YGR113W	DAM1	2	N-acetylserine
+P53267	YGR113W	DAM1	20	Phosphoserine%3B
+P53267	YGR113W	DAM1	31	Phosphoserine
+P53267	YGR113W	DAM1	257	Phosphoserine%3B
+P53267	YGR113W	DAM1	265	Phosphoserine%3B
+P53267	YGR113W	DAM1	292	Phosphoserine%3B
+P53202	YGR003W	CUL3	688	Glycyl
+Q02554	YMR240C	CUS1	104	Phosphothreonine
+Q02554	YMR240C	CUS1	112	Phosphothreonine
+Q02554	YMR240C	CUS1	114	Phosphoserine
+P54838	YML070W	DAK1	2	N-acetylserine
+P54838	YML070W	DAK1	2	Phosphoserine
+P54838	YML070W	DAK1	5	Phosphoserine
+P54838	YML070W	DAK1	365	Phosphoserine
+P54838	YML070W	DAK1	512	Phosphoserine
+Q12382	YOR311C	DGK1	44	Phosphoserine
+Q12382	YOR311C	DGK1	45	Phosphoserine
+Q12382	YOR311C	DGK1	46	Phosphoserine
+Q12382	YOR311C	DGK1	11	N-linked
+Q12382	YOR311C	DGK1	197	N-linked
+Q12382	YOR311C	DGK1	270	N-linked
+P54861	YLL001W	DNM1	629	Phosphoserine
+P40059	YER088C	DOT6	245	Phosphoserine
+P40059	YER088C	DOT6	247	Phosphoserine
+P40059	YER088C	DOT6	487	Phosphoserine
+P40059	YER088C	DOT6	489	Phosphothreonine
+P40059	YER088C	DOT6	491	Phosphoserine
+P32469	YLR172C	DPH5	172	Phosphoserine
+P32469	YLR172C	DPH5	298	Phosphoserine
+P32892	YLL008W	DRS1	208	Phosphoserine
+P23501	YKR053C	YSR3	62	N-linked
+P07262	YOR375C	GDH1	2	N-acetylserine
+P07262	YOR375C	GDH1	325	Glycyl
+P07262	YOR375C	GDH1	371	Glycyl
+P07262	YOR375C	GDH1	433	Glycyl
+Q08496	YOR080W	DIA2	393	Phosphoserine
+P04819	YDL164C	CDC9	58	Phosphoserine
+P04819	YDL164C	CDC9	75	Phosphoserine
+P04819	YDL164C	CDC9	119	Phosphoserine
+P04819	YDL164C	CDC9	123	Phosphoserine
+Q03921	YDR141C	DOP1	244	Phosphoserine
+P46957	YJR006W	POL31	1	N-acetylmethionine
+P46957	YJR006W	POL31	20	Phosphoserine
+P36152	YKR071C	DRE2	206	Phosphoserine
+Q04792	YMR250W	GAD1	318	N6-(pyridoxal
+P35732	YKL054C	DEF1	260	Phosphoserine
+P35732	YKL054C	DEF1	273	Phosphoserine
+P35732	YKL054C	DEF1	307	Phosphoserine
+P35732	YKL054C	DEF1	338	Phosphothreonine
+P35732	YKL054C	DEF1	646	Phosphoserine
+P32330	YKL121W	DGR2	716	Phosphoserine
+P39708	YAL062W	GDH3	326	Glycyl
+P39708	YAL062W	GDH3	372	Glycyl
+P39708	YAL062W	GDH3	436	Glycyl
+Q04603	YDR121W	DPB4	183	Phosphoserine%3B
+Q04217	YMR128W	ECM16	181	Phosphoserine
+P40318	YIL030C	SSM4	1	N-acetylmethionine
+P47110	YJR043C	POL32	223	Phosphothreonine
+P47110	YJR043C	POL32	230	Phosphoserine
+P53255	YGR093W	DRN1	242	Phosphoserine
+P32325	YDR052C	DBF4	59	Phosphoserine
+P32325	YDR052C	DBF4	84	Phosphoserine
+P32325	YDR052C	DBF4	235	Phosphoserine
+P32325	YDR052C	DBF4	623	Phosphoserine
+Q03373	YDR480W	DIG2	34	Phosphoserine
+Q03373	YDR480W	DIG2	225	Phosphoserine
+Q03373	YDR480W	DIG2	266	Phosphoserine
+Q03373	YDR480W	DIG2	270	Phosphoserine
+P40366	YJL065C	DLS1	17	Phosphoserine
+Q06819	YPR082C	DIB1	2	N-acetylalanine
+P39976	YEL071W	DLD3	17	Glycyl
+P31116	YJR139C	HOM6	290	Glycyl
+P36037	YKL213C	DOA1	332	Phosphoserine
+Q12395	YLR128W	DCN1	12	Phosphoserine
+Q06151	YLR270W	DCS1	2	N-acetylserine
+Q06151	YLR270W	DCS1	60	Phosphoserine
+Q06151	YLR270W	DCS1	66	Phosphothreonine
+Q06151	YLR270W	DCS1	66	Phosphothreonine%3B
+Q06151	YLR270W	DCS1	70	Phosphotyrosine
+Q06151	YLR270W	DCS1	120	Phosphothreonine
+P89113	YOL052C-A	DDR2	24	N-linked
+P89113	YOL052C-A	DDR2	27	N-linked
+P69771	YKR035W-A	DID2	5	Phosphoserine
+P38823	YHR115C	DMA1	150	Glycyl
+P38823	YHR115C	DMA1	204	Glycyl
+P38823	YHR115C	DMA1	217	Glycyl
+P38823	YHR115C	DMA1	237	Glycyl
+P38823	YHR115C	DMA1	240	Glycyl
+P38823	YHR115C	DMA1	260	Glycyl
+P38823	YHR115C	DMA1	300	Glycyl
+P38823	YHR115C	DMA1	306	Glycyl
+P38823	YHR115C	DMA1	313	Glycyl
+P38823	YHR115C	DMA1	317	Glycyl
+Q08949	YPL194W	DDC1	436	Phosphoserine
+Q05031	YMR238W	DFG5	437	GPI-anchor
+Q05031	YMR238W	DFG5	89	N-linked
+Q05031	YMR238W	DFG5	114	N-linked
+Q05031	YMR238W	DFG5	138	N-linked
+Q05031	YMR238W	DFG5	208	N-linked
+Q05031	YMR238W	DFG5	231	N-linked
+Q05031	YMR238W	DFG5	245	N-linked
+Q05031	YMR238W	DFG5	270	N-linked
+Q05031	YMR238W	DFG5	273	N-linked
+Q05031	YMR238W	DFG5	417	N-linked
+Q08650	YOR245C	DGA1	17	Phosphoserine
+P13663	YDR158W	HOM2	13	Phosphothreonine
+P13663	YDR158W	HOM2	318	Phosphoserine
+P13663	YDR158W	HOM2	323	Phosphoserine
+Q03063	YPL049C	DIG1	45	Phosphoserine
+Q03063	YPL049C	DIG1	126	Phosphoserine
+Q03063	YPL049C	DIG1	142	Phosphoserine
+Q03063	YPL049C	DIG1	272	Phosphoserine
+Q03063	YPL049C	DIG1	275	Phosphoserine
+Q03063	YPL049C	DIG1	330	Phosphoserine
+Q03063	YPL049C	DIG1	379	Phosphothreonine
+Q03063	YPL049C	DIG1	395	Phosphoserine
+Q03063	YPL049C	DIG1	428	Phosphoserine
+P53388	YPL265W	DIP5	22	Phosphoserine
+P53388	YPL265W	DIP5	76	Glycyl
+P53924	YNL116W	DMA2	206	Phosphoserine
+P53924	YNL116W	DMA2	211	Glycyl
+P53924	YNL116W	DMA2	256	Glycyl
+P53924	YNL116W	DMA2	258	Glycyl
+P53924	YNL116W	DMA2	288	Glycyl
+P53924	YNL116W	DMA2	310	Glycyl
+P53924	YNL116W	DMA2	333	Glycyl
+P53924	YNL116W	DMA2	343	Glycyl
+P53924	YNL116W	DMA2	346	Glycyl
+P53924	YNL116W	DMA2	366	Glycyl
+P53924	YNL116W	DMA2	406	Glycyl
+P53924	YNL116W	DMA2	412	Glycyl
+P53924	YNL116W	DMA2	423	Glycyl
+P38859	YHR164C	DNA2	4	Phosphothreonine
+P38859	YHR164C	DNA2	17	Phosphoserine%3B
+P38859	YHR164C	DNA2	237	Phosphoserine%3B
+P38859	YHR164C	DNA2	962	Phosphothreonine
+P02994	YPR080W;	YBR118W	2	N%2CN%2CN-trimethylglycine%3B
+P02994	YPR080W;	YBR118W	3	N6%2CN6-dimethyllysine%3B
+P02994	YPR080W;	YBR118W	3	N6-methyllysine%3B
+P02994	YPR080W;	YBR118W	18	Phosphoserine
+P02994	YPR080W;	YBR118W	30	N6-methyllysine%3B
+P02994	YPR080W;	YBR118W	72	Phosphothreonine
+P02994	YPR080W;	YBR118W	79	N6%2CN6%2CN6-trimethyllysine%3B
+P02994	YPR080W;	YBR118W	82	Phosphothreonine
+P02994	YPR080W;	YBR118W	163	Phosphoserine
+P02994	YPR080W;	YBR118W	259	Phosphothreonine
+P02994	YPR080W;	YBR118W	289	Phosphoserine
+P02994	YPR080W;	YBR118W	316	N6%2CN6-dimethyllysine%3B
+P02994	YPR080W;	YBR118W	316	N6-methyllysine%3B
+P02994	YPR080W;	YBR118W	390	N6-methyllysine%3B
+P02994	YPR080W;	YBR118W	414	Phosphoserine
+P02994	YPR080W;	YBR118W	430	Phosphothreonine
+P02994	YPR080W;	YBR118W	458	Lysine
+P02994	YPR080W;	YBR118W	224	Glycyl
+P02994	YPR080W;	YBR118W	242	Glycyl
+P02994	YPR080W;	YBR118W	253	Glycyl
+P02994	YPR080W;	YBR118W	271	Glycyl
+P02994	YPR080W;	YBR118W	393	Glycyl
+P02994	YPR080W;	YBR118W	437	Glycyl
+Q03653	YMR212C	EFR3	227	Phosphoserine
+Q03653	YMR212C	EFR3	231	Phosphothreonine
+Q03653	YMR212C	EFR3	564	Phosphoserine
+Q03653	YMR212C	EFR3	625	Phosphoserine
+Q03653	YMR212C	EFR3	632	Phosphoserine
+Q03653	YMR212C	EFR3	643	Phosphoserine
+Q03653	YMR212C	EFR3	675	Phosphoserine
+Q03653	YMR212C	EFR3	687	Phosphothreonine
+Q03653	YMR212C	EFR3	690	Phosphothreonine
+Q03653	YMR212C	EFR3	735	Phosphoserine
+Q03653	YMR212C	EFR3	771	Phosphoserine
+Q03653	YMR212C	EFR3	774	Phosphoserine
+P09032	YOR260W	GCD1	296	Phosphoserine
+P09032	YOR260W	GCD1	300	Phosphoserine
+P09032	YOR260W	GCD1	306	Phosphothreonine
+P38121	YBL035C	POL12	126	Phosphoserine
+P13382	YNL102W	POL1	2	N-acetylserine
+P13382	YNL102W	POL1	31	Phosphoserine
+P13382	YNL102W	POL1	82	Phosphoserine
+P13382	YNL102W	POL1	83	Phosphoserine
+P13382	YNL102W	POL1	84	Phosphoserine
+P13382	YNL102W	POL1	169	Phosphoserine
+P13382	YNL102W	POL1	170	Phosphoserine
+P13382	YNL102W	POL1	172	Phosphothreonine
+P13382	YNL102W	POL1	240	Phosphoserine
+P13382	YNL102W	POL1	274	Phosphoserine
+P13382	YNL102W	POL1	309	Phosphothreonine
+P13382	YNL102W	POL1	313	Phosphothreonine
+Q05521	YDR284C	DPP1	285	Phosphoserine
+Q08729	YOR264W	DSE3	395	Phosphoserine
+P48510	YMR276W	DSK2	13	Glycyl
+P48510	YMR276W	DSK2	76	Glycyl
+P40568	YIR010W	DSN1	250	Phosphoserine
+P36049	YKL172W	EBP2	104	Phosphoserine
+P36049	YKL172W	EBP2	177	Phosphoserine
+P36049	YKL172W	EBP2	183	Phosphoserine
+Q99252	YOR092W	ECM3	291	Phosphoserine
+Q99252	YOR092W	ECM3	338	Phosphoserine
+P53168	YGL061C	DUO1	2	N-acetylserine
+P36041	YKL204W	EAP1	30	Phosphoserine
+P36041	YKL204W	EAP1	281	Phosphoserine
+P36041	YKL204W	EAP1	282	Phosphoserine
+P36041	YKL204W	EAP1	327	Phosphoserine
+P36041	YKL204W	EAP1	344	Phosphoserine
+P36041	YKL204W	EAP1	387	Phosphoserine
+P42835	YNL327W	EGT2	1020	GPI-anchor
+P42835	YNL327W	EGT2	65	N-linked
+P42835	YNL327W	EGT2	103	N-linked
+P42835	YNL327W	EGT2	161	N-linked
+P42835	YNL327W	EGT2	175	N-linked
+P42835	YNL327W	EGT2	249	N-linked
+P42835	YNL327W	EGT2	332	N-linked
+P42835	YNL327W	EGT2	401	N-linked
+P42835	YNL327W	EGT2	435	N-linked
+P42835	YNL327W	EGT2	465	N-linked
+P42835	YNL327W	EGT2	485	N-linked
+P42835	YNL327W	EGT2	506	N-linked
+P42835	YNL327W	EGT2	526	N-linked
+P42835	YNL327W	EGT2	544	N-linked
+P42835	YNL327W	EGT2	556	N-linked
+P42835	YNL327W	EGT2	635	N-linked
+P42835	YNL327W	EGT2	636	N-linked
+P42835	YNL327W	EGT2	657	N-linked
+P42835	YNL327W	EGT2	709	N-linked
+P42835	YNL327W	EGT2	756	N-linked
+P47120	YJR070C	LIA1	2	N-acetylserine
+P47120	YJR070C	LIA1	126	Phosphoserine
+P47120	YJR070C	LIA1	187	Phosphothreonine
+P47120	YJR070C	LIA1	281	Phosphoserine
+P27344	YBR278W	DPB3	186	Phosphoserine
+P27344	YBR278W	DPB3	188	Phosphoserine
+P27344	YBR278W	DPB3	189	Phosphoserine
+P40487	YIL103W	DPH1	44	Phosphoserine
+P47013	YJL134W	LCB3	16	Phosphothreonine
+P47013	YJL134W	LCB3	18	Phosphoserine
+P38844	YHR143W	DSE2	308	GPI-anchor
+P43616	YFR044C	DUG1	451	Phosphoserine
+P32528	YBR208C	DUR1,2	803	Phosphoserine
+P32528	YBR208C	DUR1,2	1798	N6-biotinyllysine
+P53759	YML080W	DUS1	2	N-acetylthreonine
+P53063	YGL246C	RAI1	198	Phosphoserine
+Q06337	YDR359C	EAF1	841	Phosphoserine
+Q06337	YDR359C	EAF1	971	Phosphothreonine
+P53911	YNL136W	EAF7	200	Phosphoserine
+P53911	YNL136W	EAF7	225	Phosphoserine
+Q03212	YMR171C	EAR1	519	Phosphoserine
+Q03212	YMR171C	EAR1	538	Phosphoserine
+Q03212	YMR171C	EAR1	110	N-linked
+Q03212	YMR171C	EAR1	203	N-linked
+Q03212	YMR171C	EAR1	210	N-linked
+Q03212	YMR171C	EAR1	256	N-linked
+Q03212	YMR171C	EAR1	295	N-linked
+P38167	YBL101C	ECM21	18	Phosphoserine
+P38167	YBL101C	ECM21	115	Phosphoserine
+P38167	YBL101C	ECM21	140	Phosphoserine
+P38167	YBL101C	ECM21	286	Phosphoserine
+P38167	YBL101C	ECM21	527	Phosphoserine
+P38167	YBL101C	ECM21	550	Phosphoserine
+P38167	YBL101C	ECM21	775	Phosphoserine
+P38167	YBL101C	ECM21	1035	Phosphoserine
+P38167	YBL101C	ECM21	191	Glycyl
+P38167	YBL101C	ECM21	577	Glycyl
+P38167	YBL101C	ECM21	651	Glycyl
+P38167	YBL101C	ECM21	712	Glycyl
+P38167	YBL101C	ECM21	794	Glycyl
+P38167	YBL101C	ECM21	807	Glycyl
+P38167	YBL101C	ECM21	1024	Glycyl
+P38737	YHL030W	ECM29	2	N-acetylserine
+P38737	YHL030W	ECM29	1692	Phosphoserine
+P32497	YMR309C	NIP1	98	Phosphoserine
+P32497	YMR309C	NIP1	99	Phosphoserine
+P32497	YMR309C	NIP1	103	Phosphoserine
+Q12050	YOR144C	ELG1	6	Phosphoserine
+P25574	YCL045C	EMC1	73	N-linked
+P25574	YCL045C	EMC1	106	N-linked
+P25574	YCL045C	EMC1	192	N-linked
+P25574	YCL045C	EMC1	202	N-linked
+P25574	YCL045C	EMC1	420	N-linked
+P25574	YCL045C	EMC1	443	N-linked
+P25574	YCL045C	EMC1	574	N-linked
+P25574	YCL045C	EMC1	578	N-linked
+P40077	YER124C	DSE1	553	Glycyl
+Q12432	YPR023C	EAF3	201	Phosphoserine
+P32471	YAL003W	EFB1	2	N-acetylalanine
+P32471	YAL003W	EFB1	31	Phosphoserine
+P32471	YAL003W	EFB1	86	Phosphoserine
+P32471	YAL003W	EFB1	13	Glycyl
+P29547	YPL048W	CAM1	2	N-acetylserine
+P29547	YPL048W	CAM1	32	Phosphothreonine
+P32324	YOR133W;	YDR385W	509	N6%2CN6%2CN6-trimethyllysine%3B
+P32324	YOR133W;	YDR385W	509	N6%2CN6-dimethyllysine%3B
+P32324	YOR133W;	YDR385W	509	N6-methyllysine%3B
+P32324	YOR133W;	YDR385W	579	Phosphoserine
+P32324	YOR133W;	YDR385W	613	N6%2CN6-dimethyllysine%3B
+P32324	YOR133W;	YDR385W	613	N6-methyllysine%3B
+P32324	YOR133W;	YDR385W	699	Diphthamide
+P32324	YOR133W;	YDR385W	713	Phosphothreonine
+P32324	YOR133W;	YDR385W	763	Phosphothreonine
+P32324	YOR133W;	YDR385W	841	Glycyl
+P47163	YJR129C	EFM3	177	Phosphothreonine
+P24482	YPR175W	DPB2	122	Phosphoserine
+P24482	YPR175W	DPB2	141	Phosphoserine%3B
+P24482	YPR175W	DPB2	613	Phosphoserine
+P39985	YEL055C	POL5	789	Phosphoserine
+Q06673	YLR436C	ECM30	635	Phosphoserine
+Q06673	YLR436C	ECM30	1065	Phosphoserine
+P38728	YHL043W	ECM34	45	N-linked
+Q05902	YLR299W	ECM38	119	N-linked
+Q05902	YLR299W	ECM38	191	N-linked
+Q05902	YLR299W	ECM38	270	N-linked
+Q05902	YLR299W	ECM38	298	N-linked
+Q05902	YLR299W	ECM38	454	N-linked
+Q05902	YLR299W	ECM38	517	N-linked
+P47138	YJR097W	JJJ3	2	N-acetylserine
+P14020	YPR183W	DPM1	2	N-acetylserine
+P14020	YPR183W	DPM1	141	Phosphoserine%3B
+P15436	YDL102W	POL3	30	Phosphoserine
+P15436	YDL102W	POL3	37	Phosphoserine
+P39009	YDL101C	DUN1	10	Phosphoserine
+P39009	YDL101C	DUN1	139	Phosphoserine
+P39009	YDL101C	DUN1	380	Phosphothreonine
+Q04067	YDR429C	TIF35	2	N-acetylserine
+Q04067	YDR429C	TIF35	131	Phosphoserine
+Q03764	YDR147W	EKI1	23	Phosphoserine
+Q02884	YPL101W	ELP4	222	Phosphoserine
+Q04409	YDR516C	EMI2	2	N-acetylserine
+Q04409	YDR516C	EMI2	2	Phosphoserine
+Q04409	YDR516C	EMI2	470	Phosphoserine
+P38333	YBR247C	ENP1	172	Phosphoserine%3B
+P38333	YBR247C	ENP1	190	Phosphoserine
+P38333	YBR247C	ENP1	404	Phosphoserine
+P54781	YMR015C	ERG5	164	Glycyl
+P54781	YMR015C	ERG5	198	Glycyl
+P53080	YGL222C	EDC1	2	N-acetylserine
+P53080	YGL222C	EDC1	82	Phosphoserine
+P39998	YEL015W	EDC3	257	Phosphoserine
+P39998	YEL015W	EDC3	261	Phosphoserine
+P14741	YKR026C	GCN3	2	N-acetylserine
+P14741	YKR026C	GCN3	291	Phosphothreonine
+P32501	YDR211W	GCD6	478	Phosphoserine
+P32501	YDR211W	GCD6	481	Phosphoserine
+P32501	YDR211W	GCD6	507	Phosphoserine
+P32501	YDR211W	GCD6	525	Phosphoserine
+P32501	YDR211W	GCD6	538	Phosphoserine
+P32501	YDR211W	GCD6	707	Phosphoserine
+Q05775	YLR192C	HCR1	75	Phosphothreonine
+Q05775	YLR192C	HCR1	92	Phosphoserine
+P36053	YKL160W	ELF1	55	Phosphoserine
+P36053	YKL160W	ELF1	117	Phosphoserine
+P36053	YKL160W	ELF1	124	Phosphoserine
+P36053	YKL160W	ELF1	142	Phosphoserine
+P25358	YCR034W	ELO2	334	Phosphothreonine
+P25358	YCR034W	ELO2	336	Phosphoserine
+P25358	YCR034W	ELO2	338	Phosphoserine
+P25358	YCR034W	ELO2	32	N-linked
+P39013	YNL084C	END3	276	Phosphoserine
+Q05785	YLR206W	ENT2	165	Phosphothreonine
+Q05785	YLR206W	ENT2	167	Phosphoserine
+Q05785	YLR206W	ENT2	430	Phosphothreonine
+Q05785	YLR206W	ENT2	434	Phosphoserine
+Q05785	YLR206W	ENT2	450	Phosphothreonine
+Q05785	YLR206W	ENT2	468	Phosphothreonine
+Q05785	YLR206W	ENT2	470	Phosphothreonine
+Q05785	YLR206W	ENT2	426	Glycyl
+Q12003	YPL236C	ENV7	13	S-palmitoyl
+Q12003	YPL236C	ENV7	14	S-palmitoyl
+Q12003	YPL236C	ENV7	15	S-palmitoyl
+O13529	YHR021W-A	ECM12	2	N-linked
+O13529	YHR021W-A	ECM12	132	N-linked
+O13529	YHR021W-A	ECM12	137	N-linked
+P39715	YAL059W	ECM1	188	Phosphoserine
+P34216	YBL047C	EDE1	238	Phosphothreonine
+P34216	YBL047C	EDE1	241	Phosphoserine
+P34216	YBL047C	EDE1	244	Phosphoserine
+P34216	YBL047C	EDE1	245	Phosphothreonine
+P34216	YBL047C	EDE1	248	Phosphoserine
+P34216	YBL047C	EDE1	249	Phosphoserine
+P34216	YBL047C	EDE1	251	Phosphothreonine
+P34216	YBL047C	EDE1	265	Phosphoserine
+P34216	YBL047C	EDE1	419	Phosphoserine
+P34216	YBL047C	EDE1	450	Phosphothreonine
+P34216	YBL047C	EDE1	477	Phosphothreonine
+P34216	YBL047C	EDE1	487	Phosphothreonine
+P34216	YBL047C	EDE1	495	Phosphoserine
+P34216	YBL047C	EDE1	848	Phosphoserine
+P34216	YBL047C	EDE1	931	Phosphoserine
+P34216	YBL047C	EDE1	950	Phosphoserine
+P34216	YBL047C	EDE1	964	Phosphoserine
+P34216	YBL047C	EDE1	1008	Phosphoserine
+P34216	YBL047C	EDE1	1012	Phosphoserine
+P34216	YBL047C	EDE1	1020	Phosphoserine
+P34216	YBL047C	EDE1	1046	Phosphothreonine
+P34216	YBL047C	EDE1	1069	Phosphoserine
+P34216	YBL047C	EDE1	1087	Phosphoserine
+P34216	YBL047C	EDE1	1093	Phosphoserine
+P34216	YBL047C	EDE1	1095	Phosphoserine
+P34216	YBL047C	EDE1	1096	Phosphoserine
+P34216	YBL047C	EDE1	1100	Phosphoserine
+P34216	YBL047C	EDE1	1111	Phosphothreonine
+P34216	YBL047C	EDE1	1181	Phosphoserine
+P34216	YBL047C	EDE1	1187	Phosphoserine
+P34216	YBL047C	EDE1	1307	Phosphothreonine
+P34216	YBL047C	EDE1	1343	Phosphoserine
+P34216	YBL047C	EDE1	674	Glycyl
+P34216	YBL047C	EDE1	1329	Glycyl
+P36008	YKL081W	TEF4	2	N-acetylserine
+P53978	YNL014W	HEF3	2	N-acetylserine
+P53978	YNL014W	HEF3	187	N6%2CN6%2CN6-trimethyllysine
+P53978	YNL014W	HEF3	196	N6%2CN6%2CN6-trimethyllysine
+P53978	YNL014W	HEF3	789	N6%2CN6%2CN6-trimethyllysine
+P53978	YNL014W	HEF3	972	Phosphothreonine
+P53978	YNL014W	HEF3	974	Phosphoserine
+P53978	YNL014W	HEF3	1039	Phosphoserine
+P53978	YNL014W	HEF3	1040	Phosphoserine
+P12754	YGR083C	GCD2	2	N-acetylserine
+P12754	YGR083C	GCD2	106	Phosphoserine
+P12754	YGR083C	GCD2	121	Phosphothreonine
+P32801	YKL048C	ELM1	152	Phosphoserine
+P32801	YKL048C	ELM1	516	Phosphoserine
+P32801	YKL048C	ELM1	519	Phosphoserine
+P32476	YGR175C	ERG1	284	Glycyl
+P32476	YGR175C	ERG1	289	Glycyl
+P32476	YGR175C	ERG1	311	Glycyl
+P38819	YHR110W	ERP5	171	N-linked
+Q08649	YOR244W	ESA1	17	Phosphoserine
+Q08649	YOR244W	ESA1	262	N6-acetyllysine%3B
+Q06340	YDR363W	ESC2	90	Phosphoserine
+Q06340	YDR363W	ESC2	125	Phosphoserine
+Q06340	YDR363W	ESC2	126	Phosphoserine
+Q06344	YDR365C	ESF1	86	Phosphoserine
+Q06344	YDR365C	ESF1	220	Phosphothreonine
+Q06344	YDR365C	ESF1	223	Phosphoserine
+Q06344	YDR365C	ESF1	225	Phosphoserine
+Q06344	YDR365C	ESF1	367	Phosphoserine
+Q06344	YDR365C	ESF1	369	Phosphoserine
+Q06344	YDR365C	ESF1	372	Phosphoserine
+Q06344	YDR365C	ESF1	542	Phosphothreonine
+P22696	YJR017C	ESS1	161	Phosphoserine
+P32474	YDR518W	EUG1	159	N-linked
+P32474	YDR518W	EUG1	174	N-linked
+P32474	YDR518W	EUG1	207	N-linked
+P32474	YDR518W	EUG1	293	N-linked
+P32474	YDR518W	EUG1	462	N-linked
+Q02908	YPL086C	ELP3	453	Glycyl
+P00925	YHR174W	ENO2	138	Phosphoserine
+P00925	YHR174W	ENO2	188	Phosphoserine
+P00925	YHR174W	ENO2	313	Phosphothreonine
+P00925	YHR174W	ENO2	324	Phosphothreonine
+P00925	YHR174W	ENO2	60	Glycyl
+P00925	YHR174W	ENO2	243	Glycyl
+P00925	YHR174W	ENO2	358	Glycyl
+Q12518	YDL161W	ENT1	160	Phosphothreonine
+Q12518	YDL161W	ENT1	163	Phosphoserine
+Q12518	YDL161W	ENT1	180	Phosphothreonine
+Q12518	YDL161W	ENT1	328	Phosphoserine
+Q12518	YDL161W	ENT1	364	Phosphothreonine
+Q12518	YDL161W	ENT1	366	Phosphothreonine
+Q12518	YDL161W	ENT1	384	Phosphothreonine
+Q12518	YDL161W	ENT1	386	Phosphothreonine
+Q12518	YDL161W	ENT1	388	Phosphothreonine
+Q12518	YDL161W	ENT1	395	Phosphothreonine%3B
+Q12518	YDL161W	ENT1	415	Phosphothreonine%3B
+Q12518	YDL161W	ENT1	357	Glycyl
+P47160	YJR125C	ENT3	2	N-acetylserine
+P47160	YJR125C	ENT3	196	Phosphoserine
+P47160	YJR125C	ENT3	198	Phosphoserine
+P47160	YJR125C	ENT3	203	Phosphoserine
+P47160	YJR125C	ENT3	212	Phosphoserine
+P47160	YJR125C	ENT3	223	Phosphoserine
+Q03769	YDR153C	ENT5	1	N-acetylmethionine
+Q03769	YDR153C	ENT5	322	Phosphoserine
+Q03769	YDR153C	ENT5	324	Phosphoserine
+Q03769	YDR153C	ENT5	363	Phosphoserine
+Q03769	YDR153C	ENT5	368	Phosphothreonine
+Q03769	YDR153C	ENT5	394	Phosphoserine
+Q03769	YDR153C	ENT5	401	Phosphoserine
+Q08651	YOR246C	ENV9	282	N-linked
+P25087	YML008C	ERG6	2	N-acetylserine
+P25087	YML008C	ERG6	99	Phosphoserine
+P40456	YIL151C	ESL1	170	Phosphoserine
+P40456	YIL151C	ESL1	190	Phosphoserine
+Q07872	YLL038C	ENT4	195	Phosphoserine
+P40557	YIL005W	EPS1	85	N-linked
+P40557	YIL005W	EPS1	264	N-linked
+P40557	YIL005W	EPS1	299	N-linked
+P40557	YIL005W	EPS1	370	N-linked
+P38604	YHR072W	ERG7	2	N-acetylthreonine
+P38836	YHR132C	ECM14	41	N-linked
+P38836	YHR132C	ECM14	295	N-linked
+Q05958	YLR228C	ECM22	431	Phosphoserine
+Q05958	YLR228C	ECM22	445	Phosphoserine
+Q05958	YLR228C	ECM22	464	Phosphoserine
+P32644	YER176W	ECM32	227	Phosphoserine
+P32644	YER176W	ECM32	392	Phosphoserine
+P32644	YER176W	ECM32	465	Phosphothreonine
+P38248	YBR078W	ECM33	339	Phosphoserine
+P38248	YBR078W	ECM33	406	GPI-anchor
+P38248	YBR078W	ECM33	21	N-linked
+P38248	YBR078W	ECM33	56	N-linked
+P38248	YBR078W	ECM33	82	N-linked
+P38248	YBR078W	ECM33	196	N-linked
+P38248	YBR078W	ECM33	209	N-linked
+P38248	YBR078W	ECM33	227	N-linked
+P38248	YBR078W	ECM33	234	N-linked
+P38248	YBR078W	ECM33	241	N-linked
+P38248	YBR078W	ECM33	267	N-linked
+P38248	YBR078W	ECM33	279	N-linked
+P38248	YBR078W	ECM33	304	N-linked
+P38248	YBR078W	ECM33	328	N-linked
+P38248	YBR078W	ECM33	389	N-linked
+P43605	YFR027W	ECO1	223	N6-acetyllysine%3B
+P38249	YBR079C	RPG1	508	Phosphoserine
+P38249	YBR079C	RPG1	691	Phosphoserine
+P38249	YBR079C	RPG1	935	Phosphothreonine
+P40217	YMR146C	TIF34	302	Phosphoserine
+Q05050	YMR031C	EIS1	2	N-acetylserine
+Q05050	YMR031C	EIS1	2	Phosphoserine
+Q05050	YMR031C	EIS1	88	Phosphoserine
+Q05050	YMR031C	EIS1	130	Phosphoserine
+Q05050	YMR031C	EIS1	182	Phosphoserine
+Q05050	YMR031C	EIS1	401	Phosphoserine
+Q05050	YMR031C	EIS1	584	Phosphoserine
+Q05050	YMR031C	EIS1	710	Phosphoserine
+Q05050	YMR031C	EIS1	720	Phosphothreonine
+Q05050	YMR031C	EIS1	763	Phosphoserine
+Q05050	YMR031C	EIS1	775	Phosphoserine
+Q05050	YMR031C	EIS1	816	Phosphoserine
+Q05050	YMR031C	EIS1	828	Phosphoserine
+Q05050	YMR031C	EIS1	829	Phosphoserine
+Q05050	YMR031C	EIS1	838	Phosphoserine
+P40319	YLR372W	ELO3	2	N-linked
+P40319	YLR372W	ELO3	20	N-linked
+P40319	YLR372W	ELO3	66	N-linked
+P53861	YNL230C	ELA1	235	Phosphoserine
+P53861	YNL230C	ELA1	278	Phosphoserine
+P53753	YNR067C	DSE4	138	N-linked
+P53753	YNR067C	DSE4	186	N-linked
+P53753	YNR067C	DSE4	223	N-linked
+P53753	YNR067C	DSE4	259	N-linked
+P53753	YNR067C	DSE4	280	N-linked
+P53753	YNR067C	DSE4	303	N-linked
+P53753	YNR067C	DSE4	307	N-linked
+P53753	YNR067C	DSE4	393	N-linked
+P53753	YNR067C	DSE4	533	N-linked
+P53753	YNR067C	DSE4	886	N-linked
+P06103	YOR361C	PRT1	61	Phosphoserine
+P06103	YOR361C	PRT1	67	Phosphotyrosine
+P06103	YOR361C	PRT1	669	Phosphoserine
+P00924	YGR254W	ENO1	119	Phosphoserine
+P00924	YGR254W	ENO1	138	Phosphoserine
+P00924	YGR254W	ENO1	188	Phosphoserine
+P00924	YGR254W	ENO1	313	Phosphothreonine
+P00924	YGR254W	ENO1	324	Phosphothreonine
+P00924	YGR254W	ENO1	60	Glycyl
+P00924	YGR254W	ENO1	243	Glycyl
+P00924	YGR254W	ENO1	358	Glycyl
+P32353	YLR056W	ERG3	324	Glycyl
+P32353	YLR056W	ERG3	344	Glycyl
+Q03071	YPL046C	ELC1	2	N-acetylserine
+Q03071	YPL046C	ELC1	2	Phosphoserine
+P53938	YNL080C	EOS1	103	N-linked
+P53938	YNL080C	EOS1	104	N-linked
+Q12452	YLR100W	ERG27	345	Phosphothreonine
+P38748	YHL010C	ETP1	376	Phosphoserine
+P38748	YHL010C	ETP1	369	Glycyl
+P38748	YHL010C	ETP1	410	Glycyl
+P38748	YHL010C	ETP1	450	Glycyl
+P38071	YBR026C	ETR1	339	Phosphoserine
+P23776	YLR300W	EXG1	165	N-linked
+P23776	YLR300W	EXG1	325	N-linked
+P52911	YDR261C	EXG2	50	N-linked
+P52911	YDR261C	EXG2	77	N-linked
+P52911	YDR261C	EXG2	86	N-linked
+P52911	YDR261C	EXG2	90	N-linked
+P52911	YDR261C	EXG2	106	N-linked
+P52911	YDR261C	EXG2	157	N-linked
+P52911	YDR261C	EXG2	220	N-linked
+P52911	YDR261C	EXG2	281	N-linked
+P52911	YDR261C	EXG2	285	N-linked
+P52911	YDR261C	EXG2	310	N-linked
+P52911	YDR261C	EXG2	317	N-linked
+P52911	YDR261C	EXG2	322	N-linked
+P52911	YDR261C	EXG2	401	N-linked
+P52911	YDR261C	EXG2	480	N-linked
+P52911	YDR261C	EXG2	539	N-linked
+Q04660	YMR049C	ERB1	23	Phosphoserine
+Q04660	YMR049C	ERB1	72	Phosphoserine
+Q04660	YMR049C	ERB1	76	Phosphoserine
+Q04660	YMR049C	ERB1	146	Phosphoserine
+Q04660	YMR049C	ERB1	149	Phosphoserine
+Q04660	YMR049C	ERB1	418	Phosphoserine
+Q04660	YMR049C	ERB1	127	Glycyl
+P05453	YDR172W	SUP35	2	N-acetylserine
+P05453	YDR172W	SUP35	571	Phosphoserine
+P19097	YPL231W	FAS2	50	Phosphoserine
+P19097	YPL231W	FAS2	180	O-(pantetheine
+P19097	YPL231W	FAS2	523	Phosphoserine
+P19097	YPL231W	FAS2	958	Phosphoserine
+P19097	YPL231W	FAS2	1440	Phosphoserine
+P19097	YPL231W	FAS2	37	Glycyl
+P53917	YNL127W	FAR11	18	Phosphoserine
+P53917	YNL127W	FAR11	81	Phosphoserine
+P53917	YNL127W	FAR11	524	Phosphoserine
+P53917	YNL127W	FAR11	527	Phosphoserine
+P53917	YNL127W	FAR11	528	Phosphoserine
+P21268	YJL157C	FAR1	87	Phosphoserine%3B
+P21268	YJL157C	FAR1	110	Phosphoserine
+P21268	YJL157C	FAR1	114	Phosphoserine
+P21268	YJL157C	FAR1	306	Phosphothreonine
+P15646	YDL014W	NOP1	16	Asymmetric
+P15646	YDL014W	NOP1	16	Omega-N-methylarginine%3B
+P15646	YDL014W	NOP1	22	Omega-N-methylarginine%3B
+P15646	YDL014W	NOP1	30	Asymmetric
+P15646	YDL014W	NOP1	34	Asymmetric
+P15646	YDL014W	NOP1	34	Omega-N-methylarginine%3B
+P15646	YDL014W	NOP1	40	Omega-N-methylarginine%3B
+P15646	YDL014W	NOP1	48	Asymmetric
+P15646	YDL014W	NOP1	52	Asymmetric
+P15646	YDL014W	NOP1	52	Omega-N-methylarginine%3B
+P15646	YDL014W	NOP1	58	Omega-N-methylarginine%3B
+P15646	YDL014W	NOP1	70	Asymmetric
+P15646	YDL014W	NOP1	70	Omega-N-methylarginine%3B
+P15646	YDL014W	NOP1	73	Asymmetric
+P15646	YDL014W	NOP1	73	Omega-N-methylarginine%3B
+P15646	YDL014W	NOP1	81	Asymmetric
+P15646	YDL014W	NOP1	81	Omega-N-methylarginine%3B
+P15646	YDL014W	NOP1	150	Glycyl
+P40988	YMR319C	FET4	48	Phosphoserine
+P40988	YMR319C	FET4	50	Phosphoserine
+P40988	YMR319C	FET4	39	Glycyl
+P53918	YNL125C	ESBP6	57	Phosphoserine
+P53918	YNL125C	ESBP6	112	Phosphoserine
+P53918	YNL125C	ESBP6	172	Phosphoserine
+P53918	YNL125C	ESBP6	637	Phosphoserine
+P53918	YNL125C	ESBP6	230	N-linked
+P53918	YNL125C	ESBP6	471	N-linked
+P53918	YNL125C	ESBP6	492	N-linked
+P38224	YBR040W	FIG1	288	Phosphoserine
+P38224	YBR040W	FIG1	293	Phosphothreonine
+P38224	YBR040W	FIG1	296	Phosphoserine
+P40020	YER032W	FIR1	81	Phosphoserine
+P40020	YER032W	FIR1	172	Phosphoserine
+P40020	YER032W	FIR1	225	Phosphoserine
+Q08906	YOR382W	FIT2	130	GPI-anchor
+Q08906	YOR382W	FIT2	92	N-linked
+P12385	YBR143C	SUP45	182	N5-methylglutamine
+P12385	YBR143C	SUP45	421	Phosphoserine
+P12385	YBR143C	SUP45	331	Glycyl
+Q03103	YML130C	ERO1	21	N-linked
+Q03103	YML130C	ERO1	35	N-linked
+Q03103	YML130C	ERO1	53	N-linked
+Q03103	YML130C	ERO1	130	N-linked
+Q03103	YML130C	ERO1	342	N-linked
+Q03103	YML130C	ERO1	425	N-linked
+Q03103	YML130C	ERO1	458	N-linked
+Q03103	YML130C	ERO1	468	N-linked
+Q03103	YML130C	ERO1	491	N-linked
+P17261	YCR075C	ERS1	177	N-linked
+Q03661	YMR219W	ESC1	500	Phosphothreonine
+Q03661	YMR219W	ESC1	532	Phosphoserine
+Q03661	YMR219W	ESC1	579	Phosphoserine
+Q03661	YMR219W	ESC1	583	Phosphoserine
+Q03661	YMR219W	ESC1	608	Phosphoserine
+Q03661	YMR219W	ESC1	662	Phosphoserine
+Q03661	YMR219W	ESC1	865	Phosphoserine
+Q03661	YMR219W	ESC1	866	Phosphoserine
+Q03661	YMR219W	ESC1	888	Phosphoserine
+Q03661	YMR219W	ESC1	911	Phosphoserine
+Q03661	YMR219W	ESC1	937	Phosphoserine
+Q03661	YMR219W	ESC1	1092	Phosphoserine
+Q03661	YMR219W	ESC1	1096	Phosphoserine
+Q03661	YMR219W	ESC1	1098	Phosphoserine
+Q03661	YMR219W	ESC1	1166	Phosphoserine
+Q03661	YMR219W	ESC1	1176	Phosphoserine
+Q03661	YMR219W	ESC1	1178	Phosphoserine
+Q03661	YMR219W	ESC1	1214	Phosphoserine
+Q03661	YMR219W	ESC1	1254	Phosphoserine
+Q03661	YMR219W	ESC1	1290	Phosphoserine
+Q03661	YMR219W	ESC1	1326	Phosphoserine
+Q03661	YMR219W	ESC1	1332	Phosphoserine
+Q03661	YMR219W	ESC1	1403	Phosphoserine
+Q03661	YMR219W	ESC1	1409	Phosphoserine
+Q03661	YMR219W	ESC1	1450	Phosphoserine
+Q03661	YMR219W	ESC1	1454	Phosphoserine
+Q03661	YMR219W	ESC1	1539	Phosphoserine
+Q03661	YMR219W	ESC1	1590	Phosphoserine
+Q03661	YMR219W	ESC1	1591	Phosphoserine
+P53743	YNR054C	ESF2	7	Phosphoserine
+P53743	YNR054C	ESF2	13	Phosphoserine
+P53743	YNR054C	ESF2	14	Phosphoserine
+P42940	YGR207C	CIR1	2	N-acetylserine
+Q08421	YOR051C	ETT1	30	Phosphoserine
+P39875	YOR033C	EXO1	372	Phosphoserine
+P38261	YBR102C	EXO84	58	Phosphothreonine
+P38261	YBR102C	EXO84	139	Phosphoserine
+P38261	YBR102C	EXO84	482	Phosphoserine
+P38261	YBR102C	EXO84	219	Glycyl
+P09201	YLR377C	FBP1	12	Phosphoserine
+P34756	YFR019W	FAB1	2	N-acetylserine
+P34756	YFR019W	FAB1	186	Phosphoserine
+P34756	YFR019W	FAB1	1627	Phosphoserine
+P34756	YFR019W	FAB1	1630	Phosphoserine
+P34756	YFR019W	FAB1	1938	Phosphoserine
+P34756	YFR019W	FAB1	1953	Phosphothreonine
+P32604	YJL155C	FBP26	435	Phosphoserine
+P32604	YJL155C	FBP26	446	Phosphoserine
+Q04952	YMR306W	FKS3	844	N-linked
+Q04952	YMR306W	FKS3	874	N-linked
+Q04952	YMR306W	FKS3	955	N-linked
+Q04952	YMR306W	FKS3	1002	N-linked
+Q04952	YMR306W	FKS3	1170	N-linked
+Q04952	YMR306W	FKS3	1360	N-linked
+Q04952	YMR306W	FKS3	1579	N-linked
+Q04952	YMR306W	FKS3	1761	N-linked
+P36170	YKR102W	FLO10	1146	GPI-anchor
+P36170	YKR102W	FLO10	122	N-linked
+P36170	YKR102W	FLO10	157	N-linked
+P36170	YKR102W	FLO10	279	N-linked
+P36170	YKR102W	FLO10	389	N-linked
+P36170	YKR102W	FLO10	452	N-linked
+P36170	YKR102W	FLO10	515	N-linked
+P36170	YKR102W	FLO10	578	N-linked
+P36170	YKR102W	FLO10	656	N-linked
+P36170	YKR102W	FLO10	686	N-linked
+P36170	YKR102W	FLO10	879	N-linked
+P36170	YKR102W	FLO10	1092	N-linked
+P36170	YKR102W	FLO10	1099	N-linked
+P08640	YIR019C	FLO11	1346	GPI-anchor
+P08640	YIR019C	FLO11	817	N-linked
+P08640	YIR019C	FLO11	874	N-linked
+P32768	YAR050W	FLO1	1514	GPI-anchor
+P32768	YAR050W	FLO1	135	N-linked
+P32768	YAR050W	FLO1	187	N-linked
+P32768	YAR050W	FLO1	262	N-linked
+P32768	YAR050W	FLO1	329	N-linked
+P32768	YAR050W	FLO1	374	N-linked
+P32768	YAR050W	FLO1	419	N-linked
+P32768	YAR050W	FLO1	464	N-linked
+P32768	YAR050W	FLO1	509	N-linked
+P32768	YAR050W	FLO1	554	N-linked
+P32768	YAR050W	FLO1	599	N-linked
+P32768	YAR050W	FLO1	644	N-linked
+P32768	YAR050W	FLO1	689	N-linked
+P32768	YAR050W	FLO1	734	N-linked
+P32768	YAR050W	FLO1	1114	N-linked
+Q05040	YMR029C	FAR8	115	Phosphoserine
+Q05040	YMR029C	FAR8	132	Phosphothreonine
+Q08907	YOR383C	FIT3	182	GPI-anchor
+P53971	YNL023C	FAP1	951	Phosphothreonine
+P53971	YNL023C	FAP1	958	Phosphoserine
+Q03254	YMR277W	FCP1	701	Phosphoserine
+Q03254	YMR277W	FCP1	718	Phosphoserine
+Q03254	YMR277W	FCP1	720	Phosphoserine
+Q03254	YMR277W	FCP1	74	Glycyl
+Q12119	YER060W-A	FCY22	46	Phosphothreonine
+P17064	YER056C	FCY2	18	Phosphoserine
+P17064	YER056C	FCY2	16	Glycyl
+P39676	YGR234W	YHB1	22	Phosphothreonine
+P07149	YKL182W	FAS1	1	N-acetylmethionine
+P07149	YKL182W	FAS1	733	Phosphothreonine
+P07149	YKL182W	FAS1	1121	Phosphoserine
+P07149	YKL182W	FAS1	1364	Glycyl
+P40039	YER060W	FCY21	43	Phosphoserine
+P40039	YER060W	FCY21	46	Phosphothreonine
+Q08991	YPL279C	FEX2	109	N-linked
+Q08991	YPL279C	FEX2	117	N-linked
+Q08991	YPL279C	FEX2	235	N-linked
+P25653	YCR089W	FIG2	1588	GPI-anchor
+P25653	YCR089W	FIG2	29	N-linked
+P25653	YCR089W	FIG2	231	N-linked
+P25653	YCR089W	FIG2	298	N-linked
+P25653	YCR089W	FIG2	347	N-linked
+P25653	YCR089W	FIG2	386	N-linked
+P25653	YCR089W	FIG2	426	N-linked
+P25653	YCR089W	FIG2	495	N-linked
+P25653	YCR089W	FIG2	535	N-linked
+P25653	YCR089W	FIG2	661	N-linked
+P25653	YCR089W	FIG2	674	N-linked
+P25653	YCR089W	FIG2	713	N-linked
+P25653	YCR089W	FIG2	889	N-linked
+P25653	YCR089W	FIG2	907	N-linked
+P25653	YCR089W	FIG2	1079	N-linked
+P25653	YCR089W	FIG2	1400	N-linked
+P42837	YNL325C	FIG4	829	Phosphoserine
+P38911	YML074C	FPR3	2	N-acetylserine
+P38911	YML074C	FPR3	80	Phosphoserine
+P38911	YML074C	FPR3	81	Phosphoserine
+P38911	YML074C	FPR3	89	Phosphothreonine
+P38911	YML074C	FPR3	184	Phosphotyrosine%3B
+P38911	YML074C	FPR3	186	Phosphoserine%3B
+P20081	YNL135C	FPR1	2	N-acetylserine
+P20081	YNL135C	FPR1	51	Phosphoserine
+P38631	YLR342W	FKS1	269	Phosphothreonine
+P38631	YLR342W	FKS1	272	Phosphothreonine
+P38631	YLR342W	FKS1	259	Glycyl
+P38631	YLR342W	FKS1	275	Glycyl
+P38631	YLR342W	FKS1	386	Glycyl
+P38631	YLR342W	FKS1	910	Glycyl
+P38631	YLR342W	FKS1	915	Glycyl
+P38631	YLR342W	FKS1	1539	Glycyl
+P38631	YLR342W	FKS1	1547	Glycyl
+Q07825	YLL029W	FRA1	69	Phosphoserine
+Q07825	YLL029W	FRA1	92	Phosphoserine
+Q07825	YLL029W	FRA1	95	Phosphoserine
+P32791	YLR214W	FRE1	69	N-linked
+P32791	YLR214W	FRE1	100	N-linked
+P32791	YLR214W	FRE1	124	N-linked
+P53746	YNR060W	FRE4	51	N-linked
+P53746	YNR060W	FRE4	80	N-linked
+P53746	YNR060W	FRE4	101	N-linked
+P53746	YNR060W	FRE4	113	N-linked
+P53746	YNR060W	FRE4	127	N-linked
+P53746	YNR060W	FRE4	135	N-linked
+P08417	YPL262W	FUM1	428	Phosphothreonine
+P28003	YAL034C	FUN19	194	Phosphothreonine
+P28003	YAL034C	FUN19	207	Phosphoserine
+P28003	YAL034C	FUN19	211	Phosphoserine
+P11412	YNL241C	ZWF1	2	N-acetylserine
+P11412	YNL241C	ZWF1	142	Phosphoserine
+P11412	YNL241C	ZWF1	145	Phosphotyrosine
+P04385	YBR020W	GAL1	381	Phosphoserine
+P04386	YPL248C	GAL4	694	Phosphotyrosine
+P04386	YPL248C	GAL4	696	Phosphoserine
+P04386	YPL248C	GAL4	699	Phosphoserine
+P04386	YPL248C	GAL4	703	Phosphoserine
+P04386	YPL248C	GAL4	712	Phosphoserine
+Q04739	YER027C	GAL83	12	Phosphoserine
+Q04739	YER027C	GAL83	21	Phosphoserine
+Q04739	YER027C	GAL83	44	Phosphoserine
+Q04739	YER027C	GAL83	135	Phosphoserine
+Q04739	YER027C	GAL83	276	Phosphoserine
+Q04739	YER027C	GAL83	279	Phosphoserine
+P39719	YAL053W	FLC2	28	N-linked
+P39719	YAL053W	FLC2	65	N-linked
+P39719	YAL053W	FLC2	81	N-linked
+P39719	YAL053W	FLC2	156	N-linked
+P39719	YAL053W	FLC2	323	N-linked
+P36033	YKL220C	FRE2	85	N-linked
+P36033	YKL220C	FRE2	108	N-linked
+P36033	YKL220C	FRE2	120	N-linked
+P36033	YKL220C	FRE2	134	N-linked
+P36033	YKL220C	FRE2	341	N-linked
+Q12473	YLL051C	FRE6	89	N-linked
+Q12473	YLL051C	FRE6	112	N-linked
+Q12473	YLL051C	FRE6	124	N-linked
+P12709	YBR196C	PGI1	2	N-acetylserine
+P12709	YBR196C	PGI1	53	Phosphothreonine
+P12709	YBR196C	PGI1	220	Phosphothreonine
+P17649	YGR019W	UGA1	326	N6-(pyridoxal
+P38225	YBR041W	FAT1	184	N-linked
+P38225	YBR041W	FAT1	289	N-linked
+P38225	YBR041W	FAT1	534	N-linked
+P38225	YBR041W	FAT1	591	N-linked
+P38993	YMR058W	FET3	27	N-linked
+P38993	YMR058W	FET3	74	N-linked
+P38993	YMR058W	FET3	77	N-linked
+P38993	YMR058W	FET3	88	N-linked
+P38993	YMR058W	FET3	113	N-linked
+P38993	YMR058W	FET3	194	N-linked
+P38993	YMR058W	FET3	198	N-linked
+P38993	YMR058W	FET3	244	N-linked
+P38993	YMR058W	FET3	265	N-linked
+P38993	YMR058W	FET3	292	N-linked
+P38993	YMR058W	FET3	300	N-linked
+P38993	YMR058W	FET3	359	N-linked
+P38993	YMR058W	FET3	381	N-linked
+Q08913	YOR390W	FEX1	109	N-linked
+Q08913	YOR390W	FEX1	117	N-linked
+Q08913	YOR390W	FEX1	235	N-linked
+P39521	YPR104C	FHL1	44	Phosphoserine
+P39521	YPR104C	FHL1	228	Phosphoserine
+P39521	YPR104C	FHL1	230	Phosphothreonine
+P39521	YPR104C	FHL1	247	Phosphothreonine
+P39521	YPR104C	FHL1	264	Phosphoserine
+P53121	YGL139W	FLC3	616	Phosphoserine
+P53121	YGL139W	FLC3	635	Phosphoserine
+P53121	YGL139W	FLC3	779	Phosphoserine
+P53121	YGL139W	FLC3	782	Phosphoserine
+P53121	YGL139W	FLC3	149	N-linked
+P53121	YGL139W	FLC3	321	N-linked
+P53121	YGL139W	FLC3	547	N-linked
+Q08967	YPL221W	FLC1	610	Phosphoserine
+Q08967	YPL221W	FLC1	626	Phosphothreonine
+Q08967	YPL221W	FLC1	771	Phosphoserine
+Q08967	YPL221W	FLC1	774	Phosphoserine
+Q08967	YPL221W	FLC1	143	N-linked
+Q08967	YPL221W	FLC1	281	N-linked
+P53739	YNR047W	FPK1	140	Phosphoserine
+P53739	YNR047W	FPK1	144	Phosphoserine
+P53739	YNR047W	FPK1	171	Phosphoserine
+P53739	YNR047W	FPK1	175	Phosphoserine
+P53739	YNR047W	FPK1	185	Phosphoserine
+P53739	YNR047W	FPK1	300	Phosphoserine
+P53739	YNR047W	FPK1	414	Phosphoserine
+P53739	YNR047W	FPK1	462	Phosphoserine
+P23900	YLL043W	FPS1	150	Phosphoserine
+P23900	YLL043W	FPS1	168	Phosphothreonine
+P23900	YLL043W	FPS1	209	Phosphoserine
+P23900	YLL043W	FPS1	212	Phosphoserine
+P38310	YBR207W	FTH1	449	Phosphoserine
+P38310	YBR207W	FTH1	453	Phosphoserine
+P00358	YJR009C	TDH2	302	Phosphoserine
+P00358	YJR009C	TDH2	46	Glycyl
+P00358	YJR009C	TDH2	63	Glycyl
+P00359	YGR192C	TDH3	302	Phosphoserine
+P00359	YGR192C	TDH3	46	Glycyl
+P00359	YGR192C	TDH3	63	Glycyl
+P38260	YBR101C	FES1	12	Phosphoserine
+P43561	YFL041W	FET5	24	N-linked
+P43561	YFL041W	FET5	86	N-linked
+P43561	YFL041W	FET5	115	N-linked
+P43561	YFL041W	FET5	196	N-linked
+P43561	YFL041W	FET5	200	N-linked
+P43561	YFL041W	FET5	246	N-linked
+P43561	YFL041W	FET5	295	N-linked
+P43561	YFL041W	FET5	364	N-linked
+P43561	YFL041W	FET5	455	N-linked
+P41813	YNL068C	FKH2	708	Phosphoserine
+P41813	YNL068C	FKH2	832	Phosphoserine
+P41813	YNL068C	FKH2	833	Phosphoserine
+P40989	YGR032W	GSC2	288	Phosphothreonine
+P40989	YGR032W	GSC2	291	Phosphothreonine
+P40989	YGR032W	GSC2	278	Glycyl
+P40989	YGR032W	GSC2	405	Glycyl
+P40989	YGR032W	GSC2	929	Glycyl
+P40989	YGR032W	GSC2	934	Glycyl
+P40989	YGR032W	GSC2	1558	Glycyl
+P40989	YGR032W	GSC2	1566	Glycyl
+Q08905	YOR381W	FRE3	85	N-linked
+Q08905	YOR381W	FRE3	108	N-linked
+Q08905	YOR381W	FRE3	120	N-linked
+Q08905	YOR381W	FRE3	134	N-linked
+Q08908	YOR384W	FRE5	117	N-linked
+Q12209	YLR047C	FRE8	371	N-linked
+Q12209	YLR047C	FRE8	383	N-linked
+Q12209	YLR047C	FRE8	384	N-linked
+Q03002	YPL141C	FRK1	441	Phosphoserine
+Q03898	YDR130C	FIN1	54	Phosphoserine
+Q03898	YDR130C	FIN1	68	Phosphothreonine
+Q03898	YDR130C	FIN1	74	Phosphoserine
+Q03898	YDR130C	FIN1	88	Phosphoserine
+Q04433	YDR534C	FIT1	506	GPI-anchor
+Q04433	YDR534C	FIT1	412	N-linked
+Q04433	YDR534C	FIT1	464	N-linked
+Q04433	YDR534C	FIT1	503	N-linked
+P39712	YAL063C	FLO9	1299	GPI-anchor
+P39712	YAL063C	FLO9	135	N-linked
+P39712	YAL063C	FLO9	187	N-linked
+P39712	YAL063C	FLO9	203	N-linked
+P39712	YAL063C	FLO9	257	N-linked
+P39712	YAL063C	FLO9	262	N-linked
+P39712	YAL063C	FLO9	270	N-linked
+P39712	YAL063C	FLO9	329	N-linked
+P39712	YAL063C	FLO9	419	N-linked
+P39712	YAL063C	FLO9	464	N-linked
+P39712	YAL063C	FLO9	509	N-linked
+P39712	YAL063C	FLO9	554	N-linked
+P39712	YAL063C	FLO9	599	N-linked
+P39712	YAL063C	FLO9	644	N-linked
+P39712	YAL063C	FLO9	689	N-linked
+P39712	YAL063C	FLO9	734	N-linked
+P39712	YAL063C	FLO9	888	N-linked
+Q07651	YDL222C	FMP45	230	Phosphoserine
+Q07651	YDL222C	FMP45	232	Phosphoserine
+Q07651	YDL222C	FMP45	235	Phosphothreonine
+Q07651	YDL222C	FMP45	73	N-linked
+P31380	YAL019W	FUN30	232	Phosphoserine
+P31380	YAL019W	FUN30	369	Phosphoserine
+P31380	YAL019W	FUN30	451	Phosphoserine
+Q12035	YLR051C	FCF2	1	N-acetylmethionine
+Q06205	YLR449W	FPR4	80	Phosphoserine
+Q06205	YLR449W	FPR4	82	Phosphoserine
+Q04991	YMR221C	FMP42	238	Phosphoserine
+Q04991	YMR221C	FMP42	249	Phosphoserine
+Q04991	YMR221C	FMP42	269	Phosphoserine
+P53848	YNL256W	FOL1	2	N-acetylserine
+P53848	YNL256W	FOL1	286	Phosphoserine
+P38894	YHR211W	FLO5	1052	GPI-anchor
+P38894	YHR211W	FLO5	135	N-linked
+P38894	YHR211W	FLO5	187	N-linked
+P38894	YHR211W	FLO5	203	N-linked
+P38894	YHR211W	FLO5	262	N-linked
+P38894	YHR211W	FLO5	663	N-linked
+P38894	YHR211W	FLO5	749	N-linked
+Q12029	YOR271C	FSF1	2	N-acetylalanine
+P16892	YBL016W	FUS3	180	Phosphothreonine
+P16892	YBL016W	FUS3	182	Phosphotyrosine
+P16892	YBL016W	FUS3	345	Glycyl
+P53913	YNL133C	FYV6	2	N-acetylserine
+P45976	YJR093C	FIP1	50	Phosphoserine
+P04397	YBR019C	GAL10	562	Phosphoserine
+P13181	YLR081W	GAL2	32	Phosphoserine
+P13181	YLR081W	GAL2	35	Phosphoserine
+P13181	YLR081W	GAL2	39	Phosphoserine
+P13181	YLR081W	GAL2	48	Phosphoserine
+P13181	YLR081W	GAL2	50	Phosphoserine
+P13181	YLR081W	GAL2	53	Phosphoserine
+P13181	YLR081W	GAL2	55	Phosphoserine
+P13045	YDR009W	GAL3	1	N-acetylmethionine
+P43574	YFL021W	GAT1	167	Phosphoserine
+P43574	YFL021W	GAT1	262	Phosphoserine
+P43574	YFL021W	GAT1	270	Phosphoserine
+P43574	YFL021W	GAT1	369	Phosphothreonine
+P43574	YFL021W	GAT1	399	Phosphoserine
+P43574	YFL021W	GAT1	418	Phosphoserine
+P39012	YLR088W	GAA1	87	N-linked
+P28006	YOR178C	GAC1	415	Phosphoserine
+P28006	YOR178C	GAC1	424	Phosphoserine
+P40056	YER083C	GET2	2	N-acetylserine
+P40056	YER083C	GET2	45	Phosphoserine
+P40056	YER083C	GET2	173	N-linked
+P40056	YER083C	GET2	196	N-linked
+P14742	YKL104C	GFA1	253	Phosphoserine
+P14742	YKL104C	GFA1	334	Phosphothreonine
+P14742	YKL104C	GFA1	336	Phosphoserine
+P40036	YER054C	GIP2	51	Phosphoserine
+P40036	YER054C	GIP2	52	Phosphothreonine
+P40036	YER054C	GIP2	155	Phosphoserine
+P40036	YER054C	GIP2	221	Phosphoserine
+P40036	YER054C	GIP2	238	Phosphoserine
+P39732	YAL031C	GIP4	497	Phosphoserine
+P39732	YAL031C	GIP4	501	Phosphoserine
+P39732	YAL031C	GIP4	609	Phosphoserine
+P25346	YCR098C	GIT1	80	N-linked
+P36143	YKR058W	GLG1	230	O-linked
+P36143	YKR058W	GLG1	598	O-linked
+Q05670	YMR232W	FUS2	20	Phosphothreonine
+Q05670	YMR232W	FUS2	67	Phosphoserine
+Q05670	YMR232W	FUS2	72	Phosphoserine
+Q05670	YMR232W	FUS2	84	Phosphoserine
+Q05670	YMR232W	FUS2	88	Phosphothreonine
+Q05670	YMR232W	FUS2	100	Phosphoserine
+Q05670	YMR232W	FUS2	106	Phosphoserine
+Q08559	YOR183W	FYV12	91	N-linked
+P46949	YGR196C	FYV8	92	Phosphoserine
+P46949	YGR196C	FYV8	100	Phosphoserine
+P46949	YGR196C	FYV8	134	Phosphoserine
+P46949	YGR196C	FYV8	163	Phosphoserine
+P46949	YGR196C	FYV8	180	Phosphoserine
+P46949	YGR196C	FYV8	182	Phosphoserine
+P46949	YGR196C	FYV8	237	Phosphoserine
+P46949	YGR196C	FYV8	238	Phosphoserine
+P46949	YGR196C	FYV8	532	Phosphoserine
+P08431	YBR018C	GAL7	27	Phosphoserine
+P04387	YML051W	GAL80	1	N-acetylmethionine
+P25555	YCL011C	GBP2	130	Phosphothreonine
+P51601	YGR267C	FOL2	15	Phosphothreonine
+P51601	YGR267C	FOL2	23	Phosphoserine
+P43535	YFR009W	GCN20	2	N-acetylalanine
+Q04839	YMR255W	GFD1	87	Phosphoserine
+Q04839	YMR255W	GFD1	106	Phosphoserine
+Q04839	YMR255W	GFD1	111	Phosphoserine
+P22146	YMR307W	GAS1	528	GPI-anchor
+P22146	YMR307W	GAS1	40	N-linked
+P22146	YMR307W	GAS1	57	N-linked
+P22146	YMR307W	GAS1	95	N-linked
+P22146	YMR307W	GAS1	149	N-linked
+P22146	YMR307W	GAS1	165	N-linked
+P22146	YMR307W	GAS1	253	N-linked
+P22146	YMR307W	GAS1	283	N-linked
+P22146	YMR307W	GAS1	321	N-linked
+P22146	YMR307W	GAS1	409	N-linked
+P22146	YMR307W	GAS1	495	N-linked
+Q06135	YLR343W	GAS2	531	GPI-anchor
+Q06135	YLR343W	GAS2	498	N-linked
+P39993	YEL022W	GEA2	46	Phosphoserine
+P39993	YEL022W	GEA2	284	Phosphoserine
+Q06648	YDR309C	GIC2	254	Phosphoserine
+Q06648	YDR309C	GIC2	258	Phosphoserine
+Q06648	YDR309C	GIC2	337	Phosphoserine
+Q06648	YDR309C	GIC2	345	Phosphoserine
+Q06648	YDR309C	GIC2	367	Phosphoserine
+Q03833	YDR096W	GIS1	70	Phosphoserine
+Q03833	YDR096W	GIS1	343	Phosphoserine
+Q03833	YDR096W	GIS1	690	Phosphoserine
+Q03833	YDR096W	GIS1	694	Phosphoserine
+Q03833	YDR096W	GIS1	696	Phosphoserine
+Q03833	YDR096W	GIS1	734	Phosphoserine
+Q03833	YDR096W	GIS1	747	Phosphoserine
+P38196	YBL042C	FUI1	54	Phosphothreonine
+P38196	YBL042C	FUI1	56	Phosphoserine
+P38196	YBL042C	FUI1	635	Glycyl
+P11710	YCL027W	FUS1	178	Phosphothreonine
+P11710	YCL027W	FUS1	190	Phosphoserine
+P11710	YCL027W	FUS1	256	Phosphoserine
+P11710	YCL027W	FUS1	281	Phosphothreonine
+P11710	YCL027W	FUS1	424	Phosphothreonine
+P38297	YBR179C	FZO1	398	Glycyl
+P38297	YBR179C	FZO1	464	Glycyl
+P18852	YJR086W	STE18	107	Cysteine
+P18852	YJR086W	STE18	106	S-palmitoyl
+P18852	YJR086W	STE18	107	S-farnesyl
+P47102	YJR031C	GEA1	49	Phosphoserine
+Q04233	YML006C	GIS4	165	Phosphoserine
+Q04233	YML006C	GIS4	304	Phosphoserine
+Q04233	YML006C	GIS4	616	Phosphoserine
+Q04233	YML006C	GIS4	622	Phosphoserine
+Q04233	YML006C	GIS4	707	Phosphoserine
+Q04233	YML006C	GIS4	720	Phosphoserine
+P32614	YEL047C	FRD1	66	Phosphoserine
+P31381	YAL022C	FUN26	45	Phosphoserine
+P31381	YAL022C	FUN26	58	Phosphoserine
+P19145	YKR039W	GAP1	76	Glycyl
+P28007	YHR089C	GAR1	4	Asymmetric
+P28007	YHR089C	GAR1	8	Asymmetric
+P28007	YHR089C	GAR1	11	Asymmetric
+P28007	YHR089C	GAR1	15	Asymmetric
+P28007	YHR089C	GAR1	19	Asymmetric
+P28007	YHR089C	GAR1	147	Asymmetric
+P28007	YHR089C	GAR1	154	Asymmetric
+P28007	YHR089C	GAR1	158	Asymmetric
+P28007	YHR089C	GAR1	162	Asymmetric
+P28007	YHR089C	GAR1	165	Asymmetric
+P28007	YHR089C	GAR1	171	Asymmetric
+P28007	YHR089C	GAR1	174	Asymmetric
+P28007	YHR089C	GAR1	180	Asymmetric
+P28007	YHR089C	GAR1	184	Asymmetric
+P28007	YHR089C	GAR1	189	Asymmetric
+P28007	YHR089C	GAR1	193	Asymmetric
+P28007	YHR089C	GAR1	197	Asymmetric
+P28007	YHR089C	GAR1	201	Asymmetric
+P28007	YHR089C	GAR1	77	Glycyl
+Q03655	YMR215W	GAS3	498	GPI-anchor
+Q03655	YMR215W	GAS3	201	N-linked
+Q03655	YMR215W	GAS3	269	N-linked
+Q03655	YMR215W	GAS3	350	N-linked
+Q03655	YMR215W	GAS3	385	N-linked
+Q03655	YMR215W	GAS3	404	N-linked
+Q03655	YMR215W	GAS3	422	N-linked
+P39726	YAL044C	GCV3	102	N6-lipoyllysine
+Q08271	YOL132W	GAS4	447	GPI-anchor
+Q08271	YOL132W	GAS4	151	N-linked
+Q08271	YOL132W	GAS4	398	N-linked
+Q08193	YOL030W	GAS5	462	GPI-anchor
+Q08193	YOL030W	GAS5	24	N-linked
+Q08193	YOL030W	GAS5	60	N-linked
+Q08193	YOL030W	GAS5	166	N-linked
+Q08193	YOL030W	GAS5	299	N-linked
+Q08193	YOL030W	GAS5	344	N-linked
+Q08193	YOL030W	GAS5	359	N-linked
+P38011	YMR116C	ASC1	2	N-acetylalanine
+P38011	YMR116C	ASC1	96	Phosphothreonine
+P38011	YMR116C	ASC1	168	Phosphothreonine
+P38011	YMR116C	ASC1	46	Glycyl
+P38011	YMR116C	ASC1	53	Glycyl
+P38011	YMR116C	ASC1	107	Glycyl
+P38011	YMR116C	ASC1	137	Glycyl
+P38011	YMR116C	ASC1	161	Glycyl
+P07261	YPL075W	GCR1	447	Phosphothreonine
+P07261	YPL075W	GCR1	449	Phosphoserine
+P07261	YPL075W	GCR1	482	Phosphoserine
+P07261	YPL075W	GCR1	489	Phosphoserine
+P07261	YPL075W	GCR1	538	Phosphoserine
+P14065	YOR120W	GCY1	306	Phosphoserine
+P32775	YEL011W	GLC3	190	Phosphoserine
+P17695	YDR513W	GRX2	37	Phosphoserine
+P17695	YDR513W	GRX2	61	S-glutathionyl
+P17695	YDR513W	GRX2	91	Phosphoserine
+P37303	YEL046C	GLY1	213	N6-(pyridoxal
+P37303	YEL046C	GLY1	367	Phosphoserine
+P37303	YEL046C	GLY1	369	Phosphoserine
+P37303	YEL046C	GLY1	370	Phosphothreonine
+P37303	YEL046C	GLY1	228	Glycyl
+P38875	YHR188C	GPI16	184	N-linked
+P40106	YER062C	GPP2	90	Phosphoserine
+P40106	YER062C	GPP2	64	Glycyl
+P40106	YER062C	GPP2	144	Glycyl
+P35197	YDL226C	GCS1	151	Phosphothreonine
+P35197	YDL226C	GCS1	157	Phosphoserine
+P35197	YDL226C	GCS1	161	Phosphothreonine
+P35197	YDL226C	GCS1	168	Phosphoserine
+P35197	YDL226C	GCS1	170	Phosphothreonine
+P35197	YDL226C	GCS1	260	Phosphoserine
+Q03016	YPL137C	GIP3	68	Phosphoserine
+Q03016	YPL137C	GIP3	99	Phosphothreonine
+Q03016	YPL137C	GIP3	103	Phosphoserine
+Q03016	YPL137C	GIP3	143	Phosphoserine
+Q03016	YPL137C	GIP3	260	Phosphoserine
+Q03016	YPL137C	GIP3	264	Phosphothreonine
+Q03016	YPL137C	GIP3	269	Phosphoserine
+P03069	YEL009C	GCN4	17	Phosphoserine
+P03069	YEL009C	GCN4	165	Phosphothreonine%3B
+P03069	YEL009C	GCN4	218	Phosphoserine
+Q01722	YNL199C	GCR2	151	Phosphoserine
+Q01722	YNL199C	GCR2	406	Phosphoserine
+Q01722	YNL199C	GCR2	409	Phosphoserine
+P32621	YEL042W	GDA1	41	N-linked
+P32621	YEL042W	GDA1	280	N-linked
+P32621	YEL042W	GDA1	335	N-linked
+Q02979	YPL110C	GDE1	653	Phosphoserine
+Q02979	YPL110C	GDE1	983	Phosphoserine
+P37291	YLR058C	SHM2	20	Phosphothreonine
+P37291	YLR058C	SHM2	26	Phosphoserine
+P37291	YLR058C	SHM2	248	N6-(pyridoxal
+P37291	YLR058C	SHM2	429	Phosphoserine
+P37291	YLR058C	SHM2	456	Glycyl
+P40107	YGL225W	VRG4	119	N-linked
+P40107	YGL225W	VRG4	242	N-linked
+P40107	YGL225W	VRG4	246	N-linked
+P40107	YGL225W	VRG4	249	N-linked
+P0CE11	YER039C	HVG1	149	N-linked
+P0CE11	YER039C	HVG1	153	N-linked
+P43577	YFL017C	GNA1	2	N-acetylserine
+P10823	YER020W	GPA2	2	N-myristoyl
+P10823	YER020W	GPA2	4	S-palmitoyl
+Q08886	YOR371C	GPB1	91	Phosphoserine
+Q08886	YOR371C	GPB1	161	Phosphothreonine
+Q05584	YDR272W	GLO2	257	Phosphoserine
+P38682	YER122C	GLO3	170	Phosphoserine
+P38682	YER122C	GLO3	306	Phosphoserine
+P38682	YER122C	GLO3	389	Phosphoserine
+P38682	YER122C	GLO3	398	Phosphoserine
+P48813	YDR508C	GNP1	29	Phosphoserine
+P48813	YDR508C	GNP1	113	Phosphoserine
+P48813	YDR508C	GNP1	124	Phosphoserine
+P48813	YDR508C	GNP1	127	Phosphothreonine
+P48813	YDR508C	GNP1	34	Glycyl
+P48813	YDR508C	GNP1	39	Glycyl
+P48813	YDR508C	GNP1	41	Glycyl
+P48813	YDR508C	GNP1	61	Glycyl
+P48813	YDR508C	GNP1	132	Glycyl
+P53839	YNL274C	GOR1	31	Phosphothreonine
+Q00055	YDL022W	GPD1	2	N-acetylserine
+Q00055	YDL022W	GPD1	24	Phosphoserine
+Q00055	YDL022W	GPD1	27	Phosphoserine
+Q06636	YDR302W	GPI11	16	Phosphoserine
+P49095	YMR189W	GCV2	773	N6-(pyridoxal
+Q06336	YDR358W	GGA1	348	Phosphothreonine
+Q06336	YDR358W	GGA1	353	Phosphoserine
+Q06336	YDR358W	GGA1	357	Phosphoserine
+Q06336	YDR358W	GGA1	378	Phosphoserine
+Q06336	YDR358W	GGA1	394	Phosphoserine
+P38817	YHR108W	GGA2	180	Glycyl
+P38817	YHR108W	GGA2	287	Glycyl
+P38138	YBR229C	ROT2	114	N-linked
+P38138	YBR229C	ROT2	126	N-linked
+P38138	YBR229C	ROT2	142	N-linked
+P38138	YBR229C	ROT2	173	N-linked
+P38138	YBR229C	ROT2	345	N-linked
+P38138	YBR229C	ROT2	783	N-linked
+P38138	YBR229C	ROT2	791	N-linked
+P38138	YBR229C	ROT2	867	N-linked
+P38138	YBR229C	ROT2	880	N-linked
+P38138	YBR229C	ROT2	907	N-linked
+P38138	YBR229C	ROT2	941	N-linked
+Q04924	YDR221W	GTB1	145	N-linked
+Q04924	YDR221W	GTB1	240	N-linked
+Q04924	YDR221W	GTB1	358	N-linked
+Q04924	YDR221W	GTB1	520	N-linked
+Q04924	YDR221W	GTB1	525	N-linked
+Q04924	YDR221W	GTB1	688	N-linked
+Q04924	YDR221W	GTB1	699	N-linked
+Q12434	YDL135C	RDI1	2	N-acetylalanine
+Q12434	YDL135C	RDI1	27	Phosphothreonine
+Q12434	YDL135C	RDI1	40	Phosphoserine
+P41818	YMR311C	GLC8	12	Phosphoserine
+P41818	YMR311C	GLC8	118	Phosphothreonine%3B
+P41818	YMR311C	GLC8	158	Phosphoserine
+P41818	YMR311C	GLC8	184	Phosphoserine
+P47011	YJL137C	GLG2	230	O-linked
+P47011	YJL137C	GLG2	232	O-linked
+P47011	YJL137C	GLG2	367	O-linked
+P38263	YBR105C	VID24	27	Phosphoserine
+P38263	YBR105C	VID24	20	Glycyl
+Q12263	YDR507C	GIN4	406	Phosphoserine
+Q12263	YDR507C	GIN4	465	Phosphoserine
+Q12263	YDR507C	GIN4	471	Phosphoserine
+Q12263	YDR507C	GIN4	617	Phosphoserine
+Q12263	YDR507C	GIN4	689	Phosphoserine
+Q12263	YDR507C	GIN4	719	Phosphoserine
+Q12263	YDR507C	GIN4	805	Phosphoserine
+Q12263	YDR507C	GIN4	807	Phosphoserine
+Q12263	YDR507C	GIN4	883	Phosphoserine
+Q12263	YDR507C	GIN4	884	Phosphothreonine
+Q12263	YDR507C	GIN4	930	Phosphoserine
+P32288	YPR035W	GLN1	2	N-acetylalanine
+P32288	YPR035W	GLN1	5	Phosphoserine
+P32288	YPR035W	GLN1	283	Glycyl
+P32288	YPR035W	GLN1	324	Glycyl
+P32288	YPR035W	GLN1	363	Glycyl
+P25373	YCL035C	GRX1	27	S-glutathionyl
+P25373	YCL035C	GRX1	11	Glycyl
+Q12680	YDL171C	GLT1	2070	Phosphothreonine
+P37292	YBR263W	SHM1	265	N6-(pyridoxal
+Q07830	YLL031C	GPI13	66	N-linked
+Q07830	YLL031C	GPI13	71	N-linked
+Q07830	YLL031C	GPI13	100	N-linked
+Q07830	YLL031C	GPI13	182	N-linked
+Q07830	YLL031C	GPI13	203	N-linked
+Q07830	YLL031C	GPI13	411	N-linked
+Q07830	YLL031C	GPI13	681	N-linked
+Q07830	YLL031C	GPI13	682	N-linked
+Q07830	YLL031C	GPI13	707	N-linked
+Q07830	YLL031C	GPI13	742	N-linked
+P41277	YIL053W	GPP1	90	Phosphoserine
+P41277	YIL053W	GPP1	64	Glycyl
+P41277	YIL053W	GPP1	64	Glycyl
+P41277	YIL053W	GPP1	144	Glycyl
+P18494	YER040W	GLN3	251	Phosphoserine
+P18494	YER040W	GLN3	267	Phosphoserine
+P18494	YER040W	GLN3	285	Phosphoserine
+P18494	YER040W	GLN3	469	Phosphoserine
+P18494	YER040W	GLN3	552	Phosphoserine
+P18494	YER040W	GLN3	562	Phosphoserine
+P36148	YKR067W	GPT2	632	Phosphoserine
+P36148	YKR067W	GPT2	637	Phosphoserine
+P36148	YKR067W	GPT2	647	Phosphoserine
+P36148	YKR067W	GPT2	651	Phosphoserine
+P36148	YKR067W	GPT2	654	Phosphoserine
+P36148	YKR067W	GPT2	657	Phosphoserine
+P36148	YKR067W	GPT2	664	Phosphoserine
+P36148	YKR067W	GPT2	668	Phosphoserine
+P36148	YKR067W	GPT2	671	Phosphoserine
+P36148	YKR067W	GPT2	673	Phosphothreonine
+P36148	YKR067W	GPT2	688	Phosphoserine
+P36148	YKR067W	GPT2	692	Phosphothreonine
+P36148	YKR067W	GPT2	693	Phosphoserine
+Q04410	YDR517W	GRH1	1	N-acetylmethionine
+Q04410	YDR517W	GRH1	155	Phosphoserine
+Q04322	YMR192W	GYL1	1	N-acetylmethionine
+Q04322	YMR192W	GYL1	17	Phosphothreonine
+Q04322	YMR192W	GYL1	37	Phosphoserine
+Q04322	YMR192W	GYL1	73	Phosphoserine
+Q04322	YMR192W	GYL1	139	Phosphoserine
+Q04322	YMR192W	GYL1	498	Glycyl
+P48365	YDL234C	GYP7	265	Phosphoserine
+P48365	YDL234C	GYP7	339	Phosphoserine
+P23337	YFR015C	GSY1	159	Phosphoserine
+P23337	YFR015C	GSY1	363	Phosphoserine
+P23337	YFR015C	GSY1	560	Phosphoserine
+P23337	YFR015C	GSY1	651	Phosphoserine
+P23337	YFR015C	GSY1	655	Phosphoserine
+P23337	YFR015C	GSY1	660	Phosphoserine%3B
+P23337	YFR015C	GSY1	662	Phosphoserine%3B
+P23337	YFR015C	GSY1	667	Phosphothreonine
+P04911	YDR225W	HTA1	2	N-acetylserine
+P04911	YDR225W	HTA1	5	N6-acetyllysine
+P04911	YDR225W	HTA1	8	N6-acetyllysine
+P04911	YDR225W	HTA1	106	N5-methylglutamine
+P04911	YDR225W	HTA1	129	Phosphoserine
+P04911	YDR225W	HTA1	127	Glycyl
+P02294	YBL002W	HTB2	7	N6-acetyllysine%3B
+P02294	YBL002W	HTB2	8	N6-acetyllysine%3B
+P02294	YBL002W	HTB2	11	Phosphoserine
+P02294	YBL002W	HTB2	12	N6-acetyllysine
+P02294	YBL002W	HTB2	17	N6-acetyllysine%3B
+P02294	YBL002W	HTB2	7	Glycyl
+P02294	YBL002W	HTB2	8	Glycyl
+P02294	YBL002W	HTB2	17	Glycyl
+P02294	YBL002W	HTB2	18	Glycyl
+P02294	YBL002W	HTB2	124	Glycyl
+P38736	YHL031C	GOS1	2	N-acetylserine
+P38736	YHL031C	GOS1	164	Phosphoserine
+P39717	YAL056W	GPB2	24	Phosphoserine
+P40531	YIL041W	GVP36	2	N-acetylserine
+P40531	YIL041W	GVP36	2	Phosphoserine
+P40531	YIL041W	GVP36	319	Phosphoserine
+P40531	YIL041W	GVP36	13	Glycyl
+P40531	YIL041W	GVP36	305	Glycyl
+P40531	YIL041W	GVP36	313	Glycyl
+Q08484	YOR070C	GYP1	69	Phosphoserine
+Q08484	YOR070C	GYP1	250	Phosphoserine
+P48566	YNL293W	MSB3	147	Phosphoserine
+P48566	YNL293W	MSB3	484	Phosphoserine
+Q12753	YPR008W	HAA1	125	Phosphoserine
+Q12753	YPR008W	HAA1	231	Phosphoserine
+Q12753	YPR008W	HAA1	241	Phosphoserine
+Q12753	YPR008W	HAA1	291	Phosphoserine
+P32835	YLR293C	GSP1	2	N-acetylserine
+P32835	YLR293C	GSP1	2	Phosphoserine
+P53551	YPL127C	HHO1	174	Phosphoserine
+Q12341	YPL001W	HAT1	354	Phosphoserine
+P41921	YPL091W	GLR1	1	N-acetylmethionine
+P32836	YOR185C	GSP2	2	N-acetylserine
+P32836	YOR185C	GSP2	2	Phosphoserine
+P39996	YEL017W	GTT3	66	Phosphoserine
+P39996	YEL017W	GTT3	72	Phosphoserine
+P39996	YEL017W	GTT3	99	Phosphoserine
+P39996	YEL017W	GTT3	116	Phosphoserine
+P38970	YJL165C	HAL5	17	Phosphoserine
+P38970	YJL165C	HAL5	19	Phosphoserine
+P38970	YJL165C	HAL5	68	Phosphoserine
+P38970	YJL165C	HAL5	72	Phosphoserine
+P38970	YJL165C	HAL5	160	Phosphoserine
+P38970	YJL165C	HAL5	273	Phosphoserine
+P38970	YJL165C	HAL5	277	Phosphoserine
+P38970	YJL165C	HAL5	324	Phosphoserine
+P38970	YJL165C	HAL5	333	Phosphoserine
+P38970	YJL165C	HAL5	336	Phosphoserine
+P38970	YJL165C	HAL5	358	Phosphoserine
+P38970	YJL165C	HAL5	391	Phosphoserine
+P38970	YJL165C	HAL5	395	Phosphoserine
+P38199	YBL032W	HEK2	358	Phosphoserine
+P38199	YBL032W	HEK2	360	Phosphoserine
+P38199	YBL032W	HEK2	362	Phosphoserine
+Q12361	YDL035C	GPR1	373	Phosphoserine
+Q12361	YDL035C	GPR1	903	Phosphoserine
+P24814	YJR090C	GRR1	199	Phosphoserine
+P24814	YJR090C	GRR1	300	Phosphoserine
+Q04697	YML048W	GSF2	89	N-linked
+Q04697	YML048W	GSF2	173	N-linked
+P32806	YJL044C	GYP6	436	Phosphoserine
+Q96VH4	YCL026C-B	HBN1	2	N-acetylserine
+Q12096	YOR320C	GNT1	136	N-linked
+Q12096	YOR320C	GNT1	177	N-linked
+Q12096	YOR320C	GNT1	187	N-linked
+Q12096	YOR320C	GNT1	425	N-linked
+Q04080	YDR434W	GPI17	100	N-linked
+Q04080	YDR434W	GPI17	170	N-linked
+Q04080	YDR434W	GPI17	228	N-linked
+Q04080	YDR434W	GPI17	247	N-linked
+Q04080	YDR434W	GPI17	299	N-linked
+P38211	YBR004C	GPI18	69	N-linked
+P38211	YBR004C	GPI18	101	N-linked
+P40367	YJL062W	LAS21	145	N-linked
+P40367	YJL062W	LAS21	185	N-linked
+P40367	YJL062W	LAS21	298	N-linked
+P40367	YJL062W	LAS21	506	N-linked
+P47122	YJR072C	NPA3	304	Phosphoserine
+P47122	YJR072C	NPA3	308	Phosphoserine
+P47122	YJR072C	NPA3	313	Phosphoserine
+P47122	YJR072C	NPA3	352	Phosphoserine
+P47122	YJR072C	NPA3	369	Glycyl
+Q12068	YOL151W	GRE2	333	Phosphoserine
+P40956	YGL181W	GTS1	153	Phosphoserine
+P40956	YGL181W	GTS1	181	Phosphotyrosine
+P40956	YGL181W	GTS1	184	Phosphoserine
+P40956	YGL181W	GTS1	187	Phosphoserine
+P40956	YGL181W	GTS1	240	Phosphoserine
+P40956	YGL181W	GTS1	249	Phosphothreonine
+P38625	YMR217W	GUA1	241	Glycyl
+P38625	YMR217W	GUA1	426	Glycyl
+Q12180	YOL089C	HAL9	221	Phosphoserine
+Q12180	YOL089C	HAL9	937	Phosphoserine
+Q05580	YDR266C	HEL2	2	N-acetylserine
+Q05580	YDR266C	HEL2	57	Phosphothreonine
+Q05580	YDR266C	HEL2	354	Phosphoserine
+P53258	YGR100W	MDR1	2	N-acetylserine
+P53258	YGR100W	MDR1	764	Phosphoserine
+P53258	YGR100W	MDR1	871	Phosphoserine
+Q12344	YPL249C	GYP5	25	Phosphoserine
+Q12344	YPL249C	GYP5	30	Phosphoserine
+Q12344	YPL249C	GYP5	89	Phosphothreonine
+Q12344	YPL249C	GYP5	389	Phosphoserine
+P27472	YLR258W	GSY2	159	Phosphoserine
+P27472	YLR258W	GSY2	363	Phosphoserine
+P27472	YLR258W	GSY2	467	Phosphoserine
+P27472	YLR258W	GSY2	651	Phosphoserine
+P27472	YLR258W	GSY2	655	Phosphoserine%3B
+P27472	YLR258W	GSY2	661	Phosphoserine%3B
+P27472	YLR258W	GSY2	663	Phosphoserine%3B
+P27472	YLR258W	GSY2	668	Phosphothreonine%3B
+P36125	YKR030W	GMH1	2	N-acetylserine
+P41911	YOL059W	GPD2	70	Phosphoserine
+P41911	YOL059W	GPD2	72	Phosphoserine
+P41911	YOL059W	GPD2	75	Phosphoserine
+P49018	YDR331W	GPI8	256	N-linked
+P49018	YDR331W	GPI8	346	N-linked
+Q12214	YPR068C	HOS1	110	Phosphoserine
+Q01448	YBR215W	HPC2	47	Phosphoserine
+Q01448	YBR215W	HPC2	49	Phosphoserine
+Q01448	YBR215W	HPC2	435	Phosphoserine
+Q05905	YLR301W	HRI1	143	Phosphoserine
+P09950	YDR232W	HEM1	337	N6-(pyridoxal
+P28789	YDL205C	HEM3	251	S-(dipyrrolylmethanemethyl)cysteine
+Q12276	YOR227W	HER1	102	Phosphoserine
+Q12276	YOR227W	HER1	128	Phosphothreonine
+Q12276	YOR227W	HER1	277	Phosphoserine
+Q12276	YOR227W	HER1	1013	Phosphoserine
+Q12276	YOR227W	HER1	1130	Phosphothreonine
+Q12276	YOR227W	HER1	1200	Phosphoserine
+Q12276	YOR227W	HER1	1204	Phosphoserine
+Q12276	YOR227W	HER1	1207	Phosphoserine
+P41809	YDR420W	HKR1	24	N-linked
+P41809	YDR420W	HKR1	1252	N-linked
+P41809	YDR420W	HKR1	1293	N-linked
+P41809	YDR420W	HKR1	1342	N-linked
+P41809	YDR420W	HKR1	1400	N-linked
+P54839	YML126C	ERG13	276	Phosphoserine
+P40480	YIL112W	HOS4	14	Phosphoserine
+P40480	YIL112W	HOS4	16	Phosphoserine
+P40480	YIL112W	HOS4	37	Phosphothreonine
+P40480	YIL112W	HOS4	67	Phosphoserine
+P40480	YIL112W	HOS4	290	Phosphoserine
+P40480	YIL112W	HOS4	507	Phosphoserine
+P40480	YIL112W	HOS4	698	Phosphoserine
+P40480	YIL112W	HOS4	700	Phosphothreonine
+P40480	YIL112W	HOS4	778	Phosphoserine
+P48570	YDL182W	LYS20	385	Phosphoserine
+P48570	YDL182W	LYS20	396	Phosphothreonine
+P48570	YDL182W	LYS20	401	Phosphoserine
+P48570	YDL182W	LYS20	410	Phosphoserine
+Q99332	YOR324C	FRT1	167	Phosphoserine
+Q99332	YOR324C	FRT1	342	Phosphoserine
+P17629	YDR138W	HPR1	234	Phosphoserine
+P47171	YJR140C	HIR3	302	Phosphothreonine
+P47171	YJR140C	HIR3	304	Phosphoserine
+P48353	YMR161W	HLJ1	109	Phosphoserine
+P12683	YML075C	HMG1	552	Phosphothreonine
+P12683	YML075C	HMG1	115	N-linked
+P12683	YML075C	HMG1	181	N-linked
+P12683	YML075C	HMG1	452	N-linked
+P12683	YML075C	HMG1	490	N-linked
+P02293	YDR224C	HTB1	7	N6-acetyllysine%3B
+P02293	YDR224C	HTB1	8	N6-acetyllysine%3B
+P02293	YDR224C	HTB1	11	Phosphoserine
+P02293	YDR224C	HTB1	12	N6-acetyllysine
+P02293	YDR224C	HTB1	17	N6-acetyllysine%3B
+P02293	YDR224C	HTB1	7	Glycyl
+P02293	YDR224C	HTB1	8	Glycyl
+P02293	YDR224C	HTB1	17	Glycyl
+P02293	YDR224C	HTB1	18	Glycyl
+P02293	YDR224C	HTB1	124	Glycyl
+P32769	YKR084C	HBS1	124	Phosphoserine
+Q07653	YDL223C	HBT1	41	Phosphoserine
+Q07653	YDL223C	HBT1	303	Phosphoserine
+Q07653	YDL223C	HBT1	363	Phosphoserine
+Q07653	YDL223C	HBT1	491	Phosphoserine
+Q07653	YDL223C	HBT1	561	Phosphoserine
+Q07653	YDL223C	HBT1	671	Phosphoserine
+Q07653	YDL223C	HBT1	855	Phosphotyrosine
+Q07653	YDL223C	HBT1	857	Phosphoserine
+Q07653	YDL223C	HBT1	1005	Phosphoserine
+Q07653	YDL223C	HBT1	1034	Phosphoserine
+P25364	YCR065W	HCM1	342	Phosphothreonine
+P25364	YCR065W	HCM1	496	Phosphoserine
+Q12373	YLL022C	HIF1	174	Phosphoserine
+Q03281	YDR458C	HEH2	123	Phosphoserine
+P05373	YGL040C	HEM2	254	Phosphoserine
+P04912	YBL003C	HTA2	2	N-acetylserine
+P04912	YBL003C	HTA2	5	N6-acetyllysine
+P04912	YBL003C	HTA2	8	N6-acetyllysine
+P04912	YBL003C	HTA2	106	N5-methylglutamine
+P04912	YBL003C	HTA2	129	Phosphoserine
+P04912	YBL003C	HTA2	127	Glycyl
+Q12692	YOL012C	HTZ1	2	N-acetylserine
+Q12692	YOL012C	HTZ1	4	N6-acetyllysine
+Q12692	YOL012C	HTZ1	9	N6-acetyllysine
+Q12692	YOL012C	HTZ1	11	N6-acetyllysine
+Q12692	YOL012C	HTZ1	15	N6-acetyllysine
+P61830	YBR010W;	YNL031C	5	N6%2CN6%2CN6-trimethyllysine%3B
+P61830	YBR010W;	YNL031C	5	N6%2CN6-dimethyllysine%3B
+P61830	YBR010W;	YNL031C	5	N6-methyllysine%3B
+P61830	YBR010W;	YNL031C	10	N6-acetyllysine%3B
+P61830	YBR010W;	YNL031C	10	N6-methyllysine%3B
+P61830	YBR010W;	YNL031C	11	Phosphoserine
+P61830	YBR010W;	YNL031C	15	N6%2CN6-dimethyllysine%3B
+P61830	YBR010W;	YNL031C	15	N6-acetyllysine%3B
+P61830	YBR010W;	YNL031C	19	N6-acetyllysine%3B
+P61830	YBR010W;	YNL031C	19	N6-methyllysine%3B
+P61830	YBR010W;	YNL031C	24	N6-acetyllysine%3B
+P61830	YBR010W;	YNL031C	24	N6-methyllysine%3B
+P61830	YBR010W;	YNL031C	28	N6%2CN6%2CN6-trimethyllysine%3B
+P61830	YBR010W;	YNL031C	28	N6%2CN6-dimethyllysine%3B
+P61830	YBR010W;	YNL031C	28	N6-acetyllysine%3B
+P61830	YBR010W;	YNL031C	28	N6-methyllysine%3B
+P61830	YBR010W;	YNL031C	37	N6%2CN6%2CN6-trimethyllysine%3B
+P61830	YBR010W;	YNL031C	37	N6%2CN6-dimethyllysine%3B
+P61830	YBR010W;	YNL031C	37	N6-acetyllysine%3B
+P61830	YBR010W;	YNL031C	37	N6-methyllysine%3B
+P61830	YBR010W;	YNL031C	57	N6-acetyllysine
+P61830	YBR010W;	YNL031C	65	N6-acetyllysine
+P61830	YBR010W;	YNL031C	80	N6%2CN6%2CN6-trimethyllysine%3B
+P61830	YBR010W;	YNL031C	80	N6%2CN6-dimethyllysine%3B
+P61830	YBR010W;	YNL031C	80	N6-methyllysine%3B
+P02309	YBR009C;	YNL030W	6	N6-acetyllysine
+P02309	YBR009C;	YNL030W	13	N6-acetyllysine
+P02309	YBR009C;	YNL030W	17	N6-acetyllysine
+P02309	YBR009C;	YNL030W	61	Phosphoserine
+P02309	YBR009C;	YNL030W	65	Phosphoserine
+P02309	YBR009C;	YNL030W	80	N6-acetyllysine
+Q01766	YPR005C	HAL1	266	Phosphoserine
+P06774	YGL237C	HAP2	2	N-acetylserine
+P06774	YGL237C	HAP2	52	Phosphoserine
+P06774	YGL237C	HAP2	265	Phosphothreonine
+Q02516	YOR358W	HAP5	7	Phosphoserine
+Q03532	YMR290C	HAS1	12	Phosphoserine
+Q04458	YMR110C	HFD1	111	Phosphoserine
+P32480	YOR038C	HIR2	713	Phosphoserine
+P00498	YER055C	HIS1	1	N-acetylmethionine
+Q05787	YLR207W	HRD3	101	N-linked
+Q05787	YLR207W	HRD3	123	N-linked
+Q05787	YLR207W	HRD3	142	N-linked
+Q05787	YLR207W	HRD3	429	N-linked
+Q05787	YLR207W	HRD3	611	N-linked
+Q99383	YOL123W	HRP1	2	Phosphoserine
+Q99383	YOL123W	HRP1	3	Phosphoserine
+Q99383	YOL123W	HRP1	206	Phosphoserine
+Q99383	YOL123W	HRP1	458	Phosphothreonine
+Q99383	YOL123W	HRP1	462	Phosphoserine
+P29295	YPL204W	HRR25	143	Phosphoserine
+P32479	YBL008W	HIR1	610	Phosphoserine
+P07172	YIL116W	HIS5	230	N6-(pyridoxal
+P40037	YER057C	HMF1	52	Glycyl
+P19807	YGL077C	HNM1	22	Phosphoserine
+P19807	YGL077C	HNM1	42	Phosphoserine
+P19807	YGL077C	HNM1	7	N-linked
+P19807	YGL077C	HNM1	20	N-linked
+P19807	YGL077C	HNM1	248	N-linked
+P19807	YGL077C	HNM1	341	N-linked
+P47124	YJR075W	HOC1	37	N-linked
+Q9URQ5	YCR020W-B	HTL1	2	N-acetylserine
+P32874	YMR207C	HFA1	804	N6-biotinyllysine
+Q02959	YPL116W	HOS3	582	Phosphoserine
+Q02959	YPL116W	HOS3	583	Phosphoserine
+Q02959	YPL116W	HOS3	613	Phosphoserine
+Q02959	YPL116W	HOS3	629	Phosphoserine
+P34244	YKL101W	HSL1	511	Phosphoserine
+P34244	YKL101W	HSL1	629	Phosphoserine
+P34244	YKL101W	HSL1	685	Phosphoserine
+P34244	YKL101W	HSL1	837	Phosphoserine
+P34244	YKL101W	HSL1	866	Phosphoserine
+P34244	YKL101W	HSL1	1220	Phosphoserine
+P34244	YKL101W	HSL1	1250	Phosphoserine
+P34244	YKL101W	HSL1	1284	Phosphoserine
+P34244	YKL101W	HSL1	1287	Phosphoserine
+P34244	YKL101W	HSL1	1325	Phosphoserine
+P48362	YGR187C	HGH1	2	N-acetylthreonine
+P06775	YGR191W	HIP1	76	Phosphothreonine
+P12684	YLR450W	HMG2	565	Phosphothreonine
+P12684	YLR450W	HMG2	115	N-linked
+P12684	YLR450W	HMG2	150	N-linked
+P12684	YLR450W	HMG2	158	N-linked
+P12684	YLR450W	HMG2	179	N-linked
+P12684	YLR450W	HMG2	428	N-linked
+P12684	YLR450W	HMG2	455	N-linked
+Q05164	YOL155C	HPF1	946	GPI-anchor
+Q05164	YOL155C	HPF1	28	N-linked
+Q05164	YOL155C	HPF1	35	N-linked
+Q05164	YOL155C	HPF1	493	N-linked
+Q05164	YOL155C	HPF1	601	N-linked
+Q05164	YOL155C	HPF1	638	N-linked
+P38753	YHL002W	HSE1	2	N-acetylserine
+P38753	YHL002W	HSE1	162	Phosphoserine
+P10961	YGL073W	HSF1	1	N-acetylmethionine
+P10961	YGL073W	HSF1	97	Phosphothreonine
+P10961	YGL073W	HSF1	450	Phosphoserine
+P10961	YGL073W	HSF1	458	Phosphoserine
+P10961	YGL073W	HSF1	471	Phosphoserine
+P10961	YGL073W	HSF1	478	Phosphoserine
+P10961	YGL073W	HSF1	528	Phosphoserine
+P22943	YFL014W	HSP12	21	Phosphoserine%3B
+P22943	YFL014W	HSP12	24	Phosphoserine
+P22943	YFL014W	HSP12	59	Phosphoserine
+P22943	YFL014W	HSP12	73	Phosphoserine
+P22943	YFL014W	HSP12	97	Phosphoserine
+P32485	YLR113W	HOG1	2	N-acetylthreonine
+P32485	YLR113W	HOG1	174	Phosphothreonine
+P32485	YLR113W	HOG1	176	Phosphotyrosine
+Q12122	YDL131W	LYS21	399	Phosphoserine
+Q12122	YDL131W	LYS21	410	Phosphothreonine
+Q03213	YMR172W	HOT1	146	Phosphoserine
+Q03213	YMR172W	HOT1	153	Phosphoserine
+P15992	YBR072W	HSP26	2	N-acetylserine
+P15992	YBR072W	HSP26	42	Phosphothreonine
+P15992	YBR072W	HSP26	90	Phosphoserine
+P15992	YBR072W	HSP26	163	Phosphothreonine
+P15992	YBR072W	HSP26	208	Phosphoserine
+P15992	YBR072W	HSP26	211	Phosphoserine
+P25619	YCR021C	HSP30	308	Phosphoserine
+P25619	YCR021C	HSP30	331	Phosphothreonine
+P40325	YGR268C	HUA1	2	N-acetylserine
+P40325	YGR268C	HUA1	3	Glycyl
+P40325	YGR268C	HUA1	18	Glycyl
+Q12345	YLR052W	IES3	157	Phosphoserine
+Q12345	YLR052W	IES3	211	Phosphoserine
+P39730	YAL035W	FUN12	405	Phosphoserine
+Q04432	YDR533C	HSP31	138	Cysteine
+Q12329	YDR171W	HSP42	182	Phosphoserine
+Q12329	YDR171W	HSP42	213	Phosphoserine
+Q12329	YDR171W	HSP42	214	Phosphoserine
+Q12329	YDR171W	HSP42	215	Phosphoserine
+Q12329	YDR171W	HSP42	223	Phosphoserine
+P53119	YGL141W	HUL5	1	N-acetylmethionine
+P32465	YHR094C	HXT1	23	Phosphoserine
+P32465	YHR094C	HXT1	38	Phosphoserine
+P32465	YHR094C	HXT1	44	Phosphoserine
+P32465	YHR094C	HXT1	228	N-linked
+P32466	YDR345C	HXT3	23	Phosphoserine
+P32466	YDR345C	HXT3	225	N-linked
+P32466	YDR345C	HXT3	416	N-linked
+P38695	YHR096C	HXT5	126	N-linked
+P38695	YHR096C	HXT5	249	N-linked
+P38695	YHR096C	HXT5	61	Glycyl
+P39004	YDR342C	HXT7	556	Phosphothreonine
+P39004	YDR342C	HXT7	91	N-linked
+P39004	YDR342C	HXT7	228	N-linked
+P39004	YDR342C	HXT7	560	Glycyl
+P46958	YJL146W	IDS2	1	N-acetylmethionine
+P46958	YJL146W	IDS2	13	Phosphothreonine
+P46958	YJL146W	IDS2	23	Phosphoserine
+P46958	YJL146W	IDS2	27	Phosphoserine
+P46958	YJL146W	IDS2	39	Phosphoserine
+P46958	YJL146W	IDS2	122	Phosphoserine
+P46958	YJL146W	IDS2	130	Phosphoserine
+P46958	YJL146W	IDS2	136	Phosphoserine
+P46958	YJL146W	IDS2	147	Phosphoserine
+P46958	YJL146W	IDS2	148	Phosphoserine
+P40060	YER092W	IES5	124	Phosphothreonine
+P20459	YJR007W	SUI2	52	Phosphoserine%3B
+P20459	YJR007W	SUI2	292	Phosphoserine
+P20459	YJR007W	SUI2	294	Phosphoserine
+P28817	YDR036C	EHD3	326	Phosphothreonine
+P0CY09	YCL067C	HMLALPHA2	1	N-acetylmethionine
+Q04178	YDR399W	HPT1	2	N-acetylserine
+P38922	YNL004W	HRB1	343	Phosphoserine
+P38922	YNL004W	HRB1	355	Phosphoserine
+Q08732	YOR267C	HRK1	37	Phosphoserine
+Q08732	YOR267C	HRK1	382	Phosphoserine
+Q08732	YOR267C	HRK1	472	Phosphoserine
+Q08732	YOR267C	HRK1	495	Phosphothreonine
+Q08732	YOR267C	HRK1	498	Phosphoserine
+P50079	YGR223C	HSV2	61	N-linked
+P50079	YGR223C	HSV2	155	N-linked
+P50079	YGR223C	HSV2	256	N-linked
+P50079	YGR223C	HSV2	280	N-linked
+P50079	YGR223C	HSV2	315	N-linked
+P50079	YGR223C	HSV2	421	N-linked
+P04806	YFR053C	HXK1	245	Phosphoserine
+P04806	YFR053C	HXK1	272	Phosphoserine
+P04807	YGL253W	HXK2	15	Phosphoserine
+P04807	YGL253W	HXK2	38	Phosphothreonine
+P04807	YGL253W	HXK2	158	Phosphoserine
+P04807	YGL253W	HXK2	245	Phosphoserine
+P04807	YGL253W	HXK2	272	Phosphoserine
+Q12520	YPL244C	HUT1	165	N-linked
+P15496	YPL117C	IDI1	7	Phosphoserine
+P09064	YPL237W	SUI3	40	Phosphoserine
+P09064	YPL237W	SUI3	69	Phosphothreonine
+P09064	YPL237W	SUI3	80	Phosphoserine
+P09064	YPL237W	SUI3	92	Phosphoserine
+P09064	YPL237W	SUI3	112	Phosphoserine
+P09064	YPL237W	SUI3	116	Phosphothreonine
+P09064	YPL237W	SUI3	118	Phosphoserine
+P10081	YKR059W;	YJL138C	2	N-acetylserine
+P10081	YKR059W;	YJL138C	73	Phosphothreonine
+P10081	YKR059W;	YJL138C	77	Phosphoserine
+P10081	YKR059W;	YJL138C	129	Phosphoserine
+P10081	YKR059W;	YJL138C	146	Phosphothreonine
+P39936	YGL049C	TIF4632	74	Phosphoserine
+P39936	YGL049C	TIF4632	196	Phosphothreonine
+P39936	YGL049C	TIF4632	301	Phosphothreonine
+P39936	YGL049C	TIF4632	503	Phosphoserine
+P39936	YGL049C	TIF4632	913	Phosphoserine
+P39979	YEL066W	HPA3	2	N-acetylserine
+P19882	YLR259C	HSP60	102	Phosphothreonine
+P19882	YLR259C	HSP60	485	Phosphoserine
+P22202	YER103W	SSA4	552	Phosphoserine
+P53686	YPL015C	HST2	2	N-acetylserine
+P53686	YPL015C	HST2	340	Phosphoserine
+P54862	YOL156W	HXT11	87	N-linked
+P54862	YOL156W	HXT11	227	N-linked
+P40886	YJL214W	HXT8	92	N-linked
+P40886	YJL214W	HXT8	102	N-linked
+P40886	YJL214W	HXT8	429	N-linked
+P53892	YNL164C	IBD2	100	Phosphoserine
+P53892	YNL164C	IBD2	106	Phosphoserine
+P53892	YNL164C	IBD2	211	Phosphothreonine
+P38284	YBR157C	ICS2	217	Phosphoserine
+P38274	YBR133C	HSL7	317	Phosphoserine
+P38274	YBR133C	HSL7	614	Phosphothreonine
+P0CS90	YJR045C	SSC1	330	Phosphothreonine
+P19211	YJR047C	ANB1	2	Phosphoserine
+P19211	YJR047C	ANB1	7	Phosphothreonine
+P19211	YJR047C	ANB1	51	Hypusine
+Q12522	YPR016C	TIF6	174	Phosphoserine%3B
+Q12522	YPR016C	TIF6	175	Phosphoserine%3B
+Q12522	YPR016C	TIF6	231	Phosphoserine
+P06168	YLR355C	ILV5	355	Phosphoserine
+Q03824	YMR163C	INP2	275	N-linked
+Q03824	YMR163C	INP2	343	N-linked
+Q03824	YMR163C	INP2	344	N-linked
+Q03824	YMR163C	INP2	379	N-linked
+Q03824	YMR163C	INP2	517	N-linked
+Q03824	YMR163C	INP2	569	N-linked
+Q03824	YMR163C	INP2	574	N-linked
+Q12271	YOR109W	INP53	497	Phosphoserine
+Q12271	YOR109W	INP53	986	Phosphoserine
+Q12271	YOR109W	INP53	1035	Phosphoserine
+Q12271	YOR109W	INP53	1105	Phosphothreonine
+P00724	YIL162W	SUC2	23	N-linked
+P00724	YIL162W	SUC2	64	N-linked
+P00724	YIL162W	SUC2	97	N-linked
+P00724	YIL162W	SUC2	111	N-linked
+P00724	YIL162W	SUC2	118	N-linked
+P00724	YIL162W	SUC2	165	N-linked
+P00724	YIL162W	SUC2	266	N-linked
+P00724	YIL162W	SUC2	275	N-linked
+P00724	YIL162W	SUC2	356	N-linked
+P00724	YIL162W	SUC2	369	N-linked
+P00724	YIL162W	SUC2	384	N-linked
+P00724	YIL162W	SUC2	398	N-linked
+P00724	YIL162W	SUC2	512	N-linked
+P32589	YPL106C	SSE1	2	N-acetylserine
+P32589	YPL106C	SSE1	242	Phosphothreonine
+P32589	YPL106C	SSE1	660	Phosphoserine
+P32589	YPL106C	SSE1	195	Glycyl
+P17709	YCL040W	GLK1	2	N-acetylserine
+P17709	YCL040W	GLK1	2	Phosphoserine
+P17709	YCL040W	GLK1	470	Phosphoserine
+P43581	YFL011W	HXT10	75	N-linked
+P40441	YIL170W	HXT12	194	N-linked
+P23585	YMR011W	HXT2	2	N-acetylserine
+P23585	YMR011W	HXT2	11	Phosphoserine
+P23585	YMR011W	HXT2	13	Phosphoserine
+P23585	YMR011W	HXT2	17	Phosphoserine
+P23585	YMR011W	HXT2	20	Phosphoserine
+P23585	YMR011W	HXT2	29	Phosphothreonine
+P23585	YMR011W	HXT2	32	Phosphoserine
+P23585	YMR011W	HXT2	266	Phosphoserine%3B
+P23585	YMR011W	HXT2	539	Phosphoserine%3B
+P23585	YMR011W	HXT2	82	N-linked
+P32467	YHR092C	HXT4	425	N-linked
+P32467	YHR092C	HXT4	45	Glycyl
+P39003	YDR343C	HXT6	91	N-linked
+P39003	YDR343C	HXT6	228	N-linked
+P39003	YDR343C	HXT6	560	Glycyl
+P40885	YJL219W	HXT9	87	N-linked
+P40885	YJL219W	HXT9	227	N-linked
+P43598	YFR017C	IGD1	64	Phosphoserine
+P43598	YFR017C	IGD1	65	Phosphothreonine
+P43598	YFR017C	IGD1	95	Phosphoserine
+P43598	YFR017C	IGD1	96	Phosphoserine
+P43598	YFR017C	IGD1	132	Phosphothreonine
+P43598	YFR017C	IGD1	164	Phosphoserine
+Q02821	YNL189W	SRP1	1	N-acetylmethionine
+P40069	YER110C	KAP123	646	Phosphoserine
+Q03694	YMR204C	INP1	273	Phosphoserine
+P47046	YJL051W	IRC8	690	Phosphoserine
+P28241	YOR136W	IDH2	105	Phosphothreonine
+P28241	YOR136W	IDH2	153	Phosphothreonine
+P28241	YOR136W	IDH2	327	Phosphothreonine
+P28241	YOR136W	IDH2	349	Phosphothreonine
+P40154	YNL215W	IES2	67	Phosphoserine
+P40154	YNL215W	IES2	129	Phosphoserine
+P47170	YJR138W	IML1	680	Phosphoserine
+P47170	YJR138W	IML1	737	Phosphoserine
+P53901	YNL152W	INN1	392	Phosphoserine
+P50942	YNL106C	INP52	152	Phosphoserine
+P50942	YNL106C	INP52	522	Phosphoserine
+P50942	YNL106C	INP52	1005	Phosphoserine
+P50942	YNL106C	INP52	1016	Phosphoserine
+P50942	YNL106C	INP52	1032	Phosphothreonine
+P50942	YNL106C	INP52	1095	Phosphoserine
+Q04213	YMR044W	IOC4	2	Phosphoserine
+Q04213	YMR044W	IOC4	9	Phosphothreonine
+Q04213	YMR044W	IOC4	65	Phosphoserine
+Q04213	YMR044W	IOC4	73	Phosphoserine
+Q04213	YMR044W	IOC4	242	Phosphoserine
+P07250	YDR173C	ARG82	1	N-acetylmethionine
+P07250	YDR173C	ARG82	97	Phosphoserine
+P07260	YOL139C	CDC33	2	Phosphoserine%3B
+P07260	YOL139C	CDC33	15	Phosphoserine%3B
+P07260	YOL139C	CDC33	22	Phosphothreonine
+P07260	YOL139C	CDC33	28	Phosphoserine
+P07260	YOL139C	CDC33	30	Phosphoserine
+P07260	YOL139C	CDC33	114	Glycyl
+P39520	YLR223C	IFH1	208	Phosphoserine
+P39520	YLR223C	IFH1	1041	Phosphoserine
+P43579	YFL013C	IES1	27	Phosphoserine
+P43579	YFL013C	IES1	487	Phosphoserine
+P43579	YFL013C	IES1	493	Phosphoserine
+P43579	YFL013C	IES1	504	Phosphoserine
+P43579	YFL013C	IES1	507	Phosphothreonine
+P32481	YER025W	GCD11	60	Phosphothreonine
+P32481	YER025W	GCD11	258	Phosphoserine
+P39935	YGR162W	TIF4631	181	Phosphothreonine
+P39935	YGR162W	TIF4631	883	Phosphoserine
+P39935	YGR162W	TIF4631	888	Phosphothreonine
+P39935	YGR162W	TIF4631	908	Phosphoserine
+P39935	YGR162W	TIF4631	948	Phosphoserine
+P23301	YEL034W	HYP2	2	N-acetylserine
+P23301	YEL034W	HYP2	2	Phosphoserine
+P23301	YEL034W	HYP2	10	Phosphothreonine
+P23301	YEL034W	HYP2	51	Hypusine
+P23301	YEL034W	HYP2	74	Phosphoserine
+P23301	YEL034W	HYP2	86	Glycyl
+Q9P305	YHR132W-A	IGO2	2	N-acetylserine
+Q9P305	YHR132W-A	IGO2	6	Phosphoserine
+Q9P305	YHR132W-A	IGO2	63	Phosphoserine
+Q9P305	YHR132W-A	IGO2	108	Phosphoserine
+Q9P305	YHR132W-A	IGO2	119	Phosphoserine
+P47042	YJL057C	IKS1	96	Phosphoserine
+P47169	YJR137C	MET5	903	Phosphoserine
+P05694	YER091C	MET6	89	Phosphoserine
+P05694	YER091C	MET6	242	Phosphoserine
+P05694	YER091C	MET6	566	Phosphothreonine
+P05694	YER091C	MET6	629	Phosphoserine
+P05694	YER091C	MET6	706	Phosphoserine
+P38920	YMR167W	MLH1	441	Phosphoserine%3B
+P40457	YIL149C	MLP2	1512	Phosphoserine
+P40457	YIL149C	MLP2	1670	Phosphoserine
+P53152	YGL087C	MMS2	71	Phosphoserine
+P38888	YHR204W	MNL1	86	N-linked
+P38888	YHR204W	MNL1	517	N-linked
+P38888	YHR204W	MNL1	672	N-linked
+P38888	YHR204W	MNL1	762	N-linked
+P41821	YNL291C	MID1	32	N-linked
+P41821	YNL291C	MID1	70	N-linked
+P41821	YNL291C	MID1	112	N-linked
+P41821	YNL291C	MID1	125	N-linked
+P41821	YNL291C	MID1	159	N-linked
+P41821	YNL291C	MID1	175	N-linked
+P41821	YNL291C	MID1	228	N-linked
+P41821	YNL291C	MID1	238	N-linked
+P41821	YNL291C	MID1	265	N-linked
+P41821	YNL291C	MID1	282	N-linked
+P41821	YNL291C	MID1	285	N-linked
+P41821	YNL291C	MID1	291	N-linked
+P41821	YNL291C	MID1	324	N-linked
+P34072	YNL076W	MKS1	25	Phosphothreonine
+P34072	YNL076W	MKS1	247	Phosphoserine
+P34072	YNL076W	MKS1	276	Phosphoserine
+P34072	YNL076W	MKS1	442	Phosphoserine
+P34072	YNL076W	MKS1	518	Phosphoserine%3B
+P32047	YNL074C	MLF3	8	Phosphoserine
+P32047	YNL074C	MLF3	11	Phosphoserine
+P32047	YNL074C	MLF3	14	Phosphoserine
+P32047	YNL074C	MLF3	56	Phosphoserine
+P32047	YNL074C	MLF3	74	Phosphoserine
+P32047	YNL074C	MLF3	79	Phosphoserine
+P32047	YNL074C	MLF3	121	Phosphothreonine
+P32047	YNL074C	MLF3	145	Phosphoserine
+P32047	YNL074C	MLF3	156	Phosphoserine
+P32047	YNL074C	MLF3	160	Phosphoserine
+P32047	YNL074C	MLF3	169	Phosphothreonine
+P32047	YNL074C	MLF3	171	Phosphoserine
+P32047	YNL074C	MLF3	173	Phosphothreonine
+P32047	YNL074C	MLF3	183	Phosphoserine
+P32047	YNL074C	MLF3	189	Phosphoserine
+P32047	YNL074C	MLF3	227	Phosphotyrosine
+P32047	YNL074C	MLF3	228	Phosphoserine
+P32047	YNL074C	MLF3	257	Phosphoserine
+P32047	YNL074C	MLF3	265	Phosphoserine
+P32047	YNL074C	MLF3	295	Phosphotyrosine
+P32047	YNL074C	MLF3	297	Phosphoserine
+P32047	YNL074C	MLF3	320	Phosphoserine
+P32047	YNL074C	MLF3	353	Phosphoserine
+P32047	YNL074C	MLF3	439	Phosphoserine
+Q12372	YLL061W	MMP1	6	Phosphoserine
+Q12372	YLL061W	MMP1	21	Phosphothreonine
+Q12372	YLL061W	MMP1	23	Phosphoserine
+Q06324	YLR190W	MMR1	12	Phosphothreonine
+Q06324	YLR190W	MMR1	16	Phosphoserine
+Q06324	YLR190W	MMR1	37	Phosphoserine
+P46982	YJL186W	MNN5	113	N-linked
+P46982	YJL186W	MNN5	136	N-linked
+P46982	YJL186W	MNN5	259	N-linked
+P46982	YJL186W	MNN5	264	N-linked
+P40549	YIL014W	MNT3	34	N-linked
+P40549	YIL014W	MNT3	168	N-linked
+P53745	YNR059W	MNT4	132	N-linked
+P53745	YNR059W	MNT4	167	N-linked
+P53745	YNR059W	MNT4	223	N-linked
+P53745	YNR059W	MNT4	349	N-linked
+P43563	YFL034C-B	MOB2	33	Phosphotyrosine
+P43563	YFL034C-B	MOB2	59	Phosphoserine
+P43563	YFL034C-B	MOB2	76	Phosphothreonine
+P23641	YJR077C	MIR1	2	N-acetylserine%3B
+P23641	YJR077C	MIR1	4	Phosphoserine
+P23641	YJR077C	MIR1	145	Phosphoserine
+P47083	YJR002W	MPP10	2	N-acetylserine
+P47083	YJR002W	MPP10	176	Phosphoserine
+P47083	YJR002W	MPP10	177	Phosphoserine
+P47083	YJR002W	MPP10	181	Phosphotyrosine
+Q06211	YPR164W	MMS1	1294	Phosphothreonine
+Q12205	YLR057W	MNL2	45	N-linked
+P38069	YBR015C	MNN2	34	N-linked
+P38069	YBR015C	MNN2	363	N-linked
+P38069	YBR015C	MNN2	473	N-linked
+P53129	YGL124C	MON1	22	Phosphoserine
+P53129	YGL124C	MON1	71	Phosphoserine
+P53379	YDR144C	MKC7	575	GPI-anchor
+P53379	YDR144C	MKC7	180	N-linked
+P53379	YDR144C	MKC7	190	N-linked
+P53379	YDR144C	MKC7	219	N-linked
+P53379	YDR144C	MKC7	229	N-linked
+P53379	YDR144C	MKC7	232	N-linked
+P53379	YDR144C	MKC7	286	N-linked
+P53379	YDR144C	MKC7	346	N-linked
+P53379	YDR144C	MKC7	471	N-linked
+P53379	YDR144C	MKC7	517	N-linked
+P40577	YIR025W	MND2	293	Phosphoserine
+P39106	YER001W	MNN1	50	N-linked
+P39106	YER001W	MNN1	225	N-linked
+P39106	YER001W	MNN1	254	N-linked
+P39106	YER001W	MNN1	383	N-linked
+P35724	YKL064W	MNR2	114	Phosphoserine
+P35724	YKL064W	MNR2	175	Phosphoserine
+P35724	YKL064W	MNR2	177	Phosphothreonine
+P35724	YKL064W	MNR2	182	Phosphoserine
+P35724	YKL064W	MNR2	383	Phosphoserine
+P35724	YKL064W	MNR2	571	Phosphothreonine
+P35724	YKL064W	MNR2	576	Phosphoserine
+P35724	YKL064W	MNR2	582	Phosphoserine
+P53059	YGL257C	MNT2	187	N-linked
+P38257	YBR098W	MMS4	2	N-acetylserine
+P38257	YBR098W	MMS4	48	Phosphoserine
+P38257	YBR098W	MMS4	49	Phosphoserine
+P38257	YBR098W	MMS4	61	Phosphoserine
+P40484	YIL106W	MOB1	34	Phosphoserine
+P40484	YIL106W	MOB1	36	Phosphoserine
+P40484	YIL106W	MOB1	80	Phosphoserine
+P40484	YIL106W	MOB1	229	Phosphoserine
+P54785	YMR070W	MOT3	1	N-acetylmethionine
+P41940	YDL055C	PSA1	153	Phosphothreonine
+P41940	YDL055C	PSA1	244	Glycyl
+P53725	YNR024W	MPP6	2	N-acetylserine
+P53725	YNR024W	MPP6	42	Phosphoserine
+P53725	YNR024W	MPP6	150	Phosphoserine
+Q08471	YOR066W	MSA1	268	Phosphoserine
+P32333	YPL082C	MOT1	93	Phosphoserine
+P32333	YPL082C	MOT1	677	Phosphoserine
+P53163	YGL068W	MNP1	34	N-linked
+P32906	YJR131W	MNS1	96	N-linked
+P32906	YJR131W	MNS1	155	N-linked
+P32906	YJR131W	MNS1	224	N-linked
+Q12404	YOR288C	MPD1	47	N-linked
+Q12404	YOR288C	MPD1	307	N-linked
+P35728	YKL059C	MPE1	221	Phosphoserine
+P39016	YGL178W	MPT5	662	Phosphoserine
+P39016	YGL178W	MPT5	834	Phosphoserine
+P39016	YGL178W	MPT5	838	Phosphoserine
+P53045	YGR060W	ERG25	96	Glycyl
+P33748	YMR037C	MSN2	288	Phosphoserine
+P33748	YMR037C	MSN2	304	Phosphoserine
+P33748	YMR037C	MSN2	451	Phosphoserine
+P33748	YMR037C	MSN2	582	Phosphoserine
+P33748	YMR037C	MSN2	633	Phosphoserine
+P40029	YER042W	MXR1	58	Phosphoserine
+P40850	YNL085W	MKT1	358	Phosphoserine
+P40850	YNL085W	MKT1	362	Phosphoserine
+P40850	YNL085W	MKT1	371	Phosphoserine
+P40850	YNL085W	MKT1	4	Glycyl
+P53604	YNR049C	MSO1	1	N-acetylmethionine
+P53604	YNR049C	MSO1	102	Phosphoserine
+P20676	YOR098C	NUP1	2	N-acetylserine
+P20676	YOR098C	NUP1	54	Phosphoserine
+P20676	YOR098C	NUP1	161	Phosphoserine
+P20676	YOR098C	NUP1	381	Phosphothreonine
+P20676	YOR098C	NUP1	383	Phosphoserine
+P20676	YOR098C	NUP1	637	Phosphoserine
+Q12454	YDR067C	OCA6	2	Phosphothreonine
+P31755	YGL038C	OCH1	203	N-linked
+P31755	YGL038C	OCH1	281	N-linked
+P31755	YGL038C	OCH1	341	N-linked
+P31755	YGL038C	OCH1	393	N-linked
+P38325	YBR230C	OM14	12	Phosphoserine
+P38325	YBR230C	OM14	15	Phosphoserine
+Q06593	YPR194C	OPT2	374	N-linked
+Q06593	YPR194C	OPT2	860	N-linked
+Q06144	YLR350W	ORM2	9	Phosphoserine
+Q06144	YLR350W	ORM2	15	Phosphoserine
+Q06144	YLR350W	ORM2	18	Phosphothreonine
+Q06144	YLR350W	ORM2	22	Phosphoserine
+Q06144	YLR350W	ORM2	29	Phosphoserine
+Q06144	YLR350W	ORM2	51	Phosphoserine
+P43558	YFL044C	OTU1	160	Glycyl
+P32336	YOR373W	NUD1	388	Phosphothreonine
+P32336	YOR373W	NUD1	392	Phosphothreonine
+P32336	YOR373W	NUD1	417	Phosphoserine
+P32336	YOR373W	NUD1	419	Phosphoserine
+P32336	YOR373W	NUD1	357	Glycyl
+P16387	YER178W	PDA1	313	Phosphoserine%3B
+Q06810	YPR075C	OPY2	285	Phosphoserine
+Q06810	YPR075C	OPY2	348	Phosphoserine
+Q06810	YPR075C	OPY2	172	N-linked
+Q06810	YPR075C	OPY2	185	N-linked
+P54784	YML065W	ORC1	237	Phosphoserine
+P07991	YLR438W	CAR2	272	N6-(pyridoxal
+P07991	YLR438W	CAR2	390	Glycyl
+P16451	YGR193C	PDX1	73	N6-lipoyllysine
+Q02630	YMR047C	NUP116	886	Phosphoserine
+P19262	YDR148C	KGD2	114	N6-lipoyllysine
+P19262	YDR148C	KGD2	340	Phosphothreonine
+P12695	YNL071W	LAT1	75	N6-lipoyllysine
+P54790	YLL004W	ORC3	2	N-acetylserine
+P05150	YJL088W	ARG3	2	N-acetylserine
+P52593	YML103C	NUP188	340	Phosphoserine
+P52593	YML103C	NUP188	406	Glycyl
+P21957	YHL020C	OPI1	10	Phosphoserine
+P54791	YPR162C	ORC4	9	Phosphoserine
+P38351	YBR279W	PAF1	147	Phosphoserine
+P38351	YBR279W	PAF1	422	Phosphothreonine
+Q12033	YOR275C	RIM20	2	N-acetylserine
+P37304	YDR251W	PAM1	659	Phosphoserine
+P37304	YDR251W	PAM1	732	Phosphoserine
+P37304	YDR251W	PAM1	767	Phosphoserine
+P36102	YKL025C	PAN3	57	Phosphothreonine
+P36102	YKL025C	PAN3	252	Phosphoserine
+P53298	YGR179C	OKP1	70	Phosphoserine
+P28273	YKL215C	OXP1	930	Phosphoserine
+P28273	YKL215C	OXP1	1077	Phosphoserine
+P40897	YJL212C	OPT1	48	Phosphothreonine
+P40897	YJL212C	OPT1	50	Phosphothreonine
+P40897	YJL212C	OPT1	51	Phosphothreonine
+P40897	YJL212C	OPT1	46	N-linked
+P40897	YJL212C	OPT1	640	N-linked
+P32833	YBR060C	ORC2	60	Phosphothreonine
+P32833	YBR060C	ORC2	187	Phosphothreonine
+P32833	YBR060C	ORC2	188	Phosphoserine
+P32567	YMR165C	PAH1	110	Phosphoserine
+P32567	YMR165C	PAH1	114	Phosphoserine
+P32567	YMR165C	PAH1	168	Phosphoserine
+P32567	YMR165C	PAH1	511	Phosphoserine
+P32567	YMR165C	PAH1	602	Phosphoserine%3B
+P32567	YMR165C	PAH1	723	Phosphothreonine%3B
+P32567	YMR165C	PAH1	744	Phosphoserine%3B
+P32567	YMR165C	PAH1	748	Phosphoserine
+P32567	YMR165C	PAH1	773	Phosphoserine
+P32567	YMR165C	PAH1	774	Phosphoserine
+P32567	YMR165C	PAH1	810	Phosphoserine
+P32567	YMR165C	PAH1	814	Phosphoserine
+P32567	YMR165C	PAH1	816	Phosphothreonine
+P32567	YMR165C	PAH1	844	Phosphoserine
+P32567	YMR165C	PAH1	847	Phosphoserine
+P38826	YHR118C	ORC6	146	Phosphothreonine
+Q05518	YDR348C	PAL1	14	Phosphoserine
+Q05518	YDR348C	PAL1	45	Phosphoserine
+Q05518	YDR348C	PAL1	47	Phosphothreonine
+Q05518	YDR348C	PAL1	49	Phosphoserine
+Q05518	YDR348C	PAL1	64	Phosphoserine
+Q05518	YDR348C	PAL1	114	Phosphoserine
+Q05518	YDR348C	PAL1	121	Phosphoserine
+Q05518	YDR348C	PAL1	153	Phosphothreonine
+Q05518	YDR348C	PAL1	304	Phosphothreonine
+Q05518	YDR348C	PAL1	307	Phosphoserine
+Q05518	YDR348C	PAL1	135	Glycyl
+Q05518	YDR348C	PAL1	138	Glycyl
+Q05518	YDR348C	PAL1	292	Glycyl
+Q05518	YDR348C	PAL1	328	Glycyl
+Q05518	YDR348C	PAL1	445	Glycyl
+P53179	YGL045W	RIM8	521	Glycyl
+P48565	YNL294C	RIM21	409	Phosphoserine
+P32521	YIR006C	PAN1	241	Phosphothreonine
+P32521	YIR006C	PAN1	570	Phosphothreonine
+P32521	YIR006C	PAN1	747	Phosphoserine
+P32521	YIR006C	PAN1	757	Phosphoserine
+P32521	YIR006C	PAN1	993	Phosphothreonine
+P32521	YIR006C	PAN1	995	Phosphothreonine
+P32521	YIR006C	PAN1	1003	Phosphoserine
+P32521	YIR006C	PAN1	1180	Phosphoserine
+P32521	YIR006C	PAN1	1250	Phosphoserine
+P32521	YIR006C	PAN1	1253	Phosphoserine
+P32521	YIR006C	PAN1	1281	Phosphoserine
+P32521	YIR006C	PAN1	1321	Phosphothreonine
+Q12451	YDL019C	OSH2	2	N-acetylserine
+Q12451	YDL019C	OSH2	7	Phosphoserine
+Q12451	YDL019C	OSH2	422	Phosphoserine
+Q12451	YDL019C	OSH2	445	Phosphoserine
+Q12451	YDL019C	OSH2	451	Phosphoserine
+Q12451	YDL019C	OSH2	455	Phosphoserine
+Q12451	YDL019C	OSH2	458	Phosphoserine
+Q12451	YDL019C	OSH2	459	Phosphoserine
+Q12451	YDL019C	OSH2	486	Phosphoserine
+Q12451	YDL019C	OSH2	488	Phosphothreonine
+Q12451	YDL019C	OSH2	512	Phosphoserine
+Q12451	YDL019C	OSH2	515	Phosphoserine
+Q12451	YDL019C	OSH2	717	Phosphoserine
+Q12451	YDL019C	OSH2	783	Phosphothreonine
+Q12451	YDL019C	OSH2	787	Phosphoserine
+Q12451	YDL019C	OSH2	825	Phosphoserine
+Q12451	YDL019C	OSH2	1151	Phosphoserine
+Q02201	YKR003W	OSH6	16	Phosphoserine
+P50946	YNL099C	OCA1	2	N-acetylthreonine
+P50946	YNL099C	OCA1	24	Phosphoserine
+P33767	YEL002C	WBP1	60	N-linked
+P33767	YEL002C	WBP1	332	N-linked
+P43611	YFR039C	OSW7	354	Phosphotyrosine
+P32263	YER023W	PRO3	246	Phosphothreonine
+P32263	YER023W	PRO3	279	Phosphoserine
+P32263	YER023W	PRO3	171	Glycyl
+P41543	YJL002C	OST1	18	N-linked
+P41543	YJL002C	OST1	99	N-linked
+P41543	YJL002C	OST1	217	N-linked
+P41543	YJL002C	OST1	336	N-linked
+P41543	YJL002C	OST1	400	N-linked
+Q08952	YPL196W	OXR1	1	N-acetylmethionine
+Q08952	YPL196W	OXR1	178	Phosphoserine
+P40091	YER149C	PEA2	230	Phosphoserine
+P40219	YMR148W	OSW5	102	Phosphoserine
+Q03558	YHR179W	OYE2	353	Phosphoserine
+Q03558	YHR179W	OYE2	379	Phosphoserine
+P25644	YCR077C	PAT1	2	N-acetylserine
+P25644	YCR077C	PAT1	456	Phosphoserine
+P25644	YCR077C	PAT1	457	Phosphoserine
+P24867	YNL289W	PCL1	39	Phosphothreonine%3B
+P24867	YNL289W	PCL1	43	Phosphoserine%3B
+P24867	YNL289W	PCL1	82	Glycyl
+P24867	YNL289W	PCL1	121	Glycyl
+Q08966	YPL219W	PCL8	32	Phosphoserine
+P15873	YBR088C	POL30	127	Glycyl
+P15873	YBR088C	POL30	164	Glycyl
+P15873	YBR088C	POL30	164	Glycyl
+P26263	YGR087C	PDC6	2	N-acetylserine
+P26263	YGR087C	PDC6	223	Phosphoserine
+P26263	YGR087C	PDC6	266	Phosphothreonine
+P26263	YGR087C	PDC6	353	Phosphothreonine
+P26263	YGR087C	PDC6	522	Phosphothreonine
+P26263	YGR087C	PDC6	212	Glycyl
+P26263	YGR087C	PDC6	233	Glycyl
+P26263	YGR087C	PDC6	269	Glycyl
+P26263	YGR087C	PDC6	505	Glycyl
+P29468	YKR002W	PAP1	452	Phosphoserine
+P29468	YKR002W	PAP1	550	Phosphoserine
+Q12515	YDL173W	PAR32	2	N-acetylalanine
+Q12515	YDL173W	PAR32	36	Phosphoserine
+Q12515	YDL173W	PAR32	39	Phosphoserine
+Q12515	YDL173W	PAR32	47	Phosphoserine
+Q12515	YDL173W	PAR32	123	Phosphoserine
+Q12515	YDL173W	PAR32	138	Phosphoserine
+Q12515	YDL173W	PAR32	141	Phosphoserine
+Q12515	YDL173W	PAR32	147	Phosphoserine
+Q12515	YDL173W	PAR32	246	Phosphoserine
+P40186	YIL050W	PCL7	69	Phosphoserine
+P17967	YCL043C	PDI1	82	N-linked
+P17967	YCL043C	PDI1	117	N-linked
+P17967	YCL043C	PDI1	155	N-linked
+P17967	YCL043C	PDI1	174	N-linked
+P17967	YCL043C	PDI1	425	N-linked
+P40530	YIL042C	PKP1	148	Phosphohistidine%3B
+P12383	YGL013C	PDR1	21	Phosphoserine
+P12383	YGL013C	PDR1	930	Phosphoserine
+P12383	YGL013C	PDR1	942	Phosphoserine
+P12383	YGL013C	PDR1	948	Phosphoserine
+P33302	YOR153W	PDR5	22	Phosphoserine
+P33302	YOR153W	PDR5	49	Phosphothreonine
+P33302	YOR153W	PDR5	51	Phosphothreonine
+P33302	YOR153W	PDR5	54	Phosphoserine
+P33302	YOR153W	PDR5	58	Phosphoserine
+P33302	YOR153W	PDR5	61	Phosphoserine
+P33302	YOR153W	PDR5	837	Phosphoserine
+P33302	YOR153W	PDR5	840	Phosphoserine
+P33302	YOR153W	PDR5	841	Phosphoserine
+P33302	YOR153W	PDR5	849	Phosphoserine
+P33302	YOR153W	PDR5	850	Phosphoserine
+P33302	YOR153W	PDR5	854	Phosphoserine
+P33302	YOR153W	PDR5	734	N-linked
+P33302	YOR153W	PDR5	1447	N-linked
+P33302	YOR153W	PDR5	825	Glycyl
+P53224	YGR038W	ORM1	29	Phosphoserine
+P53224	YGR038W	ORM1	32	Phosphoserine
+P53224	YGR038W	ORM1	56	Phosphoserine
+P35845	YAR042W	SWH1	394	Phosphoserine
+P35845	YAR042W	SWH1	490	Phosphoserine
+P35845	YAR042W	SWH1	500	Phosphoserine
+P35845	YAR042W	SWH1	678	Phosphoserine
+P35845	YAR042W	SWH1	683	Phosphoserine
+P35845	YAR042W	SWH1	691	Phosphoserine
+P35845	YAR042W	SWH1	692	Phosphothreonine
+P35845	YAR042W	SWH1	694	Phosphothreonine
+P35845	YAR042W	SWH1	708	Phosphoserine
+P35845	YAR042W	SWH1	712	Phosphoserine
+P38713	YHR073W	OSH3	190	Phosphoserine
+P38713	YHR073W	OSH3	193	Phosphoserine
+P38713	YHR073W	OSH3	210	Phosphothreonine
+P38713	YHR073W	OSH3	323	Phosphothreonine
+P38713	YHR073W	OSH3	324	Phosphoserine
+P38713	YHR073W	OSH3	325	Phosphothreonine
+P38713	YHR073W	OSH3	352	Phosphothreonine
+P38713	YHR073W	OSH3	605	Phosphoserine
+P38755	YHR001W	OSH7	276	Glycyl
+P08018	YJL128C	PBS2	68	Phosphoserine
+P08018	YJL128C	PBS2	269	Phosphoserine
+P08018	YJL128C	PBS2	514	Phosphoserine
+P08018	YJL128C	PBS2	518	Phosphothreonine
+P13259	YGR202C	PCT1	16	Phosphoserine
+P13259	YGR202C	PCT1	59	Phosphothreonine
+P13259	YGR202C	PCT1	346	Phosphoserine
+P13259	YGR202C	PCT1	401	Phosphoserine%3B
+Q99220	YDR057W	YOS9	52	N-linked
+Q99220	YDR057W	YOS9	74	N-linked
+Q99220	YDR057W	YOS9	380	N-linked
+P04147	YER165W	PAB1	2	N-acetylalanine
+P04147	YER165W	PAB1	107	Omega-N-methylarginine
+P04147	YER165W	PAB1	249	Phosphoserine
+P04147	YER165W	PAB1	332	Phosphoserine
+P04147	YER165W	PAB1	405	Phosphoserine
+P04147	YER165W	PAB1	7	Glycyl
+P04147	YER165W	PAB1	337	Glycyl
+P25580	YCL052C	PBN1	24	N-linked
+P25580	YCL052C	PBN1	85	N-linked
+P25580	YCL052C	PBN1	120	N-linked
+P25580	YCL052C	PBN1	212	N-linked
+P25580	YCL052C	PBN1	365	N-linked
+P40038	YER059W	PCL6	61	Phosphoserine
+P40038	YER059W	PCL6	281	Phosphoserine
+P40038	YER059W	PCL6	312	Phosphoserine
+P40038	YER059W	PCL6	317	Phosphothreonine
+P40550	YIL013C	PDR11	595	N-linked
+P40550	YIL013C	PDR11	1289	N-linked
+P40550	YIL013C	PDR11	1324	N-linked
+P40550	YIL013C	PDR11	1346	N-linked
+Q04182	YDR406W	PDR15	558	N-linked
+Q04182	YDR406W	PDR15	744	N-linked
+P53756	YNR070W	PDR18	48	N-linked
+P53756	YNR070W	PDR18	144	N-linked
+P53756	YNR070W	PDR18	205	N-linked
+P53756	YNR070W	PDR18	350	N-linked
+P53756	YNR070W	PDR18	697	N-linked
+P53756	YNR070W	PDR18	733	N-linked
+P53756	YNR070W	PDR18	958	N-linked
+P53756	YNR070W	PDR18	1320	N-linked
+Q04264	YMR076C	PDS5	1231	Phosphoserine
+Q04264	YMR076C	PDS5	1233	Phosphoserine
+P36139	YKR046C	PET10	2	N-acetylserine
+P53112	YGL153W	PEX14	2	N-acetylserine
+P53112	YGL153W	PEX14	313	Phosphoserine
+P48363	YGR078C	PAC10	1	N-acetylmethionine
+P38075	YBR035C	PDX3	29	Glycyl
+P47116	YJR059W	PTK2	56	Phosphothreonine
+P47116	YJR059W	PTK2	59	Phosphoserine
+P47116	YJR059W	PTK2	80	Phosphoserine
+P47116	YJR059W	PTK2	623	Phosphoserine
+P47116	YJR059W	PTK2	632	Phosphoserine
+P47116	YJR059W	PTK2	694	Phosphoserine
+P47116	YJR059W	PTK2	700	Phosphothreonine
+P47116	YJR059W	PTK2	711	Phosphoserine
+P47116	YJR059W	PTK2	737	Phosphothreonine
+P47116	YJR059W	PTK2	752	Phosphoserine
+P47116	YJR059W	PTK2	755	Phosphoserine
+P47116	YJR059W	PTK2	778	Phosphoserine
+P47116	YJR059W	PTK2	781	Phosphoserine
+P29461	YOR208W	PTP2	258	Phosphoserine
+P29461	YOR208W	PTP2	430	Phosphoserine
+P07244	YGL234W	ADE5,7	455	Phosphoserine
+P07244	YGL234W	ADE5,7	458	Phosphoserine
+P03962	YEL021W	URA3	2	N-acetylserine
+P03962	YEL021W	URA3	93	Glycyl
+P03962	YEL021W	URA3	209	Glycyl
+P03962	YEL021W	URA3	253	Glycyl
+P25339	YGL014W	PUF4	205	Phosphothreonine
+P25339	YGL014W	PUF4	212	Phosphothreonine
+P25339	YGL014W	PUF4	252	Phosphothreonine
+P25339	YGL014W	PUF4	256	Phosphoserine
+Q06991	YLR414C	PUN1	100	N-linked
+Q06991	YLR414C	PUN1	209	N-linked
+Q06991	YLR414C	PUN1	260	Glycyl
+P38972	YGR061C	ADE6	2	N-acetylthreonine
+P11154	YGL062W	PYC1	734	N6-carboxylysine
+P11154	YGL062W	PYC1	1135	N6-biotinyllysine
+P28272	YKL216W	URA1	46	Glycyl
+Q12355	YDR055W	PST1	419	GPI-anchor
+Q12355	YDR055W	PST1	57	N-linked
+Q12355	YDR055W	PST1	76	N-linked
+Q12355	YDR055W	PST1	83	N-linked
+Q12355	YDR055W	PST1	86	N-linked
+Q12355	YDR055W	PST1	196	N-linked
+Q12355	YDR055W	PST1	210	N-linked
+Q12355	YDR055W	PST1	228	N-linked
+Q12355	YDR055W	PST1	235	N-linked
+Q12355	YDR055W	PST1	242	N-linked
+Q12355	YDR055W	PST1	263	N-linked
+Q12355	YDR055W	PST1	268	N-linked
+Q12355	YDR055W	PST1	280	N-linked
+Q12355	YDR055W	PST1	292	N-linked
+Q12355	YDR055W	PST1	305	N-linked
+Q12355	YDR055W	PST1	329	N-linked
+P39927	YGR156W	PTI1	272	Phosphoserine
+P27616	YAR015W	ADE1	2	N-acetylserine
+Q05911	YLR359W	ADE13	196	Glycyl
+P32641	YER173W	RAD24	652	Phosphoserine
+P32641	YER173W	RAD24	654	Phosphoserine
+Q00578	YIL143C	SSL2	752	Phosphoserine
+Q04231	YML011C	RAD33	2	N-acetylserine
+Q04231	YML011C	RAD33	19	Glycyl
+P22216	YPL153C	RAD53	24	Phosphoserine
+P22216	YPL153C	RAD53	175	Phosphoserine
+P22216	YPL153C	RAD53	547	Phosphoserine
+P22216	YPL153C	RAD53	560	Phosphoserine
+P22216	YPL153C	RAD53	774	Phosphoserine
+P22216	YPL153C	RAD53	793	Phosphoserine
+P06779	YJR052W	RAD7	64	Phosphoserine
+P06779	YJR052W	RAD7	85	Phosphoserine
+P32864	YOR370C	MRS6	470	Phosphoserine
+P25635	YCR057C	PWP2	225	Phosphoserine
+P25635	YCR057C	PWP2	232	Phosphoserine
+P25635	YCR057C	PWP2	651	Phosphoserine
+P25635	YCR057C	PWP2	664	Phosphoserine
+P25635	YCR057C	PWP2	912	Phosphoserine
+P25635	YCR057C	PWP2	913	Phosphoserine
+P34230	YKL188C	PXA2	33	N-linked
+P34230	YKL188C	PXA2	39	N-linked
+P34230	YKL188C	PXA2	162	N-linked
+P34230	YKL188C	PXA2	230	N-linked
+P34230	YKL188C	PXA2	241	N-linked
+P34230	YKL188C	PXA2	267	N-linked
+P34230	YKL188C	PXA2	295	N-linked
+P34230	YKL188C	PXA2	560	N-linked
+P34230	YKL188C	PXA2	608	N-linked
+P34230	YKL188C	PXA2	620	N-linked
+P34230	YKL188C	PXA2	647	N-linked
+P34230	YKL188C	PXA2	836	N-linked
+P32327	YBR218C	PYC2	2	N-acetylserine
+P32327	YBR218C	PYC2	735	N6-carboxylysine
+P32327	YBR218C	PYC2	1136	N6-biotinyllysine
+P13298	YML106W	URA5	213	Phosphoserine
+P13298	YML106W	URA5	225	Phosphoserine
+P06777	YPL022W	RAD1	613	Phosphoserine
+P06777	YPL022W	RAD1	1071	Phosphoserine
+P06777	YPL022W	RAD1	1072	Phosphothreonine
+P32628	YEL037C	RAD23	94	Phosphothreonine
+P32628	YEL037C	RAD23	121	Phosphoserine
+P32628	YEL037C	RAD23	139	Phosphothreonine
+P32628	YEL037C	RAD23	49	Glycyl
+P53037	YGR170W	PSD2	1043	Pyruvic
+P31374	YAL017W	PSK1	10	Phosphoserine
+P31374	YAL017W	PSK1	192	Phosphoserine
+P31374	YAL017W	PSK1	202	Phosphoserine
+P31374	YAL017W	PSK1	255	Phosphoserine
+P31374	YAL017W	PSK1	286	Phosphoserine
+P31374	YAL017W	PSK1	327	Phosphoserine
+P31374	YAL017W	PSK1	926	Phosphoserine
+P31374	YAL017W	PSK1	1018	Phosphoserine
+P31374	YAL017W	PSK1	1023	Phosphoserine
+P31374	YAL017W	PSK1	1035	Phosphoserine
+P31374	YAL017W	PSK1	1055	Phosphoserine
+P31374	YAL017W	PSK1	1079	Phosphothreonine
+Q01329	YAL043C	PTA1	500	Phosphoserine
+Q04373	YDR496C	PUF6	31	Phosphoserine%3B
+Q04373	YDR496C	PUF6	34	Phosphoserine
+Q04373	YDR496C	PUF6	34	Phosphoserine%3B
+Q04373	YDR496C	PUF6	35	Phosphoserine
+Q04373	YDR496C	PUF6	35	Phosphoserine%3B
+Q02256	YIR026C	YVH1	196	Phosphoserine
+P21304	YLR196W	PWP1	52	Phosphoserine
+P21304	YLR196W	PWP1	131	Phosphoserine
+P50896	YDR505C	PSP1	31	Phosphoserine
+P50896	YDR505C	PSP1	34	Phosphoserine
+P50896	YDR505C	PSP1	36	Phosphoserine
+P50896	YDR505C	PSP1	237	Phosphoserine
+P50896	YDR505C	PSP1	334	Phosphothreonine
+P50896	YDR505C	PSP1	520	Phosphoserine
+P34222	YBL057C	PTH2	152	Glycyl
+Q08647	YOR243C	PUS7	2	N-acetylserine
+P39006	YNL169C	PSD1	463	Pyruvic
+P25044	YDL230W	PTP1	83	Phosphoserine%3B
+P40048	YER075C	PTP3	75	Phosphothreonine
+P40048	YER075C	PTP3	248	Phosphoserine
+P40048	YER075C	PTP3	297	Phosphoserine
+P40048	YER075C	PTP3	368	Phosphoserine
+P40454	YIL153W	RRD1	341	Phosphoserine
+P32588	YNL016W	PUB1	2	N-acetylserine
+Q12221	YPR042C	PUF2	72	Phosphoserine
+Q12221	YPR042C	PUF2	198	Phosphoserine
+Q12221	YPR042C	PUF2	872	Phosphoserine
+Q12221	YPR042C	PUF2	876	Phosphoserine
+Q07807	YLL013C	PUF3	83	Phosphothreonine
+Q07807	YLL013C	PUF3	207	Phosphoserine
+Q07807	YLL013C	PUF3	210	Phosphoserine
+P21264	YOR128C	ADE2	37	Phosphoserine
+P41909	YPL147W	PXA1	142	N-linked
+P41909	YPL147W	PXA1	281	N-linked
+P41909	YPL147W	PXA1	403	N-linked
+P36166	YKR090W	PXL1	43	Phosphoserine
+P36166	YKR090W	PXL1	63	Phosphoserine
+P53335	YGR280C	PXR1	230	Phosphoserine
+P10622	YDL130W	RPP1B	2	N-acetylserine
+P10622	YDL130W	RPP1B	96	Phosphoserine
+P36159	YKR079C	TRZ1	824	Phosphoserine
+P51862	YLR371W	ROM2	2	N-acetylserine
+P51862	YLR371W	ROM2	76	Phosphoserine
+P51862	YLR371W	ROM2	193	Phosphoserine
+P51862	YLR371W	ROM2	223	Phosphoserine
+P51862	YLR371W	ROM2	566	Phosphoserine
+P51862	YLR371W	ROM2	628	Phosphoserine
+Q01080	YNL248C	RPA49	34	Phosphoserine
+Q01080	YNL248C	RPA49	151	Phosphoserine
+P27999	YGL070C	RPB9	40	Phosphoserine
+Q02933	YPL123C	RNY1	37	N-linked
+Q02933	YPL123C	RNY1	70	N-linked
+Q02933	YPL123C	RNY1	103	N-linked
+Q02933	YPL123C	RNY1	123	N-linked
+P10964	YOR341W	RPA190	889	Phosphoserine
+P10964	YOR341W	RPA190	1636	Phosphoserine
+P07703	YPR110C	RPC40	2	N-acetylserine
+P07703	YPR110C	RPC40	17	Phosphoserine
+P16370	YIL021W	RPB3	2	N-acetylserine
+Q12250	YDL147W	RPN5	2	N-acetylserine
+Q06103	YPR108W	RPN7	8	Phosphoserine
+Q06103	YPR108W	RPN7	77	Phosphoserine
+P38061	YBL092W	RPL32	40	Phosphoserine
+P05319	YOL039W	RPP2A	16	Phosphothreonine
+P05319	YOL039W	RPP2A	40	Phosphoserine
+P05319	YOL039W	RPP2A	43	Phosphoserine
+P05319	YOL039W	RPP2A	49	Phosphoserine
+P05319	YOL039W	RPP2A	96	Phosphoserine
+P05319	YOL039W	RPP2A	2	Glycyl
+P05319	YOL039W	RPP2A	48	Glycyl
+P02400	YDR382W	RPP2B	29	Phosphoserine
+P02400	YDR382W	RPP2B	100	Phosphoserine
+P02400	YDR382W	RPP2B	49	Glycyl
+Q12495	YPR018W	RLF2	78	Phosphothreonine
+Q12495	YPR018W	RLF2	94	Phosphoserine
+Q12495	YPR018W	RLF2	509	Phosphothreonine
+Q03195	YDR091C	RLI1	349	Phosphoserine
+Q12224	YPL089C	RLM1	120	Phosphoserine
+Q12224	YPL089C	RLM1	164	Phosphoserine
+Q12224	YPL089C	RLM1	374	Phosphoserine
+Q12224	YPL089C	RLM1	377	Phosphoserine
+P36534	YPL173W	MRPL40	2	N-acetylserine
+P43620	YFR048W	RMD8	2	N-acetylserine
+P0CX26	YJR094W-A	RPL43B	40	Phosphoserine
+P0CX28	YHR141C	RPL42B	40	N6-methyllysine%3B
+P0CX28	YHR141C	RPL42B	55	N6-methyllysine%3B
+Q02326	YML073C	RPL6A	2	N-acetylserine
+Q02326	YML073C	RPL6A	12	Phosphoserine
+Q02326	YML073C	RPL6A	128	Glycyl
+P05317	YLR340W	RPP0	68	Phosphoserine
+P05317	YLR340W	RPP0	302	Phosphoserine%3B
+P05317	YLR340W	RPP0	14	Glycyl
+P05317	YLR340W	RPP0	97	Glycyl
+P05317	YLR340W	RPP0	144	Glycyl
+Q07915	YLR009W	RLP24	172	Phosphoserine
+P11745	YMR235C	RNA1	360	Phosphoserine
+P05747	YFR032C-A	RPL29	52	Glycyl
+P0CX27	YNL162W	RPL42A	40	N6-methyllysine%3B
+P0CX27	YNL162W	RPL42A	55	N6-methyllysine%3B
+P02406	YGL103W	RPL28	96	Glycyl
+P0CX85	YDL136W	RPL35B	13	Phosphoserine
+P0CX85	YDL136W	RPL35B	50	Phosphoserine
+P14126	YOR063W	RPL3	24	Phosphoserine
+P14126	YOR063W	RPL3	103	Phosphothreonine
+P14126	YOR063W	RPL3	156	Phosphoserine
+P14126	YOR063W	RPL3	243	Pros-methylhistidine
+P14126	YOR063W	RPL3	297	Phosphoserine
+P14126	YOR063W	RPL3	39	Glycyl
+P14126	YOR063W	RPL3	136	Glycyl
+P0CH09	YKR094C	RPL40B	76	Glycyl
+P0CH09	YKR094C	RPL40B	93	Glycyl
+P10664	YBR031W	RPL4A	2	N-acetylserine
+Q12487	YOR150W	MRPL23	2	N-acetylserine
+P0CX42	YER117W	RPL23B	2	N-acetylserine
+P0CX42	YER117W	RPL23B	106	N6%2CN6-dimethyllysine%3B
+P0CX42	YER117W	RPL23B	110	N6%2CN6-dimethyllysine%3B
+P04456	YOL127W	RPL25	61	Glycyl
+P05318	YDL081C	RPP1A	2	N-acetylserine
+P05318	YDL081C	RPP1A	96	Phosphoserine
+P0CH08	YIL148W	RPL40A	76	Glycyl
+P0CH08	YIL148W	RPL40A	93	Glycyl
+P0CX25	YPR043W	RPL43A	40	Phosphoserine
+P26321	YPL131W	RPL5	167	Phosphoserine
+P26321	YPL131W	RPL5	176	Phosphoserine
+P26321	YPL131W	RPL5	235	Phosphoserine
+P26321	YPL131W	RPL5	164	Glycyl
+P05739	YLR448W	RPL6B	12	Phosphoserine
+P05739	YLR448W	RPL6B	128	Glycyl
+P38144	YBR245C	ISW1	694	Phosphothreonine
+P38144	YBR245C	ISW1	846	Phosphoserine
+Q08773	YOR304W	ISW2	17	Phosphoserine
+Q08773	YOR304W	ISW2	19	Phosphoserine
+Q08773	YOR304W	ISW2	831	Phosphoserine
+Q08773	YOR304W	ISW2	1079	Phosphothreonine
+Q08773	YOR304W	ISW2	1082	Phosphoserine
+Q03419	YDR492W	IZH1	79	N-linked
+Q03419	YDR492W	IZH1	207	N-linked
+P36224	YMR294W	JNM1	91	Phosphoserine
+P07170	YDR226W	ADK1	2	N-acetylserine
+P07170	YDR226W	ADK1	3	N-acetylserine
+Q12055	YDL166C	FAP7	183	Phosphotyrosine
+Q12055	YDL166C	FAP7	188	Phosphoserine
+Q12055	YDL166C	FAP7	196	Phosphoserine
+P06245	YPL203W	TPK2	1	N-acetylmethionine
+P06245	YPL203W	TPK2	224	Phosphothreonine
+Q04746	YMR065W	KAR5	159	N-linked
+Q04746	YMR065W	KAR5	206	N-linked
+Q04746	YMR065W	KAR5	313	N-linked
+Q04746	YMR065W	KAR5	404	N-linked
+P39962	YER123W	YCK3	517	S-palmitoyl
+P39962	YER123W	YCK3	518	S-palmitoyl
+P39962	YER123W	YCK3	519	S-palmitoyl
+P39962	YER123W	YCK3	520	S-palmitoyl
+P39962	YER123W	YCK3	522	S-palmitoyl
+P39962	YER123W	YCK3	523	S-palmitoyl
+P39962	YER123W	YCK3	524	S-palmitoyl
+P27466	YFR014C	CMK1	343	Phosphotyrosine
+P27466	YFR014C	CMK1	357	Phosphoserine
+P27466	YFR014C	CMK1	417	Phosphoserine
+P27466	YFR014C	CMK1	418	Phosphoserine
+P27466	YFR014C	CMK1	420	Phosphoserine
+P27466	YFR014C	CMK1	429	Phosphoserine
+P34167	YPR163C	TIF3	65	Phosphoserine
+P34167	YPR163C	TIF3	71	Phosphoserine
+P38431	YPR041W	TIF5	170	Phosphoserine
+P38431	YPR041W	TIF5	172	Phosphoserine
+P38431	YPR041W	TIF5	191	Phosphothreonine
+P38431	YPR041W	TIF5	228	Phosphoserine
+P38431	YPR041W	TIF5	317	Phosphothreonine
+P38431	YPR041W	TIF5	397	Phosphoserine
+P53897	YNL157W	IGO1	32	Phosphoserine
+P53897	YNL157W	IGO1	64	Phosphoserine
+P50094	YML056C	IMD4	125	Phosphoserine
+Q06704	YLR309C	IMH1	308	Phosphoserine
+Q06704	YLR309C	IMH1	660	Phosphoserine
+Q06704	YLR309C	IMH1	827	Phosphoserine
+Q06704	YLR309C	IMH1	830	Phosphothreonine
+P47031	YJL082W	IML2	265	Phosphoserine
+P47031	YJL082W	IML2	268	Phosphoserine
+P47031	YJL082W	IML2	378	Phosphoserine
+P47031	YJL082W	IML2	380	Phosphothreonine
+P47031	YJL082W	IML2	383	Phosphoserine
+P47031	YJL082W	IML2	392	Phosphoserine
+P32351	YIL154C	IMP2'	24	Phosphothreonine
+P11986	YJL153C	INO1	368	Phosphoserine
+P53115	YGL150C	INO80	65	Phosphoserine
+P53115	YGL150C	INO80	115	Phosphoserine
+P53115	YGL150C	INO80	133	Phosphoserine
+P53115	YGL150C	INO80	610	Phosphoserine
+P07278	YIL033C	BCY1	3	Phosphoserine
+P07278	YIL033C	BCY1	4	Phosphoserine
+P07278	YIL033C	BCY1	9	Phosphoserine
+P07278	YIL033C	BCY1	68	Phosphoserine
+P07278	YIL033C	BCY1	70	Phosphoserine
+P07278	YIL033C	BCY1	74	Phosphoserine
+P07278	YIL033C	BCY1	77	Phosphoserine
+P07278	YIL033C	BCY1	79	Phosphoserine
+P07278	YIL033C	BCY1	81	Phosphoserine
+P07278	YIL033C	BCY1	83	Phosphoserine
+P07278	YIL033C	BCY1	84	Phosphoserine
+P07278	YIL033C	BCY1	129	Phosphothreonine
+P07278	YIL033C	BCY1	130	Phosphoserine
+P07278	YIL033C	BCY1	131	Phosphothreonine
+P07278	YIL033C	BCY1	144	Phosphothreonine
+P07278	YIL033C	BCY1	145	Phosphoserine%3B
+P07278	YIL033C	BCY1	147	Phosphoserine
+P07278	YIL033C	BCY1	150	Phosphothreonine
+P07278	YIL033C	BCY1	160	Phosphothreonine
+P23292	YNL154C	YCK2	2	N-acetylserine
+P23292	YNL154C	YCK2	455	Phosphoserine
+P23292	YNL154C	YCK2	545	S-palmitoyl
+P23292	YNL154C	YCK2	546	S-palmitoyl
+P23292	YNL154C	YCK2	465	Glycyl
+P19158	YOL081W	IRA2	635	Phosphothreonine
+P30605	YDR497C	ITR1	12	Phosphothreonine
+P30605	YDR497C	ITR1	26	Phosphoserine
+P30605	YDR497C	ITR1	31	Phosphoserine
+P30605	YDR497C	ITR1	35	Phosphoserine
+P30605	YDR497C	ITR1	37	Phosphoserine
+P30605	YDR497C	ITR1	46	Phosphoserine
+P30605	YDR497C	ITR1	371	N-linked
+P30605	YDR497C	ITR1	573	Glycyl
+Q07959	YLR023C	IZH3	45	N-linked
+Q07959	YLR023C	IZH3	123	N-linked
+Q07959	YLR023C	IZH3	153	N-linked
+Q07959	YLR023C	IZH3	256	N-linked
+Q07959	YLR023C	IZH3	319	N-linked
+P53863	YNL227C	JJJ1	393	Phosphoserine
+P53863	YNL227C	JJJ1	504	Phosphothreonine
+P22517	YOL016C	CMK2	316	Phosphothreonine%3B
+P22517	YOL016C	CMK2	353	Phosphotyrosine
+P22517	YOL016C	CMK2	354	Phosphoserine
+P22517	YOL016C	CMK2	367	Phosphoserine
+P22517	YOL016C	CMK2	371	Phosphoserine
+P22517	YOL016C	CMK2	387	Phosphoserine%3B
+P22517	YOL016C	CMK2	443	Phosphoserine
+Q12494	YDR017C	KCS1	150	Phosphoserine
+Q12494	YDR017C	KCS1	396	Phosphoserine
+Q12494	YDR017C	KCS1	469	Phosphoserine
+Q12494	YDR017C	KCS1	537	Phosphoserine
+Q12494	YDR017C	KCS1	539	Phosphoserine
+Q12494	YDR017C	KCS1	566	Phosphoserine
+Q12494	YDR017C	KCS1	583	Phosphoserine
+Q12494	YDR017C	KCS1	589	Phosphoserine
+Q12494	YDR017C	KCS1	646	Phosphoserine
+Q12494	YDR017C	KCS1	664	Phosphoserine
+Q12494	YDR017C	KCS1	670	Phosphoserine
+Q06142	YLR347C	KAP95	2	N-acetylserine
+Q06142	YLR347C	KAP95	836	Phosphoserine
+P32337	YMR308C	PSE1	2	N-acetylserine
+P32337	YMR308C	PSE1	830	Phosphothreonine
+P53067	YGL241W	KAP114	1	N-acetylmethionine
+P47135	YJR091C	JSN1	129	Phosphoserine
+P47135	YJR091C	JSN1	131	Phosphothreonine
+P47135	YJR091C	JSN1	160	Phosphoserine
+P47135	YJR091C	JSN1	168	Phosphoserine
+P47135	YJR091C	JSN1	913	Phosphoserine
+Q02932	YPL125W	KAP120	2	N-acetylalanine
+P01094	YMR174C	PAI3	1	N-acetylmethionine
+P53877	YNL182C	IPI3	388	Phosphoserine
+P18963	YBR140C	IRA1	497	Phosphoserine
+P18963	YBR140C	IRA1	915	Phosphoserine
+P18963	YBR140C	IRA1	1342	Phosphoserine
+P18963	YBR140C	IRA1	1753	Phosphoserine%3B
+P18963	YBR140C	IRA1	3004	Phosphoserine%3B
+P47056	YJL037W	IRC18	74	N-linked
+P47056	YJL037W	IRC18	104	N-linked
+P00817	YBR011C	IPP1	65	Phosphothreonine
+P00817	YBR011C	IPP1	251	Phosphothreonine
+P00817	YBR011C	IPP1	266	Phosphoserine
+P00817	YBR011C	IPP1	286	Phosphoserine
+P00817	YBR011C	IPP1	239	Glycyl
+P00817	YBR011C	IPP1	279	Glycyl
+Q12280	YPL242C	IQG1	264	Phosphothreonine
+Q12280	YPL242C	IQG1	268	Phosphoserine
+Q12280	YPL242C	IQG1	299	Phosphothreonine
+P32488	YMR081C	ISF1	119	Phosphoserine
+Q07532	YDL115C	IWR1	2	N-acetylserine
+P33417	YKL032C	IXR1	532	Phosphoserine
+P0CT04	YNL015W	PBI2	74	Phosphothreonine
+P36115	YKR019C	IRS4	180	Phosphoserine
+Q12358	YLL057C	JLP1	52	Phosphoserine
+P05986	YKL166C	TPK3	15	Phosphoserine
+P05986	YKL166C	TPK3	55	Phosphoserine
+P11927	YNL188W	KAR1	233	Phosphothreonine
+P32526	YPL269W	KAR9	496	Phosphoserine
+P23291	YHR135C	YCK1	522	Phosphoserine
+P23291	YHR135C	YCK1	523	Phosphoserine
+P23291	YHR135C	YCK1	527	Phosphoserine
+P23291	YHR135C	YCK1	537	S-palmitoyl
+P23291	YHR135C	YCK1	538	S-palmitoyl
+P35844	YPL145C	KES1	370	Phosphothreonine
+P35844	YPL145C	KES1	389	Phosphoserine
+P13134	YNL238W	KEX2	42	N-linked
+P13134	YNL238W	KEX2	163	N-linked
+P13134	YNL238W	KEX2	404	N-linked
+P13134	YNL238W	KEX2	480	N-linked
+P38692	YHR102W	KIC1	735	Phosphoserine
+P38991	YPL209C	IPL1	5	Phosphoserine%3B
+P38991	YPL209C	IPL1	76	Phosphoserine
+P38991	YPL209C	IPL1	260	Phosphothreonine%3B
+P38250	YBR086C	IST2	638	Phosphoserine
+P38250	YBR086C	IST2	701	Phosphothreonine
+P38250	YBR086C	IST2	704	Phosphoserine
+P38250	YBR086C	IST2	720	Phosphoserine
+P38250	YBR086C	IST2	726	Phosphothreonine
+P38250	YBR086C	IST2	729	Phosphoserine
+P38250	YBR086C	IST2	730	Phosphotyrosine
+P38250	YBR086C	IST2	757	Phosphoserine
+P38250	YBR086C	IST2	793	Phosphoserine
+P38250	YBR086C	IST2	844	Phosphoserine
+P38250	YBR086C	IST2	847	Phosphoserine
+P38250	YBR086C	IST2	850	Phosphothreonine
+P25389	YCL024W	KCC4	396	Phosphoserine
+P25389	YCL024W	KCC4	675	Phosphoserine
+P25389	YCL024W	KCC4	707	Phosphoserine
+P25389	YCL024W	KCC4	777	Phosphoserine
+P25389	YCL024W	KCC4	822	Phosphoserine
+P25389	YCL024W	KCC4	825	Phosphoserine
+P25389	YCL024W	KCC4	871	Phosphoserine
+P17423	YHR025W	THR1	133	Glycyl
+P13185	YDR122W	KIN1	534	Phosphoserine
+P13185	YDR122W	KIN1	593	Phosphoserine
+P13185	YDR122W	KIN1	646	Phosphoserine
+P13185	YDR122W	KIN1	764	Phosphoserine
+P13185	YDR122W	KIN1	986	Phosphoserine
+P06242	YDL108W	KIN28	162	Phosphothreonine%3B
+P24583	YBL105C	PKC1	226	Phosphoserine
+P24583	YBL105C	PKC1	761	Phosphoserine
+Q06505	YPR133C	SPN1	15	Phosphothreonine
+Q06505	YPR133C	SPN1	23	Phosphoserine%3B
+Q06505	YPR133C	SPN1	40	Phosphoserine
+Q06505	YPR133C	SPN1	85	Phosphoserine
+Q06505	YPR133C	SPN1	86	Phosphothreonine
+Q06505	YPR133C	SPN1	89	Phosphoserine
+Q03361	YDR475C	JIP4	48	Phosphoserine
+Q03361	YDR475C	JIP4	51	Phosphoserine
+Q03361	YDR475C	JIP4	360	Phosphoserine
+Q03361	YDR475C	JIP4	510	Phosphoserine
+Q03361	YDR475C	JIP4	552	Phosphoserine
+Q03361	YDR475C	JIP4	577	Phosphoserine
+Q03361	YDR475C	JIP4	775	Phosphoserine
+P00549	YAL038W	CDC19	2	N-acetylserine
+P00549	YAL038W	CDC19	9	Phosphoserine
+P00549	YAL038W	CDC19	16	Phosphoserine
+P00549	YAL038W	CDC19	31	Phosphothreonine
+P00549	YAL038W	CDC19	70	Phosphoserine
+P00549	YAL038W	CDC19	184	Phosphothreonine
+P00549	YAL038W	CDC19	213	Phosphoserine
+P00549	YAL038W	CDC19	316	Phosphoserine
+P00549	YAL038W	CDC19	450	Phosphoserine
+P00549	YAL038W	CDC19	478	Phosphothreonine
+P00549	YAL038W	CDC19	204	Glycyl
+P00549	YAL038W	CDC19	255	Glycyl
+P00549	YAL038W	CDC19	446	Glycyl
+P14681	YGR040W	KSS1	183	Phosphothreonine
+P14681	YGR040W	KSS1	185	Phosphotyrosine
+P50090	YGR238C	KEL2	455	Phosphothreonine
+P50090	YGR238C	KEL2	509	Phosphoserine
+P13186	YLR096W	KIN2	22	Phosphoserine
+P13186	YLR096W	KIN2	146	Phosphoserine
+P13186	YLR096W	KIN2	549	Phosphoserine
+P13186	YLR096W	KIN2	609	Phosphoserine
+P13186	YLR096W	KIN2	888	Phosphoserine
+Q01919	YOR233W	KIN4	365	Phosphoserine
+Q01919	YOR233W	KIN4	388	Phosphoserine
+Q01919	YOR233W	KIN4	521	Phosphoserine
+Q01919	YOR233W	KIN4	748	Phosphoserine
+P52489	YOR347C	PYK2	24	Phosphoserine
+P42846	YNL308C	KRI1	177	Phosphoserine
+P42846	YNL308C	KRI1	184	Phosphoserine
+P42846	YNL308C	KRI1	185	Phosphoserine
+P42846	YNL308C	KRI1	486	Phosphoserine
+P54070	YPL053C	KTR6	82	N-linked
+P54070	YPL053C	KTR6	98	N-linked
+Q06554	YLR247C	IRC20	2	N-acetylserine
+Q06554	YLR247C	IRC20	810	Phosphoserine
+P32361	YHR079C	IRE1	840	Phosphoserine%3B
+P32361	YHR079C	IRE1	841	Phosphoserine%3B
+P32361	YHR079C	IRE1	111	N-linked
+P32361	YHR079C	IRE1	213	N-linked
+P32361	YHR079C	IRE1	298	N-linked
+P32361	YHR079C	IRE1	397	N-linked
+P30606	YOL103W	ITR2	394	N-linked
+Q04934	YDR229W	IVY1	59	Phosphoserine
+Q04934	YDR229W	IVY1	84	Phosphoserine
+Q04934	YDR229W	IVY1	85	Phosphoserine
+Q04934	YDR229W	IVY1	335	Phosphoserine
+P36035	YKL217W	JEN1	2	N-acetylserine
+P36035	YKL217W	JEN1	4	Phosphoserine
+P36035	YKL217W	JEN1	11	Phosphoserine
+P36035	YKL217W	JEN1	61	Phosphoserine
+P36035	YKL217W	JEN1	66	Phosphoserine
+P36035	YKL217W	JEN1	70	Phosphothreonine
+P36035	YKL217W	JEN1	584	Phosphoserine
+P36035	YKL217W	JEN1	603	Phosphoserine
+P36035	YKL217W	JEN1	606	Phosphoserine
+P36035	YKL217W	JEN1	9	Glycyl
+P36035	YKL217W	JEN1	338	Glycyl
+P46997	YJL162C	JJJ2	229	Phosphoserine
+P06244	YJL164C	TPK1	2	N-acetylserine
+Q08979	YPL263C	KEL3	47	Phosphoserine
+Q04066	YDR428C	BNA7	9	Phosphoserine
+P38853	YHR158C	KEL1	20	Phosphoserine
+P38853	YHR158C	KEL1	23	Phosphoserine
+P38853	YHR158C	KEL1	25	Phosphoserine
+P38853	YHR158C	KEL1	94	Phosphoserine
+P38853	YHR158C	KEL1	467	Phosphothreonine
+P38853	YHR158C	KEL1	477	Phosphothreonine
+P38853	YHR158C	KEL1	503	Phosphoserine
+P38853	YHR158C	KEL1	604	Phosphothreonine
+P38853	YHR158C	KEL1	613	Phosphoserine
+P38853	YHR158C	KEL1	626	Phosphothreonine
+P38853	YHR158C	KEL1	689	Phosphoserine
+P38853	YHR158C	KEL1	691	Phosphoserine
+P38853	YHR158C	KEL1	717	Phosphoserine
+P38853	YHR158C	KEL1	748	Phosphoserine
+P38853	YHR158C	KEL1	837	Phosphoserine
+P38853	YHR158C	KEL1	848	Phosphoserine
+P38853	YHR158C	KEL1	958	Phosphoserine
+P38853	YHR158C	KEL1	997	Phosphoserine
+P38853	YHR158C	KEL1	1003	Phosphoserine
+P38853	YHR158C	KEL1	1022	Phosphoserine
+P40309	YJL094C	KHA1	557	Phosphoserine
+P40309	YJL094C	KHA1	562	Glycyl
+P25341	YCR091W	KIN82	203	Phosphoserine
+P40504	YIL085C	KTR7	89	N-linked
+P40504	YIL085C	KTR7	144	N-linked
+P09620	YGL203C	KEX1	660	Phosphoserine
+P09620	YGL203C	KEX1	81	N-linked
+P09620	YGL203C	KEX1	459	N-linked
+P09620	YGL203C	KEX1	467	N-linked
+P15454	YDR454C	GUK1	2	N-acetylserine
+P15454	YDR454C	GUK1	149	Phosphoserine
+P15454	YDR454C	GUK1	157	Phosphotyrosine
+P17260	YNL322C	KRE1	288	GPI-anchor
+P38691	YHR082C	KSP1	416	Phosphoserine
+P38691	YHR082C	KSP1	419	Phosphoserine
+P38691	YHR082C	KSP1	501	Phosphothreonine
+P38691	YHR082C	KSP1	504	Phosphothreonine
+P38691	YHR082C	KSP1	526	Phosphothreonine
+P38691	YHR082C	KSP1	529	Phosphoserine
+P38691	YHR082C	KSP1	646	Phosphoserine
+P38691	YHR082C	KSP1	845	Phosphoserine
+P38691	YHR082C	KSP1	884	Phosphoserine
+P38691	YHR082C	KSP1	1005	Phosphothreonine
+P38691	YHR082C	KSP1	1014	Phosphoserine
+P38800	YHR080C	LAM4	66	Phosphothreonine
+P38800	YHR080C	LAM4	747	Phosphoserine
+P20485	YLR133W	CKI1	30	Phosphoserine%3B
+P20485	YLR133W	CKI1	48	Phosphoserine
+P20485	YLR133W	CKI1	51	Phosphoserine
+P20485	YLR133W	CKI1	54	Phosphothreonine
+P20485	YLR133W	CKI1	85	Phosphoserine%3B
+P22023	YOR336W	KRE5	115	N-linked
+P22023	YOR336W	KRE5	228	N-linked
+P22023	YOR336W	KRE5	293	N-linked
+P22023	YOR336W	KRE5	457	N-linked
+P22023	YOR336W	KRE5	519	N-linked
+P22023	YOR336W	KRE5	523	N-linked
+P22023	YOR336W	KRE5	644	N-linked
+P22023	YOR336W	KRE5	870	N-linked
+P22023	YOR336W	KRE5	1091	N-linked
+P22023	YOR336W	KRE5	1150	N-linked
+P22023	YOR336W	KRE5	1195	N-linked
+P33550	YKR061W	KTR2	65	N-linked
+P33550	YKR061W	KTR2	81	N-linked
+P33550	YKR061W	KTR2	92	N-linked
+P33550	YKR061W	KTR2	167	N-linked
+P43560	YFL042C	LAM5	110	Phosphothreonine
+P43560	YFL042C	LAM5	113	Phosphoserine
+P43560	YFL042C	LAM5	140	Phosphoserine
+P43560	YFL042C	LAM5	143	Phosphothreonine
+P43560	YFL042C	LAM5	149	Phosphoserine
+P36004	YKL168C	KKQ8	19	Phosphoserine
+P36004	YKL168C	KKQ8	232	Phosphoserine
+P36004	YKL168C	KKQ8	238	Phosphoserine
+P36004	YKL168C	KKQ8	241	Phosphoserine
+P32350	YLL019C	KNS1	562	Phosphothreonine
+P32895	YKL181W	PRS1	199	Phosphoserine
+P32895	YKL181W	PRS1	218	Phosphoserine
+P32895	YKL181W	PRS1	271	Phosphoserine
+P32895	YKL181W	PRS1	295	Phosphoserine
+P40970	YDR062W	LCB2	366	N6-(pyridoxal
+P39002	YIL009W	FAA3	2	N-acetylserine
+P40079	YER127W	LCP5	2	N-acetylserine
+P25587	YCL005W	LDB16	180	Phosphothreonine
+P25587	YCL005W	LDB16	184	Phosphothreonine
+P25587	YCL005W	LDB16	241	Phosphoserine
+Q02799	YPL054W	LEE1	21	Phosphoserine
+Q02799	YPL054W	LEE1	30	Phosphoserine
+Q02799	YPL054W	LEE1	282	Phosphoserine
+P53281	YGR136W	LSB1	2	N-acetylserine
+P53281	YGR136W	LSB1	48	Phosphoserine
+P53281	YGR136W	LSB1	114	Phosphoserine
+P53281	YGR136W	LSB1	116	Phosphoserine
+P53281	YGR136W	LSB1	41	Glycyl
+P53281	YGR136W	LSB1	79	Glycyl
+P53281	YGR136W	LSB1	118	Glycyl
+P53281	YGR136W	LSB1	219	Glycyl
+P42838	YNL323W	LEM3	36	Phosphoserine
+P42838	YNL323W	LEM3	113	N-linked
+P42838	YNL323W	LEM3	240	N-linked
+P42838	YNL323W	LEM3	256	N-linked
+P42838	YNL323W	LEM3	279	N-linked
+P42838	YNL323W	LEM3	298	N-linked
+P42838	YNL323W	LEM3	332	N-linked
+Q12265	YOL061W	PRS5	119	Phosphotyrosine
+Q12265	YOL061W	PRS5	120	Phosphothreonine
+Q12265	YOL061W	PRS5	123	Phosphoserine
+Q12265	YOL061W	PRS5	127	Phosphothreonine
+Q12265	YOL061W	PRS5	183	Phosphoserine
+Q12265	YOL061W	PRS5	332	Phosphoserine
+P27810	YOR099W	KTR1	120	N-linked
+Q92325	YOL025W	LAG2	16	Glycyl
+Q12446	YOR181W	LAS17	334	Phosphothreonine
+Q12446	YOR181W	LAS17	337	Phosphoserine
+Q12446	YOR181W	LAS17	588	Phosphoserine
+P07264	YGL009C	LEU1	488	Phosphoserine
+P07264	YGL009C	LEU1	494	Phosphothreonine
+P07264	YGL009C	LEU1	495	Phosphoserine
+P53966	YNL029C	KTR5	86	N-linked
+P32807	YMR284W	YKU70	370	Phosphoserine
+P32807	YMR284W	YKU70	371	Phosphoserine
+P32807	YMR284W	YKU70	372	Phosphoserine
+P25045	YMR296C	LCB1	121	Phosphothreonine
+Q06147	YLR260W	LCB5	91	S-palmitoyl
+Q06147	YLR260W	LCB5	94	S-palmitoyl
+P36016	YKL073W	LHS1	128	N-linked
+P36016	YKL073W	LHS1	458	N-linked
+P36016	YKL073W	LHS1	474	N-linked
+P36016	YKL073W	LHS1	481	N-linked
+P36016	YKL073W	LHS1	489	N-linked
+P36016	YKL073W	LHS1	527	N-linked
+P36016	YKL073W	LHS1	844	N-linked
+P40026	YER038C	KRE29	81	Phosphoserine
+P40026	YER038C	KRE29	101	Phosphoserine
+P27809	YDR483W	KRE2	197	N-linked
+P30624	YOR317W	FAA1	189	Glycyl
+P32486	YPR159W	KRE6	81	Phosphoserine
+P32486	YPR159W	KRE6	116	Phosphoserine
+P32486	YPR159W	KRE6	133	Phosphoserine
+P32486	YPR159W	KRE6	134	Phosphoserine
+P32486	YPR159W	KRE6	136	Phosphoserine
+P32486	YPR159W	KRE6	139	Phosphoserine
+P32486	YPR159W	KRE6	374	N-linked
+P32486	YPR159W	KRE6	461	N-linked
+P32486	YPR159W	KRE6	538	N-linked
+P32486	YPR159W	KRE6	563	N-linked
+P32486	YPR159W	KRE6	691	N-linked
+P33399	YDL051W	LHP1	2	N-acetylserine
+P33399	YDL051W	LHP1	15	Phosphoserine
+P33399	YDL051W	LHP1	19	Phosphoserine
+P33399	YDL051W	LHP1	104	Omega-N-methylarginine
+P33399	YDL051W	LHP1	230	Phosphoserine
+P33399	YDL051W	LHP1	233	Phosphoserine
+P33399	YDL051W	LHP1	235	Phosphoserine
+Q05979	YLR231C	BNA5	252	N6-(pyridoxal
+P28496	YKL008C	LAC1	2	N-acetylserine
+P28496	YKL008C	LAC1	23	Phosphoserine
+P28496	YKL008C	LAC1	24	Phosphoserine
+P28496	YKL008C	LAC1	103	N-linked
+P38703	YHL003C	LAG1	23	Phosphoserine
+P38703	YHL003C	LAG1	24	Phosphoserine
+P38703	YHL003C	LAG1	103	N-linked
+P38851	YHR155W	LAM1	1205	N-linked
+Q08001	YLR072W	LAM6	343	Phosphothreonine
+Q08001	YLR072W	LAM6	591	Phosphoserine
+Q08001	YLR072W	LAM6	593	Phosphothreonine
+Q08001	YLR072W	LAM6	594	Phosphoserine
+Q08001	YLR072W	LAM6	597	Phosphoserine
+Q04377	YDR499W	LCD1	10	Phosphoserine
+Q04377	YDR499W	LCD1	11	Phosphoserine
+Q04377	YDR499W	LCD1	76	Phosphoserine
+Q02786	YPL056C	LCL1	81	GPI-anchor
+P38439	YOR123C	LEO1	105	Phosphoserine
+P38439	YOR123C	LEO1	132	Phosphoserine
+P38439	YOR123C	LEO1	188	Phosphoserine
+P38439	YOR123C	LEO1	358	Phosphoserine
+P38439	YOR123C	LEO1	372	Phosphoserine
+Q12342	YDL146W	LDB17	7	Phosphoserine
+Q12342	YDL146W	LDB17	463	Phosphoserine
+Q12342	YDL146W	LDB17	466	Phosphoserine
+P47055	YJL038C	LOH1	42	N-linked
+P47055	YJL038C	LOH1	62	N-linked
+P47055	YJL038C	LOH1	136	N-linked
+P25579	YCL051W	LRE1	393	Phosphoserine
+P25579	YCL051W	LRE1	398	Phosphoserine
+P25579	YCL051W	LRE1	516	Phosphoserine
+P25579	YCL051W	LRE1	552	Phosphoserine
+P43586	YFR001W	LOC1	24	Phosphoserine
+P35688	YDL240W	LRG1	1	N-acetylmethionine
+P35688	YDL240W	LRG1	562	Phosphoserine
+P40495	YIL094C	LYS12	98	Phosphoserine
+Q04087	YDR439W	LRS4	168	Phosphoserine
+Q04087	YDR439W	LRS4	230	Phosphoserine
+P43603	YFR024C-A	LSB3	227	Phosphoserine
+P43603	YFR024C-A	LSB3	298	Phosphothreonine
+P43603	YFR024C-A	LSB3	300	Phosphoserine
+P43603	YFR024C-A	LSB3	303	Phosphoserine
+P43603	YFR024C-A	LSB3	393	Phosphothreonine
+P43603	YFR024C-A	LSB3	397	Phosphoserine
+P43603	YFR024C-A	LSB3	402	Phosphoserine
+P43603	YFR024C-A	LSB3	416	Phosphoserine
+Q12230	YPL004C	LSP1	233	Phosphothreonine
+P22134	YER142C	MAG1	110	Phosphoserine
+Q12176	YDR060W	MAK21	2	N-acetylserine
+Q12176	YDR060W	MAK21	62	Phosphoserine
+Q12176	YDR060W	MAK21	73	Phosphoserine
+Q12176	YDR060W	MAK21	80	Phosphoserine
+Q12176	YDR060W	MAK21	275	Phosphoserine
+Q12176	YDR060W	MAK21	708	Phosphotyrosine
+Q12176	YDR060W	MAK21	710	Phosphoserine
+Q12176	YDR060W	MAK21	874	Phosphoserine
+Q12176	YDR060W	MAK21	878	Phosphoserine
+Q12176	YDR060W	MAK21	977	Phosphoserine
+Q12176	YDR060W	MAK21	978	Phosphoserine
+Q12176	YDR060W	MAK21	1024	Phosphoserine
+Q12246	YOR171C	LCB4	111	Phosphoserine
+Q12246	YOR171C	LCB4	120	Phosphoserine
+Q12246	YOR171C	LCB4	154	Phosphoserine
+Q12246	YOR171C	LCB4	160	Phosphoserine
+Q12246	YOR171C	LCB4	451	Phosphoserine%3B
+Q12246	YOR171C	LCB4	454	Phosphoserine
+Q12246	YOR171C	LCB4	455	Phosphoserine%3B
+Q12246	YOR171C	LCB4	460	Phosphoserine
+Q12246	YOR171C	LCB4	43	S-palmitoyl
+Q12246	YOR171C	LCB4	46	S-palmitoyl
+Q12246	YOR171C	LCB4	148	Glycyl
+Q12502	YOR322C	LDB19	93	Phosphothreonine
+Q12502	YOR322C	LDB19	384	Phosphoserine
+Q12502	YOR322C	LDB19	619	Phosphothreonine
+Q12502	YOR322C	LDB19	808	Phosphoserine
+Q12502	YOR322C	LDB19	486	Glycyl
+Q02783	YPL060W	MFM1	202	N-linked
+P32487	YNL268W	LYP1	64	Phosphoserine
+P32487	YNL268W	LYP1	75	Phosphoserine
+P32487	YNL268W	LYP1	77	Phosphothreonine
+P32487	YNL268W	LYP1	79	Phosphoserine
+P32487	YNL268W	LYP1	87	Phosphoserine
+P32487	YNL268W	LYP1	90	Phosphothreonine
+P32487	YNL268W	LYP1	54	Glycyl
+P38828	YHR121W	LSM12	2	N-acetylserine
+P53048	YGR289C	MAL11	523	N-linked
+Q01662	YLR244C	MAP1	2	N-acetylserine
+P38174	YBL091C	MAP2	35	Phosphoserine
+P34239	YKL176C	LST4	401	Phosphoserine
+P07866	YAL024C	LTE1	271	Phosphoserine
+P07866	YAL024C	LTE1	559	Phosphoserine
+P07866	YAL024C	LTE1	689	Phosphoserine
+P07866	YAL024C	LTE1	691	Phosphothreonine
+P07866	YAL024C	LTE1	808	Phosphoserine
+P07866	YAL024C	LTE1	810	Phosphoserine
+P07866	YAL024C	LTE1	1028	Phosphoserine
+P07866	YAL024C	LTE1	1109	Phosphoserine
+Q07508	YDL087C	LUC7	2	N-acetylserine
+P35192	YMR021C	MAC1	143	Phosphoserine
+P47074	YJL013C	MAD3	268	Phosphoserine
+P41910	YDR005C	MAF1	90	Phosphoserine
+P41910	YDR005C	MAF1	209	Phosphoserine
+P41910	YDR005C	MAF1	210	Phosphoserine
+P41910	YDR005C	MAF1	347	Phosphothreonine
+Q07376	YDL054C	MCH1	255	Phosphoserine
+Q07376	YDL054C	MCH1	60	N-linked
+Q07376	YDL054C	MCH1	131	N-linked
+Q07376	YDL054C	MCH1	194	N-linked
+P36032	YKL221W	MCH2	72	N-linked
+Q08777	YOR306C	MCH5	125	N-linked
+Q08777	YOR306C	MCH5	194	N-linked
+Q08777	YOR306C	MCH5	419	N-linked
+Q06675	YDR318W	MCM21	88	Phosphothreonine
+P11746	YMR043W	MCM1	2	N-acetylserine
+P11746	YMR043W	MCM1	2	Phosphoserine
+P11746	YMR043W	MCM1	144	Phosphoserine
+P17505	YKL085W	MDH1	177	Phosphoserine
+P17505	YKL085W	MDH1	199	Phosphothreonine
+P53145	YGL099W	LSG1	103	Phosphoserine
+P34078	YKL143W	LTV1	2	N-acetylserine
+P34078	YKL143W	LTV1	288	Phosphoserine
+P34078	YKL143W	LTV1	293	Phosphoserine
+P34078	YKL143W	LTV1	299	Phosphoserine
+P34078	YKL143W	LTV1	303	Phosphoserine
+P40957	YGL086W	MAD1	502	Phosphothreonine
+P20484	YKL021C	MAK11	2	N-acetylserine
+P20484	YKL021C	MAK11	376	Phosphoserine
+P20484	YKL021C	MAK11	380	Phosphoserine
+P20484	YKL021C	MAK11	382	Phosphothreonine
+P38112	YBR142W	MAK5	135	Phosphothreonine
+P38112	YBR142W	MAK5	138	Phosphoserine
+P38112	YBR142W	MAK5	678	Phosphoserine
+P36007	YKL218C	SRY1	53	N6-(pyridoxal
+P22855	YGL156W	AMS1	2	N-acetylserine
+Q92328	YOL009C	MDM12	49	Glycyl
+P38295	YBR177C	EHT1	114	Glycyl
+P29469	YBL023C	MCM2	14	Phosphoserine
+P29469	YBL023C	MCM2	16	Phosphoserine
+P29469	YBL023C	MCM2	23	Phosphoserine
+P29469	YBL023C	MCM2	164	Phosphoserine
+P29469	YBL023C	MCM2	170	Phosphoserine
+P30665	YPR019W	MCM4	52	Phosphoserine
+P30665	YPR019W	MCM4	56	Phosphoserine
+P30665	YPR019W	MCM4	69	Phosphoserine
+P53091	YGL201C	MCM6	78	Phosphoserine
+P53091	YGL201C	MCM6	249	Phosphoserine
+P53091	YGL201C	MCM6	372	Phosphoserine
+P53091	YGL201C	MCM6	766	Phosphothreonine
+P38132	YBR202W	MCM7	811	Phosphothreonine
+P38132	YBR202W	MCM7	819	Phosphoserine
+P38132	YBR202W	MCM7	838	Phosphoserine
+Q99257	YPL169C	MEX67	2	N-acetylserine
+P34166	YNL145W	MFA2	35	Cysteine
+P34166	YNL145W	MFA2	35	S-farnesyl
+P40578	YIR033W	MGA2	255	Phosphoserine
+P40578	YIR033W	MGA2	467	Phosphoserine
+P43638	YJL042W	MHP1	1	N-acetylmethionine
+P43638	YJL042W	MHP1	81	Phosphoserine
+P43638	YJL042W	MHP1	222	Phosphothreonine
+P43638	YJL042W	MHP1	309	Phosphoserine
+P43638	YJL042W	MHP1	311	Phosphoserine
+P43638	YJL042W	MHP1	354	Phosphoserine
+P43638	YJL042W	MHP1	357	Phosphoserine
+P43638	YJL042W	MHP1	577	Phosphothreonine
+P43638	YJL042W	MHP1	221	Glycyl
+Q12019	YLR106C	MDN1	1026	Phosphothreonine
+Q12019	YLR106C	MDN1	2971	Phosphoserine
+Q12019	YLR106C	MDN1	4353	Phosphoserine
+Q12019	YLR106C	MDN1	4388	Phosphothreonine
+Q12019	YLR106C	MDN1	4555	Phosphoserine
+P34165	YDR461W	MFA1	33	Cysteine
+P34165	YDR461W	MFA1	33	S-farnesyl
+P40002	YEL007W	MIT1	152	Phosphoserine
+P32490	YOR231W	MKK1	192	Phosphoserine
+P53141	YGL106W	MLC1	116	Glycyl
+P38998	YIR034C	LYS1	2	N-acetylalanine%3B
+P07702	YBR115C	LYS2	880	O-(pantetheine
+P07702	YBR115C	LYS2	541	Glycyl
+P07702	YBR115C	LYS2	1276	Glycyl
+O14467	YOR298C-A	MBF1	143	Phosphoserine
+P19659	YOL051W	GAL11	2	N-acetylserine
+P19659	YOL051W	GAL11	335	Phosphoserine
+P19659	YOL051W	GAL11	736	Phosphoserine
+P19659	YOL051W	GAL11	752	Phosphoserine
+P19659	YOL051W	GAL11	783	Phosphoserine
+P19659	YOL051W	GAL11	785	Phosphoserine
+P19659	YOL051W	GAL11	789	Phosphoserine
+P19659	YOL051W	GAL11	793	Phosphothreonine
+P19659	YOL051W	GAL11	831	Phosphoserine
+P19659	YOL051W	GAL11	1003	Phosphoserine
+P19659	YOL051W	GAL11	1008	Phosphoserine
+P19659	YOL051W	GAL11	1018	Phosphoserine
+P19659	YOL051W	GAL11	1034	Phosphoserine
+Q02205	YKR007W	MEH1	146	Phosphoserine
+Q02205	YKR007W	MEH1	149	Phosphoserine
+Q02205	YKR007W	MEH1	2	N-myristoyl
+Q02205	YKR007W	MEH1	7	S-palmitoyl
+Q02205	YKR007W	MEH1	8	S-palmitoyl
+P33441	YML062C	MFT1	266	Phosphoserine
+P35201	YKL089W	MIF2	325	Phosphoserine
+P27705	YGL035C	MIG1	278	Phosphoserine
+P27705	YGL035C	MIG1	302	Phosphoserine
+P27705	YGL035C	MIG1	310	Phosphoserine
+P27705	YGL035C	MIG1	311	Phosphoserine
+P27705	YGL035C	MIG1	314	Phosphoserine
+P27705	YGL035C	MIG1	377	Phosphoserine
+Q06820	YPR083W	MDM36	42	Phosphoserine
+Q02574	YLR288C	MEC3	452	Phosphoserine
+Q12321	YPR070W	MED1	155	Phosphoserine
+Q12321	YPR070W	MED1	423	Phosphoserine
+P32570	YBR253W	SRB6	2	N-acetylserine
+P43623	YFR055W	IRC7	208	N6-(pyridoxal
+P36027	YLR332W	MID2	260	Phosphoserine
+P36027	YLR332W	MID2	327	Phosphoserine
+P36027	YLR332W	MID2	329	Phosphoserine
+P36027	YLR332W	MID2	355	Phosphoserine
+P36027	YLR332W	MID2	35	N-linked
+P36027	YLR332W	MID2	211	N-linked
+Q02455	YKR095W	MLP1	2	N-acetylserine
+Q02455	YKR095W	MLP1	337	Phosphothreonine
+Q02455	YKR095W	MLP1	379	Phosphoserine
+Q02455	YKR095W	MLP1	1670	Phosphoserine
+Q02455	YKR095W	MLP1	1710	Phosphoserine
+Q02455	YKR095W	MLP1	1733	Phosphoserine
+Q02455	YKR095W	MLP1	1803	Phosphoserine
+P32354	YIL150C	MCM10	17	Phosphothreonine
+P32354	YIL150C	MCM10	18	Phosphoserine
+P32354	YIL150C	MCM10	453	Phosphoserine
+P32354	YIL150C	MCM10	454	Phosphoserine
+P22133	YOL126C	MDH2	6	Phosphothreonine
+P53094	YGL197W	MDS3	472	Phosphoserine
+P53094	YGL197W	MDS3	475	Phosphoserine
+P53094	YGL197W	MDS3	621	Phosphoserine
+P53094	YGL197W	MDS3	639	Phosphoserine
+P53094	YGL197W	MDS3	693	Phosphoserine
+P53094	YGL197W	MDS3	698	Phosphoserine
+P53094	YGL197W	MDS3	744	Phosphoserine
+P53094	YGL197W	MDS3	747	Phosphoserine
+P53094	YGL197W	MDS3	756	Phosphoserine
+P53094	YGL197W	MDS3	757	Phosphoserine
+P53094	YGL197W	MDS3	781	Phosphoserine
+P53094	YGL197W	MDS3	785	Phosphothreonine
+P53094	YGL197W	MDS3	787	Phosphoserine
+P53094	YGL197W	MDS3	900	Phosphoserine
+P53094	YGL197W	MDS3	904	Phosphoserine
+P53094	YGL197W	MDS3	930	Phosphothreonine
+P53094	YGL197W	MDS3	1187	Phosphoserine
+P47025	YJL112W	MDV1	376	Phosphoserine
+P19263	YLR071C	RGR1	2	N-acetylthreonine
+P19263	YLR071C	RGR1	7	Phosphoserine
+P19263	YLR071C	RGR1	1036	Phosphothreonine
+P39014	YIL046W	MET30	67	Phosphoserine
+P47164	YJR130C	STR2	443	N6-(pyridoxal
+P19358	YDR502C	SAM2	2	N-acetylserine
+P36051	YKL165C	MCD4	90	N-linked
+P36051	YKL165C	MCD4	138	N-linked
+P36051	YKL165C	MCD4	198	N-linked
+P36051	YKL165C	MCD4	202	N-linked
+P36051	YKL165C	MCD4	286	N-linked
+P36051	YKL165C	MCD4	312	N-linked
+P21965	YNL307C	MCK1	2	N-acetylserine
+P21965	YNL307C	MCK1	198	Phosphoserine
+P21965	YNL307C	MCK1	199	Phosphotyrosine
+P21965	YNL307C	MCK1	202	Phosphoserine
+P24279	YEL032W	MCM3	761	Phosphoserine
+P24279	YEL032W	MCM3	777	Phosphoserine
+P24279	YEL032W	MCM3	781	Phosphoserine
+P24279	YEL032W	MCM3	868	Phosphothreonine
+Q12343	YOR174W	MED4	2	N-acetylserine
+Q12343	YOR174W	MED4	237	Phosphothreonine%3B
+Q12343	YOR174W	MED4	242	Phosphoserine
+P40513	YIL070C	MAM33	91	Phosphothreonine
+Q12296	YOL060C	MAM3	439	Phosphoserine
+Q12296	YOL060C	MAM3	447	Phosphoserine
+Q12296	YOL060C	MAM3	527	Phosphoserine
+Q12296	YOL060C	MAM3	603	Phosphoserine
+Q12296	YOL060C	MAM3	604	Phosphotyrosine
+Q12296	YOL060C	MAM3	607	Phosphothreonine
+Q12296	YOL060C	MAM3	614	Phosphoserine
+P39678	YDL056W	MBP1	110	Phosphoserine
+P39678	YDL056W	MBP1	325	Phosphothreonine
+P39678	YDL056W	MBP1	326	Phosphoserine
+P39678	YDL056W	MBP1	330	Phosphoserine
+P39678	YDL056W	MBP1	827	Phosphoserine
+P23493	YKL093W	MBR1	159	Phosphothreonine
+P23493	YKL093W	MBR1	177	Phosphoserine
+P23493	YKL093W	MBR1	224	Phosphoserine
+P23493	YKL093W	MBR1	227	Phosphoserine
+P36060	YKL150W	MCR1	278	Phosphoserine
+P53885	YNL173C	MDG1	160	Phosphoserine
+P53885	YNL173C	MDG1	216	Phosphothreonine
+P53885	YNL173C	MDG1	288	Phosphoserine
+P53885	YNL173C	MDG1	314	Glycyl
+Q12124	YDL005C	MED2	6	Phosphoserine
+Q12124	YDL005C	MED2	208	Phosphoserine%3B
+P40260	YGR121C	MEP1	442	Phosphoserine
+P40260	YGR121C	MEP1	445	Phosphoserine
+P32389	YNL103W	MET4	416	Phosphoserine
+P32389	YNL103W	MET4	564	Phosphoserine
+Q08268	YOL119C	MCH4	131	N-linked
+Q08268	YOL119C	MCH4	54	Glycyl
+Q01846	YML104C	MDM1	670	Phosphoserine
+Q01846	YML104C	MDM1	673	Phosphoserine
+Q01846	YML104C	MDM1	692	Phosphoserine
+P40356	YGL025C	PGD1	1	N-acetylmethionine
+P38782	YHR058C	MED6	225	Phosphoserine
+P41948	YNL142W	MEP2	4	N-linked
+P38849	YHR151C	MTC6	32	N-linked
+P38849	YHR151C	MTC6	60	N-linked
+P38849	YHR151C	MTC6	80	N-linked
+P38849	YHR151C	MTC6	89	N-linked
+P38849	YHR151C	MTC6	156	N-linked
+P38849	YHR151C	MTC6	171	N-linked
+P38849	YHR151C	MTC6	175	N-linked
+P38849	YHR151C	MTC6	202	N-linked
+P38849	YHR151C	MTC6	240	N-linked
+P38849	YHR151C	MTC6	259	N-linked
+P38849	YHR151C	MTC6	311	N-linked
+P38849	YHR151C	MTC6	362	N-linked
+P38849	YHR151C	MTC6	433	N-linked
+P0CX81	YHR055C	CUP1-2	30	Glycyl
+P36006	YKL129C	MYO3	357	Phosphoserine
+P47018	YJL123C	MTC1	273	Phosphoserine
+P47018	YJL123C	MTC1	436	Phosphoserine
+P53176	YGL051W	MST27	3	Phosphothreonine
+P36084	YKL074C	MUD2	49	Phosphoserine
+P39552	YAR033W	MST28	3	Phosphothreonine
+P0CY08	YCR039C	MATALPHA2	1	N-acetylmethionine
+P38335	YBR255W	MTC4	85	Phosphoserine
+P38335	YBR255W	MTC4	263	Phosphothreonine
+P38335	YBR255W	MTC4	481	Phosphoserine
+P38335	YBR255W	MTC4	491	Phosphoserine
+P38335	YBR255W	MTC4	493	Phosphotyrosine
+P46151	YPL023C	MET12	120	Phosphoserine
+P46151	YPL023C	MET12	301	Phosphoserine
+P46151	YPL023C	MET12	358	Phosphoserine
+Q06489	YPR118W	MRI1	2	N-acetylserine
+Q06489	YPR118W	MRI1	351	Phosphoserine
+Q06106	YPR112C	MRD1	220	Phosphoserine
+Q06106	YPR112C	MRD1	264	Phosphoserine
+Q12117	YDR033W	MRH1	289	Phosphoserine
+Q12117	YDR033W	MRH1	295	Phosphothreonine
+Q12117	YDR033W	MRH1	299	Phosphoserine
+P50873	YDL079C	MRK1	13	Phosphoserine
+P35719	YKL142W	MRP8	23	Phosphoserine
+P35719	YKL142W	MRP8	137	Glycyl
+P50276	YGR055W	MUP1	552	Phosphothreonine
+P50276	YGR055W	MUP1	573	Phosphoserine
+P50276	YGR055W	MUP1	28	Glycyl
+P38994	YDR208W	MSS4	207	Phosphoserine
+P38994	YDR208W	MSS4	222	Phosphothreonine
+P38994	YDR208W	MSS4	225	Phosphoserine
+P38994	YDR208W	MSS4	659	Phosphothreonine
+P38994	YDR208W	MSS4	661	Phosphoserine
+Q02642	YPL037C	EGD1	151	Phosphothreonine
+P25588	YCL061C	MRC1	144	Phosphoserine
+P25588	YCL061C	MRC1	409	Phosphoserine
+P25588	YCL061C	MRC1	411	Phosphoserine
+P25588	YCL061C	MRC1	434	Phosphoserine
+P25588	YCL061C	MRC1	605	Phosphoserine
+P25588	YCL061C	MRC1	607	Phosphoserine
+P25588	YCL061C	MRC1	609	Phosphothreonine
+P25588	YCL061C	MRC1	801	Phosphoserine
+P25588	YCL061C	MRC1	807	Phosphoserine
+P25588	YCL061C	MRC1	911	Phosphoserine
+Q06815	YPR079W	MRL1	335	Phosphoserine
+Q06815	YPR079W	MRL1	339	Phosphoserine
+Q06815	YPR079W	MRL1	342	Phosphoserine
+Q06815	YPR079W	MRL1	371	Phosphoserine
+Q06815	YPR079W	MRL1	380	Phosphoserine
+Q06815	YPR079W	MRL1	116	N-linked
+Q06815	YPR079W	MRL1	136	N-linked
+Q06815	YPR079W	MRL1	178	N-linked
+Q06815	YPR079W	MRL1	215	N-linked
+P36157	YKR077W	MSA2	157	Phosphoserine
+P36157	YKR077W	MSA2	292	Phosphoserine
+P32334	YGR014W	MSB2	1300	Phosphoserine
+P32334	YGR014W	MSB2	30	N-linked
+P32334	YGR014W	MSB2	859	N-linked
+P32334	YGR014W	MSB2	885	N-linked
+P32334	YGR014W	MSB2	945	N-linked
+P32334	YGR014W	MSB2	1049	N-linked
+P32334	YGR014W	MSB2	1088	N-linked
+P32334	YGR014W	MSB2	1175	N-linked
+P38694	YHR039C	MSC7	15	N-linked
+P38694	YHR039C	MSC7	565	N-linked
+P38694	YHR039C	MSC7	627	N-linked
+P34232	YKL186C	MTR2	125	Phosphothreonine
+P48563	YNL297C	MON2	2	N-acetylalanine
+P48563	YNL297C	MON2	564	Phosphoserine
+P48563	YNL297C	MON2	567	Phosphoserine
+P48563	YNL297C	MON2	571	Phosphoserine
+Q05812	YLR219W	MSC3	57	Phosphoserine
+Q05812	YLR219W	MSC3	64	Phosphoserine
+Q05812	YLR219W	MSC3	127	Phosphoserine
+Q05812	YLR219W	MSC3	151	Phosphoserine
+Q05812	YLR219W	MSC3	155	Phosphoserine
+Q05812	YLR219W	MSC3	363	Phosphoserine
+Q05812	YLR219W	MSC3	646	Phosphothreonine
+Q05812	YLR219W	MSC3	660	Phosphoserine
+P53214	YGR023W	MTL1	481	Phosphoserine
+P53214	YGR023W	MTL1	482	Phosphoserine
+P29952	YER003C	PMI40	2	N-acetylserine
+P29952	YER003C	PMI40	107	Phosphoserine
+P10507	YLR163C	MAS1	243	Phosphoserine
+P21339	YOR188W	MSB1	538	Phosphoserine
+P21339	YOR188W	MSB1	776	Phosphoserine
+P21339	YOR188W	MSB1	816	Phosphoserine
+Q03104	YML128C	MSC1	237	Phosphothreonine
+Q03104	YML128C	MSC1	243	Phosphoserine
+P38590	YNL053W	MSG5	22	Phosphoserine
+P38590	YNL053W	MSG5	98	Phosphoserine
+P38590	YNL053W	MSG5	151	Phosphoserine
+P38590	YNL053W	MSG5	178	Phosphothreonine
+Q03834	YDR097C	MSH6	102	Phosphoserine
+Q03834	YDR097C	MSH6	145	Phosphoserine
+Q03834	YDR097C	MSH6	150	Phosphoserine
+Q03834	YDR097C	MSH6	201	Phosphoserine
+Q03834	YDR097C	MSH6	451	Phosphothreonine
+P33749	YKL062W	MSN4	1	N-acetylmethionine
+P33749	YKL062W	MSN4	178	Phosphoserine
+P33749	YKL062W	MSN4	263	Phosphoserine
+P33749	YKL062W	MSN4	316	Phosphoserine
+P33749	YKL062W	MSN4	319	Phosphoserine
+P33749	YKL062W	MSN4	479	Phosphothreonine
+P33749	YKL062W	MSN4	558	Phosphoserine
+P47047	YJL050W	MTR4	34	Phosphothreonine
+P47047	YJL050W	MTR4	84	Phosphoserine
+P47047	YJL050W	MTR4	843	Phosphoserine
+Q08750	YOR298W	MUM3	285	N-linked
+P19524	YOR326W	MYO2	2	N-acetylserine
+P19524	YOR326W	MYO2	1097	Phosphothreonine
+P19524	YOR326W	MYO2	1121	Phosphoserine
+P16603	YHR042W	NCP1	666	Glycyl
+Q06389	YDR373W	FRQ1	2	N-myristoyl
+P0CX80	YHR053C	CUP1-1	30	Glycyl
+Q04439	YMR109W	MYO5	357	Phosphoserine
+Q04439	YMR109W	MYO5	359	Phosphotyrosine
+Q04439	YMR109W	MYO5	777	Phosphoserine
+Q04439	YMR109W	MYO5	992	Phosphoserine
+Q04439	YMR109W	MYO5	1205	Phosphoserine
+Q12387	YOL076W	MDM20	2	N-acetylserine
+P12945	YDL040C	NAT1	2	N-acetylserine
+P12945	YDL040C	NAT1	674	Phosphoserine
+P52919	YLR457C	NBP1	251	Phosphoserine
+P52919	YLR457C	NBP1	260	Phosphoserine
+Q12163	YDR162C	NBP2	102	Phosphoserine
+Q12163	YDR162C	NBP2	196	Phosphoserine
+Q12163	YDR162C	NBP2	235	Phosphoserine
+Q12374	YPR155C	NCA2	29	Phosphoserine
+Q02866	YPL070W	MUK1	67	Phosphoserine
+Q02866	YPL070W	MUK1	163	Phosphoserine
+Q02866	YPL070W	MUK1	185	Phosphoserine
+Q02866	YPL070W	MUK1	245	Phosphoserine
+P25293	YKR048C	NAP1	20	Phosphothreonine
+P25293	YKR048C	NAP1	24	Phosphothreonine
+P25293	YKR048C	NAP1	27	Phosphoserine
+P25293	YKR048C	NAP1	53	Phosphothreonine
+P25293	YKR048C	NAP1	69	Phosphoserine
+P25293	YKR048C	NAP1	76	Phosphoserine
+P25293	YKR048C	NAP1	82	Phosphoserine
+P25293	YKR048C	NAP1	98	Phosphoserine
+P25293	YKR048C	NAP1	104	Phosphoserine
+P25293	YKR048C	NAP1	140	Phosphoserine
+P25293	YKR048C	NAP1	159	Phosphoserine%3B
+P25293	YKR048C	NAP1	177	Phosphoserine%3B
+P25293	YKR048C	NAP1	397	Phosphoserine%3B
+P25293	YKR048C	NAP1	50	Glycyl
+P42939	YGR206W	MVB12	1	N-acetylmethionine
+P42939	YGR206W	MVB12	94	Phosphoserine
+Q03735	YML117W	NAB6	2	N-acetylserine
+Q03735	YML117W	NAB6	464	Phosphoserine
+Q03735	YML117W	NAB6	467	Phosphoserine
+P53919	YNL124W	NAF1	255	Phosphoserine
+P30771	YMR080C	NAM7	56	Phosphoserine
+P30771	YMR080C	NAM7	869	Phosphoserine
+Q08229	YOL070C	NBA1	138	Phosphoserine
+Q08229	YOL070C	NBA1	208	Phosphoserine
+Q08229	YOL070C	NBA1	403	Phosphothreonine
+P38205	YBL024W	NCL1	426	Phosphothreonine
+P38205	YBL024W	NCL1	431	Phosphoserine
+P38205	YBL024W	NCL1	667	Phosphoserine
+P38996	YPL190C	NAB3	86	Phosphothreonine
+P38996	YPL190C	NAB3	451	Phosphothreonine
+P38879	YHR193C	EGD2	2	N-acetylserine
+P38879	YHR193C	EGD2	93	Phosphoserine
+Q08887	YOR372C	NDD1	319	Phosphothreonine%3B
+P36010	YKL067W	YNK1	95	Phosphothreonine
+P25374	YCL017C	NFS1	299	N6-(pyridoxal
+Q99271	YLR138W	NHA1	568	Phosphoserine
+Q99271	YLR138W	NHA1	765	Phosphothreonine
+Q99271	YLR138W	NHA1	768	Phosphoserine
+Q99271	YLR138W	NHA1	774	Phosphoserine
+P53914	YNL132W	KRE33	1001	Phosphoserine
+P53914	YNL132W	KRE33	1007	Phosphoserine
+P53914	YNL132W	KRE33	1010	Phosphoserine
+P40096	YER159C	BUR6	27	Phosphoserine
+P40096	YER159C	BUR6	141	Phosphoserine
+P32500	YML031W	NDC1	401	Phosphoserine
+P32500	YML031W	NDC1	412	Phosphoserine
+P40460	YIL144W	NDC80	38	Phosphothreonine
+P40460	YIL144W	NDC80	248	Phosphothreonine
+P32831	YBR212W	NGR1	1	N-acetylmethionine
+P32831	YBR212W	NGR1	524	Phosphoserine
+P39744	YOR206W	NOC2	70	Phosphoserine
+P39744	YOR206W	NOC2	149	Phosphoserine
+P39744	YOR206W	NOC2	160	Phosphoserine
+P39744	YOR206W	NOC2	166	Phosphoserine
+P39744	YOR206W	NOC2	698	Phosphoserine
+P39744	YOR206W	NOC2	708	Phosphoserine
+P25353	YCR026C	NPP1	161	N-linked
+P25353	YCR026C	NPP1	204	N-linked
+P25353	YCR026C	NPP1	264	N-linked
+P25353	YCR026C	NPP1	296	N-linked
+P25353	YCR026C	NPP1	403	N-linked
+P53718	YNR009W	NRM1	145	Phosphoserine
+Q08485	YOR071C	NRT1	560	Phosphoserine
+Q08485	YOR071C	NRT1	572	Phosphoserine
+P53898	YNL156C	NSG2	90	Phosphoserine
+Q12457	YDR026C	NSI1	64	Phosphothreonine
+P48234	YGR145W	ENP2	529	Phosphoserine
+P48234	YGR145W	ENP2	550	Phosphoserine
+P48234	YGR145W	ENP2	555	Phosphoserine
+Q07623	YDL213C	NOP6	45	Phosphoserine
+Q07623	YDL213C	NOP6	160	Phosphoserine
+P27476	YGR159C	NSR1	353	Asymmetric
+P27476	YGR159C	NSR1	362	Asymmetric
+P27476	YGR159C	NSR1	366	Asymmetric
+P27476	YGR159C	NSR1	375	Asymmetric
+P27476	YGR159C	NSR1	379	Asymmetric
+P27476	YGR159C	NSR1	382	Asymmetric
+Q08214	YOL043C	NTG2	194	Glycyl
+Q03210	YML118W	NGL3	62	Phosphoserine
+Q04121	YDR456W	NHX1	490	Phosphothreonine
+Q04121	YDR456W	NHX1	494	Phosphoserine
+Q04121	YDR456W	NHX1	498	Phosphothreonine
+Q04121	YDR456W	NHX1	499	Phosphoserine
+Q04121	YDR456W	NHX1	569	Phosphoserine
+Q04121	YDR456W	NHX1	420	N-linked
+Q04121	YDR456W	NHX1	515	N-linked
+Q04121	YDR456W	NHX1	550	N-linked
+Q04121	YDR456W	NHX1	563	N-linked
+P32770	YDL167C	NRP1	345	Phosphoserine
+P32770	YDL167C	NRP1	455	Phosphoserine
+P32770	YDL167C	NRP1	630	Phosphoserine
+P37838	YPL043W	NOP4	247	Phosphoserine
+P37838	YPL043W	NOP4	379	Phosphothreonine
+Q12080	YPL146C	NOP53	31	Phosphoserine
+P22211	YNL183C	NPR1	47	Phosphoserine%3B
+P22211	YNL183C	NPR1	85	Phosphoserine
+P22211	YNL183C	NPR1	90	Phosphoserine
+P22211	YNL183C	NPR1	100	Phosphoserine
+P22211	YNL183C	NPR1	111	Phosphoserine
+P22211	YNL183C	NPR1	116	Phosphoserine
+P22211	YNL183C	NPR1	125	Phosphoserine
+P22211	YNL183C	NPR1	137	Phosphoserine
+P22211	YNL183C	NPR1	141	Phosphoserine
+P22211	YNL183C	NPR1	257	Phosphoserine%3B
+P22211	YNL183C	NPR1	259	Phosphoserine
+P22211	YNL183C	NPR1	260	Phosphoserine
+P22211	YNL183C	NPR1	288	Phosphoserine
+P22211	YNL183C	NPR1	292	Phosphoserine
+P22211	YNL183C	NPR1	317	Phosphoserine
+P22211	YNL183C	NPR1	320	Phosphoserine
+P22211	YNL183C	NPR1	328	Phosphoserine
+P22211	YNL183C	NPR1	334	Phosphotyrosine
+P22211	YNL183C	NPR1	336	Phosphoserine
+P22211	YNL183C	NPR1	353	Phosphoserine
+P22211	YNL183C	NPR1	356	Phosphoserine
+P22211	YNL183C	NPR1	357	Phosphoserine%3B
+P22211	YNL183C	NPR1	385	Phosphoserine
+P53935	YNL091W	NST1	266	Phosphoserine
+Q12311	YPR031W	NTO1	728	Phosphoserine
+Q02629	YKL068W	NUP100	763	Phosphoserine
+Q02629	YKL068W	NUP100	783	Phosphoserine
+Q92317	YDR397C	NCB2	135	Phosphoserine
+Q92317	YDR397C	NCB2	137	Phosphoserine
+Q92317	YDR397C	NCB2	142	Phosphoserine
+P49954	YLR351C	NIT3	34	Phosphothreonine
+Q06178	YLR328W	NMA1	91	Phosphoserine
+Q06178	YLR328W	NMA1	95	Phosphoserine
+Q06178	YLR328W	NMA1	96	Phosphoserine
+Q06178	YLR328W	NMA1	111	Phosphoserine
+P46970	YJR132W	NMD5	977	Phosphoserine
+P53939	YNL078W	NIS1	260	Phosphoserine
+P53939	YNL078W	NIS1	264	Phosphoserine
+P53939	YNL078W	NIS1	300	Phosphoserine
+P53939	YNL078W	NIS1	302	Phosphoserine
+P34909	YER068W	MOT2	310	Phosphothreonine
+P34909	YER068W	MOT2	312	Phosphoserine
+P34909	YER068W	MOT2	326	Phosphothreonine
+P34909	YER068W	MOT2	360	Phosphoserine
+P34909	YER068W	MOT2	270	Glycyl
+P32494	YDR176W	NGG1	134	Phosphoserine
+P32494	YDR176W	NGG1	407	Phosphoserine
+P32494	YDR176W	NGG1	464	Phosphothreonine
+Q6Q547	YHR072W-A	NOP10	36	Phosphoserine
+Q6Q547	YHR072W-A	NOP10	28	Glycyl
+Q01560	YDR432W	NPL3	182	Phosphoserine
+Q01560	YDR432W	NPL3	224	Phosphoserine
+Q12499	YOR310C	NOP58	281	Glycyl
+P39923	YEL062W	NPR2	362	Phosphoserine
+Q08972	YPL226W	NEW1	443	Phosphoserine
+Q08972	YPL226W	NEW1	1191	Phosphothreonine
+P0CE68	YKR103W	NFT1	4	N-linked
+Q03435	YDL002C	NHP10	2	N-acetylserine
+P53253	YGR089W	NNF2	10	Glycyl
+Q08208	YOL041C	NOP12	70	Phosphoserine
+Q08208	YOL041C	NOP12	181	Phosphothreonine
+Q08208	YOL041C	NOP12	184	Phosphoserine
+Q12460	YLR197W	NOP56	321	Phosphoserine
+P47035	YJL076W	NET1	60	Phosphoserine
+P47035	YJL076W	NET1	166	Phosphoserine
+P47035	YJL076W	NET1	231	Phosphoserine
+P47035	YJL076W	NET1	252	Phosphoserine
+P47035	YJL076W	NET1	437	Phosphoserine
+P47035	YJL076W	NET1	439	Phosphoserine
+P47035	YJL076W	NET1	447	Phosphoserine
+P47035	YJL076W	NET1	452	Phosphoserine
+P47035	YJL076W	NET1	497	Phosphoserine
+P47035	YJL076W	NET1	676	Phosphothreonine
+P47035	YJL076W	NET1	830	Phosphoserine
+P47035	YJL076W	NET1	1042	Phosphothreonine
+P47035	YJL076W	NET1	1056	Phosphoserine
+P47035	YJL076W	NET1	1059	Phosphoserine
+Q07896	YLR002C	NOC3	395	Phosphoserine
+Q03790	YMR153W	NUP53	2	N-acetylalanine
+Q03790	YMR153W	NUP53	101	Phosphoserine
+Q03790	YMR153W	NUP53	297	Phosphoserine
+Q03790	YMR153W	NUP53	438	Phosphoserine
+Q12493	YDR383C	NKP1	222	Phosphoserine
+P36003	YKL171W	NNK1	178	Phosphoserine
+P36003	YKL171W	NNK1	179	Phosphoserine
+P36003	YKL171W	NNK1	405	Phosphoserine
+P36003	YKL171W	NNK1	426	Phosphoserine
+P36003	YKL171W	NNK1	737	Phosphoserine
+P36003	YKL171W	NNK1	739	Phosphotyrosine
+Q02892	YPL093W	NOG1	563	Phosphoserine
+Q12514	YPR072W	NOT5	306	Phosphothreonine
+Q12514	YPR072W	NOT5	377	Phosphoserine
+Q12514	YPR072W	NOT5	338	Glycyl
+P38742	YHL023C	NPR3	76	Phosphoserine
+P38742	YHL023C	NPR3	486	Phosphoserine
+P38742	YHL023C	NPR3	987	Phosphoserine
+P32499	YLR335W	NUP2	17	Phosphoserine
+P32499	YLR335W	NUP2	20	Phosphoserine
+P32499	YLR335W	NUP2	137	Phosphoserine
+P32499	YLR335W	NUP2	165	Phosphoserine
+P32499	YLR335W	NUP2	203	Phosphoserine
+P32499	YLR335W	NUP2	205	Phosphoserine
+P32499	YLR335W	NUP2	348	Phosphoserine
+P32499	YLR335W	NUP2	351	Phosphoserine
+P32499	YLR335W	NUP2	361	Phosphothreonine
+P32499	YLR335W	NUP2	581	Phosphoserine
+P32499	YLR335W	NUP2	590	Phosphothreonine
+P49686	YDR192C	NUP42	137	Phosphoserine
+P49686	YDR192C	NUP42	298	Phosphoserine
+Q05166	YDL088C	ASM4	458	Phosphoserine
+Q05166	YDL088C	ASM4	464	Phosphoserine
+Q12066	YDL089W	NUR1	3	Phosphoserine
+Q12066	YDL089W	NUR1	417	Phosphoserine
+Q12066	YDL089W	NUR1	474	Phosphoserine
+P39720	YAL051W	OAF1	155	Phosphoserine
+P53949	YNL056W	OCA2	181	Phosphoserine
+P38837	YHR133C	NSG1	39	Phosphoserine
+P38837	YHR133C	NSG1	76	Phosphoserine
+Q12143	YPL233W	NSL1	2	N-acetylserine
+P14907	YJL041W	NSP1	238	Phosphoserine
+P14907	YJL041W	NSP1	361	Phosphoserine
+P14907	YJL041W	NSP1	456	Phosphoserine
+P14907	YJL041W	NSP1	631	Phosphoserine
+P35729	YKL057C	NUP120	417	Phosphothreonine
+P40064	YER105C	NUP157	1	N-acetylmethionine
+P40064	YER105C	NUP157	1034	Phosphoserine
+P40477	YIL115C	NUP159	404	Phosphoserine
+P40477	YIL115C	NUP159	657	Phosphoserine
+P40477	YIL115C	NUP159	724	Phosphoserine
+P40477	YIL115C	NUP159	735	Phosphoserine
+P40477	YIL115C	NUP159	745	Phosphoserine
+P40477	YIL115C	NUP159	803	Phosphothreonine
+P40477	YIL115C	NUP159	805	Phosphoserine
+P40477	YIL115C	NUP159	819	Phosphoserine
+P40477	YIL115C	NUP159	889	Phosphoserine
+P40477	YIL115C	NUP159	940	Phosphoserine
+P40010	YER006W	NUG1	337	Phosphoserine
+Q00402	YDR150W	NUM1	611	Phosphoserine
+Q00402	YDR150W	NUM1	675	Phosphoserine
+Q00402	YDR150W	NUM1	746	Phosphoserine
+Q00402	YDR150W	NUM1	881	Phosphoserine
+Q00402	YDR150W	NUM1	945	Phosphoserine
+Q00402	YDR150W	NUM1	1009	Phosphoserine
+Q00402	YDR150W	NUM1	1201	Phosphoserine
+Q00402	YDR150W	NUM1	1265	Phosphoserine
+Q00402	YDR150W	NUM1	1329	Phosphoserine
+Q00402	YDR150W	NUM1	2162	Phosphoserine
+Q00402	YDR150W	NUM1	2164	Phosphoserine
+Q00402	YDR150W	NUM1	2197	Phosphoserine
+Q00402	YDR150W	NUM1	2217	Phosphoserine
+Q00402	YDR150W	NUM1	2220	Phosphoserine
+Q00402	YDR150W	NUM1	2221	Phosphoserine
+Q00402	YDR150W	NUM1	2360	Phosphoserine
+Q00402	YDR150W	NUM1	2424	Phosphoserine
+Q00402	YDR150W	NUM1	2494	Phosphoserine
+Q00402	YDR150W	NUM1	2545	Phosphoserine
+P39705	YAR002W	NUP60	10	Phosphoserine
+P39705	YAR002W	NUP60	49	Phosphoserine
+P39705	YAR002W	NUP60	81	Phosphoserine
+P39705	YAR002W	NUP60	89	Phosphoserine
+P39705	YAR002W	NUP60	162	Phosphoserine
+P39705	YAR002W	NUP60	171	Phosphoserine
+P39705	YAR002W	NUP60	214	Phosphoserine
+P39705	YAR002W	NUP60	222	Phosphoserine
+P39705	YAR002W	NUP60	352	Phosphoserine
+P39705	YAR002W	NUP60	360	Phosphoserine
+P39705	YAR002W	NUP60	374	Phosphoserine
+P39705	YAR002W	NUP60	382	Phosphoserine
+P39705	YAR002W	NUP60	460	Phosphothreonine
+P39705	YAR002W	NUP60	480	Phosphoserine
+P39705	YAR002W	NUP60	483	Phosphoserine
+P38881	YHR195W	NVJ1	156	Phosphoserine
+P38881	YHR195W	NVJ1	199	Phosphoserine
+P38881	YHR195W	NVJ1	285	Phosphoserine
+P38881	YHR195W	NVJ1	298	Phosphoserine
+P38302	YBR188C	NTC20	139	Phosphoserine
+P31378	YAL015C	NTG1	194	Glycyl
+P49687	YGL092W	NUP145	273	Phosphoserine
+P49687	YGL092W	NUP145	403	Phosphoserine
+P49687	YGL092W	NUP145	404	Phosphoserine
+P49687	YGL092W	NUP145	414	Phosphoserine
+P49687	YGL092W	NUP145	667	Phosphoserine
+P49687	YGL092W	NUP145	679	Phosphoserine
+P49687	YGL092W	NUP145	689	Phosphoserine
+P49687	YGL092W	NUP145	751	Phosphothreonine
+P38219	YBR025C	OLA1	89	Phosphothreonine
+P38219	YBR025C	OLA1	116	Phosphoserine
+P38219	YBR025C	OLA1	119	Phosphoserine
+P38219	YBR025C	OLA1	98	Glycyl
+P53204	YGR010W	NMA2	85	Phosphoserine
+P53204	YGR010W	NMA2	89	Phosphoserine
+P53204	YGR010W	NMA2	90	Phosphoserine
+P53883	YNL175C	NOP13	2	N-acetylserine
+P53883	YNL175C	NOP13	2	Phosphoserine
+P53883	YNL175C	NOP13	105	Phosphothreonine
+P53883	YNL175C	NOP13	335	Phosphoserine
+P25655	YCR093W	CDC39	2102	Phosphothreonine
+P06102	YIL038C	NOT3	303	Phosphoserine
+P06102	YIL038C	NOT3	307	Phosphoserine
+P06102	YIL038C	NOT3	322	Phosphoserine
+P06102	YIL038C	NOT3	446	Phosphoserine
+P06102	YIL038C	NOT3	450	Phosphoserine
+P06102	YIL038C	NOT3	565	Phosphoserine
+P06102	YIL038C	NOT3	569	Phosphoserine
+P06102	YIL038C	NOT3	571	Phosphothreonine
+P06102	YIL038C	NOT3	657	Phosphoserine
+P06102	YIL038C	NOT3	535	Glycyl
+P39997	YEL016C	NPP2	62	N-linked
+P39997	YEL016C	NPP2	69	N-linked
+P39997	YEL016C	NPP2	112	N-linked
+P39997	YEL016C	NPP2	153	N-linked
+P39997	YEL016C	NPP2	441	N-linked
+P53617	YNL251C	NRD1	263	Phosphoserine
+P53617	YNL251C	NRD1	265	Phosphoserine
+P53617	YNL251C	NRD1	271	Phosphoserine
+P40007	YER002W	NOP16	176	Phosphoserine
+P40007	YER002W	NOP16	178	Phosphoserine
+P40991	YNL061W	NOP2	580	Phosphoserine
+Q08287	YOL144W	NOP8	234	Phosphoserine
+Q08287	YOL144W	NOP8	239	Phosphoserine
+Q08287	YOL144W	NOP8	268	Phosphoserine
+Q08287	YOL144W	NOP8	370	Phosphoserine
+Q04958	YML059C	NTE1	300	Phosphoserine
+Q04958	YML059C	NTE1	312	Phosphoserine
+Q04958	YML059C	NTE1	632	Phosphoserine
+Q04958	YML059C	NTE1	634	Phosphoserine
+Q04958	YML059C	NTE1	653	Phosphoserine
+Q04958	YML059C	NTE1	661	Phosphoserine
+Q04958	YML059C	NTE1	670	Phosphoserine
+Q04958	YML059C	NTE1	680	Phosphoserine
+Q04958	YML059C	NTE1	739	Phosphoserine
+Q04958	YML059C	NTE1	803	Phosphothreonine
+P33331	YER009W	NTF2	2	N-acetylserine
+P33331	YER009W	NTF2	53	Glycyl
+P36118	YKR022C	NTR2	40	Phosphoserine
+P36118	YKR022C	NTR2	153	Phosphoserine
+P36118	YKR022C	NTR2	197	Phosphoserine
+P36161	YKR082W	NUP133	2	N-acetylserine
+P38181	YBL079W	NUP170	1247	Phosphoserine
+P53742	YNR053C	NOG2	60	Phosphoserine
+P53742	YNR053C	NOG2	85	Phosphoserine
+P53742	YNR053C	NOG2	155	Phosphoserine
+Q12200	YPL006W	NCR1	123	N-linked
+Q12200	YPL006W	NCR1	145	N-linked
+Q12200	YPL006W	NCR1	178	N-linked
+Q12200	YPL006W	NCR1	314	N-linked
+Q12200	YPL006W	NCR1	401	N-linked
+Q12200	YPL006W	NCR1	513	N-linked
+Q12200	YPL006W	NCR1	900	N-linked
+Q12200	YPL006W	NCR1	940	N-linked
+Q03125	YDR043C	NRG1	163	Phosphoserine
+P51533	YOR328W	PDR10	754	N-linked
+Q02785	YPL058C	PDR12	2	N-acetylserine
+Q02785	YPL058C	PDR12	32	Phosphoserine
+Q02785	YPL058C	PDR12	52	Phosphoserine
+Q02785	YPL058C	PDR12	56	Phosphoserine
+Q02785	YPL058C	PDR12	1405	N-linked
+Q02785	YPL058C	PDR12	426	Glycyl
+Q07418	YDL065C	PEX19	62	Phosphoserine
+Q07418	YDL065C	PEX19	304	Phosphoserine
+Q07418	YDL065C	PEX19	339	Cysteine
+Q07418	YDL065C	PEX19	339	S-farnesyl
+Q06169	YLR324W	PEX30	2	N-acetylserine
+Q06169	YLR324W	PEX30	52	Phosphoserine
+Q06169	YLR324W	PEX30	420	Phosphoserine
+Q06169	YLR324W	PEX30	424	Phosphoserine
+P07269	YDL106C	PHO2	542	Phosphothreonine
+P17442	YGR233C	PHO81	956	Phosphoserine
+P25360	YCR037C	PHO87	162	N-linked
+P25360	YCR037C	PHO87	202	N-linked
+P25360	YCR037C	PHO87	274	N-linked
+P25360	YCR037C	PHO87	102	Glycyl
+Q12057	YOR104W	PIN2	141	Phosphothreonine
+Q12057	YOR104W	PIN2	91	N-linked
+Q12057	YOR104W	PIN2	132	N-linked
+Q12057	YOR104W	PIN2	276	N-linked
+Q03407	YDR490C	PKH1	294	Phosphoserine
+Q03407	YDR490C	PKH1	296	Phosphoserine
+P39105	YMR008C	PLB1	634	GPI-anchor
+P39105	YMR008C	PLB1	26	N-linked
+P39105	YMR008C	PLB1	33	N-linked
+P39105	YMR008C	PLB1	52	N-linked
+P39105	YMR008C	PLB1	78	N-linked
+P39105	YMR008C	PLB1	92	N-linked
+P39105	YMR008C	PLB1	123	N-linked
+P39105	YMR008C	PLB1	160	N-linked
+P39105	YMR008C	PLB1	170	N-linked
+P39105	YMR008C	PLB1	215	N-linked
+P39105	YMR008C	PLB1	277	N-linked
+P39105	YMR008C	PLB1	307	N-linked
+P39105	YMR008C	PLB1	345	N-linked
+P39105	YMR008C	PLB1	388	N-linked
+P39105	YMR008C	PLB1	459	N-linked
+P39105	YMR008C	PLB1	489	N-linked
+P39105	YMR008C	PLB1	513	N-linked
+P39105	YMR008C	PLB1	541	N-linked
+P39105	YMR008C	PLB1	565	N-linked
+P39105	YMR008C	PLB1	582	N-linked
+Q03674	YMR006C	PLB2	680	GPI-anchor
+Q03674	YMR006C	PLB2	47	N-linked
+Q03674	YMR006C	PLB2	80	N-linked
+Q03674	YMR006C	PLB2	94	N-linked
+Q03674	YMR006C	PLB2	125	N-linked
+Q03674	YMR006C	PLB2	162	N-linked
+Q03674	YMR006C	PLB2	181	N-linked
+Q03674	YMR006C	PLB2	193	N-linked
+Q03674	YMR006C	PLB2	217	N-linked
+Q03674	YMR006C	PLB2	279	N-linked
+Q03674	YMR006C	PLB2	309	N-linked
+Q03674	YMR006C	PLB2	365	N-linked
+Q03674	YMR006C	PLB2	390	N-linked
+Q03674	YMR006C	PLB2	491	N-linked
+Q03674	YMR006C	PLB2	515	N-linked
+Q03674	YMR006C	PLB2	524	N-linked
+Q03674	YMR006C	PLB2	543	N-linked
+Q03674	YMR006C	PLB2	567	N-linked
+Q03674	YMR006C	PLB2	584	N-linked
+Q03674	YMR006C	PLB2	598	N-linked
+Q03674	YMR006C	PLB2	630	N-linked
+Q03674	YMR006C	PLB2	634	N-linked
+Q03674	YMR006C	PLB2	642	N-linked
+Q03674	YMR006C	PLB2	648	N-linked
+Q03674	YMR006C	PLB2	652	N-linked
+Q03674	YMR006C	PLB2	658	N-linked
+P27801	YLR148W	PEP3	907	Phosphoserine
+P40335	YJL053W	PEP8	216	Phosphoserine
+P53203	YGR004W	PEX31	432	Phosphoserine
+P53203	YGR004W	PEX31	435	Phosphothreonine
+P46988	YJL179W	PFD1	2	N-acetylserine
+P52553	YLR200W	YKE2	2	N-acetylserine
+P07270	YFR034C	PHO4	100	Phosphoserine%3B
+P07270	YFR034C	PHO4	114	Phosphoserine%3B
+P07270	YFR034C	PHO4	128	Phosphoserine%3B
+P07270	YFR034C	PHO4	152	Phosphoserine%3B
+P07270	YFR034C	PHO4	204	Phosphoserine
+P07270	YFR034C	PHO4	223	Phosphoserine%3B
+P07270	YFR034C	PHO4	242	Phosphoserine
+P07270	YFR034C	PHO4	243	Phosphoserine
+P20052	YOL001W	PHO80	234	Phosphoserine%3B
+P20052	YOL001W	PHO80	267	Phosphoserine%3B
+P06738	YPR160W	GPH1	31	Phosphothreonine
+P06738	YPR160W	GPH1	333	Phosphoserine
+P06738	YPR160W	GPH1	751	N6-(pyridoxal
+P40187	YIL045W	PIG2	162	Phosphoserine
+P40187	YIL045W	PIG2	196	Phosphoserine
+P40187	YIL045W	PIG2	296	Phosphoserine
+P40187	YIL045W	PIG2	304	Phosphoserine
+Q12252	YOL084W	PHM7	115	N-linked
+Q12252	YOL084W	PHM7	132	N-linked
+P53297	YGR178C	PBP1	106	Phosphoserine
+P53297	YGR178C	PBP1	193	Phosphothreonine
+P53297	YGR178C	PBP1	215	Phosphoserine
+P53297	YGR178C	PBP1	436	Phosphoserine
+P53297	YGR178C	PBP1	344	Glycyl
+P06169	YLR044C	PDC1	2	N-acetylserine
+P06169	YLR044C	PDC1	223	Phosphoserine
+P06169	YLR044C	PDC1	266	Phosphothreonine
+P06169	YLR044C	PDC1	336	Phosphothreonine
+P06169	YLR044C	PDC1	353	Phosphothreonine
+P06169	YLR044C	PDC1	522	Phosphothreonine
+P06169	YLR044C	PDC1	526	Phosphoserine
+P06169	YLR044C	PDC1	212	Glycyl
+P06169	YLR044C	PDC1	233	Glycyl
+P06169	YLR044C	PDC1	269	Glycyl
+P06169	YLR044C	PDC1	332	Glycyl
+P06169	YLR044C	PDC1	484	Glycyl
+P06169	YLR044C	PDC1	505	Glycyl
+P06169	YLR044C	PDC1	520	Glycyl
+P38848	YHR150W	PEX28	361	N-linked
+P35056	YDR244W	PEX5	1	N-acetylmethionine
+P35056	YDR244W	PEX5	61	Phosphoserine
+P35056	YDR244W	PEX5	6	Glycyl
+P35056	YDR244W	PEX5	18	Glycyl
+P35056	YDR244W	PEX5	24	Glycyl
+P53900	YNL153C	GIM3	1	N-acetylmethionine
+P53896	YNL158W	PGA1	72	N-linked
+P53896	YNL158W	PGA1	80	N-linked
+P32854	YOR036W	PEP12	2	Phosphoserine
+P32854	YOR036W	PEP12	23	Phosphoserine
+Q02969	YPL112C	PEX25	58	Phosphoserine
+Q02969	YPL112C	PEX25	63	Phosphoserine
+Q02969	YPL112C	PEX25	289	Phosphoserine
+P53903	YNL149C	PGA2	2	N-acetylserine
+P53903	YNL149C	PGA2	119	Phosphoserine
+P07271	YML061C	PIF1	70	Phosphoserine
+P07271	YML061C	PIF1	72	Phosphoserine
+P07271	YML061C	PIF1	169	Phosphoserine
+P07271	YML061C	PIF1	584	Phosphoserine
+P14242	YNL082W	PMS1	393	Phosphoserine
+P14242	YNL082W	PMS1	566	Phosphoserine
+P47190	YOR321W	PMT3	124	N-linked
+P47190	YOR321W	PMT3	324	N-linked
+P47190	YOR321W	PMT3	398	N-linked
+P52867	YDL093W	PMT5	33	N-linked
+P52867	YDL093W	PMT5	213	N-linked
+P52867	YDL093W	PMT5	380	N-linked
+P52867	YDL093W	PMT5	386	N-linked
+P42934	YGR199W	PMT6	2	N-acetylserine
+P42934	YGR199W	PMT6	156	N-linked
+P42934	YGR199W	PMT6	404	N-linked
+P42934	YGR199W	PMT6	481	N-linked
+Q05788	YLR209C	PNP1	2	N-acetylserine
+Q05788	YLR209C	PNP1	275	Phosphoserine
+P47180	YJR153W	PGU1	318	N-linked
+P47180	YJR153W	PGU1	330	N-linked
+P37012	YMR105C	PGM2	2	N-acetylserine
+P37012	YMR105C	PGM2	111	Phosphothreonine
+P37012	YMR105C	PGM2	117	Phosphothreonine
+P37012	YMR105C	PGM2	119	Phosphoserine
+Q03262	YMR278W	PRM15	158	Phosphoserine
+P25297	YML123C	PHO84	302	Phosphothreonine
+P25297	YML123C	PHO84	303	Phosphoserine
+P25297	YML123C	PHO84	316	Phosphoserine
+P25297	YML123C	PHO84	317	Phosphothreonine
+P25297	YML123C	PHO84	321	Phosphoserine
+P25297	YML123C	PHO84	577	Phosphoserine
+P25297	YML123C	PHO84	579	Phosphoserine
+P25297	YML123C	PHO84	581	Phosphoserine
+P25297	YML123C	PHO84	6	Glycyl
+P25297	YML123C	PHO84	298	Glycyl
+P38264	YBR106W	PHO88	157	Phosphoserine
+P27514	YNR013C	PHO91	295	Phosphoserine
+P27514	YNR013C	PHO91	311	Phosphoserine
+P27514	YNR013C	PHO91	312	Phosphoserine
+Q03306	YDR466W	PKH3	696	Phosphoserine
+Q03306	YDR466W	PKH3	753	Phosphoserine
+Q03306	YDR466W	PKH3	871	Phosphoserine
+P05030	YGL008C	PMA1	61	Phosphoserine
+P05030	YGL008C	PMA1	175	Phosphothreonine
+P05030	YGL008C	PMA1	911	Phosphoserine
+P05030	YGL008C	PMA1	912	Phosphothreonine
+P05030	YGL008C	PMA1	918	Phosphothreonine
+P05030	YGL008C	PMA1	252	Glycyl
+P05030	YGL008C	PMA1	555	Glycyl
+P53261	YGR103W	NOP7	288	Phosphoserine
+P53261	YGR103W	NOP7	308	Phosphothreonine
+P16861	YGR240C	PFK1	3	Phosphoserine
+P16861	YGR240C	PFK1	166	Phosphoserine
+P16861	YGR240C	PFK1	179	Phosphoserine
+P16861	YGR240C	PFK1	185	Phosphoserine
+P16861	YGR240C	PFK1	189	Phosphoserine
+P16861	YGR240C	PFK1	192	Phosphoserine
+P16861	YGR240C	PFK1	217	Phosphoserine
+P16861	YGR240C	PFK1	450	Phosphothreonine
+P16861	YGR240C	PFK1	89	Glycyl
+P16861	YGR240C	PFK1	625	Glycyl
+P16862	YMR205C	PFK2	152	Phosphothreonine
+P16862	YMR205C	PFK2	163	Phosphoserine
+P16862	YMR205C	PFK2	171	Phosphoserine
+P16862	YMR205C	PFK2	803	Phosphoserine
+P00560	YCR012W	PGK1	2	N-acetylserine
+P00560	YCR012W	PGK1	93	Phosphothreonine
+P00560	YCR012W	PGK1	110	Phosphoserine
+P00560	YCR012W	PGK1	130	Phosphoserine
+P00560	YCR012W	PGK1	154	Phosphoserine
+P00560	YCR012W	PGK1	172	Phosphoserine
+P00560	YCR012W	PGK1	203	Phosphothreonine
+P00560	YCR012W	PGK1	241	Phosphothreonine
+P00560	YCR012W	PGK1	298	Phosphothreonine
+P00560	YCR012W	PGK1	318	Phosphoserine
+P00560	YCR012W	PGK1	331	Phosphothreonine
+P00560	YCR012W	PGK1	392	Phosphothreonine
+P00560	YCR012W	PGK1	82	Glycyl
+P00560	YCR012W	PGK1	197	Glycyl
+P00560	YCR012W	PGK1	258	Glycyl
+P00560	YCR012W	PGK1	274	Glycyl
+P00560	YCR012W	PGK1	302	Glycyl
+P33401	YKL127W	PGM1	2	N-acetylserine
+P33401	YKL127W	PGM1	120	Phosphoserine
+P38244	YBR074W	PFF1	96	N-linked
+P38244	YBR074W	PFF1	121	N-linked
+P38244	YBR074W	PFF1	189	N-linked
+P38244	YBR074W	PFF1	217	N-linked
+P38244	YBR074W	PFF1	656	N-linked
+P38244	YBR074W	PFF1	768	N-linked
+P38244	YBR074W	PFF1	796	N-linked
+P38244	YBR074W	PFF1	811	N-linked
+P38244	YBR074W	PFF1	866	N-linked
+P38244	YBR074W	PFF1	937	N-linked
+P39104	YNL267W	PIK1	10	Phosphoserine
+P39104	YNL267W	PIK1	236	Phosphoserine
+P39104	YNL267W	PIK1	384	Phosphoserine
+P39104	YNL267W	PIK1	394	Phosphothreonine
+P39104	YNL267W	PIK1	396	Phosphoserine
+P39104	YNL267W	PIK1	592	Phosphoserine
+P53252	YGR086C	PIL1	14	Phosphothreonine
+P53252	YGR086C	PIL1	16	Phosphoserine
+P53252	YGR086C	PIL1	45	Phosphoserine
+P53252	YGR086C	PIL1	98	Phosphoserine
+P53252	YGR086C	PIL1	163	Phosphoserine
+P53252	YGR086C	PIL1	230	Phosphoserine
+P53252	YGR086C	PIL1	233	Phosphothreonine
+P53252	YGR086C	PIL1	299	Phosphoserine
+P53252	YGR086C	PIL1	29	Glycyl
+Q12236	YOL100W	PKH2	138	Phosphoserine
+Q12236	YOL100W	PKH2	619	Phosphoserine
+Q12236	YOL100W	PKH2	1009	Phosphoserine
+Q04383	YDR501W	PLM2	281	Phosphoserine
+Q04383	YDR501W	PLM2	295	Phosphoserine
+Q04383	YDR501W	PLM2	302	Phosphoserine
+Q04383	YDR501W	PLM2	384	Phosphoserine
+Q12412	YOR161C	PNS1	259	N-linked
+Q12445	YLR018C	POM34	270	Phosphoserine
+Q12445	YLR018C	POM34	273	Phosphothreonine
+Q12445	YLR018C	POM34	292	Phosphoserine
+Q12445	YLR018C	POM34	294	Phosphoserine
+P23287	YLR433C	CNA1	2	N-acetylserine
+P39966	YER089C	PTC2	376	Phosphothreonine
+P39966	YER089C	PTC2	380	Phosphothreonine
+P11491	YDR481C	PHO8	123	Phosphoserine
+P11491	YDR481C	PHO8	268	N-linked
+P11491	YDR481C	PHO8	401	N-linked
+Q04004	YDR183W	PLP1	1	N-acetylmethionine
+P32634	YER132C	PMD1	298	Phosphothreonine
+P32634	YER132C	PMD1	838	Phosphoserine
+P32634	YER132C	PMD1	1289	Phosphoserine
+P32634	YER132C	PMD1	1307	Phosphoserine
+P32634	YER132C	PMD1	1356	Phosphoserine
+P32634	YER132C	PMD1	1664	Phosphoserine
+Q06644	YDR307W	PMT7	347	N-linked
+Q99216	YOR145C	PNO1	47	Phosphoserine
+Q99216	YOR145C	PNO1	51	Phosphothreonine
+P38693	YHR215W	PHO12	97	N-linked
+P38693	YHR215W	PHO12	162	N-linked
+P38693	YHR215W	PHO12	192	N-linked
+P38693	YHR215W	PHO12	250	N-linked
+P38693	YHR215W	PHO12	315	N-linked
+P38693	YHR215W	PHO12	356	N-linked
+P38693	YHR215W	PHO12	390	N-linked
+P38693	YHR215W	PHO12	439	N-linked
+P38693	YHR215W	PHO12	445	N-linked
+P38693	YHR215W	PHO12	461	N-linked
+Q08108	YOL011W	PLB3	659	GPI-anchor
+Q08108	YOL011W	PLB3	56	N-linked
+Q08108	YOL011W	PLB3	82	N-linked
+Q08108	YOL011W	PLB3	129	N-linked
+Q08108	YOL011W	PLB3	166	N-linked
+Q08108	YOL011W	PLB3	221	N-linked
+Q08108	YOL011W	PLB3	283	N-linked
+Q08108	YOL011W	PLB3	313	N-linked
+Q08108	YOL011W	PLB3	351	N-linked
+Q08108	YOL011W	PLB3	495	N-linked
+Q08108	YOL011W	PLB3	519	N-linked
+Q08108	YOL011W	PLB3	547	N-linked
+Q08108	YOL011W	PLB3	571	N-linked
+Q08108	YOL011W	PLB3	588	N-linked
+Q08108	YOL011W	PLB3	614	N-linked
+P41812	YNL221C	POP1	524	Phosphothreonine
+P00950	YKL152C	GPM1	12	Phosphoserine
+P00950	YKL152C	GPM1	49	Phosphotyrosine
+P00950	YKL152C	GPM1	116	Phosphoserine
+P00950	YKL152C	GPM1	127	Phosphoserine
+P00950	YKL152C	GPM1	128	Phosphoserine
+P00950	YKL152C	GPM1	185	Phosphoserine
+P00950	YKL152C	GPM1	197	Phosphoserine
+P00950	YKL152C	GPM1	31	Glycyl
+P00950	YKL152C	GPM1	57	Glycyl
+P00950	YKL152C	GPM1	71	Glycyl
+P00950	YKL152C	GPM1	139	Glycyl
+P00950	YKL152C	GPM1	175	Glycyl
+P00950	YKL152C	GPM1	191	Glycyl
+P33775	YDL095W	PMT1	2	N-acetylserine
+P33775	YDL095W	PMT1	390	N-linked
+P33775	YDL095W	PMT1	513	N-linked
+P33775	YDL095W	PMT1	743	N-linked
+P31382	YAL023C	PMT2	2	N-acetylserine
+P31382	YAL023C	PMT2	32	Phosphoserine
+P31382	YAL023C	PMT2	38	Phosphoserine
+P31382	YAL023C	PMT2	39	Phosphoserine
+P31382	YAL023C	PMT2	131	N-linked
+P31382	YAL023C	PMT2	155	N-linked
+P31382	YAL023C	PMT2	403	N-linked
+P46971	YJR143C	PMT4	759	N-linked
+P39685	YMR129W	POM152	45	Phosphoserine
+P39685	YMR129W	POM152	60	Phosphoserine
+P39685	YMR129W	POM152	280	N-linked
+P23594	YDL134C	PPH21	369	Leucine
+P00635	YBR093C	PHO5	97	N-linked
+P00635	YBR093C	PHO5	103	N-linked
+P00635	YBR093C	PHO5	162	N-linked
+P00635	YBR093C	PHO5	192	N-linked
+P00635	YBR093C	PHO5	250	N-linked
+P00635	YBR093C	PHO5	315	N-linked
+P00635	YBR093C	PHO5	356	N-linked
+P00635	YBR093C	PHO5	390	N-linked
+P00635	YBR093C	PHO5	439	N-linked
+P00635	YBR093C	PHO5	445	N-linked
+P00635	YBR093C	PHO5	456	N-linked
+P00635	YBR093C	PHO5	461	N-linked
+P40035	YER053C	PIC2	1	N-acetylmethionine
+P40473	YIL122W	POG1	152	Phosphoserine
+P40473	YIL122W	POG1	168	Phosphoserine
+P40473	YIL122W	POG1	314	Phosphoserine
+P39008	YNR052C	POP2	1	N-acetylmethionine
+P39008	YNR052C	POP2	97	Phosphothreonine%3B
+P17157	YPL031C	PHO85	18	Phosphotyrosine
+P17157	YPL031C	PHO85	289	Glycyl
+P53191	YGL023C	PIB2	46	Phosphoserine
+P53191	YGL023C	PIB2	53	Phosphoserine
+P53191	YGL023C	PIB2	56	Phosphothreonine
+P53191	YGL023C	PIB2	73	Phosphoserine
+P53191	YGL023C	PIB2	113	Phosphoserine
+P53191	YGL023C	PIB2	124	Phosphoserine
+P53191	YGL023C	PIB2	148	Phosphoserine
+P53191	YGL023C	PIB2	165	Phosphoserine
+P53191	YGL023C	PIB2	174	Phosphoserine
+P53191	YGL023C	PIB2	300	Phosphoserine
+P53191	YGL023C	PIB2	309	Phosphoserine
+P53191	YGL023C	PIB2	381	Phosphoserine
+P07283	YFL045C	SEC53	240	Phosphoserine
+P38336	YBR257W	POP4	64	Phosphoserine
+P38291	YBR167C	POP7	115	Phosphoserine
+P23595	YDL188C	PPH22	38	Phosphoserine
+P23595	YDL188C	PPH22	43	Phosphothreonine
+P23595	YDL188C	PPH22	377	Leucine
+P34221	YBL056W	PTC3	324	Phosphoserine
+P34221	YBL056W	PTC3	332	Phosphoserine
+P35842	YAR071W	PHO11	97	N-linked
+P35842	YAR071W	PHO11	162	N-linked
+P35842	YAR071W	PHO11	192	N-linked
+P35842	YAR071W	PHO11	250	N-linked
+P35842	YAR071W	PHO11	315	N-linked
+P35842	YAR071W	PHO11	356	N-linked
+P35842	YAR071W	PHO11	390	N-linked
+P35842	YAR071W	PHO11	439	N-linked
+P35842	YAR071W	PHO11	445	N-linked
+P35842	YAR071W	PHO11	461	N-linked
+P53549	YOR259C	RPT4	2	N-acetylserine
+Q01939	YGL048C	RPT6	2	N-acetylthreonine
+P25375	YCL057W	PRD1	73	Phosphoserine
+Q04119	YDR452W	PPN1	58	N-linked
+Q04119	YDR452W	PPN1	505	N-linked
+Q04119	YDR452W	PPN1	511	N-linked
+Q04119	YDR452W	PPN1	6	Glycyl
+Q06449	YPR154W	PIN3	2	N-acetylserine
+Q06449	YPR154W	PIN3	52	Phosphoserine
+Q06449	YPR154W	PIN3	55	Phosphoserine
+Q06449	YPR154W	PIN3	80	Glycyl
+P34217	YBL051C	PIN4	56	Phosphoserine
+P34217	YBL051C	PIN4	189	Phosphoserine
+P34217	YBL051C	PIN4	191	Phosphoserine
+P34217	YBL051C	PIN4	194	Phosphoserine
+P34217	YBL051C	PIN4	197	Phosphoserine
+P34217	YBL051C	PIN4	305	Phosphothreonine
+P34217	YBL051C	PIN4	393	Phosphoserine
+P34217	YBL051C	PIN4	466	Phosphoserine
+P34217	YBL051C	PIN4	541	Phosphoserine
+P34217	YBL051C	PIN4	636	Phosphoserine
+P34217	YBL051C	PIN4	638	Phosphoserine
+P34217	YBL051C	PIN4	640	Phosphoserine
+P34217	YBL051C	PIN4	653	Phosphoserine
+P34217	YBL051C	PIN4	655	Phosphoserine
+Q12017	YOR281C	PLP2	35	Phosphoserine
+Q12017	YOR281C	PLP2	62	Phosphoserine
+Q12161	YOL054W	PSH1	143	Phosphoserine
+Q12161	YOL054W	PSH1	191	Phosphoserine
+Q12161	YOL054W	PSH1	310	Phosphothreonine
+Q12161	YOL054W	PSH1	403	Phosphoserine
+P08456	YER026C	CHO1	4	Phosphoserine
+P08456	YER026C	CHO1	34	Phosphoserine
+P08456	YER026C	CHO1	42	Phosphoserine
+P08456	YER026C	CHO1	46	Phosphoserine
+P08456	YER026C	CHO1	47	Phosphoserine
+P08456	YER026C	CHO1	50	Phosphoserine
+P28708	YKL116C	PRR1	1	N-acetylmethionine
+P28708	YKL116C	PRR1	132	Phosphoserine
+P23639	YML092C	PRE8	108	Glycyl
+P50109	YML017W	PSP2	238	Phosphoserine
+P50109	YML017W	PSP2	340	Phosphoserine
+Q07949	YLR019W	PSR2	9	S-palmitoyl
+Q07949	YLR019W	PSR2	10	S-palmitoyl
+P32901	YKR093W	PTR2	37	Phosphotyrosine
+P32901	YKR093W	PTR2	39	Phosphoserine
+P32901	YKR093W	PTR2	45	Phosphoserine
+P32901	YKR093W	PTR2	594	Phosphoserine
+P38193	YBL046W	PSY4	347	Phosphothreonine
+P32857	YKL039W	PTM1	480	Phosphoserine
+P32857	YKL039W	PTM1	483	Phosphothreonine
+P32857	YKL039W	PTM1	498	Phosphothreonine
+P32857	YKL039W	PTM1	132	N-linked
+P23394	YDR243C	PRP28	69	Phosphoserine
+P22141	YER012W	PRE1	1	N-acetylmethionine
+P22141	YER012W	PRE1	76	Phosphoserine
+P33329	YDR436W	PPZ2	55	Phosphoserine
+P33329	YDR436W	PPZ2	71	Phosphoserine
+P33329	YDR436W	PPZ2	161	Phosphothreonine
+P33329	YDR436W	PPZ2	203	Phosphoserine
+P33329	YDR436W	PPZ2	224	Phosphoserine
+P33329	YDR436W	PPZ2	271	Phosphothreonine
+P33329	YDR436W	PPZ2	275	Phosphoserine
+P33329	YDR436W	PPZ2	310	Phosphoserine
+P33329	YDR436W	PPZ2	2	N-myristoyl
+P40494	YIL095W	PRK1	402	Phosphoserine
+P40494	YIL095W	PRK1	428	Phosphoserine
+P40494	YIL095W	PRK1	484	Phosphoserine
+P40494	YIL095W	PRK1	553	Phosphothreonine
+P40494	YIL095W	PRK1	556	Phosphoserine
+P53835	YNL279W	PRM1	135	N-linked
+P53835	YNL279W	PRM1	145	N-linked
+P53835	YNL279W	PRM1	188	N-linked
+P53835	YNL279W	PRM1	197	N-linked
+P53835	YNL279W	PRM1	231	N-linked
+P53835	YNL279W	PRM1	252	N-linked
+P53835	YNL279W	PRM1	272	N-linked
+P53835	YNL279W	PRM1	280	N-linked
+P53835	YNL279W	PRM1	490	N-linked
+P53835	YNL279W	PRM1	505	N-linked
+P53835	YNL279W	PRM1	512	N-linked
+P53835	YNL279W	PRM1	531	N-linked
+P53835	YNL279W	PRM1	573	N-linked
+P53835	YNL279W	PRM1	587	N-linked
+P21243	YGL011C	SCL1	2	N-acetylserine
+P21243	YGL011C	SCL1	237	Phosphoserine
+P21243	YGL011C	SCL1	232	Glycyl
+P21242	YOR362C	PRE10	2	N-acetylthreonine
+P26570	YML016C	PPZ1	49	Phosphoserine
+P26570	YML016C	PPZ1	171	Phosphothreonine
+P26570	YML016C	PPZ1	209	Phosphoserine
+P26570	YML016C	PPZ1	222	Phosphoserine
+P26570	YML016C	PPZ1	261	Phosphothreonine
+P26570	YML016C	PPZ1	265	Phosphoserine
+P26570	YML016C	PPZ1	690	Phosphoserine
+P26570	YML016C	PPZ1	2	N-myristoyl
+P49960	YMR268C	PRP24	19	Phosphoserine
+P33203	YKL012W	PRP40	576	Phosphothreonine
+P40303	YOL038W	PRE6	60	Phosphothreonine
+P38624	YJL001W	PRE3	1	N-acetylmethionine
+P25451	YER094C	PUP3	31	Phosphoserine
+P25451	YER094C	PUP3	70	Glycyl
+Q08217	YOL045W	PSK2	118	Phosphothreonine
+P14747	YML057W	CMP2	31	Phosphothreonine
+P14747	YML057W	CMP2	489	Phosphoserine
+P14747	YML057W	CMP2	520	Phosphoserine
+P24031	YBR092C	PHO3	97	N-linked
+P24031	YBR092C	PHO3	103	N-linked
+P24031	YBR092C	PHO3	162	N-linked
+P24031	YBR092C	PHO3	192	N-linked
+P24031	YBR092C	PHO3	250	N-linked
+P24031	YBR092C	PHO3	315	N-linked
+P24031	YBR092C	PHO3	356	N-linked
+P24031	YBR092C	PHO3	390	N-linked
+P24031	YBR092C	PHO3	439	N-linked
+P24031	YBR092C	PHO3	445	N-linked
+P24031	YBR092C	PHO3	456	N-linked
+P24031	YBR092C	PHO3	461	N-linked
+P52290	YDL024C	DIA3	98	N-linked
+P52290	YDL024C	DIA3	163	N-linked
+P52290	YDL024C	DIA3	193	N-linked
+P52290	YDL024C	DIA3	202	N-linked
+P52290	YDL024C	DIA3	238	N-linked
+P52290	YDL024C	DIA3	251	N-linked
+P52290	YDL024C	DIA3	316	N-linked
+P52290	YDL024C	DIA3	357	N-linked
+P52290	YDL024C	DIA3	391	N-linked
+P52290	YDL024C	DIA3	457	N-linked
+P52290	YDL024C	DIA3	462	N-linked
+P40347	YPR073C	LTP1	57	Phosphoserine
+P40476	YIL117C	PRM5	129	Phosphoserine
+P40476	YIL117C	PRM5	279	Phosphoserine
+P40476	YIL117C	PRM5	282	Phosphoserine
+P40476	YIL117C	PRM5	288	Phosphoserine
+P40476	YIL117C	PRM5	314	Glycyl
+P53131	YGL120C	PRP43	8	Phosphoserine
+P53131	YGL120C	PRP43	9	Phosphoserine
+P40327	YDL007W	RPT2	2	N-myristoyl
+P40327	YDL007W	RPT2	234	Glycyl
+P40327	YDL007W	RPT2	255	Glycyl
+P40327	YDL007W	RPT2	290	Glycyl
+P33297	YOR117W	RPT5	2	N-acetylalanine
+P33297	YOR117W	RPT5	180	Phosphotyrosine
+P33298	YDR394W	RPT3	1	N-acetylmethionine
+P33298	YDR394W	RPT3	280	Glycyl
+P09232	YEL060C	PRB1	594	N-linked
+P23638	YGR135W	PRE9	100	Glycyl
+P23638	YGR135W	PRE9	199	Glycyl
+P23638	YGR135W	PRE9	231	Glycyl
+P53633	YNL044W	YIP3	1	N-acetylmethionine
+P53633	YNL044W	YIP3	18	Phosphoserine
+P54885	YOR323C	PRO2	2	N-acetylserine
+P20095	YNR011C	PRP2	2	N-acetylserine
+P33299	YKL145W	RPT1	164	Phosphoserine
+P33299	YKL145W	RPT1	231	Phosphoserine
+P34227	YBL064C	PRX1	53	Phosphoserine
+P47033	YJL078C	PRY3	853	GPI-anchor
+P47033	YJL078C	PRY3	101	N-linked
+P47033	YJL078C	PRY3	360	N-linked
+P47033	YJL078C	PRY3	488	N-linked
+P47033	YJL078C	PRY3	535	N-linked
+P47033	YJL078C	PRY3	547	N-linked
+P47033	YJL078C	PRY3	569	N-linked
+P47033	YJL078C	PRY3	625	N-linked
+P32379	YGR253C	PUP2	55	Phosphothreonine
+P32379	YGR253C	PUP2	56	Phosphoserine
+P32379	YGR253C	PUP2	251	Phosphoserine
+P40302	YMR314W	PRE5	14	Phosphoserine
+P40302	YMR314W	PRE5	191	Glycyl
+Q07800	YLL010C	PSR1	110	Phosphoserine
+Q07800	YLL010C	PSR1	9	S-palmitoyl
+Q07800	YLL010C	PSR1	10	S-palmitoyl
+Q07800	YLL010C	PSR1	154	Glycyl
+P15380	YOR348C	PUT4	72	N-linked
+P15380	YOR348C	PUT4	78	N-linked
+P07259	YJL130C	URA2	2	N-acetylalanine
+P07259	YJL130C	URA2	1857	Phosphoserine%3B
+P07259	YJL130C	URA2	1853	Glycyl
+P32849	YLR032W	RAD5	2	N-acetylserine
+P32849	YLR032W	RAD5	20	Phosphoserine
+P32849	YLR032W	RAD5	23	Phosphoserine
+P32849	YLR032W	RAD5	129	Phosphoserine
+P32849	YLR032W	RAD5	130	Phosphoserine
+P14737	YDR217C	RAD9	26	Phosphoserine
+P14737	YDR217C	RAD9	56	Phosphoserine
+P14737	YDR217C	RAD9	205	Phosphoserine
+P14737	YDR217C	RAD9	218	Phosphothreonine
+P14737	YDR217C	RAD9	248	Phosphoserine
+P14737	YDR217C	RAD9	312	Phosphoserine
+P14737	YDR217C	RAD9	315	Phosphoserine
+P14737	YDR217C	RAD9	462	Phosphoserine
+P14737	YDR217C	RAD9	471	Phosphothreonine
+P14737	YDR217C	RAD9	474	Phosphothreonine
+P14737	YDR217C	RAD9	568	Phosphoserine
+P14737	YDR217C	RAD9	729	Phosphoserine
+P20051	YLR420W	URA4	98	N6-carboxylysine
+P07257	YPR191W	QCR2	141	Phosphoserine
+P07257	YPR191W	QCR2	168	Phosphoserine
+P40474	YIL121W	QDR2	21	Phosphoserine
+P40474	YIL121W	QDR2	38	Phosphothreonine
+P40474	YIL121W	QDR2	40	Phosphoserine
+P38227	YBR043C	QDR3	436	Phosphoserine
+P48581	YOR368W	RAD17	383	Phosphoserine
+P40352	YJR035W	RAD26	30	Phosphoserine
+P21827	YGL097W	SRM1	135	Phosphoserine
+P21827	YGL097W	SRM1	136	Phosphoserine
+P07276	YGR258C	RAD2	118	Phosphoserine
+P07276	YGR258C	RAD2	367	Phosphoserine
+P07276	YGR258C	RAD2	583	Phosphoserine
+Q12465	YLR084C	RAX2	41	N-linked
+Q12465	YLR084C	RAX2	45	N-linked
+Q12465	YLR084C	RAX2	69	N-linked
+Q12465	YLR084C	RAX2	88	N-linked
+Q12465	YLR084C	RAX2	124	N-linked
+Q12465	YLR084C	RAX2	134	N-linked
+Q12465	YLR084C	RAX2	145	N-linked
+Q12465	YLR084C	RAX2	158	N-linked
+Q12465	YLR084C	RAX2	166	N-linked
+Q12465	YLR084C	RAX2	171	N-linked
+Q12465	YLR084C	RAX2	187	N-linked
+Q12465	YLR084C	RAX2	200	N-linked
+Q12465	YLR084C	RAX2	235	N-linked
+Q12465	YLR084C	RAX2	238	N-linked
+Q12465	YLR084C	RAX2	244	N-linked
+Q12465	YLR084C	RAX2	333	N-linked
+Q12465	YLR084C	RAX2	365	N-linked
+Q12465	YLR084C	RAX2	379	N-linked
+Q12465	YLR084C	RAX2	432	N-linked
+Q12465	YLR084C	RAX2	445	N-linked
+Q12465	YLR084C	RAX2	516	N-linked
+Q12465	YLR084C	RAX2	524	N-linked
+Q12465	YLR084C	RAX2	613	N-linked
+Q12465	YLR084C	RAX2	620	N-linked
+Q12465	YLR084C	RAX2	626	N-linked
+Q12465	YLR084C	RAX2	640	N-linked
+Q12465	YLR084C	RAX2	677	N-linked
+Q12465	YLR084C	RAX2	705	N-linked
+Q12465	YLR084C	RAX2	713	N-linked
+Q12465	YLR084C	RAX2	721	N-linked
+Q12465	YLR084C	RAX2	731	N-linked
+Q12465	YLR084C	RAX2	749	N-linked
+Q12465	YLR084C	RAX2	758	N-linked
+Q12465	YLR084C	RAX2	792	N-linked
+Q12465	YLR084C	RAX2	821	N-linked
+Q12465	YLR084C	RAX2	848	N-linked
+Q12465	YLR084C	RAX2	861	N-linked
+Q12465	YLR084C	RAX2	884	N-linked
+Q12465	YLR084C	RAX2	890	N-linked
+Q12465	YLR084C	RAX2	908	N-linked
+Q12465	YLR084C	RAX2	923	N-linked
+Q12465	YLR084C	RAX2	942	N-linked
+Q12465	YLR084C	RAX2	956	N-linked
+Q12465	YLR084C	RAX2	980	N-linked
+Q12465	YLR084C	RAX2	983	N-linked
+Q12465	YLR084C	RAX2	1011	N-linked
+Q12465	YLR084C	RAX2	1024	N-linked
+Q12465	YLR084C	RAX2	1031	N-linked
+Q12465	YLR084C	RAX2	1060	N-linked
+Q12465	YLR084C	RAX2	1071	N-linked
+Q12465	YLR084C	RAX2	1098	N-linked
+Q12465	YLR084C	RAX2	1126	N-linked
+P31244	YBR114W	RAD16	25	Phosphoserine
+P31244	YBR114W	RAD16	109	Phosphoserine
+P11938	YNL216W	RAP1	486	Phosphothreonine
+P11938	YNL216W	RAP1	731	Phosphoserine
+P53295	YGR173W	RBG2	364	Phosphoserine
+Q08096	YOL010W	RCL1	2	N-acetylserine
+Q03446	YDR003W	RCR2	161	Phosphoserine
+Q03446	YDR003W	RCR2	191	Phosphothreonine
+P39531	YJL204C	RCY1	409	Phosphoserine
+P03872	R0040C	REP2	1	N-acetylmethionine
+P06780	YPR165W	RHO1	2	N-acetylserine
+P06780	YPR165W	RHO1	206	Cysteine
+P06780	YPR165W	RHO1	206	S-geranylgeranyl
+Q05672	YDL189W	RBS1	198	Phosphoserine
+Q05672	YDL189W	RBS1	435	Phosphoserine
+Q05672	YDL189W	RBS1	439	Phosphoserine
+Q05672	YDL189W	RBS1	447	Phosphoserine
+Q08273	YOL133W	HRT1	15	Phosphoserine
+P21538	YBR049C	REB1	355	Phosphoserine
+P21538	YBR049C	REB1	807	Glycyl
+P10862	YCR066W	RAD18	155	Phosphothreonine
+P10862	YCR066W	RAD18	174	Phosphoserine
+P10862	YCR066W	RAD18	204	Glycyl
+P12753	YNL250W	RAD50	469	Phosphoserine
+P12753	YNL250W	RAD50	568	Phosphothreonine
+Q08760	YOR301W	RAX1	167	Phosphoserine
+Q12044	YOR220W	RCN2	104	Phosphoserine
+Q12044	YOR220W	RCN2	110	Phosphoserine
+Q12044	YOR220W	RCN2	132	Phosphothreonine
+Q12044	YOR220W	RCN2	152	Phosphoserine
+Q12044	YOR220W	RCN2	157	Phosphoserine
+Q12044	YOR220W	RCN2	160	Phosphoserine
+Q12044	YOR220W	RCN2	183	Phosphoserine
+Q12044	YOR220W	RCN2	187	Phosphoserine
+Q12044	YOR220W	RCN2	193	Phosphoserine
+Q12044	YOR220W	RCN2	201	Phosphoserine
+Q12044	YOR220W	RCN2	255	Phosphoserine
+Q04779	YMR075W	RCO1	1	N-acetylmethionine
+Q04779	YMR075W	RCO1	68	Phosphoserine
+Q04779	YMR075W	RCO1	683	Phosphoserine
+P19541	YPL133C	RDS2	102	Phosphoserine
+P19541	YPL133C	RDS2	231	Phosphothreonine
+Q00816	YDR028C	REG1	2	N-acetylserine
+Q00816	YDR028C	REG1	73	Phosphothreonine
+Q00816	YDR028C	REG1	75	Phosphoserine
+Q00816	YDR028C	REG1	242	Phosphoserine
+Q00816	YDR028C	REG1	254	Phosphoserine
+Q00816	YDR028C	REG1	311	Phosphoserine
+Q00816	YDR028C	REG1	421	Phosphoserine
+Q00816	YDR028C	REG1	480	Phosphotyrosine
+Q00816	YDR028C	REG1	490	Phosphoserine
+Q00816	YDR028C	REG1	570	Phosphoserine
+Q00816	YDR028C	REG1	572	Phosphoserine
+Q00816	YDR028C	REG1	576	Phosphoserine
+Q00816	YDR028C	REG1	610	Phosphoserine
+Q00816	YDR028C	REG1	614	Phosphoserine
+Q00816	YDR028C	REG1	680	Phosphoserine
+Q00816	YDR028C	REG1	896	Phosphothreonine
+Q00816	YDR028C	REG1	898	Phosphoserine
+Q00816	YDR028C	REG1	980	Phosphoserine
+P38344	YBR267W	REI1	140	Phosphothreonine
+P39729	YAL036C	RBG1	2	N-acetylserine
+P38623	YLR248W	RCK2	46	Phosphoserine
+P38623	YLR248W	RCK2	50	Phosphoserine
+P38623	YLR248W	RCK2	187	Phosphoserine
+P38623	YLR248W	RCK2	350	Phosphothreonine
+P38623	YLR248W	RCK2	520	Phosphoserine
+P36054	YKL159C	RCN1	113	Phosphoserine
+P36054	YKL159C	RCN1	117	Phosphoserine
+P36054	YKL159C	RCN1	182	Phosphothreonine
+P38086	YBR073W	RDH54	649	Glycyl
+P01119	YOR101W	RAS1	306	Cysteine
+P01119	YOR101W	RAS1	305	S-palmitoyl
+P01119	YOR101W	RAS1	306	S-farnesyl
+P01120	YNL098C	RAS2	198	Phosphoserine
+P01120	YNL098C	RAS2	202	Phosphoserine
+P01120	YNL098C	RAS2	207	Phosphoserine
+P01120	YNL098C	RAS2	214	Phosphoserine
+P01120	YNL098C	RAS2	235	Phosphoserine
+P01120	YNL098C	RAS2	238	Phosphoserine
+P01120	YNL098C	RAS2	319	Cysteine
+P01120	YNL098C	RAS2	318	S-palmitoyl
+P01120	YNL098C	RAS2	319	S-farnesyl
+P01120	YNL098C	RAS2	131	Glycyl
+P47104	YJR033C	RAV1	1244	Phosphoserine
+P47104	YJR033C	RAV1	1248	Phosphoserine
+Q12192	YOR279C	RFM1	215	Phosphoserine
+P40043	YER067W	RGI1	68	Glycyl
+P32862	YKL038W	RGT1	202	Phosphoserine
+P32862	YKL038W	RGT1	205	Phosphoserine
+P32862	YKL038W	RGT1	208	Phosphoserine
+P32862	YKL038W	RGT1	229	Phosphoserine
+P32862	YKL038W	RGT1	283	Phosphoserine
+P32862	YKL038W	RGT1	284	Phosphoserine
+P32862	YKL038W	RGT1	410	Phosphoserine
+P32862	YKL038W	RGT1	414	Phosphoserine
+P32862	YKL038W	RGT1	1130	Phosphoserine
+P25378	YCR027C	RHB1	1	N-acetylmethionine
+P25378	YCR027C	RHB1	206	Cysteine
+P25378	YCR027C	RHB1	206	S-farnesyl
+Q12305	YOR285W	RDL1	26	Phosphoserine
+P53331	YGR276C	RNH70	24	Phosphoserine
+P38630	YOR217W	RFC1	38	Phosphothreonine
+P38630	YOR217W	RFC1	40	Phosphoserine
+P38630	YOR217W	RFC1	63	Phosphothreonine
+P38629	YNL290W	RFC3	2	N-acetylserine
+Q06624	YPR180W	AOS1	9	Phosphoserine
+Q06624	YPR180W	AOS1	35	Glycyl
+P43565	YFL033C	RIM15	380	Phosphoserine
+P43565	YFL033C	RIM15	476	Phosphoserine
+P43565	YFL033C	RIM15	704	Phosphothreonine
+P43565	YFL033C	RIM15	709	Phosphoserine
+P43565	YFL033C	RIM15	733	Phosphoserine
+P43565	YFL033C	RIM15	736	Phosphoserine
+P43565	YFL033C	RIM15	737	Phosphoserine
+P43565	YFL033C	RIM15	747	Phosphothreonine
+P43565	YFL033C	RIM15	1044	Phosphoserine
+P43565	YFL033C	RIM15	1048	Phosphoserine
+P43565	YFL033C	RIM15	1064	Phosphoserine
+P43565	YFL033C	RIM15	1075	Phosphothreonine%3B
+P43565	YFL033C	RIM15	1421	Phosphoserine
+P43565	YFL033C	RIM15	1531	Phosphoserine
+P43565	YFL033C	RIM15	1538	Phosphoserine
+P43565	YFL033C	RIM15	1542	Phosphoserine
+P43565	YFL033C	RIM15	1565	Phosphoserine
+P43565	YFL033C	RIM15	1764	Phosphoserine
+P39083	YOR127W	RGA1	278	Phosphothreonine
+P39083	YOR127W	RGA1	291	Phosphoserine
+P39083	YOR127W	RGA1	532	Phosphothreonine
+Q06108	YPR115W	RGC1	136	Phosphoserine
+Q06108	YPR115W	RGC1	249	Phosphoserine
+Q06108	YPR115W	RGC1	252	Phosphoserine
+Q06108	YPR115W	RGC1	481	Phosphoserine
+Q06108	YPR115W	RGC1	537	Phosphoserine
+Q06108	YPR115W	RGC1	652	Phosphoserine
+Q06108	YPR115W	RGC1	765	Phosphoserine
+Q06108	YPR115W	RGC1	813	Phosphoserine
+Q06108	YPR115W	RGC1	817	Phosphothreonine
+Q06108	YPR115W	RGC1	857	Phosphothreonine
+Q06108	YPR115W	RGC1	866	Phosphoserine
+Q06108	YPR115W	RGC1	879	Phosphoserine
+Q06108	YPR115W	RGC1	918	Phosphoserine
+Q06108	YPR115W	RGC1	966	Phosphoserine
+Q06108	YPR115W	RGC1	969	Phosphoserine
+Q06108	YPR115W	RGC1	975	Phosphoserine
+Q06108	YPR115W	RGC1	1059	Phosphoserine
+Q06108	YPR115W	RGC1	1081	Phosphoserine
+Q06108	YPR115W	RGC1	1082	Phosphoserine
+P16664	YDR137W	RGP1	351	Phosphoserine
+P16664	YDR137W	RGP1	354	Phosphoserine
+P16664	YDR137W	RGP1	357	Phosphoserine
+P16664	YDR137W	RGP1	363	Phosphoserine
+P16664	YDR137W	RGP1	364	Phosphoserine
+P16664	YDR137W	RGP1	370	Phosphoserine
+Q12300	YDL138W	RGT2	136	N-linked
+Q12300	YDL138W	RGT2	385	N-linked
+P21524	YER070W	RNR1	227	Phosphoserine
+P21524	YER070W	RNR1	816	Phosphoserine
+P21524	YER070W	RNR1	837	Phosphoserine
+P21524	YER070W	RNR1	887	Phosphoserine
+P21524	YER070W	RNR1	387	Glycyl
+P21524	YER070W	RNR1	853	Glycyl
+Q07844	YLL034C	RIX7	42	Phosphoserine
+P26785	YNL069C	RPL16B	2	N-acetylserine%3B
+P26785	YNL069C	RPL16B	43	Phosphoserine
+P26785	YNL069C	RPL16B	181	Phosphoserine
+P26785	YNL069C	RPL16B	185	Phosphoserine
+P26785	YNL069C	RPL16B	187	Phosphoserine
+P26785	YNL069C	RPL16B	176	Glycyl
+P46990	YJL177W	RPL17B	70	Phosphothreonine
+P46990	YJL177W	RPL17B	46	Glycyl
+P36105	YKL006W	RPL14A	2	N-acetylserine
+P0CX49	YOL120C	RPL18A	50	N6%2CN6%2CN6-trimethyllysine
+P0CX49	YOL120C	RPL18A	116	Glycyl
+P0CX24	YOR312C	RPL20B	32	Phosphoserine
+P0CX24	YOR312C	RPL20B	125	Glycyl
+P0CX24	YOR312C	RPL20B	131	Glycyl
+P0CX24	YOR312C	RPL20B	149	Glycyl
+Q12672	YPL079W	RPL21B	32	Glycyl
+P0CX41	YBL087C	RPL23A	2	N-acetylserine
+P0CX41	YBL087C	RPL23A	106	N6%2CN6-dimethyllysine%3B
+P0CX41	YBL087C	RPL23A	110	N6%2CN6-dimethyllysine%3B
+P30775	YGL143C	MRF1	287	N5-methylglutamine
+P53893	YNL163C	RIA1	431	Phosphoserine
+P22336	YAR007C	RFA1	2	N-acetylserine
+P22336	YAR007C	RFA1	178	Phosphoserine%3B
+P26754	YNL312W	RFA2	27	Phosphoserine
+P26754	YNL312W	RFA2	122	Phosphoserine
+P40348	YJR068W	RFC2	1	N-acetylmethionine
+P06781	YNL090W	RHO2	189	Cysteine
+P06781	YNL090W	RHO2	188	S-palmitoyl
+P06781	YNL090W	RHO2	189	S-geranylgeranyl
+Q3E757	YGR085C	RPL11B	2	N-acetylserine
+Q3E757	YGR085C	RPL11B	75	N6%2CN6%2CN6-trimethyllysine
+P48743	YLR176C	RFX1	173	Phosphoserine
+Q06407	YDR379W	RGA2	763	Phosphoserine
+P38339	YBR260C	RGD1	386	Phosphothreonine
+P40160	YNL207W	RIO2	346	Phosphoserine
+P49723	YGR180C	RNR4	1	N-acetylmethionine
+P49723	YGR180C	RNR4	169	Phosphoserine
+P49723	YGR180C	RNR4	332	Phosphoserine
+P49723	YGR180C	RNR4	334	Phosphothreonine
+P49723	YGR180C	RNR4	336	Phosphoserine
+P49723	YGR180C	RNR4	337	Glycyl
+P38145	YBR256C	RIB5	95	Phosphoserine
+Q00245	YIL118W	RHO3	228	Cysteine
+Q00245	YIL118W	RHO3	228	S-farnesyl
+P53879	YNL180C	RHO5	223	Phosphoserine
+P53879	YNL180C	RHO5	228	Phosphoserine
+P53879	YNL180C	RHO5	232	Phosphothreonine
+P53879	YNL180C	RHO5	244	Phosphothreonine
+P53879	YNL180C	RHO5	328	Cysteine
+P53879	YNL180C	RHO5	328	S-geranylgeranyl
+P53879	YNL180C	RHO5	276	Glycyl
+P09938	YJL026W	RNR2	15	Phosphoserine
+P09938	YJL026W	RNR2	24	Phosphoserine
+P09938	YJL026W	RNR2	41	Phosphoserine
+P21672	YIL066C	RNR3	227	Phosphoserine
+P21672	YIL066C	RNR3	806	Phosphoserine
+P21672	YIL066C	RNR3	827	Phosphoserine
+P21672	YIL066C	RNR3	868	Phosphoserine
+P21672	YIL066C	RNR3	387	Glycyl
+P26784	YIL133C	RPL16A	2	N-acetylserine
+P26784	YIL133C	RPL16A	44	Phosphoserine
+P26784	YIL133C	RPL16A	188	Phosphoserine
+P26784	YIL133C	RPL16A	177	Glycyl
+Q99258	YDR487C	RIB3	3	Phosphothreonine
+P29539	YBR275C	RIF1	97	Phosphoserine
+P29539	YBR275C	RIF1	1637	Phosphoserine
+P29539	YBR275C	RIF1	1795	Phosphoserine
+P29539	YBR275C	RIF1	1852	Phosphoserine
+P38883	YHR197W	RIX1	2	N-acetylserine
+P0CX53	YEL054C	RPL12A	2	N%2CN-dimethylproline%3B
+P0CX53	YEL054C	RPL12A	4	N6%2CN6%2CN6-trimethyllysine%3B
+P0CX53	YEL054C	RPL12A	11	N6%2CN6%2CN6-trimethyllysine%3B
+P0CX53	YEL054C	RPL12A	25	Phosphoserine
+P0CX53	YEL054C	RPL12A	38	Phosphoserine
+P0CX53	YEL054C	RPL12A	67	N5-methylarginine%3B
+P0CX53	YEL054C	RPL12A	130	Glycyl
+P0CX53	YEL054C	RPL12A	146	Glycyl
+Q12690	YDL082W	RPL13A	144	Phosphothreonine
+Q12690	YDL082W	RPL13A	152	Phosphothreonine
+Q00246	YKR055W	RHO4	264	Phosphoserine
+Q00246	YKR055W	RHO4	268	Phosphoserine
+Q00246	YKR055W	RHO4	276	Phosphoserine
+Q00246	YKR055W	RHO4	288	Cysteine
+Q00246	YKR055W	RHO4	288	S-farnesyl
+P38615	YMR139W	RIM11	199	Phosphotyrosine
+Q12196	YOR119C	RIO1	402	Phosphoserine%3B
+Q12196	YOR119C	RIO1	403	Phosphoserine%3B
+Q12196	YOR119C	RIO1	409	Phosphoserine%3B
+Q12196	YOR119C	RIO1	416	Phosphoserine%3B
+Q12196	YOR119C	RIO1	417	Phosphoserine%3B
+Q12196	YOR119C	RIO1	419	Phosphoserine%3B
+P41805	YLR075W	RPL10	143	Phosphoserine
+P41805	YLR075W	RPL10	205	Phosphoserine
+P41805	YLR075W	RPL10	40	Glycyl
+P41805	YLR075W	RPL10	101	Glycyl
+P38741	YHL024W	RIM4	525	Phosphoserine
+P0C0W9	YPR102C	RPL11A	2	N-acetylserine
+P0C0W9	YPR102C	RPL11A	75	N6%2CN6%2CN6-trimethyllysine
+P0CX54	YDR418W	RPL12B	2	N%2CN-dimethylproline%3B
+P0CX54	YDR418W	RPL12B	4	N6%2CN6%2CN6-trimethyllysine%3B
+P0CX54	YDR418W	RPL12B	11	N6%2CN6%2CN6-trimethyllysine%3B
+P0CX54	YDR418W	RPL12B	25	Phosphoserine
+P0CX54	YDR418W	RPL12B	38	Phosphoserine
+P0CX54	YDR418W	RPL12B	67	N5-methylarginine%3B
+P0CX54	YDR418W	RPL12B	130	Glycyl
+P0CX54	YDR418W	RPL12B	146	Glycyl
+P0CX44	YGL135W	RPL1B	2	N-acetylserine
+P0CX44	YGL135W	RPL1B	47	N6-methyllysine%3B
+P0CX44	YGL135W	RPL1B	79	Phosphoserine
+P0CX44	YGL135W	RPL1B	86	Phosphoserine
+P0CX23	YMR242C	RPL20A	32	Phosphoserine
+P0CX23	YMR242C	RPL20A	125	Glycyl
+P0CX23	YMR242C	RPL20A	131	Glycyl
+P0CX23	YMR242C	RPL20A	149	Glycyl
+P24000	YGR148C	RPL24B	7	Phosphoserine
+P0CX46	YIL018W	RPL2B	52	Phosphoserine
+P0CX46	YIL018W	RPL2B	95	Phosphoserine
+P0CX46	YIL018W	RPL2B	159	Phosphoserine
+P0CX46	YIL018W	RPL2B	160	Phosphoserine
+P0CX46	YIL018W	RPL2B	249	Phosphoserine
+P0CX46	YIL018W	RPL2B	46	Glycyl
+P0CX46	YIL018W	RPL2B	93	Glycyl
+P0CX46	YIL018W	RPL2B	119	Glycyl
+P0CX46	YIL018W	RPL2B	145	Glycyl
+P0CX45	YFR031C-A	RPL2A	52	Phosphoserine
+P0CX45	YFR031C-A	RPL2A	95	Phosphoserine
+P0CX45	YFR031C-A	RPL2A	159	Phosphoserine
+P0CX45	YFR031C-A	RPL2A	160	Phosphoserine
+P0CX45	YFR031C-A	RPL2A	249	Phosphoserine
+P0CX45	YFR031C-A	RPL2A	46	Glycyl
+P0CX45	YFR031C-A	RPL2A	93	Glycyl
+P0CX45	YFR031C-A	RPL2A	119	Glycyl
+P0CX45	YFR031C-A	RPL2A	145	Glycyl
+P14120	YGL030W	RPL30	22	Glycyl
+P14120	YGL030W	RPL30	53	Glycyl
+P14120	YGL030W	RPL30	83	Glycyl
+P05744	YPL143W	RPL33A	2	N-acetylalanine%3B
+P05744	YPL143W	RPL33A	47	Glycyl
+P0CX84	YDL191W	RPL35A	13	Phosphoserine
+P0CX84	YDL191W	RPL35A	50	Phosphoserine
+P05745	YMR194W	RPL36A	2	N-acetylthreonine
+P49626	YDR012W	RPL4B	2	N-acetylserine
+Q02753	YBR191W	RPL21A	32	Glycyl
+P0CX82	YBR084C-A	RPL19A	30	Phosphoserine
+P0CX82	YBR084C-A	RPL19A	37	Phosphoserine
+P0CX82	YBR084C-A	RPL19A	91	Phosphoserine
+P0CX82	YBR084C-A	RPL19A	21	Glycyl
+P0CX82	YBR084C-A	RPL19A	53	Glycyl
+P0CX82	YBR084C-A	RPL19A	60	Glycyl
+P0CX82	YBR084C-A	RPL19A	146	Glycyl
+P0CX82	YBR084C-A	RPL19A	186	Glycyl
+P0CX83	YBL027W	RPL19B	30	Phosphoserine
+P0CX83	YBL027W	RPL19B	37	Phosphoserine
+P0CX83	YBL027W	RPL19B	91	Phosphoserine
+P0CX83	YBL027W	RPL19B	21	Glycyl
+P0CX83	YBL027W	RPL19B	53	Glycyl
+P0CX83	YBL027W	RPL19B	60	Glycyl
+P0CX83	YBL027W	RPL19B	146	Glycyl
+P0CX83	YBL027W	RPL19B	186	Glycyl
+P40212	YMR142C	RPL13B	144	Phosphothreonine
+P40212	YMR142C	RPL13B	152	Phosphothreonine
+P38754	YHL001W	RPL14B	2	N-acetylserine
+P05740	YKL180W	RPL17A	70	Phosphothreonine
+P05740	YKL180W	RPL17A	46	Glycyl
+P0CX50	YNL301C	RPL18B	50	N6%2CN6%2CN6-trimethyllysine
+P0CX50	YNL301C	RPL18B	116	Glycyl
+P0CX43	YPL220W	RPL1A	2	N-acetylserine
+P0CX43	YPL220W	RPL1A	47	N6-methyllysine%3B
+P0CX43	YPL220W	RPL1A	79	Phosphoserine
+P0CX43	YPL220W	RPL1A	86	Phosphoserine
+P04449	YGL031C	RPL24A	7	Phosphoserine
+P41056	YOR234C	RPL33B	2	N-acetylalanine%3B
+P41056	YOR234C	RPL33B	47	Glycyl
+P25367	YCL028W	RNQ1	143	Phosphoserine
+P25367	YCL028W	RNQ1	5	Glycyl
+P25367	YCL028W	RNQ1	84	Glycyl
+P39956	YER169W	RPH1	399	Phosphothreonine
+P39956	YER169W	RPH1	430	Phosphoserine
+P39956	YER169W	RPH1	459	Phosphoserine
+P39956	YER169W	RPH1	557	Phosphoserine
+P39956	YER169W	RPH1	561	Phosphoserine
+P39956	YER169W	RPH1	575	Phosphoserine
+P39956	YER169W	RPH1	584	Phosphoserine
+P39956	YER169W	RPH1	652	Phosphoserine
+P39956	YER169W	RPH1	689	Phosphoserine
+P35178	YDR087C	RRP1	1	N-acetylmethionine
+P35178	YDR087C	RRP1	267	Phosphoserine
+Q05022	YMR229C	RRP5	47	Phosphothreonine
+Q05022	YMR229C	RRP5	187	Phosphoserine
+Q05022	YMR229C	RRP5	188	Phosphoserine
+Q05022	YMR229C	RRP5	1724	Phosphoserine
+P25381	YCR045C	RRT12	38	N-linked
+P25381	YCR045C	RRT12	64	N-linked
+P25381	YCR045C	RRT12	106	N-linked
+P25381	YCR045C	RRT12	121	N-linked
+P25381	YCR045C	RRT12	268	N-linked
+P25381	YCR045C	RRT12	356	N-linked
+P25381	YCR045C	RRT12	449	N-linked
+P36121	YKR025W	RPC37	61	Phosphothreonine
+P32565	YIL075C	RPN2	2	N-acetylserine
+P32565	YIL075C	RPN2	801	Phosphothreonine
+P32565	YIL075C	RPN2	932	Phosphothreonine
+Q03305	YDR465C	RMT2	181	Phosphoserine
+Q03305	YDR465C	RMT2	184	Phosphoserine
+P22138	YPR010C	RPA135	2	N-acetylserine
+P22138	YPR010C	RPA135	81	Phosphoserine
+P22138	YPR010C	RPA135	1156	Phosphoserine
+P20435	YPR187W	RPO26	24	Phosphoserine
+P28000	YNL113W	RPC19	15	Phosphothreonine
+P28000	YNL113W	RPC19	33	Phosphothreonine
+P28000	YNL113W	RPC19	134	Glycyl
+P04050	YDL140C	RPO21	1471	Phosphothreonine
+P04050	YDL140C	RPO21	695	Glycyl
+P04050	YDL140C	RPO21	1246	Glycyl
+P04050	YDL140C	RPO21	1350	Glycyl
+P20433	YJL140W	RPB4	1	N-acetylmethionine
+P20433	YJL140W	RPB4	91	Phosphothreonine
+P20433	YJL140W	RPB4	92	Phosphothreonine
+P50106	YDR156W	RPA14	121	Phosphoserine
+P32349	YPR190C	RPC82	27	Phosphothreonine
+P32349	YPR190C	RPC82	392	Phosphoserine
+P32349	YPR190C	RPC82	394	Phosphoserine
+P17890	YNL151C	RPC31	189	Phosphoserine
+P35718	YKL144C	RPC25	162	Phosphoserine
+Q12377	YDL097C	RPN6	2	N-acetylserine
+Q06506	YPR137W	RRP9	2	N-acetylserine
+Q06506	YPR137W	RRP9	50	Phosphoserine
+P0CX48	YBR048W	RPS11B	2	N-acetylserine
+P0CX48	YBR048W	RPS11B	15	Glycyl
+P0CX48	YBR048W	RPS11B	46	Glycyl
+P0CX48	YBR048W	RPS11B	56	Glycyl
+P0CX48	YBR048W	RPS11B	57	Glycyl
+P0CX48	YBR048W	RPS11B	79	Glycyl
+P0CX48	YBR048W	RPS11B	96	Glycyl
+P0CX48	YBR048W	RPS11B	105	Glycyl
+P0CX48	YBR048W	RPS11B	133	Glycyl
+P0CX48	YBR048W	RPS11B	141	Glycyl
+P0CX48	YBR048W	RPS11B	148	Glycyl
+P40693	YNL002C	RLP7	2	N-acetylserine
+P40693	YNL002C	RLP7	14	Phosphoserine
+P40693	YNL002C	RLP7	120	Phosphothreonine
+P40693	YNL002C	RLP7	278	Phosphoserine
+Q02805	YOR018W	ROD1	138	Phosphoserine
+Q02805	YOR018W	ROD1	141	Phosphoserine
+Q02805	YOR018W	ROD1	436	Phosphoserine
+Q02805	YOR018W	ROD1	536	Phosphoserine
+Q02805	YOR018W	ROD1	720	Phosphoserine
+Q02805	YOR018W	ROD1	725	Phosphoserine
+Q02805	YOR018W	ROD1	401	Glycyl
+P53046	YGR070W	ROM1	1	N-acetylmethionine
+P53046	YGR070W	ROM1	154	Phosphoserine
+P53046	YGR070W	ROM1	155	Phosphoserine
+P53046	YGR070W	ROM1	180	Phosphothreonine
+P53046	YGR070W	ROM1	433	Phosphoserine
+Q03691	YMR200W	ROT1	103	N-linked
+Q03691	YMR200W	ROT1	107	N-linked
+Q03691	YMR200W	ROT1	139	N-linked
+P47006	YJL148W	RPA34	10	Phosphoserine
+P47006	YJL148W	RPA34	12	Phosphoserine
+P47006	YJL148W	RPA34	14	Phosphoserine
+P47006	YJL148W	RPA34	60	Phosphoserine
+P46669	YOR340C	RPA43	244	Phosphoserine
+P46669	YOR340C	RPA43	251	Phosphoserine
+P46669	YOR340C	RPA43	265	Phosphoserine
+P46669	YOR340C	RPA43	269	Phosphoserine
+P46669	YOR340C	RPA43	285	Phosphoserine
+P20436	YOR224C	RPB8	2	N-acetylserine
+P20436	YOR224C	RPB8	68	Phosphothreonine
+P22139	YOR210W	RPB10	59	Glycyl
+P25441	YDL150W	RPC53	137	Phosphoserine
+P25441	YDL150W	RPC53	138	Phosphoserine
+P25441	YDL150W	RPC53	178	Phosphoserine
+P25441	YDL150W	RPC53	182	Phosphoserine
+P25441	YDL150W	RPC53	224	Phosphoserine
+P25441	YDL150W	RPC53	228	Phosphothreonine
+P25441	YDL150W	RPC53	232	Phosphothreonine
+Q12754	YPL012W	RRP12	1059	Phosphoserine
+Q12754	YPL012W	RRP12	1067	Phosphoserine
+Q06511	YPR143W	RRP15	69	Phosphoserine
+P25359	YCR035C	RRP43	2	N-acetylalanine
+P25359	YCR035C	RRP43	26	Phosphoserine
+Q01855	YOL040C	RPS15	2	N-acetylserine
+Q01855	YOL040C	RPS15	24	Glycyl
+Q01855	YOL040C	RPS15	35	Glycyl
+Q01855	YOL040C	RPS15	64	Glycyl
+P38701	YHL015W	RPS20	2	N-acetylserine
+P38701	YHL015W	RPS20	6	Glycyl
+P38701	YHL015W	RPS20	8	Glycyl
+P38701	YHL015W	RPS20	21	Glycyl
+P38701	YHL015W	RPS20	32	Glycyl
+P38701	YHL015W	RPS20	101	Glycyl
+P0C0V8	YKR057W	RPS21A	1	N-acetylmethionine
+P08518	YOR151C	RPB2	919	Phosphoserine
+P32561	YNL330C	RPD3	394	Phosphothreonine
+P32561	YNL330C	RPD3	408	Phosphoserine
+P43588	YFR004W	RPN11	1	N-acetylmethionine
+P38764	YHR027C	RPN1	16	Phosphoserine
+P38764	YHR027C	RPN1	19	Phosphoserine
+P38764	YHR027C	RPN1	24	Phosphothreonine
+P38764	YHR027C	RPN1	178	Phosphoserine
+P38764	YHR027C	RPN1	187	Phosphoserine
+P38764	YHR027C	RPN1	695	Phosphoserine
+P40016	YER021W	RPN3	2	N-acetylalanine
+P40016	YER021W	RPN3	454	Phosphoserine
+P0CX47	YDR025W	RPS11A	2	N-acetylserine
+P0CX47	YDR025W	RPS11A	15	Glycyl
+P0CX47	YDR025W	RPS11A	46	Glycyl
+P0CX47	YDR025W	RPS11A	56	Glycyl
+P0CX47	YDR025W	RPS11A	57	Glycyl
+P0CX47	YDR025W	RPS11A	79	Glycyl
+P0CX47	YDR025W	RPS11A	96	Glycyl
+P0CX47	YDR025W	RPS11A	105	Glycyl
+P0CX47	YDR025W	RPS11A	133	Glycyl
+P0CX47	YDR025W	RPS11A	141	Glycyl
+P0CX47	YDR025W	RPS11A	148	Glycyl
+P36160	YKR081C	RPF2	73	Phosphoserine
+O13563	YLR421C	RPN13	2	N-acetylserine
+O13563	YLR421C	RPN13	133	Phosphoserine
+O13563	YLR421C	RPN13	135	Phosphoserine
+O13563	YLR421C	RPN13	140	Phosphoserine
+Q08723	YOR261C	RPN8	2	N-acetylserine
+Q08723	YOR261C	RPN8	314	Phosphoserine
+Q08723	YOR261C	RPN8	317	Phosphoserine
+Q08723	YOR261C	RPN8	319	Phosphoserine
+Q08723	YOR261C	RPN8	327	Phosphothreonine
+Q12532	YPL009C	RQC2	797	Phosphoserine
+Q04031	YDR412W	RRP17	113	Phosphoserine
+Q04031	YDR412W	RRP17	116	Phosphoserine
+Q04031	YDR412W	RRP17	122	Phosphoserine
+P38961	YDR083W	RRP8	62	Phosphoserine
+P36080	YKL082C	RRP14	2	N-acetylserine
+P40470	YIL127C	RRT14	197	Phosphoserine
+P40470	YIL127C	RRT14	202	Phosphoserine
+P40470	YIL127C	RRT14	203	Phosphoserine
+Q3E792	YGR027C	RPS25A	2	N%2CN-dimethylproline%3B
+P41058	YDL061C	RPS29B	25	Phosphoserine
+P26783	YJR123W	RPS5	2	N-acetylserine
+P26783	YJR123W	RPS5	27	Phosphothreonine
+P26783	YJR123W	RPS5	45	Glycyl
+P26783	YJR123W	RPS5	203	Glycyl
+P48164	YNL096C	RPS7B	2	N-acetylserine
+P48164	YNL096C	RPS7B	10	Phosphoserine
+P48164	YNL096C	RPS7B	31	Phosphoserine
+Q06488	YLR357W	RSC2	612	Phosphotyrosine
+Q06488	YLR357W	RSC2	682	Phosphoserine
+P43609	YFR037C	RSC8	485	Phosphoserine
+Q02950	YPL118W	MRP51	327	Phosphoserine
+Q03919	YDR139C	RUB1	76	Glycyl
+Q3E754	YJL136C	RPS21B	1	N-acetylmethionine
+P0CX31	YER074W	RPS24A	2	N-acetylserine
+P0CX31	YER074W	RPS24A	14	Phosphoserine
+P0CX31	YER074W	RPS24A	56	Phosphoserine
+P0CX31	YER074W	RPS24A	21	Glycyl
+Q08932	YPL193W	RSA1	1	N-acetylmethionine
+Q08932	YPL193W	RSA1	172	Phosphoserine
+P38781	YHR056C	RSC30	150	Phosphoserine
+Q03201	YDR041W	RSM10	193	Phosphoserine
+Q05468	YDR333C	RQC1	119	Phosphoserine
+Q05468	YDR333C	RQC1	158	Phosphothreonine
+Q05468	YDR333C	RQC1	160	Phosphoserine
+Q04225	YMR131C	RRB1	5	Phosphoserine
+P38766	YHR031C	RRM3	64	Phosphoserine
+P38712	YHR065C	RRP3	43	Phosphoserine
+P38712	YHR065C	RRP3	45	Phosphoserine
+P38712	YHR065C	RRP3	47	Phosphoserine
+P48589	YOR369C	RPS12	85	Glycyl
+P48589	YOR369C	RPS12	95	Glycyl
+P48589	YOR369C	RPS12	114	Glycyl
+P23248	YML063W	RPS1B	2	N-acetylalanine%3B
+P23248	YML063W	RPS1B	245	Phosphoserine
+P23248	YML063W	RPS1B	254	Phosphothreonine
+P23248	YML063W	RPS1B	248	Glycyl
+P0CX52	YDL083C	RPS16B	2	N-acetylserine
+P0CX52	YDL083C	RPS16B	34	Phosphoserine
+P0CX52	YDL083C	RPS16B	61	Phosphoserine
+P0CX52	YDL083C	RPS16B	70	Phosphothreonine
+P0CX52	YDL083C	RPS16B	76	Phosphoserine
+P0CX52	YDL083C	RPS16B	30	Glycyl
+P0CX52	YDL083C	RPS16B	47	Glycyl
+P0CX52	YDL083C	RPS16B	59	Glycyl
+P0CX56	YML026C	RPS18B	2	N-acetylserine
+P0CX56	YML026C	RPS18B	48	N6-methyllysine%3B
+P0CX56	YML026C	RPS18B	36	Glycyl
+P0CX56	YML026C	RPS18B	49	Glycyl
+P0CX56	YML026C	RPS18B	80	Glycyl
+P0CX56	YML026C	RPS18B	96	Glycyl
+P0CX29	YGR118W	RPS23A	64	3%2C4-dihydroxyproline
+P0CX29	YGR118W	RPS23A	56	Glycyl
+P0CX32	YIL069C	RPS24B	2	N-acetylserine
+P0CX32	YIL069C	RPS24B	14	Phosphoserine
+P0CX32	YIL069C	RPS24B	56	Phosphoserine
+P0CX32	YIL069C	RPS24B	21	Glycyl
+P0C0T4	YLR333C	RPS25B	2	N%2CN-dimethylproline%3B
+P0CX35	YJR145C	RPS4A	32	Phosphoserine
+P0CX35	YJR145C	RPS4A	115	Phosphothreonine
+P0CX35	YJR145C	RPS4A	247	Phosphoserine
+P0CX35	YJR145C	RPS4A	62	Glycyl
+P0CX35	YJR145C	RPS4A	134	Glycyl
+P0CX35	YJR145C	RPS4A	161	Glycyl
+P0CX35	YJR145C	RPS4A	168	Glycyl
+P0CX35	YJR145C	RPS4A	174	Glycyl
+P0CX35	YJR145C	RPS4A	179	Glycyl
+P0CX35	YJR145C	RPS4A	211	Glycyl
+P0CX35	YJR145C	RPS4A	233	Glycyl
+P32832	YMR091C	NPL6	86	Phosphoserine
+Q03124	YML127W	RSC9	44	Phosphoserine
+P38792	YHR069C	RRP4	2	N-acetylserine
+P38792	YHR069C	RRP4	28	Phosphoserine
+P38792	YHR069C	RRP4	268	Phosphoserine
+Q12149	YOR001W	RRP6	138	Phosphoserine
+Q12149	YOR001W	RRP6	520	Phosphothreonine
+Q12149	YOR001W	RRP6	640	Phosphoserine
+Q12149	YOR001W	RRP6	645	Phosphoserine
+P35997	YKL156W	RPS27A	40	S-methylcysteine
+P0C0X0	YLR264W	RPS28B	1	N-acetylmethionine
+P25443	YGL123W	RPS2	2	N-acetylserine
+P25443	YGL123W	RPS2	11	Asymmetric
+P25443	YGL123W	RPS2	11	Omega-N-methylarginine%3B
+P25443	YGL123W	RPS2	33	Glycyl
+P0CX34	YOR182C	RPS30B	16	Phosphoserine
+P0CX34	YOR182C	RPS30B	48	Phosphothreonine
+Q05942	YLR221C	RSA3	83	Phosphoserine
+Q05942	YLR221C	RSA3	88	Phosphothreonine
+Q05942	YLR221C	RSA3	99	Phosphoserine
+P53236	YGR056W	RSC1	670	Phosphoserine
+Q02206	YKR008W	RSC4	199	Phosphoserine
+Q02206	YKR008W	RSC4	545	Phosphoserine
+P33442	YLR441C	RPS1A	2	N-acetylalanine%3B
+P33442	YLR441C	RPS1A	245	Phosphothreonine
+P33442	YLR441C	RPS1A	254	Phosphothreonine
+P33442	YLR441C	RPS1A	248	Glycyl
+P0CX37	YPL090C	RPS6A	163	Phosphothreonine
+P0CX37	YPL090C	RPS6A	116	Glycyl
+P0CX37	YPL090C	RPS6A	131	Glycyl
+P0CX37	YPL090C	RPS6A	149	Glycyl
+P0CX37	YPL090C	RPS6A	214	Glycyl
+P0CX40	YER102W	RPS8B	62	Phosphothreonine
+P0CX40	YER102W	RPS8B	66	Phosphoserine
+P0CX40	YER102W	RPS8B	69	Phosphoserine
+P0CX40	YER102W	RPS8B	73	Phosphoserine
+P0CX40	YER102W	RPS8B	86	Phosphoserine
+P0CX40	YER102W	RPS8B	107	Phosphothreonine
+P0CX40	YER102W	RPS8B	154	Phosphoserine
+P0CX40	YER102W	RPS8B	155	Phosphoserine
+P0CX40	YER102W	RPS8B	158	Phosphoserine
+P0CX40	YER102W	RPS8B	161	Phosphoserine
+Q08417	YOR049C	RSB1	3	N-linked
+Q08417	YOR049C	RSB1	6	N-linked
+P46974	YJR127C	RSF2	231	Phosphoserine
+P46974	YJR127C	RSF2	322	Phosphoserine
+P46974	YJR127C	RSF2	544	Phosphoserine
+P46974	YJR127C	RSF2	632	Phosphoserine
+Q03516	YMR266W	RSN1	949	Phosphoserine
+P32905	YGR214W	RPS0A	2	N-acetylserine
+P40161	YNL206C	RTT106	2	N-acetylserine
+P40161	YNL206C	RTT106	408	Phosphoserine
+P40161	YNL206C	RTT106	411	Phosphoserine
+P40161	YNL206C	RTT106	450	Phosphoserine
+P53064	YGL244W	RTF1	17	Phosphoserine
+P53064	YGL244W	RTF1	69	Phosphotyrosine
+P53064	YGL244W	RTF1	71	Phosphoserine
+P53064	YGL244W	RTF1	477	Phosphoserine
+P0CX30	YPR132W	RPS23B	64	3%2C4-dihydroxyproline
+P0CX30	YPR132W	RPS23B	56	Glycyl
+P41057	YLR388W	RPS29A	25	Phosphoserine
+P05750	YNL178W	RPS3	44	Phosphothreonine
+P05750	YNL178W	RPS3	70	Phosphothreonine
+P05750	YNL178W	RPS3	97	Phosphoserine
+P05750	YNL178W	RPS3	129	Phosphoserine
+P05750	YNL178W	RPS3	146	Omega-N-methylarginine%3B
+P05750	YNL178W	RPS3	221	Phosphoserine
+P05750	YNL178W	RPS3	231	Phosphothreonine
+P05750	YNL178W	RPS3	106	Glycyl
+P05750	YNL178W	RPS3	132	Glycyl
+P05750	YNL178W	RPS3	141	Glycyl
+P05750	YNL178W	RPS3	151	Glycyl
+P05750	YNL178W	RPS3	200	Glycyl
+P05750	YNL178W	RPS3	212	Glycyl
+O13516	YPL081W	RPS9A	184	Phosphoserine
+O13516	YPL081W	RPS9A	180	Glycyl
+Q12481	YOR287C	RRP36	14	Phosphoserine
+Q12481	YOR287C	RRP36	41	Phosphoserine
+Q12481	YOR287C	RRP36	42	Phosphoserine
+P05756	YDR064W	RPS13	32	Phosphoserine
+P05756	YDR064W	RPS13	39	Glycyl
+P05756	YDR064W	RPS13	43	Glycyl
+P06367	YCR031C	RPS14A	2	N-acetylserine
+P05759	YLR167W	RPS31	122	Phosphoserine
+P05759	YLR167W	RPS31	76	Glycyl
+P0CX51	YMR143W	RPS16A	2	N-acetylserine
+P0CX51	YMR143W	RPS16A	34	Phosphoserine
+P0CX51	YMR143W	RPS16A	61	Phosphoserine
+P0CX51	YMR143W	RPS16A	70	Phosphothreonine
+P0CX51	YMR143W	RPS16A	76	Phosphoserine
+P0CX51	YMR143W	RPS16A	30	Glycyl
+P0CX51	YMR143W	RPS16A	47	Glycyl
+P0CX51	YMR143W	RPS16A	59	Glycyl
+P0CX55	YDR450W	RPS18A	2	N-acetylserine
+P0CX55	YDR450W	RPS18A	48	N6-methyllysine%3B
+P0CX55	YDR450W	RPS18A	36	Glycyl
+P0CX55	YDR450W	RPS18A	49	Glycyl
+P0CX55	YDR450W	RPS18A	80	Glycyl
+P0CX55	YDR450W	RPS18A	96	Glycyl
+Q3E7X9	YOR167C	RPS28A	1	N-acetylmethionine
+P0CX33	YLR287C-A	RPS30A	16	Phosphoserine
+P0CX33	YLR287C-A	RPS30A	48	Phosphothreonine
+P0CX36	YHR203C	RPS4B	32	Phosphoserine
+P0CX36	YHR203C	RPS4B	115	Phosphothreonine
+P0CX36	YHR203C	RPS4B	247	Phosphoserine
+P0CX36	YHR203C	RPS4B	62	Glycyl
+P0CX36	YHR203C	RPS4B	134	Glycyl
+P0CX36	YHR203C	RPS4B	161	Glycyl
+P0CX36	YHR203C	RPS4B	168	Glycyl
+P0CX36	YHR203C	RPS4B	174	Glycyl
+P0CX36	YHR203C	RPS4B	179	Glycyl
+P0CX36	YHR203C	RPS4B	211	Glycyl
+P0CX36	YHR203C	RPS4B	233	Glycyl
+P0CX38	YBR181C	RPS6B	163	Phosphothreonine
+P0CX38	YBR181C	RPS6B	116	Glycyl
+P0CX38	YBR181C	RPS6B	131	Glycyl
+P0CX38	YBR181C	RPS6B	149	Glycyl
+P0CX38	YBR181C	RPS6B	214	Glycyl
+P0CX39	YBL072C	RPS8A	62	Phosphothreonine
+P0CX39	YBL072C	RPS8A	66	Phosphoserine
+P0CX39	YBL072C	RPS8A	69	Phosphoserine
+P0CX39	YBL072C	RPS8A	73	Phosphoserine
+P0CX39	YBL072C	RPS8A	86	Phosphoserine
+P0CX39	YBL072C	RPS8A	107	Phosphothreonine
+P0CX39	YBL072C	RPS8A	154	Phosphoserine
+P0CX39	YBL072C	RPS8A	155	Phosphoserine
+P0CX39	YBL072C	RPS8A	158	Phosphoserine
+P0CX39	YBL072C	RPS8A	161	Phosphoserine
+P05755	YBR189W	RPS9B	184	Phosphoserine
+P05755	YBR189W	RPS9B	180	Glycyl
+Q06639	YDR303C	RSC3	95	Phosphoserine
+Q06639	YDR303C	RSC3	236	Phosphoserine
+P38165	YBL103C	RTG3	81	Phosphoserine
+P38165	YBL103C	RTG3	123	Phosphoserine
+P38165	YBL103C	RTG3	142	Phosphoserine
+P38165	YBL103C	RTG3	150	Phosphothreonine
+P38165	YBL103C	RTG3	227	Phosphoserine
+P38165	YBL103C	RTG3	236	Phosphoserine
+P38165	YBL103C	RTG3	241	Phosphoserine
+P38165	YBL103C	RTG3	269	Phosphoserine
+Q12443	YDL204W	RTN2	278	Phosphoserine
+Q12443	YDL204W	RTN2	137	N-linked
+P26786	YOR096W	RPS7A	2	N-acetylserine
+P26786	YOR096W	RPS7A	124	Glycyl
+P38850	YHR154W	RTT107	304	Phosphoserine
+P38850	YHR154W	RTT107	532	Phosphothreonine
+P38850	YHR154W	RTT107	591	Phosphoserine
+P38850	YHR154W	RTT107	593	Phosphoserine
+P38850	YHR154W	RTT107	720	Phosphoserine
+P38850	YHR154W	RTT107	800	Phosphoserine
+P38850	YHR154W	RTT107	806	Phosphoserine
+Q08281	YOL138C	RTC1	1036	Phosphoserine
+Q08281	YOL138C	RTC1	1080	Phosphoserine
+Q08281	YOL138C	RTC1	1087	Phosphoserine
+Q08281	YOL138C	RTC1	1089	Phosphoserine
+Q08281	YOL138C	RTC1	1123	Phosphoserine
+Q08281	YOL138C	RTC1	1133	Phosphoserine
+P53330	YGR275W	RTT102	77	Phosphoserine
+P53330	YGR275W	RTT102	122	Phosphoserine
+P53850	YNL254C	RTC4	23	Phosphoserine
+Q04947	YDR233C	RTN1	186	Phosphothreonine
+Q04947	YDR233C	RTN1	219	Phosphothreonine
+Q04947	YDR233C	RTN1	232	Phosphoserine
+P20606	YPL218W	SAR1	155	Phosphothreonine
+P20606	YPL218W	SAR1	157	Phosphoserine
+P20606	YPL218W	SAR1	133	Glycyl
+P28707	YKL117W	SBA1	2	N-acetylserine
+P06105	YJL080C	SCP160	50	Phosphothreonine
+P06105	YJL080C	SCP160	54	Phosphoserine
+P06105	YJL080C	SCP160	63	Phosphoserine
+P06105	YJL080C	SCP160	85	Phosphoserine
+P06105	YJL080C	SCP160	87	Phosphoserine
+P06105	YJL080C	SCP160	89	Phosphoserine
+P06105	YJL080C	SCP160	630	Phosphoserine
+P06105	YJL080C	SCP160	1112	Phosphoserine
+P40541	YIL026C	IRR1	28	Phosphoserine
+P40541	YIL026C	IRR1	628	Phosphoserine
+P11792	YHR205W	SCH9	570	Phosphothreonine%3B
+P11792	YHR205W	SCH9	711	Phosphoserine%3B
+P11792	YHR205W	SCH9	723	Phosphothreonine%3B
+P11792	YHR205W	SCH9	726	Phosphoserine%3B
+P11792	YHR205W	SCH9	737	Phosphothreonine%3B
+P11792	YHR205W	SCH9	758	Phosphoserine%3B
+P11792	YHR205W	SCH9	765	Phosphoserine%3B
+P32607	YOL067C	RTG1	50	Phosphoserine
+P32607	YOL067C	RTG1	52	Phosphoserine
+P32607	YOL067C	RTG1	60	Phosphothreonine
+Q03940	YDR190C	RVB1	2	N-acetylvaline
+Q12158	YDL003W	MCD1	161	Phosphoserine
+Q12158	YDL003W	MCD1	175	Phosphoserine%3B
+Q12158	YDL003W	MCD1	210	N6-acetyllysine%3B
+Q12158	YDL003W	MCD1	263	Phosphoserine%3B
+Q12158	YDL003W	MCD1	307	Phosphoserine
+Q12158	YDL003W	MCD1	354	Phosphothreonine
+P34758	YOR329C	SCD5	564	Phosphoserine
+P43612	YFR040W	SAP155	58	Phosphoserine
+P43612	YFR040W	SAP155	255	Phosphoserine
+P43612	YFR040W	SAP155	613	Phosphothreonine
+P43612	YFR040W	SAP155	618	Phosphothreonine
+P17121	YDR389W	SAC7	37	Phosphoserine
+P17121	YDR389W	SAC7	46	Phosphoserine
+P17121	YDR389W	SAC7	435	Phosphoserine
+P17121	YDR389W	SAC7	491	Phosphoserine
+P17121	YDR389W	SAC7	632	Phosphoserine
+Q12136	YDL153C	SAS10	12	Phosphoserine
+Q12136	YDL153C	SAS10	314	Phosphoserine
+Q12136	YDL153C	SAS10	316	Phosphoserine
+Q12136	YDL153C	SAS10	336	Phosphoserine
+Q12136	YDL153C	SAS10	339	Phosphoserine
+Q12136	YDL153C	SAS10	477	Phosphoserine
+Q04002	YDR180W	SCC2	43	Phosphoserine%3B
+Q04002	YDR180W	SCC2	67	Phosphothreonine
+Q04002	YDR180W	SCC2	74	Phosphoserine%3B
+Q04002	YDR180W	SCC2	127	Phosphoserine
+Q04002	YDR180W	SCC2	157	Phosphoserine
+Q04002	YDR180W	SCC2	162	Phosphoserine%3B
+Q04002	YDR180W	SCC2	163	Phosphoserine
+Q04002	YDR180W	SCC2	231	Phosphothreonine
+Q04002	YDR180W	SCC2	236	Phosphothreonine
+Q04002	YDR180W	SCC2	305	Phosphoserine
+Q04002	YDR180W	SCC2	320	Phosphoserine
+Q04002	YDR180W	SCC2	360	Phosphothreonine%3B
+Q04002	YDR180W	SCC2	753	Phosphoserine
+Q04002	YDR180W	SCC2	1179	Phosphoserine%3B
+Q04002	YDR180W	SCC2	1182	Phosphoserine
+Q04002	YDR180W	SCC2	1183	Phosphoserine%3B
+Q04002	YDR180W	SCC2	1185	Phosphoserine
+P45978	YPR129W	SCD6	2	N-acetylserine
+Q04951	YMR305C	SCW10	279	N-linked
+P13856	YGR152C	RSR1	269	Cysteine
+P13856	YGR152C	RSR1	269	S-geranylgeranyl
+P46654	YLR048W	RPS0B	2	N-acetylserine
+Q12100	YDL025C	RTK1	58	Phosphothreonine
+Q12100	YDL025C	RTK1	60	Phosphoserine
+Q12100	YDL025C	RTK1	216	Phosphoserine
+Q12100	YDL025C	RTK1	334	Glycyl
+P53289	YGR161C	RTS3	172	Phosphoserine
+P53289	YGR161C	RTS3	192	Phosphoserine
+P53289	YGR161C	RTS3	214	Phosphoserine
+P53289	YGR161C	RTS3	238	Phosphoserine
+Q12242	YOR138C	RUP1	56	Phosphoserine
+P39743	YDR388W	RVS167	2	N-acetylserine
+P39743	YDR388W	RVS167	299	Phosphoserine%3B
+P39743	YDR388W	RVS167	321	Phosphoserine%3B
+P39743	YDR388W	RVS167	379	Phosphoserine%3B
+P39743	YDR388W	RVS167	242	Glycyl
+P39743	YDR388W	RVS167	481	Glycyl
+P40856	YJL098W	SAP185	20	Glycyl
+P38352	YBR280C	SAF1	16	Phosphoserine
+P38352	YBR280C	SAF1	266	Phosphoserine
+P20840	YJR004C	SAG1	627	GPI-anchor
+P20840	YJR004C	SAG1	79	N-linked
+P20840	YJR004C	SAG1	109	N-linked
+P20840	YJR004C	SAG1	135	N-linked
+P20840	YJR004C	SAG1	248	N-linked
+P20840	YJR004C	SAG1	282	O-linked
+P20840	YJR004C	SAG1	289	O-linked
+P20840	YJR004C	SAG1	299	O-linked
+P20840	YJR004C	SAG1	303	O-linked
+P20840	YJR004C	SAG1	306	N-linked
+P20840	YJR004C	SAG1	307	O-linked
+P20840	YJR004C	SAG1	308	O-linked
+P20840	YJR004C	SAG1	311	O-linked
+P20840	YJR004C	SAG1	314	O-linked
+P20840	YJR004C	SAG1	315	O-linked
+P20840	YJR004C	SAG1	316	O-linked
+P20840	YJR004C	SAG1	329	O-linked
+P20840	YJR004C	SAG1	331	O-linked
+P20840	YJR004C	SAG1	334	O-linked
+P20840	YJR004C	SAG1	335	O-linked
+P20840	YJR004C	SAG1	338	O-linked
+P20840	YJR004C	SAG1	339	O-linked
+P20840	YJR004C	SAG1	340	O-linked
+P20840	YJR004C	SAG1	341	O-linked
+P20840	YJR004C	SAG1	342	O-linked
+P20840	YJR004C	SAG1	345	O-linked
+P20840	YJR004C	SAG1	346	O-linked
+P20840	YJR004C	SAG1	349	O-linked
+P20840	YJR004C	SAG1	350	O-linked
+P20840	YJR004C	SAG1	364	N-linked
+P20840	YJR004C	SAG1	402	N-linked
+P20840	YJR004C	SAG1	460	N-linked
+P20840	YJR004C	SAG1	485	N-linked
+P20840	YJR004C	SAG1	501	N-linked
+P20840	YJR004C	SAG1	614	N-linked
+P39954	YER043C	SAH1	2	N-acetylserine
+P39954	YER043C	SAH1	393	Phosphothreonine
+P39954	YER043C	SAH1	21	Glycyl
+P39954	YER043C	SAH1	413	Glycyl
+Q08985	YPL273W	SAM4	138	Phosphothreonine
+Q08873	YOR367W	SCP1	2	N-acetylserine
+Q08873	YOR367W	SCP1	11	Phosphoserine
+P40075	YER120W	SCS2	2	N-acetylserine
+P40075	YER120W	SCS2	106	Phosphoserine
+P40357	YGR009C	SEC9	79	Phosphoserine
+P40357	YGR009C	SEC9	92	Phosphoserine
+P40357	YGR009C	SEC9	186	Phosphoserine
+P40357	YGR009C	SEC9	190	Phosphoserine
+P40357	YGR009C	SEC9	213	Phosphoserine
+P40357	YGR009C	SEC9	271	Phosphoserine
+P40357	YGR009C	SEC9	273	Phosphoserine
+P40357	YGR009C	SEC9	315	Phosphoserine
+P40357	YGR009C	SEC9	355	Phosphothreonine
+P40357	YGR009C	SEC9	359	Phosphoserine
+Q01589	YDR077W	SED1	318	GPI-anchor
+Q01589	YDR077W	SED1	22	N-linked
+Q01589	YDR077W	SED1	56	N-linked
+Q01589	YDR077W	SED1	78	N-linked
+Q01589	YDR077W	SED1	92	N-linked
+Q01589	YDR077W	SED1	114	N-linked
+Q01589	YDR077W	SED1	136	N-linked
+Q01589	YDR077W	SED1	152	N-linked
+P34228	YBL066C	SEF1	8	Phosphoserine
+P34228	YBL066C	SEF1	263	Phosphoserine
+P34228	YBL066C	SEF1	806	Phosphoserine
+P36123	YKR028W	SAP190	774	Phosphoserine
+P36123	YKR028W	SAP190	857	Phosphoserine
+P36123	YKR028W	SAP190	862	Phosphoserine
+P36123	YKR028W	SAP190	892	Phosphoserine
+P36123	YKR028W	SAP190	990	Phosphothreonine
+P36123	YKR028W	SAP190	991	Phosphoserine
+P32368	YKL212W	SAC1	246	Glycyl
+P32368	YKL212W	SAC1	358	Glycyl
+P46674	YDR159W	SAC3	568	Phosphoserine
+P46674	YDR159W	SAC3	748	N6-acetyllysine
+P46674	YDR159W	SAC3	866	Phosphoserine
+P43589	YFR005C	SAD1	1	N-acetylmethionine
+Q08986	YPL274W	SAM3	10	Phosphoserine
+Q08986	YPL274W	SAM3	27	Phosphoserine
+Q08986	YPL274W	SAM3	44	Phosphoserine
+Q08986	YPL274W	SAM3	184	N-linked
+Q08986	YPL274W	SAM3	243	N-linked
+P53324	YGR263C	SAY1	2	N-acetylalanine
+P53324	YGR263C	SAY1	85	N-linked
+P53324	YGR263C	SAY1	283	N-linked
+P53324	YGR263C	SAY1	401	N-linked
+P38814	YHR103W	SBE22	72	Phosphoserine
+P38814	YHR103W	SBE22	201	Phosphoserine
+P38814	YHR103W	SBE22	459	Phosphoserine
+P38814	YHR103W	SBE22	517	Phosphoserine
+P38814	YHR103W	SBE22	520	Phosphoserine
+P42223	YDR351W	SBE2	82	Phosphoserine
+P42223	YDR351W	SBE2	83	Phosphoserine
+P42223	YDR351W	SBE2	450	Phosphoserine
+P42223	YDR351W	SBE2	532	Phosphoserine
+P36047	YKL193C	SDS22	56	Phosphoserine
+Q06245	YLR166C	SEC10	142	Phosphoserine
+Q06245	YLR166C	SEC10	485	Phosphoserine
+Q06245	YLR166C	SEC10	507	Phosphoserine
+P48415	YPL085W	SEC16	28	Phosphoserine
+P48415	YPL085W	SEC16	73	Phosphoserine
+P48415	YPL085W	SEC16	144	Phosphoserine
+P48415	YPL085W	SEC16	313	Phosphoserine
+P48415	YPL085W	SEC16	472	Phosphoserine
+P48415	YPL085W	SEC16	483	Phosphoserine
+P48415	YPL085W	SEC16	595	Phosphothreonine
+P48415	YPL085W	SEC16	607	Phosphoserine
+P48415	YPL085W	SEC16	660	Phosphoserine
+P48415	YPL085W	SEC16	663	Phosphoserine
+P48415	YPL085W	SEC16	665	Phosphoserine
+P48415	YPL085W	SEC16	674	Phosphoserine
+P48415	YPL085W	SEC16	678	Phosphoserine
+P48415	YPL085W	SEC16	681	Phosphoserine
+P48415	YPL085W	SEC16	701	Phosphoserine
+P48415	YPL085W	SEC16	704	Phosphoserine
+P48415	YPL085W	SEC16	706	Phosphoserine
+P48415	YPL085W	SEC16	759	Phosphoserine
+P48415	YPL085W	SEC16	762	Phosphoserine
+P48415	YPL085W	SEC16	765	Phosphoserine
+P48415	YPL085W	SEC16	768	Phosphoserine
+P48415	YPL085W	SEC16	843	Phosphoserine
+P48415	YPL085W	SEC16	1511	Phosphoserine
+P48415	YPL085W	SEC16	1515	Phosphoserine
+P48415	YPL085W	SEC16	1578	Phosphoserine
+P48415	YPL085W	SEC16	1602	Phosphoserine
+P48415	YPL085W	SEC16	1603	Phosphoserine
+P48415	YPL085W	SEC16	1611	Phosphoserine
+P48415	YPL085W	SEC16	1617	Phosphoserine
+P48415	YPL085W	SEC16	1778	Phosphoserine
+P48415	YPL085W	SEC16	1875	Phosphoserine
+P48415	YPL085W	SEC16	1973	Phosphoserine
+P48415	YPL085W	SEC16	1986	Phosphoserine
+P48415	YPL085W	SEC16	1992	Phosphoserine
+P48415	YPL085W	SEC16	2049	Phosphothreonine
+P48415	YPL085W	SEC16	2130	Phosphoserine
+P18759	YBR080C	SEC18	226	Phosphoserine
+P15303	YPR181C	SEC23	1	N-acetylmethionine
+P17065	YNL272C	SEC2	1	N-acetylmethionine
+P17065	YNL272C	SEC2	168	Phosphothreonine
+P17065	YNL272C	SEC2	171	Phosphoserine
+P17065	YNL272C	SEC2	515	Phosphoserine
+P38968	YDL195W	SEC31	349	Phosphoserine
+P38968	YDL195W	SEC31	836	Phosphoserine
+P38968	YDL195W	SEC31	974	Phosphoserine
+P38968	YDL195W	SEC31	977	Phosphoserine
+P38968	YDL195W	SEC31	980	Phosphoserine
+P38968	YDL195W	SEC31	988	Phosphoserine
+P38968	YDL195W	SEC31	992	Phosphoserine
+P38968	YDL195W	SEC31	999	Phosphoserine
+P38968	YDL195W	SEC31	1050	Phosphothreonine
+P38968	YDL195W	SEC31	1053	Phosphoserine
+P21825	YPL094C	SEC62	2	N-acetylserine
+P33754	YBR171W	SEC66	5	N-linked
+P33754	YBR171W	SEC66	12	N-linked
+Q05567	YDR294C	DPL1	380	N6-(pyridoxal
+Q07657	YDL225W	SHS1	2	N-acetylserine
+Q07657	YDL225W	SHS1	400	Phosphotyrosine
+Q07657	YDL225W	SHS1	408	Phosphoserine
+Q07657	YDL225W	SHS1	416	Phosphoserine
+Q07657	YDL225W	SHS1	447	Phosphoserine
+Q07657	YDL225W	SHS1	460	Phosphoserine
+Q07657	YDL225W	SHS1	519	Phosphoserine
+Q07657	YDL225W	SHS1	520	Phosphoserine
+Q07657	YDL225W	SHS1	522	Phosphoserine
+Q07657	YDL225W	SHS1	525	Phosphoserine
+Q07657	YDL225W	SHS1	539	Phosphothreonine
+Q07657	YDL225W	SHS1	545	Phosphoserine
+Q07657	YDL225W	SHS1	548	Phosphoserine
+Q07657	YDL225W	SHS1	426	Glycyl
+Q07657	YDL225W	SHS1	437	Glycyl
+P38717	YNL257C	SIP3	1206	N-linked
+P32900	YHR149C	SKG6	137	Phosphoserine
+P32900	YHR149C	SKG6	169	Phosphothreonine
+P32900	YHR149C	SKG6	191	Phosphoserine
+P32900	YHR149C	SKG6	193	Phosphoserine
+P32900	YHR149C	SKG6	219	Phosphoserine
+P32900	YHR149C	SKG6	221	Phosphothreonine
+P32900	YHR149C	SKG6	222	Phosphoserine
+P32900	YHR149C	SKG6	251	Phosphoserine
+P32900	YHR149C	SKG6	369	Phosphoserine
+P32900	YHR149C	SKG6	672	Phosphoserine
+P32900	YHR149C	SKG6	717	Phosphoserine
+P35207	YLR398C	SKI2	209	Phosphoserine
+Q08491	YOR076C	SKI7	88	Phosphoserine
+Q08491	YOR076C	SKI7	90	Phosphoserine
+P42843	YNL311C	SKP2	594	Phosphothreonine
+Q00772	YHR030C	SLT2	190	Phosphothreonine
+Q00772	YHR030C	SLT2	192	Phosphotyrosine
+P32566	YGR229C	SMI1	202	Phosphoserine
+P32566	YGR229C	SMI1	203	Phosphoserine
+P32566	YGR229C	SMI1	376	Phosphothreonine
+P32566	YGR229C	SMI1	381	Phosphoserine
+P32566	YGR229C	SMI1	394	Phosphoserine
+P32566	YGR229C	SMI1	400	Phosphoserine
+P32566	YGR229C	SMI1	453	Glycyl
+Q04174	YOR149C	SMP3	403	N-linked
+Q04174	YOR149C	SMP3	452	N-linked
+P38990	YER129W	SAK1	43	Phosphothreonine
+P38990	YER129W	SAK1	964	Phosphoserine
+P38990	YER129W	SAK1	1126	Phosphoserine
+P39955	YER047C	SAP1	536	Phosphoserine
+Q99314	YOR213C	SAS5	144	Phosphoserine
+Q00711	YKL148C	SDH1	90	Tele-8alpha-FAD
+P24280	YMR079W	SEC14	302	Phosphoserine
+P24280	YMR079W	SEC14	42	Glycyl
+P24280	YMR079W	SEC14	84	Glycyl
+P40510	YIL074C	SER33	2	N-acetylserine
+P40510	YIL074C	SER33	22	Phosphoserine
+P40510	YIL074C	SER33	29	Phosphoserine
+P40510	YIL074C	SER33	33	Phosphoserine
+P46995	YJL168C	SET2	10	Phosphoserine
+P46995	YJL168C	SET2	522	Phosphoserine
+Q08446	YOR057W	SGT1	168	Phosphoserine
+Q08446	YOR057W	SGT1	171	Phosphoserine
+Q08446	YOR057W	SGT1	32	Glycyl
+P38634	YLR079W	SIC1	5	Phosphothreonine%3B
+P38634	YLR079W	SIC1	33	Phosphothreonine
+P38634	YLR079W	SIC1	76	Phosphoserine
+P38634	YLR079W	SIC1	173	Phosphothreonine
+P38634	YLR079W	SIC1	198	Phosphoserine
+P38634	YLR079W	SIC1	201	Phosphoserine
+P38634	YLR079W	SIC1	268	Lysine
+P38634	YLR079W	SIC1	272	Lysine
+P38634	YLR079W	SIC1	274	Lysine
+P38262	YBR103W	SIF2	137	Phosphoserine
+Q06315	YLR187W	SKG3	10	Phosphoserine
+Q06315	YLR187W	SKG3	31	Phosphoserine
+Q06315	YLR187W	SKG3	578	Phosphothreonine
+Q06315	YLR187W	SKG3	580	Phosphoserine
+Q06315	YLR187W	SKG3	592	Phosphoserine
+Q06315	YLR187W	SKG3	701	Phosphoserine
+Q06315	YLR187W	SKG3	954	Phosphoserine
+P38314	YBR214W	SDS24	94	Phosphoserine
+P38314	YBR214W	SDS24	458	Phosphoserine
+P38314	YBR214W	SDS24	524	Phosphoserine
+P38164	YBL104C	SEA4	123	Phosphoserine
+P38164	YBL104C	SEA4	136	Phosphoserine
+P33332	YER008C	SEC3	290	Phosphothreonine
+P33332	YER008C	SEC3	606	Phosphoserine
+P89102	YDR166C	SEC5	184	Phosphoserine
+P38890	YHR207C	SET5	517	Phosphoserine
+P47166	YJR134C	SGM1	2	N-acetylserine
+P47166	YJR134C	SGM1	151	Phosphoserine
+P47166	YJR134C	SGM1	538	Phosphoserine
+P47166	YJR134C	SGM1	549	Phosphoserine
+P47166	YJR134C	SGM1	568	Phosphoserine
+P47166	YJR134C	SGM1	571	Phosphoserine
+P47166	YJR134C	SGM1	576	Phosphoserine
+P47166	YJR134C	SGM1	589	Phosphoserine
+P32578	YDR422C	SIP1	33	Phosphoserine
+P32578	YDR422C	SIP1	181	Phosphoserine
+P32578	YDR422C	SIP1	198	Phosphoserine
+P32578	YDR422C	SIP1	200	Phosphoserine
+P32578	YDR422C	SIP1	206	Phosphoserine
+P32578	YDR422C	SIP1	209	Phosphoserine
+P32578	YDR422C	SIP1	220	Phosphoserine
+P32578	YDR422C	SIP1	331	Phosphoserine
+P32578	YDR422C	SIP1	494	Phosphoserine
+P32578	YDR422C	SIP1	497	Phosphoserine
+P32578	YDR422C	SIP1	643	Phosphoserine
+P32578	YDR422C	SIP1	2	N-myristoyl
+P33336	YGR143W	SKN1	56	Phosphoserine
+P33336	YGR143W	SKN1	65	Phosphoserine
+P33336	YGR143W	SKN1	67	Phosphoserine
+P33336	YGR143W	SKN1	92	Phosphoserine
+P33336	YGR143W	SKN1	103	Phosphoserine
+P33336	YGR143W	SKN1	142	Phosphoserine
+P33336	YGR143W	SKN1	162	Phosphoserine
+P33336	YGR143W	SKN1	165	Phosphoserine
+P33336	YGR143W	SKN1	170	Phosphoserine
+P33336	YGR143W	SKN1	176	Phosphoserine
+P33336	YGR143W	SKN1	337	N-linked
+P33336	YGR143W	SKN1	426	N-linked
+P33336	YGR143W	SKN1	513	N-linked
+P33336	YGR143W	SKN1	590	N-linked
+P33336	YGR143W	SKN1	615	N-linked
+P33336	YGR143W	SKN1	743	N-linked
+Q03656	YMR216C	SKY1	383	Phosphothreonine
+Q03656	YMR216C	SKY1	386	Phosphothreonine
+Q03656	YMR216C	SKY1	388	Phosphoserine
+Q03656	YMR216C	SKY1	393	Phosphoserine
+Q03656	YMR216C	SKY1	410	Phosphoserine
+Q03656	YMR216C	SKY1	427	Phosphoserine
+Q03656	YMR216C	SKY1	432	Phosphoserine
+Q03656	YMR216C	SKY1	445	Phosphoserine
+Q03656	YMR216C	SKY1	449	Phosphoserine
+Q03656	YMR216C	SKY1	453	Phosphoserine
+P38283	YBR156C	SLI15	268	Phosphoserine
+P38283	YBR156C	SLI15	489	Phosphoserine
+P14906	YOR254C	SEC63	512	Phosphoserine
+Q04279	YMR086W	SEG1	48	Phosphoserine
+Q04279	YMR086W	SEG1	220	Phosphoserine
+Q04279	YMR086W	SEG1	235	Phosphoserine
+Q04279	YMR086W	SEG1	238	Phosphoserine
+Q04279	YMR086W	SEG1	319	Phosphoserine
+Q04279	YMR086W	SEG1	339	Phosphoserine
+Q04279	YMR086W	SEG1	352	Phosphoserine
+Q04279	YMR086W	SEG1	434	Phosphoserine
+Q04279	YMR086W	SEG1	461	Phosphoserine
+Q04279	YMR086W	SEG1	467	Phosphothreonine
+Q04279	YMR086W	SEG1	630	Phosphoserine
+Q04279	YMR086W	SEG1	675	Phosphothreonine
+Q04279	YMR086W	SEG1	758	Phosphoserine
+Q04279	YMR086W	SEG1	816	Phosphoserine
+Q04279	YMR086W	SEG1	818	Phosphoserine
+Q04279	YMR086W	SEG1	855	Phosphoserine
+P53011	YGL100W	SEH1	257	Phosphoserine
+O94742	YDR363W-A	SEM1	2	N-acetylserine
+O94742	YDR363W-A	SEM1	12	Phosphoserine
+P53953	YNL049C	SFB2	51	Phosphoserine
+P38166	YBL102W	SFT2	2	N-acetylserine
+P38166	YBL102W	SFT2	60	Phosphoserine
+P53965	YNL032W	SIW14	94	Phosphoserine
+Q04195	YDR409W	SIZ1	132	Phosphoserine
+Q04195	YDR409W	SIZ1	794	Phosphoserine
+Q3E784	YER180C-A	SLO1	2	N-acetylserine
+Q3E784	YER180C-A	SLO1	10	Phosphoserine
+Q02775	YDR088C	SLU7	120	Phosphoserine
+Q02775	YDR088C	SLU7	212	Phosphothreonine
+P40072	YER116C	SLX8	50	Phosphoserine
+P40072	YER116C	SLX8	66	Phosphothreonine
+P40072	YER116C	SLX8	67	Phosphoserine
+P11655	YNR026C	SEC12	439	N-linked
+P11655	YNR026C	SEC12	462	N-linked
+P22224	YGL233W	SEC15	286	Phosphoserine
+P22214	YLR268W	SEC22	160	Phosphoserine
+P07560	YFL005W	SEC4	201	Phosphoserine
+P07560	YFL005W	SEC4	204	Phosphoserine
+P07560	YFL005W	SEC4	214	S-geranylgeranyl
+P07560	YFL005W	SEC4	215	S-geranylgeranyl
+P11075	YDR170C	SEC7	212	Phosphoserine
+P11075	YDR170C	SEC7	215	Phosphoserine
+P11075	YDR170C	SEC7	334	Phosphothreonine
+P11075	YDR170C	SEC7	447	Phosphoserine
+P11075	YDR170C	SEC7	452	Phosphoserine
+P11075	YDR170C	SEC7	455	Phosphoserine
+P11075	YDR170C	SEC7	807	Phosphoserine
+P11075	YDR170C	SEC7	1226	Phosphoserine
+P11075	YDR170C	SEC7	1240	Phosphothreonine
+P11075	YDR170C	SEC7	1741	Phosphoserine
+P11075	YDR170C	SEC7	1752	Phosphoserine
+P11075	YDR170C	SEC7	797	Glycyl
+P32855	YPR055W	SEC8	16	Phosphoserine
+P32855	YPR055W	SEC8	19	Phosphoserine
+P40316	YDR113C	PDS1	185	Phosphoserine
+P40316	YDR113C	PDS1	186	Phosphoserine
+P40316	YDR113C	PDS1	212	Phosphoserine
+P40316	YDR113C	PDS1	213	Phosphoserine
+P40316	YDR113C	PDS1	277	Phosphoserine
+P40316	YDR113C	PDS1	292	Phosphoserine%3B
+P25365	YCR067C	SED4	65	Phosphoserine
+P25365	YCR067C	SED4	388	N-linked
+P25365	YCR067C	SED4	620	N-linked
+P25365	YCR067C	SED4	1039	N-linked
+P40054	YER081W	SER3	22	Phosphoserine
+P40054	YER081W	SER3	29	Phosphoserine
+P40054	YER081W	SER3	33	Phosphoserine
+P36124	YKR029C	SET3	236	Phosphoserine
+P36124	YKR029C	SET3	684	Phosphoserine
+P36124	YKR029C	SET3	718	Phosphoserine
+P36124	YKR029C	SET3	719	Phosphothreonine
+P36124	YKR029C	SET3	741	Phosphoserine
+Q12314	YOR021C	SFM1	204	Phosphoserine
+Q12314	YOR021C	SFM1	207	Phosphoserine
+P53313	YGR245C	SDA1	278	Phosphoserine
+P32602	YBL050W	SEC17	2	N-acetylserine
+P32602	YBL050W	SEC17	261	Glycyl
+P40482	YIL109C	SEC24	178	Phosphoserine
+P32844	YIL068C	SEC6	2	N-acetylserine
+P34250	YKL105C	SEG2	137	Phosphoserine
+P34250	YKL105C	SEG2	280	Phosphoserine
+P34250	YKL105C	SEG2	504	Phosphoserine
+P34250	YKL105C	SEG2	507	Phosphoserine
+P34250	YKL105C	SEG2	556	Phosphoserine
+P34250	YKL105C	SEG2	980	Phosphoserine
+P34250	YKL105C	SEG2	1022	Phosphoserine
+P34250	YKL105C	SEG2	526	Glycyl
+P34250	YKL105C	SEG2	743	Glycyl
+P38272	YBR130C	SHE3	343	Phosphoserine
+P38272	YBR130C	SHE3	394	Phosphoserine
+P53334	YGR279C	SCW4	89	N-linked
+P33330	YOR184W	SER1	20	Phosphothreonine
+P33330	YOR184W	SER1	112	Phosphoserine
+P33330	YOR184W	SER1	218	N6-(pyridoxal
+P38827	YHR119W	SET1	625	Phosphoserine
+P38827	YHR119W	SET1	875	Phosphothreonine
+Q12369	YLL003W	SFI1	10	Phosphoserine
+Q12369	YLL003W	SFI1	855	Phosphoserine
+P35735	YKL051W	SFK1	208	Phosphoserine
+P20134	YOR140W	SFL1	220	Phosphoserine
+P20134	YOR140W	SFL1	556	Phosphoserine
+P20134	YOR140W	SFL1	733	Phosphoserine
+Q12234	YOR216C	RUD3	55	Phosphoserine
+Q12234	YOR216C	RUD3	64	Phosphoserine
+Q12234	YOR216C	RUD3	468	Phosphoserine
+Q07458	YDL076C	RXT3	2	N-acetylserine
+P34218	YBL052C	SAS3	367	N6-acetyllysine%3B
+P40963	YMR127C	SAS2	168	N6-acetyllysine%3B
+P36048	YKL173W	SNU114	85	Phosphoserine
+P36048	YKL173W	SNU114	88	Phosphothreonine
+P10870	YDL194W	SNF3	383	N-linked
+P18888	YHL025W	SNF6	165	Phosphothreonine
+P39929	YLR025W	SNF7	72	Phosphothreonine
+P39929	YLR025W	SNF7	119	Phosphoserine
+P39929	YLR025W	SNF7	193	Phosphoserine
+P39929	YLR025W	SNF7	229	Glycyl
+P00445	YJR104C	SOD1	26	Phosphoserine
+P00445	YJR104C	SOD1	39	Phosphoserine
+P00445	YJR104C	SOD1	99	Phosphoserine
+P00445	YJR104C	SOD1	117	Phosphoserine
+P00445	YJR104C	SOD1	132	Phosphothreonine
+P00445	YJR104C	SOD1	138	Phosphothreonine
+P00445	YJR104C	SOD1	19	Glycyl
+P00445	YJR104C	SOD1	70	Glycyl
+Q03954	YDR201W	SPC19	107	Phosphoserine
+Q03954	YDR201W	SPC19	116	Phosphoserine
+Q12455	YLR146C	SPE4	5	Phosphoserine
+P06843	YER161C	SPT2	2	N-acetylserine
+P06843	YER161C	SPT2	126	Phosphoserine
+P35177	YBR081C	SPT7	78	Phosphothreonine%3B
+P35177	YBR081C	SPT7	88	Phosphoserine
+P35177	YBR081C	SPT7	1293	Phosphoserine
+P38985	YDL092W	SRP14	8	Phosphoserine
+P32342	YKL122C	SRP21	2	N-acetylserine
+P40505	YIL084C	SDS3	166	Phosphoserine
+P40505	YIL084C	SDS3	211	Phosphoserine
+P15367	YIR022W	SEC11	121	N-linked
+P38810	YHR098C	SFB3	15	Phosphoserine
+P38810	YHR098C	SFB3	72	Phosphothreonine
+P38810	YHR098C	SFB3	83	Phosphoserine
+P38810	YHR098C	SFB3	85	Phosphoserine
+P38810	YHR098C	SFB3	94	Phosphoserine
+P38810	YHR098C	SFB3	101	Phosphoserine
+P38810	YHR098C	SFB3	110	Phosphoserine
+P38810	YHR098C	SFB3	216	Phosphothreonine
+P51534	YOR035C	SHE4	18	Phosphoserine
+P40073	YER118C	SHO1	166	Phosphoserine
+P40073	YER118C	SHO1	59	N-linked
+P25294	YNL007C	SIS1	275	Phosphoserine
+P52286	YDR328C	SKP1	177	Phosphothreonine
+P33338	YNL243W	SLA2	294	Phosphothreonine
+P33338	YNL243W	SLA2	298	Phosphothreonine
+P33338	YNL243W	SLA2	308	Phosphoserine
+P33338	YNL243W	SLA2	555	Phosphoserine
+Q12078	YLR034C	SMF3	87	N-linked
+P25357	YCR033W	SNT1	187	Phosphoserine
+P25357	YCR033W	SNT1	395	Phosphoserine
+P25357	YCR033W	SNT1	796	Phosphothreonine
+P25357	YCR033W	SNT1	1037	Phosphoserine
+P50278	YNR034W	SOL1	65	Phosphoserine
+P50278	YNR034W	SOL1	68	Phosphoserine
+P50278	YNR034W	SOL1	320	Phosphothreonine
+Q08199	YOL031C	SIL1	105	N-linked
+Q08199	YOL031C	SIL1	181	N-linked
+Q08199	YOL031C	SIL1	215	N-linked
+Q08199	YOL031C	SIL1	233	N-linked
+Q08199	YOL031C	SIL1	315	N-linked
+Q08199	YOL031C	SIL1	333	N-linked
+P40472	YIL123W	SIM1	423	N-linked
+P11978	YDR227W	SIR4	692	Phosphoserine
+P11978	YDR227W	SIR4	1128	Glycyl
+P36169	YKR100C	SKG1	142	Phosphoserine
+P36169	YKR100C	SKG1	273	Phosphothreonine
+P32790	YBL007C	SLA1	447	Phosphoserine
+P32790	YBL007C	SLA1	449	Phosphoserine
+P32790	YBL007C	SLA1	454	Phosphoserine
+P32790	YBL007C	SLA1	799	Phosphoserine
+P32790	YBL007C	SLA1	831	Phosphothreonine
+P32790	YBL007C	SLA1	858	Phosphothreonine
+P32790	YBL007C	SLA1	887	Phosphothreonine
+P32790	YBL007C	SLA1	904	Phosphothreonine
+P32790	YBL007C	SLA1	984	Phosphothreonine
+P32790	YBL007C	SLA1	993	Phosphothreonine
+P32790	YBL007C	SLA1	996	Phosphoserine
+P32790	YBL007C	SLA1	1075	Phosphothreonine
+P32790	YBL007C	SLA1	471	Glycyl
+P32790	YBL007C	SLA1	548	Glycyl
+P47037	YJL074C	SMC3	112	N6-acetyllysine
+P47037	YJL074C	SMC3	113	N6-acetyllysine
+P38925	YOL122C	SMF1	24	Phosphoserine
+P38925	YOL122C	SMF1	33	Glycyl
+P38925	YOL122C	SMF1	34	Glycyl
+Q04007	YDR186C	SND1	309	Phosphoserine
+Q04007	YDR186C	SND1	310	Phosphoserine
+Q04007	YDR186C	SND1	311	Phosphoserine
+Q04007	YDR186C	SND1	332	Phosphoserine
+Q04007	YDR186C	SND1	334	Phosphoserine
+Q04007	YDR186C	SND1	692	Phosphoserine
+Q04007	YDR186C	SND1	694	Phosphoserine
+Q04007	YDR186C	SND1	706	Phosphoserine
+Q04007	YDR186C	SND1	841	Phosphoserine
+Q04007	YDR186C	SND1	668	Glycyl
+Q04007	YDR186C	SND1	670	Glycyl
+P38956	YDR073W	SNF11	2	N-acetylserine
+P22082	YOR290C	SNF2	358	Phosphoserine
+P22082	YOR290C	SNF2	383	Phosphothreonine
+P22082	YOR290C	SNF2	716	Phosphoserine
+P22082	YOR290C	SNF2	1340	Phosphoserine
+P22082	YOR290C	SNF2	543	Glycyl
+P46950	YGR197C	SNG1	91	Phosphothreonine
+P53438	YMR016C	SOK2	771	Phosphoserine
+P37262	YCR073W-A	SOL2	42	Phosphoserine
+P37262	YCR073W-A	SOL2	64	Phosphoserine
+P31109	YAL030W	SNC1	95	S-palmitoyl
+P31109	YAL030W	SNC1	63	Glycyl
+P33328	YOR327C	SNC2	58	Phosphoserine
+P33328	YOR327C	SNC2	94	S-palmitoyl
+P33328	YOR327C	SNC2	62	Glycyl
+Q12420	YOR308C	SNU66	268	Phosphoserine
+P40317	YDR006C	SOK1	40	Phosphoserine
+P40317	YDR006C	SOK1	53	Phosphoserine
+P40317	YDR006C	SOK1	191	Phosphoserine
+P40317	YDR006C	SOK1	193	Phosphoserine
+P40317	YDR006C	SOK1	245	Phosphoserine
+P25808	YFL002C	SPB4	254	Phosphoserine
+P46965	YJR010C-A	SPC1	2	N-acetylserine
+P38915	YLR055C	SPT8	85	Phosphothreonine
+P38915	YLR055C	SPT8	108	Phosphoserine
+P38915	YLR055C	SPT8	123	Phosphoserine
+P38915	YLR055C	SPT8	131	Phosphoserine
+P38915	YLR055C	SPT8	451	Phosphoserine
+Q03707	YML034W	SRC1	78	Phosphoserine
+Q03707	YML034W	SRC1	80	Phosphoserine
+Q03707	YML034W	SRC1	85	Phosphoserine
+Q03707	YML034W	SRC1	181	Phosphoserine
+Q03707	YML034W	SRC1	203	Phosphoserine
+Q03707	YML034W	SRC1	204	Phosphoserine
+Q03707	YML034W	SRC1	206	Phosphoserine
+Q03707	YML034W	SRC1	301	Phosphoserine
+Q03707	YML034W	SRC1	394	Phosphothreonine
+Q03707	YML034W	SRC1	427	Phosphoserine
+P39931	YLR250W	SSP120	212	Phosphothreonine
+P53172	YGL056C	SDS23	9	Phosphoserine
+P53172	YGL056C	SDS23	42	Phosphoserine
+P53172	YGL056C	SDS23	46	Phosphoserine
+P53172	YGL056C	SDS23	430	Phosphoserine
+Q12118	YOR007C	SGT2	308	Phosphothreonine
+P38200	YBL031W	SHE1	165	Phosphoserine
+P36024	YKR072C	SIS2	47	Phosphoserine
+P36024	YKR072C	SIS2	50	Phosphoserine
+P36024	YKR072C	SIS2	54	Phosphoserine
+P36024	YKR072C	SIS2	56	Phosphoserine
+P36024	YKR072C	SIS2	155	Phosphoserine
+P38889	YHR206W	SKN7	427	4-aspartylphosphate
+Q02100	YNL167C	SKO1	94	Phosphoserine
+Q02100	YNL167C	SKO1	113	Phosphothreonine
+Q02100	YNL167C	SKO1	399	Phosphoserine
+Q02100	YNL167C	SKO1	558	Phosphoserine
+P34252	YKL108W	SLD2	84	Phosphothreonine%3B
+Q04964	YML058W	SML1	1	N-acetylmethionine
+Q04964	YML058W	SML1	56	Phosphoserine%3B
+Q04964	YML058W	SML1	58	Phosphoserine%3B
+Q04964	YML058W	SML1	60	Phosphoserine%3B
+Q12306	YDR510W	SMT3	2	N-acetylserine
+Q12306	YDR510W	SMT3	2	Phosphoserine
+Q12306	YDR510W	SMT3	4	Phosphoserine
+Q12306	YDR510W	SMT3	98	Glycyl
+P32364	YKL079W	SMY1	583	Phosphothreonine
+P32909	YBR172C	SMY2	12	Phosphoserine
+P32909	YBR172C	SMY2	96	Phosphoserine
+P32909	YBR172C	SMY2	129	Phosphothreonine
+P32909	YBR172C	SMY2	311	Phosphothreonine
+P32909	YBR172C	SMY2	545	Phosphoserine
+P32909	YBR172C	SMY2	602	Phosphoserine
+P56508	YDR525W-A	SNA2	71	Phosphoserine
+P56508	YDR525W-A	SNA2	77	Phosphoserine
+P00447	YHR008C	SOD2	147	Phosphothreonine
+P00447	YHR008C	SOD2	149	Phosphothreonine
+P23201	YLL021W	SPA2	182	Phosphoserine
+P23201	YLL021W	SPA2	183	Phosphoserine
+P23201	YLL021W	SPA2	220	Phosphothreonine
+P23201	YLL021W	SPA2	254	Phosphoserine
+P23201	YLL021W	SPA2	274	Phosphoserine
+P23201	YLL021W	SPA2	301	Phosphoserine
+P23201	YLL021W	SPA2	585	Phosphoserine
+P23201	YLL021W	SPA2	599	Phosphoserine
+P23201	YLL021W	SPA2	646	Phosphoserine
+P23201	YLL021W	SPA2	817	Phosphoserine
+P23201	YLL021W	SPA2	820	Phosphoserine
+P23201	YLL021W	SPA2	865	Phosphoserine
+P23201	YLL021W	SPA2	883	Phosphoserine
+P23201	YLL021W	SPA2	910	Phosphoserine
+P23201	YLL021W	SPA2	937	Phosphoserine
+P23201	YLL021W	SPA2	961	Phosphoserine
+P23201	YLL021W	SPA2	979	Phosphoserine
+P23201	YLL021W	SPA2	1053	Phosphoserine
+P23201	YLL021W	SPA2	1056	Phosphoserine
+P23201	YLL021W	SPA2	1080	Phosphoserine
+P23201	YLL021W	SPA2	1173	Phosphoserine
+P23201	YLL021W	SPA2	1179	Phosphothreonine
+P23201	YLL021W	SPA2	1180	Phosphoserine
+P23201	YLL021W	SPA2	1251	Phosphothreonine
+P23201	YLL021W	SPA2	1263	Phosphoserine
+P36131	YKR037C	SPC34	199	Phosphothreonine%3B
+P53540	YNL126W	SPC98	124	Phosphoserine
+P53540	YNL126W	SPC98	136	Phosphoserine
+P40092	YER150W	SPI1	127	GPI-anchor
+P40092	YER150W	SPI1	41	N-linked
+P40092	YER150W	SPI1	59	N-linked
+P53541	YNL012W	SPO1	233	N-linked
+P53541	YNL012W	SPO1	293	N-linked
+P53541	YNL012W	SPO1	303	N-linked
+P53541	YNL012W	SPO1	500	N-linked
+P53541	YNL012W	SPO1	536	N-linked
+P53541	YNL012W	SPO1	560	N-linked
+P53541	YNL012W	SPO1	563	N-linked
+P53541	YNL012W	SPO1	572	N-linked
+P35209	YMR179W	SPT21	454	Phosphoserine
+Q06168	YLR321C	SFH1	78	Phosphoserine
+P25554	YCL010C	SGF29	139	Phosphoserine
+P22579	YOL004W	SIN3	137	Phosphoserine
+P22579	YOL004W	SIN3	303	Phosphothreonine
+P22579	YOL004W	SIN3	304	Phosphothreonine
+P22579	YOL004W	SIN3	316	Phosphoserine
+P22579	YOL004W	SIN3	1046	Phosphoserine
+P34164	YGL208W	SIP2	66	Phosphoserine
+P34164	YGL208W	SIP2	298	Phosphoserine
+P34164	YGL208W	SIP2	2	N-myristoyl
+P40210	YMR140W	SIP5	13	Phosphoserine
+P40210	YMR140W	SIP5	183	Phosphothreonine
+P40210	YMR140W	SIP5	433	Phosphothreonine
+P40210	YMR140W	SIP5	436	Phosphoserine
+P40210	YMR140W	SIP5	438	Phosphothreonine
+P53955	YNL047C	SLM2	626	Phosphoserine
+P53955	YNL047C	SLM2	649	Phosphoserine
+P53955	YNL047C	SLM2	653	Phosphoserine
+Q12098	YLR135W	SLX4	72	Phosphothreonine%3B
+Q12098	YLR135W	SLX4	113	Phosphothreonine%3B
+Q12098	YLR135W	SLX4	289	Phosphoserine%3B
+Q12098	YLR135W	SLX4	319	Phosphothreonine%3B
+Q12098	YLR135W	SLX4	329	Phosphoserine%3B
+Q12098	YLR135W	SLX4	355	Phosphoserine%3B
+P54867	YOR008C	SLG1	331	Phosphoserine
+P54867	YOR008C	SLG1	353	Phosphoserine
+P54867	YOR008C	SLG1	65	N-linked
+P40485	YIL105C	SLM1	145	Phosphoserine
+P40485	YIL105C	SLM1	150	Phosphoserine
+P40485	YIL105C	SLM1	153	Phosphoserine
+P39928	YIL147C	SLN1	502	Phosphoserine
+P39928	YIL147C	SLN1	576	Phosphohistidine%3B
+P39928	YIL147C	SLN1	758	Phosphoserine
+P39928	YIL147C	SLN1	833	Phosphoserine
+P39928	YIL147C	SLN1	1041	Phosphoserine
+P39928	YIL147C	SLN1	1044	Phosphoserine
+P39928	YIL147C	SLN1	1144	4-aspartylphosphate
+P39928	YIL147C	SLN1	100	N-linked
+P39928	YIL147C	SLN1	138	N-linked
+P39928	YIL147C	SLN1	142	N-linked
+P39928	YIL147C	SLN1	181	N-linked
+P39928	YIL147C	SLN1	224	N-linked
+P39928	YIL147C	SLN1	272	N-linked
+Q12267	YLR086W	SMC4	2	N-acetylserine
+Q12267	YLR086W	SMC4	43	Phosphothreonine
+Q12267	YLR086W	SMC4	113	Phosphoserine
+P18480	YBR289W	SNF5	818	Phosphoserine
+P32568	YDR011W	SNQ2	2	N-acetylserine
+P32568	YDR011W	SNQ2	26	Phosphoserine
+P32568	YDR011W	SNQ2	29	Phosphoserine
+P32568	YDR011W	SNQ2	64	Phosphoserine
+P32568	YDR011W	SNQ2	80	Phosphoserine
+P32568	YDR011W	SNQ2	86	Phosphoserine
+P32568	YDR011W	SNQ2	1153	Phosphothreonine
+P32568	YDR011W	SNQ2	273	N-linked
+P32568	YDR011W	SNQ2	334	N-linked
+P32568	YDR011W	SNQ2	518	N-linked
+P32568	YDR011W	SNQ2	730	N-linked
+P32568	YDR011W	SNQ2	874	N-linked
+P32568	YDR011W	SNQ2	1401	N-linked
+P53207	YGR013W	SNU71	512	Phosphoserine
+P53207	YGR013W	SNU71	514	Phosphoserine
+Q12133	YLR066W	SPC3	102	N-linked
+Q12133	YLR066W	SPC3	173	N-linked
+P36094	YKL042W	SPC42	213	Phosphoserine
+P36094	YKL042W	SPC42	217	Phosphoserine
+P36094	YKL042W	SPC42	284	Phosphoserine
+P36094	YKL042W	SPC42	329	Phosphoserine
+P17123	YHR152W	SPO12	2	N-acetylserine
+P17123	YHR152W	SPO12	118	Phosphoserine
+P17123	YHR152W	SPO12	125	Phosphoserine
+P50875	YOL148C	SPT20	446	Phosphoserine
+P50875	YOL148C	SPT20	516	Phosphothreonine
+Q06132	YLR336C	SGD1	736	Phosphoserine
+P06701	YLR442C	SIR3	2	N-acetylalanine
+P34226	YBL061C	SKT5	148	Phosphoserine
+P34226	YBL061C	SKT5	561	Phosphoserine
+P34226	YBL061C	SKT5	563	Phosphoserine
+P34226	YBL061C	SKT5	564	Phosphothreonine
+P34226	YBL061C	SKT5	693	Cysteine
+P34226	YBL061C	SKT5	693	S-farnesyl
+Q08581	YOR195W	SLK19	7	Phosphothreonine%3B
+Q08581	YOR195W	SLK19	188	Phosphoserine
+Q08581	YOR195W	SLK19	189	Phosphoserine
+Q08581	YOR195W	SLK19	201	Phosphoserine%3B
+Q08581	YOR195W	SLK19	216	Phosphoserine
+Q08581	YOR195W	SLK19	273	Phosphothreonine
+Q08581	YOR195W	SLK19	283	Phosphoserine
+Q12232	YOR154W	SLP1	25	N-linked
+Q12232	YOR154W	SLP1	378	N-linked
+Q12232	YOR154W	SLP1	381	N-linked
+Q12232	YOR154W	SLP1	408	N-linked
+Q12232	YOR154W	SLP1	448	N-linked
+Q12232	YOR154W	SLP1	486	N-linked
+P32380	YDR356W	SPC110	18	Phosphothreonine
+P32380	YDR356W	SPC110	60	Phosphoserine%3B
+P32380	YDR356W	SPC110	64	Phosphothreonine%3B
+P32380	YDR356W	SPC110	68	Phosphothreonine%3B
+P32380	YDR356W	SPC110	80	Phosphoserine
+P32380	YDR356W	SPC110	529	Phosphoserine
+P25582	YCL054W	SPB1	455	Phosphoserine
+P25582	YCL054W	SPB1	464	Phosphoserine
+P25582	YCL054W	SPB1	529	Phosphoserine
+Q04398	YDR504C	SPG3	86	N-linked
+P33419	YPL124W	SPC29	18	Phosphothreonine
+P33419	YPL124W	SPC29	65	Phosphoserine
+P33419	YPL124W	SPC29	240	Phosphothreonine%3B
+Q03029	YPL130W	SPO19	198	GPI-anchor
+P38904	YDR464W	SPP41	1014	Phosphoserine
+P38904	YDR464W	SPP41	1067	Phosphoserine
+P38904	YDR464W	SPP41	981	Glycyl
+P38904	YDR464W	SPP41	1154	Glycyl
+P32603	YOR190W	SPR1	201	N-linked
+P32573	YNL202W	SPS19	188	Glycyl
+P32558	YGL207W	SPT16	526	Phosphoserine
+P32558	YGL207W	SPT16	765	Phosphoserine
+P35210	YKL020C	SPT23	468	Phosphoserine
+P53866	YNL224C	SQS1	105	Phosphoserine
+P53866	YNL224C	SQS1	217	Phosphoserine
+P53866	YNL224C	SQS1	255	Phosphoserine
+P53866	YNL224C	SQS1	334	Phosphoserine
+P53866	YNL224C	SQS1	343	Phosphoserine
+P53866	YNL224C	SQS1	345	Phosphoserine
+P24276	YDR293C	SSD1	2	N-acetylserine
+P24276	YDR293C	SSD1	40	Phosphoserine
+P24276	YDR293C	SSD1	164	Phosphoserine
+P24276	YDR293C	SSD1	183	Phosphoserine
+P24276	YDR293C	SSD1	227	Phosphothreonine
+P24276	YDR293C	SSD1	286	Phosphoserine
+P24276	YDR293C	SSD1	322	Phosphoserine
+P24276	YDR293C	SSD1	491	Phosphoserine
+P24276	YDR293C	SSD1	492	Phosphoserine
+P24276	YDR293C	SSD1	688	Phosphotyrosine
+P32343	YKL124W	SSH4	358	Phosphoserine
+P32343	YKL124W	SSH4	212	N-linked
+P32343	YKL124W	SSH4	356	N-linked
+P32343	YKL124W	SSH4	430	N-linked
+P32343	YKL124W	SSH4	507	N-linked
+P32343	YKL124W	SSH4	557	N-linked
+P32343	YKL124W	SSH4	575	N-linked
+P32343	YKL124W	SSH4	367	Glycyl
+P15705	YOR027W	STI1	227	Phosphoserine
+P15705	YOR027W	STI1	99	Glycyl
+P15705	YOR027W	STI1	168	Glycyl
+P15705	YOR027W	STI1	384	Glycyl
+P14359	YJL151C	SNA3	125	Glycyl
+P38839	YHR136C	SPL2	59	Phosphoserine
+P38839	YHR136C	SPL2	86	Phosphoserine
+Q12516	YDL133W	SRF1	45	Phosphoserine
+Q12516	YDL133W	SRF1	167	Phosphoserine
+Q12516	YDL133W	SRF1	297	N-linked
+Q12516	YDL133W	SRF1	385	N-linked
+Q12020	YLR082C	SRL2	11	Phosphoserine
+Q12020	YLR082C	SRL2	139	Phosphoserine
+P36167	YKR091W	SRL3	212	Phosphoserine
+P25567	YCL037C	SRO9	55	Phosphoserine
+P25567	YCL037C	SRO9	148	Phosphoserine
+P25567	YCL037C	SRO9	422	Phosphoserine
+P25567	YCL037C	SRO9	156	Glycyl
+P25567	YCL037C	SRO9	301	Glycyl
+P25567	YCL037C	SRO9	342	Glycyl
+P25567	YCL037C	SRO9	352	Glycyl
+P42845	YNL309W	STB1	2	N-acetylserine
+P42845	YNL309W	STB1	7	Phosphoserine
+P42845	YNL309W	STB1	72	Phosphoserine
+P42845	YNL309W	STB1	99	Phosphothreonine
+P42845	YNL309W	STB1	102	Phosphoserine
+P42845	YNL309W	STB1	419	Phosphothreonine
+Q03497	YHL007C	STE20	2	N-acetylserine
+Q03497	YHL007C	STE20	87	Phosphoserine
+Q03497	YHL007C	STE20	165	Phosphoserine
+Q03497	YHL007C	STE20	167	Phosphothreonine
+Q03497	YHL007C	STE20	169	Phosphoserine
+Q03497	YHL007C	STE20	203	Phosphothreonine
+Q03497	YHL007C	STE20	418	Phosphoserine
+Q03497	YHL007C	STE20	502	Phosphoserine
+Q03497	YHL007C	STE20	547	Phosphoserine
+Q03497	YHL007C	STE20	562	Phosphoserine
+Q03497	YHL007C	STE20	573	Phosphothreonine
+Q03497	YHL007C	STE20	585	Phosphoserine
+Q03497	YHL007C	STE20	773	Phosphothreonine
+Q03497	YHL007C	STE20	924	Phosphoserine
+Q03497	YHL007C	STE20	927	Phosphothreonine
+P32917	YDR103W	STE5	329	Phosphoserine
+P12866	YKL209C	STE6	61	N-linked
+P12866	YKL209C	STE6	1022	Glycyl
+P06784	YDL159W	STE7	359	Phosphoserine
+P06784	YDL159W	STE7	363	Phosphothreonine
+P39932	YDR536W	STL1	197	N-linked
+P39932	YDR536W	STL1	319	N-linked
+P09959	YLR182W	SWI6	149	Phosphoserine
+P09959	YLR182W	SWI6	160	Phosphoserine%3B
+P09959	YLR182W	SWI6	176	Phosphoserine
+P09959	YLR182W	SWI6	179	Phosphothreonine
+P09959	YLR182W	SWI6	182	Phosphothreonine
+P09959	YLR182W	SWI6	547	Phosphoserine
+P46655	YGL245W	GUS1	300	Phosphothreonine
+P53277	YGR129W	SYF2	45	Phosphoserine
+P53277	YGR129W	SYF2	124	Phosphoserine
+P53277	YGR129W	SYF2	125	Phosphoserine
+P11972	YLR452C	SST2	252	Phosphoserine
+P11972	YLR452C	SST2	408	Phosphoserine
+P11972	YLR452C	SST2	539	Phosphoserine%3B
+P11972	YLR452C	SST2	587	Phosphoserine
+P41930	YPL092W	SSU1	444	Phosphoserine
+P41930	YPL092W	SSU1	448	Phosphoserine
+P41930	YPL092W	SSU1	450	Phosphoserine
+P08153	YDR146C	SWI5	225	Phosphoserine
+P08153	YDR146C	SWI5	278	Phosphoserine
+P08153	YDR146C	SWI5	300	Phosphoserine
+P08153	YDR146C	SWI5	339	Phosphothreonine
+P08153	YDR146C	SWI5	376	Phosphoserine
+P08153	YDR146C	SWI5	488	Phosphoserine
+P08153	YDR146C	SWI5	492	Phosphoserine
+P08153	YDR146C	SWI5	505	Phosphoserine
+P08153	YDR146C	SWI5	522	Phosphoserine%3B
+P08153	YDR146C	SWI5	646	Phosphoserine%3B
+P08153	YDR146C	SWI5	664	Phosphoserine%3B
+P23615	YGR116W	SPT6	94	Phosphoserine
+P23615	YGR116W	SPT6	134	Phosphoserine
+P23615	YGR116W	SPT6	136	Phosphoserine
+P23615	YGR116W	SPT6	148	Phosphoserine
+P23615	YGR116W	SPT6	155	Phosphoserine
+P23615	YGR116W	SPT6	206	Phosphoserine
+P23615	YGR116W	SPT6	295	Phosphoserine
+Q08673	YOR247W	SRL1	23	N-linked
+Q08673	YOR247W	SRL1	174	N-linked
+Q08673	YOR247W	SRL1	200	N-linked
+Q08673	YOR247W	SRL1	206	N-linked
+P10080	YHL034C	SBP1	2	N-acetylserine
+P10080	YHL034C	SBP1	91	Phosphothreonine
+P10080	YHL034C	SBP1	119	Phosphothreonine
+P10080	YHL034C	SBP1	242	Phosphothreonine
+P10080	YHL034C	SBP1	244	Phosphoserine
+P53599	YNR031C	SSK2	57	Phosphoserine
+P53599	YNR031C	SSK2	62	Phosphoserine
+P53599	YNR031C	SSK2	78	Phosphoserine
+P53599	YNR031C	SSK2	118	Phosphoserine
+P53599	YNR031C	SSK2	290	Phosphoserine
+P53599	YNR031C	SSK2	1424	Phosphoserine
+Q07084	YLR006C	SSK1	110	Phosphoserine
+Q07084	YLR006C	SSK1	195	Phosphoserine
+Q07084	YLR006C	SSK1	327	Phosphoserine
+Q07084	YLR006C	SSK1	351	Phosphoserine
+Q07084	YLR006C	SSK1	368	Phosphoserine
+Q07084	YLR006C	SSK1	380	Phosphoserine
+Q07084	YLR006C	SSK1	554	4-aspartylphosphate
+Q07084	YLR006C	SSK1	673	Phosphoserine
+Q07084	YLR006C	SSK1	693	Phosphothreonine
+Q07084	YLR006C	SSK1	703	Phosphoserine
+Q07084	YLR006C	SSK1	706	Phosphoserine
+Q12427	YDR169C	STB3	254	Phosphoserine
+P36085	YKL072W	STB6	514	Phosphoserine
+D6VTK4	YFL026W	STE2	310	Phosphoserine
+D6VTK4	YFL026W	STE2	315	Phosphoserine
+D6VTK4	YFL026W	STE2	329	Phosphothreonine
+D6VTK4	YFL026W	STE2	331	Phosphoserine
+D6VTK4	YFL026W	STE2	360	Phosphoserine
+D6VTK4	YFL026W	STE2	363	Phosphothreonine
+D6VTK4	YFL026W	STE2	366	Phosphoserine
+D6VTK4	YFL026W	STE2	382	Phosphothreonine
+D6VTK4	YFL026W	STE2	385	Phosphoserine
+D6VTK4	YFL026W	STE2	386	Phosphoserine
+D6VTK4	YFL026W	STE2	411	Phosphothreonine
+D6VTK4	YFL026W	STE2	414	Phosphothreonine
+D6VTK4	YFL026W	STE2	25	N-linked
+D6VTK4	YFL026W	STE2	32	N-linked
+D6VTK4	YFL026W	STE2	374	Glycyl
+D6VTK4	YFL026W	STE2	400	Glycyl
+D6VTK4	YFL026W	STE2	422	Glycyl
+P25344	YCL032W	STE50	202	Phosphoserine
+P25344	YCL032W	STE50	244	Phosphothreonine
+P25344	YCL032W	STE50	248	Phosphoserine
+P16965	YGR008C	STF2	28	Phosphoserine
+P16965	YGR008C	STF2	69	Phosphoserine
+P53312	YGR244C	LSC2	102	Phosphoserine
+P53312	YGR244C	LSC2	263	Phosphoserine
+P53312	YGR244C	LSC2	276	Phosphoserine
+P38359	YBR294W	SUL1	51	N-linked
+P38359	YBR294W	SUL1	93	N-linked
+P38359	YBR294W	SUL1	358	N-linked
+P38359	YBR294W	SUL1	391	N-linked
+P38359	YBR294W	SUL1	630	N-linked
+P38359	YBR294W	SUL1	653	N-linked
+P38359	YBR294W	SUL1	718	N-linked
+Q03088	YPL032C	SVL3	471	Phosphoserine
+Q03088	YPL032C	SVL3	496	Phosphothreonine
+Q03088	YPL032C	SVL3	551	Phosphoserine
+Q03088	YPL032C	SVL3	662	Phosphoserine
+Q03088	YPL032C	SVL3	739	Phosphothreonine
+Q03088	YPL032C	SVL3	756	Phosphothreonine
+Q03088	YPL032C	SVL3	757	Phosphoserine
+Q06677	YDR320C	SWA2	52	Phosphoserine
+Q06677	YDR320C	SWA2	64	Phosphoserine
+Q06677	YDR320C	SWA2	264	Phosphoserine
+Q06677	YDR320C	SWA2	308	Phosphoserine
+Q06677	YDR320C	SWA2	312	Phosphoserine
+P32828	YDL013W	SLX5	14	Phosphoserine
+P32828	YDL013W	SLX5	29	Phosphoserine
+Q08817	YOR353C	SOG2	214	Phosphothreonine
+P39543	YJL192C	SOP4	35	N-linked
+P39543	YJL192C	SOP4	53	N-linked
+P39543	YJL192C	SOP4	85	N-linked
+P39543	YJL192C	SOP4	115	N-linked
+P39543	YJL192C	SOP4	170	N-linked
+P53148	YGL093W	SPC105	77	Phosphoserine
+P53148	YGL093W	SPC105	356	Phosphothreonine
+P53148	YGL093W	SPC105	380	Phosphoserine
+P06844	YDR392W	SPT3	270	Phosphoserine
+P32916	YDR292C	SRP101	239	Phosphoserine
+P32916	YDR292C	SRP101	523	Phosphoserine
+P12954	YJL092W	SRS2	833	Phosphoserine
+P13130	YHR139C	SPS100	26	N-linked
+P13130	YHR139C	SPS100	50	N-linked
+P13130	YHR139C	SPS100	58	N-linked
+P13130	YHR139C	SPS100	64	N-linked
+P13130	YHR139C	SPS100	76	N-linked
+P13130	YHR139C	SPS100	108	N-linked
+P13130	YHR139C	SPS100	181	N-linked
+P13130	YHR139C	SPS100	190	N-linked
+P13130	YHR139C	SPS100	199	N-linked
+P13130	YHR139C	SPS100	205	N-linked
+P13130	YHR139C	SPS100	248	N-linked
+P13130	YHR139C	SPS100	281	N-linked
+Q07549	YDL123W	SNA4	134	Phosphoserine
+Q07549	YDL123W	SNA4	2	S-palmitoyl
+Q07549	YDL123W	SNA4	3	S-palmitoyl
+Q07549	YDL123W	SNA4	5	S-palmitoyl
+Q07549	YDL123W	SNA4	7	S-palmitoyl
+Q07549	YDL123W	SNA4	8	S-palmitoyl
+Q07549	YDL123W	SNA4	128	Glycyl
+Q04477	YMR117C	SPC24	2	N-acetylserine
+P40014	YER018C	SPC25	2	N-acetylalanine
+Q03012	YPL138C	SPP1	87	Phosphoserine
+P25380	YCL048W	SPS22	440	GPI-anchor
+P25380	YCL048W	SPS22	256	N-linked
+P25380	YCL048W	SPS22	314	N-linked
+P25380	YCL048W	SPS22	327	N-linked
+P27692	YML010W	SPT5	35	Phosphothreonine
+P27692	YML010W	SPT5	133	Phosphothreonine
+P27692	YML010W	SPT5	136	Phosphoserine
+P27692	YML010W	SPT5	188	Phosphoserine
+P27692	YML010W	SPT5	219	Phosphoserine
+P39015	YLR150W	STM1	2	N-acetylserine
+P39015	YLR150W	STM1	55	Phosphoserine
+P39015	YLR150W	STM1	118	Phosphoserine
+P39015	YLR150W	STM1	229	Phosphoserine
+P39015	YLR150W	STM1	46	Glycyl
+P39015	YLR150W	STM1	121	Glycyl
+P39015	YLR150W	STM1	171	Glycyl
+P39015	YLR150W	STM1	184	Glycyl
+Q05937	YLR375W	STP3	71	Phosphoserine
+Q05937	YLR375W	STP3	111	Phosphoserine
+Q07351	YDL048C	STP4	153	Phosphoserine
+Q07351	YDL048C	STP4	155	Phosphoserine
+Q12038	YPR032W	SRO7	591	Phosphoserine
+Q12038	YPR032W	SRO7	602	Phosphoserine
+P32583	YKR092C	SRP40	133	Phosphoserine
+P32583	YKR092C	SRP40	289	Phosphothreonine
+P32583	YKR092C	SRP40	293	Phosphoserine
+P32583	YKR092C	SRP40	394	Phosphoserine
+P38931	YDR443C	SSN2	370	Phosphoserine
+P38931	YDR443C	SSN2	375	Phosphoserine
+P38931	YDR443C	SSN2	425	Phosphoserine
+P38931	YDR443C	SSN2	601	Phosphothreonine
+P38931	YDR443C	SSN2	608	Phosphoserine%3B
+P38931	YDR443C	SSN2	636	Phosphoserine
+P38931	YDR443C	SSN2	748	Phosphoserine
+P37296	YMR054W	STV1	1	N-acetylmethionine
+P37296	YMR054W	STV1	223	Phosphoserine
+P37296	YMR054W	STV1	228	Phosphoserine
+P31377	YAL014C	SYN8	238	S-palmitoyl
+P36126	YKR031C	SPO14	2	N-acetylserine
+P36126	YKR031C	SPO14	8	Phosphoserine
+P36126	YKR031C	SPO14	30	Phosphoserine
+P36126	YKR031C	SPO14	145	Phosphoserine
+P36126	YKR031C	SPO14	1461	Phosphoserine
+P36126	YKR031C	SPO14	1462	Phosphothreonine
+Q07798	YLL005C	SPO75	2	N-linked
+Q07798	YLL005C	SPO75	184	N-linked
+Q07798	YLL005C	SPO75	503	N-linked
+P08459	YDR522C	SPS2	475	GPI-anchor
+P08459	YDR522C	SPS2	77	N-linked
+P08459	YDR522C	SPS2	135	N-linked
+P08459	YDR522C	SPS2	285	N-linked
+P08459	YDR522C	SPS2	303	N-linked
+P08459	YDR522C	SPS2	340	N-linked
+P08459	YDR522C	SPS2	343	N-linked
+P08459	YDR522C	SPS2	355	N-linked
+P38789	YHR066W	SSF1	301	Phosphothreonine
+P39926	YMR183C	SSO2	31	Phosphoserine
+P39926	YMR183C	SSO2	34	Phosphoserine
+P38788	YHR064C	SSZ1	477	Phosphoserine
+P38788	YHR064C	SSZ1	480	Phosphoserine
+P25379	YCL064C	CHA1	2	N-acetylserine
+P25379	YCL064C	CHA1	37	N6-(pyridoxal
+P33894	YOR219C	STE13	377	N-linked
+P33894	YOR219C	STE13	814	N-linked
+P53101	YGL184C	STR3	213	N6-(pyridoxal
+P46676	YDR310C	SUM1	2	N-acetylserine
+P46676	YDR310C	SUM1	378	Phosphoserine
+P46676	YDR310C	SUM1	379	Phosphoserine
+P46676	YDR310C	SUM1	628	Phosphoserine
+P46676	YDR310C	SUM1	681	Phosphoserine
+P46676	YDR310C	SUM1	697	Phosphothreonine
+P46676	YDR310C	SUM1	712	Phosphoserine%3B
+P46676	YDR310C	SUM1	738	Phosphoserine
+P46676	YDR310C	SUM1	817	Phosphothreonine
+P53616	YNL066W	SUN4	395	N-linked
+P33300	YPL057C	SUR1	349	Phosphoserine
+P54003	YML052W	SUR7	293	Phosphoserine
+P54003	YML052W	SUR7	301	Phosphoserine
+P54003	YML052W	SUR7	47	N-linked
+P04802	YLL018C	DPS1	2	N-acetylserine
+P04802	YLL018C	DPS1	14	Phosphoserine
+P04802	YLL018C	DPS1	301	Phosphoserine
+P04802	YLL018C	DPS1	502	Phosphoserine
+P04802	YLL018C	DPS1	546	Phosphoserine
+Q02875	YPL105C	SYH1	350	Phosphothreonine
+P54000	YMR039C	SUB1	119	Phosphoserine
+P54000	YMR039C	SUB1	268	Phosphoserine
+P54000	YMR039C	SUB1	269	Phosphoserine
+P54000	YMR039C	SUB1	289	Phosphoserine
+Q07478	YDL084W	SUB2	2	N-acetylserine
+Q07478	YDL084W	SUB2	13	Phosphoserine
+Q07478	YDL084W	SUB2	37	Phosphoserine
+Q07478	YDL084W	SUB2	169	Phosphothreonine
+P53201	YGR002C	SWC4	2	N-acetylserine
+P38326	YBR231C	SWC5	209	Phosphoserine
+P38088	YBR121C	GRS1	25	N-acetylserine
+P38088	YBR121C	GRS1	226	Phosphoserine
+P38088	YBR121C	GRS1	476	Phosphoserine
+P38088	YBR121C	GRS1	528	Phosphoserine
+P38088	YBR121C	GRS1	689	Phosphothreonine
+Q6WNK7	YBR111W-A	SUS1	68	Glycyl
+P38869	YHR181W	SVP26	115	N-linked
+P32591	YJL176C	SWI3	88	Phosphoserine
+P32591	YJL176C	SWI3	185	Phosphoserine
+P32591	YJL176C	SWI3	235	Phosphothreonine
+P32591	YJL176C	SWI3	657	Phosphoserine
+P40825	YOR335C	ALA1	504	Phosphoserine
+P40825	YOR335C	ALA1	975	Phosphoserine
+P40528	YIL047C	SYG1	172	Phosphoserine
+P40528	YIL047C	SYG1	179	Phosphoserine
+P40528	YIL047C	SYG1	859	Phosphoserine
+P40528	YIL047C	SYG1	860	Phosphoserine
+P46679	YMR053C	STB2	594	Phosphoserine
+P46679	YMR053C	STB2	625	Phosphoserine
+P23561	YLR362W	STE11	323	Phosphoserine
+P23561	YLR362W	STE11	465	Phosphoserine
+P01098	YDL130W-A	STF1	24	Phosphoserine
+P39007	YGL022W	STT3	60	N-linked
+P39007	YGL022W	STT3	535	N-linked
+P39007	YGL022W	STT3	539	N-linked
+P38198	YBL034C	STU1	997	Phosphoserine
+P38198	YBL034C	STU1	1018	Phosphoserine
+P38198	YBL034C	STU1	1047	Phosphothreonine
+P38198	YBL034C	STU1	1063	Phosphoserine
+P38198	YBL034C	STU1	1167	Phosphoserine
+P46675	YLR045C	STU2	2	Phosphoserine
+P46675	YLR045C	STU2	277	Phosphoserine
+P46675	YLR045C	STU2	813	Phosphoserine
+P32911	YNL244C	SUI1	2	N-acetylserine
+Q12254	YPL163C	SVS1	23	N-linked
+Q12254	YPL163C	SVS1	249	N-linked
+Q12254	YPL163C	SVS1	256	N-linked
+P15180	YDR037W	KRS1	2	N-acetylserine
+P15180	YDR037W	KRS1	30	Phosphoserine
+P15180	YDR037W	KRS1	62	Phosphothreonine
+P15180	YDR037W	KRS1	308	Glycyl
+P15180	YDR037W	KRS1	577	Glycyl
+P40150	YNL209W	SSB2	2	N-acetylalanine
+P40150	YNL209W	SSB2	47	Phosphothreonine
+P40150	YNL209W	SSB2	431	Phosphothreonine
+P13574	YHR084W	STE12	29	Phosphothreonine
+P13574	YHR084W	STE12	214	Phosphoserine
+P13574	YHR084W	STE12	226	Phosphoserine
+P13574	YHR084W	STE12	289	Phosphothreonine
+P13574	YHR084W	STE12	400	Phosphoserine
+P32597	YIL126W	STH1	38	Phosphoserine
+P37297	YLR305C	STT4	459	Phosphoserine
+P32944	YJL187C	SWE1	36	Phosphoserine%3B
+P32944	YJL187C	SWE1	45	Phosphothreonine%3B
+P32944	YJL187C	SWE1	56	Phosphoserine%3B
+P32944	YJL187C	SWE1	63	Phosphoserine%3B
+P32944	YJL187C	SWE1	70	Phosphoserine
+P32944	YJL187C	SWE1	74	Phosphothreonine%3B
+P32944	YJL187C	SWE1	102	Phosphoserine%3B
+P32944	YJL187C	SWE1	105	Phosphoserine%3B
+P32944	YJL187C	SWE1	111	Phosphoserine%3B
+P32944	YJL187C	SWE1	118	Phosphoserine%3B
+P32944	YJL187C	SWE1	121	Phosphothreonine%3B
+P32944	YJL187C	SWE1	124	Phosphothreonine%3B
+P32944	YJL187C	SWE1	127	Phosphoserine%3B
+P32944	YJL187C	SWE1	131	Phosphothreonine%3B
+P32944	YJL187C	SWE1	133	Phosphoserine%3B
+P32944	YJL187C	SWE1	136	Phosphoserine%3B
+P32944	YJL187C	SWE1	156	Phosphoserine%3B
+P32944	YJL187C	SWE1	169	Phosphoserine%3B
+P32944	YJL187C	SWE1	196	Phosphothreonine%3B
+P32944	YJL187C	SWE1	201	Phosphoserine%3B
+P32944	YJL187C	SWE1	225	Phosphoserine%3B
+P32944	YJL187C	SWE1	254	Phosphoserine%3B
+P32944	YJL187C	SWE1	262	Phosphoserine
+P32944	YJL187C	SWE1	263	Phosphoserine%3B
+P32944	YJL187C	SWE1	266	Phosphoserine%3B
+P32944	YJL187C	SWE1	280	Phosphothreonine%3B
+P32944	YJL187C	SWE1	284	Phosphoserine
+P32944	YJL187C	SWE1	294	Phosphoserine
+P32944	YJL187C	SWE1	312	Phosphoserine%3B
+P32944	YJL187C	SWE1	345	Phosphoserine
+P32944	YJL187C	SWE1	367	Phosphothreonine%3B
+P32944	YJL187C	SWE1	373	Phosphothreonine%3B
+P32944	YJL187C	SWE1	379	Phosphoserine%3B
+P32944	YJL187C	SWE1	384	Phosphothreonine%3B
+P32944	YJL187C	SWE1	395	Phosphoserine%3B
+P32944	YJL187C	SWE1	438	Phosphoserine%3B
+P32944	YJL187C	SWE1	610	Phosphoserine%3B
+P32944	YJL187C	SWE1	629	Phosphothreonine%3B
+P32944	YJL187C	SWE1	688	Phosphothreonine%3B
+P32944	YJL187C	SWE1	692	Phosphothreonine
+P32944	YJL187C	SWE1	741	Glycyl
+P25302	YER111C	SWI4	255	Phosphoserine
+P25302	YER111C	SWI4	806	Phosphoserine
+P15625	YFL022C	FRS2	2	N-acetylserine
+P07806	YGR094W	VAS1	73	Phosphoserine
+P07806	YGR094W	VAS1	294	Phosphoserine
+P07806	YGR094W	VAS1	332	Phosphoserine
+P07806	YGR094W	VAS1	707	Phosphoserine
+P07806	YGR094W	VAS1	1003	Phosphothreonine
+P41895	YGR186W	TFG1	198	Phosphoserine
+P41895	YGR186W	TFG1	200	Phosphothreonine
+P41895	YGR186W	TFG1	515	Phosphoserine
+P41895	YGR186W	TFG1	560	Phosphoserine
+P41895	YGR186W	TFG1	562	Phosphoserine
+P41895	YGR186W	TFG1	571	Phosphoserine
+P41895	YGR186W	TFG1	655	Phosphoserine
+Q12030	YDR167W	TAF10	58	Phosphoserine
+Q12030	YDR167W	TAF10	146	Phosphoserine
+P35189	YPL129W	TAF14	181	Glycyl
+P23255	YCR042C	TAF2	158	Phosphothreonine
+P23255	YCR042C	TAF2	161	Phosphothreonine
+P23255	YCR042C	TAF2	163	Phosphoserine
+P23255	YCR042C	TAF2	318	Phosphoserine
+Q12297	YPL011C	TAF3	237	Phosphothreonine
+Q12297	YPL011C	TAF3	310	Phosphoserine
+Q12297	YPL011C	TAF3	346	Phosphoserine
+P09436	YBL076C	ILS1	829	Phosphoserine
+P09436	YBL076C	ILS1	1059	Phosphoserine
+P09436	YBL076C	ILS1	486	Glycyl
+Q06836	YPR095C	SYT1	277	Phosphothreonine
+Q06836	YPR095C	SYT1	369	Phosphoserine
+P25638	YCR060W	TAH1	2	N-acetylserine
+P15019	YLR354C	TAL1	2	N-acetylserine
+P13188	YOR168W	GLN4	378	Phosphoserine
+P32774	YKL058W	TOA2	95	Phosphoserine
+P32774	YKL058W	TOA2	102	Phosphoserine
+P36421	YGR185C	TYS1	2	N-acetylserine
+P36421	YGR185C	TYS1	235	Phosphoserine
+P36421	YGR185C	TYS1	359	Phosphothreonine
+Q04226	YML015C	TAF11	236	Phosphoserine
+Q04226	YML015C	TAF11	238	Phosphoserine
+P38129	YBR198C	TAF5	299	Phosphoserine
+P38129	YBR198C	TAF5	411	Phosphoserine
+P38129	YBR198C	TAF5	415	Phosphoserine
+P38129	YBR198C	TAF5	787	Phosphoserine
+Q03750	YML114C	TAF8	269	Phosphoserine
+Q04545	YML081W	TDA9	527	Phosphoserine
+Q04545	YML081W	TDA9	603	Phosphoserine
+P34163	YKL140W	TGL1	462	Phosphoserine
+P34163	YKL140W	TGL1	466	Phosphoserine
+P34163	YKL140W	TGL1	521	Phosphoserine
+P34163	YKL140W	TGL1	538	Phosphoserine
+P34163	YKL140W	TGL1	539	Phosphothreonine
+P34163	YKL140W	TGL1	246	Glycyl
+Q12043	YOR081C	TGL5	645	Phosphoserine
+Q12043	YOR081C	TGL5	270	N-linked
+Q12043	YOR081C	TGL5	289	N-linked
+Q12043	YOR081C	TGL5	297	N-linked
+Q12043	YOR081C	TGL5	304	N-linked
+Q12043	YOR081C	TGL5	321	N-linked
+Q12043	YOR081C	TGL5	474	N-linked
+Q12043	YOR081C	TGL5	589	N-linked
+Q12043	YOR081C	TGL5	680	N-linked
+Q12043	YOR081C	TGL5	714	N-linked
+Q12043	YOR081C	TGL5	742	N-linked
+P04801	YIL078W	THS1	195	Phosphoserine
+P04801	YIL078W	THS1	289	Phosphoserine
+P04801	YIL078W	THS1	297	Phosphothreonine
+P04801	YIL078W	THS1	381	Phosphothreonine
+P04801	YIL078W	THS1	453	Phosphoserine
+P04801	YIL078W	THS1	457	Phosphoserine
+P04801	YIL078W	THS1	460	Phosphothreonine
+P04801	YIL078W	THS1	605	Phosphoserine
+P38854	YHR159W	TDA11	236	Phosphothreonine
+P38854	YHR159W	TDA11	244	Phosphoserine
+P38854	YHR159W	TDA11	286	Phosphoserine
+Q03533	YMR291W	TDA1	504	Phosphothreonine
+Q03533	YMR291W	TDA1	509	Phosphoserine
+Q03533	YMR291W	TDA1	518	Phosphoserine
+Q03533	YMR291W	TDA1	538	Phosphothreonine
+Q03533	YMR291W	TDA1	578	Phosphoserine
+P40045	YER071C	TDA2	2	N-acetylserine
+P02557	YFL037W	TUB2	278	Phosphoserine
+P02557	YFL037W	TUB2	280	Phosphoserine
+Q12466	YOR086C	TCB1	1000	Phosphoserine
+Q03640	YML072C	TCB3	67	Phosphoserine
+Q03640	YML072C	TCB3	112	Phosphoserine
+Q03640	YML072C	TCB3	1340	Phosphoserine
+Q03640	YML072C	TCB3	1342	Phosphoserine
+Q03640	YML072C	TCB3	1346	Phosphoserine
+Q03640	YML072C	TCB3	1350	Phosphothreonine
+Q03640	YML072C	TCB3	1354	Phosphoserine
+Q03640	YML072C	TCB3	1400	Phosphoserine
+P40533	YIL039W	TED1	38	N-linked
+P40533	YIL039W	TED1	147	N-linked
+P40533	YIL039W	TED1	229	N-linked
+P40533	YIL039W	TED1	266	N-linked
+P40533	YIL039W	TED1	307	N-linked
+Q03761	YDR145W	TAF12	2	N-acetylserine
+Q03761	YDR145W	TAF12	129	Phosphoserine
+Q03761	YDR145W	TAF12	286	Phosphoserine
+P50105	YMR005W	TAF4	36	Phosphoserine
+P50105	YMR005W	TAF4	49	Phosphoserine
+P50105	YMR005W	TAF4	80	Phosphoserine
+P53072	YGL232W	TAN1	72	Phosphoserine
+P39076	YIL142W	CCT2	2	N-acetylserine
+P39079	YDR188W	CCT6	2	N-acetylserine
+P39079	YDR188W	CCT6	249	Phosphoserine
+P38758	YHR009C	TDA3	189	Phosphoserine
+P38758	YHR009C	TDA3	204	Phosphoserine
+P38758	YHR009C	TDA3	306	Phosphoserine
+P53882	YNL176C	TDA7	628	Phosphoserine
+P53882	YNL176C	TDA7	4	N-linked
+P53882	YNL176C	TDA7	257	N-linked
+P53882	YNL176C	TDA7	492	N-linked
+P53882	YNL176C	TDA7	557	N-linked
+P53882	YNL176C	TDA7	562	N-linked
+P53882	YNL176C	TDA7	626	N-linked
+P53882	YNL176C	TDA7	512	Glycyl
+Q12004	YPR056W	TFB4	1	N-acetylmethionine
+P34111	YAL001C	TFC3	546	Phosphoserine
+P40085	YER140W	EMP65	22	Phosphoserine
+P40085	YER140W	EMP65	318	N-linked
+P38756	YHR003C	TCD1	259	Phosphoserine
+Q06466	YPR157W	TDA6	61	N-linked
+Q06466	YPR157W	TDA6	124	N-linked
+Q06466	YPR157W	TDA6	141	N-linked
+P47988	YOR337W	TEA1	22	Phosphothreonine
+P47988	YOR337W	TEA1	755	Phosphothreonine
+P18412	YBR083W	TEC1	2	N-acetylserine
+P18412	YBR083W	TEC1	325	Phosphoserine
+P53038	YGR099W	TEL2	417	Phosphoserine
+P53038	YGR099W	TEL2	419	Phosphoserine
+P32367	YBR123C	TFC1	617	Phosphoserine
+P53215	YGR024C	THG1	2	N-acetylalanine
+Q07748	YDL244W	THI13	62	N6-(pyridoxal
+Q08579	YOR192C	THI72	560	Phosphoserine
+Q08579	YOR192C	THI72	572	Phosphoserine
+P41544	YJL004C	SYS1	192	Phosphoserine
+P41544	YJL004C	SYS1	15	Glycyl
+P41896	YGR005C	TFG2	28	Phosphoserine
+P41896	YGR005C	TFG2	34	Phosphoserine
+P41896	YGR005C	TFG2	56	Phosphoserine
+Q05021	YMR227C	TAF7	99	Phosphotyrosine
+Q05021	YMR227C	TAF7	101	Phosphoserine
+Q05021	YMR227C	TAF7	104	Phosphoserine
+P40468	YIL129C	TAO3	141	Phosphoserine
+P40468	YIL129C	TAO3	1144	Phosphoserine
+P40468	YIL129C	TAO3	2264	Phosphothreonine
+P40468	YIL129C	TAO3	2267	Phosphoserine
+P40468	YIL129C	TAO3	2355	Phosphoserine
+P26637	YPL160W	CDC60	2	N-acetylserine
+P26637	YPL160W	CDC60	142	Phosphothreonine
+P00958	YGR264C	MES1	2	N-acetylserine
+P36145	YKR062W	TFA2	52	Phosphoserine
+P36145	YKR062W	TFA2	97	Phosphoserine
+P36145	YKR062W	TFA2	106	Phosphoserine
+P11747	YML098W	TAF13	131	Phosphothreonine
+P38085	YBR069C	TAT1	13	Phosphoserine
+P38085	YBR069C	TAT1	80	Phosphoserine
+P38085	YBR069C	TAT1	84	Phosphoserine
+P38085	YBR069C	TAT1	39	Glycyl
+P48606	YOR265W	RBL2	94	Phosphoserine
+P48231	YNL087W	TCB2	991	Phosphoserine
+P12612	YDR212W	TCP1	2	N-acetylserine
+P47079	YJL008C	CCT8	505	Phosphoserine
+P47079	YJL008C	CCT8	15	Glycyl
+Q07793	YDR261C-D	TY1B-DR4	416	Phosphoserine
+Q03856	YDR098C-A	TY1A-DR1	416	Phosphoserine
+O74302	YDR261C-C	TY1A-DR4	416	Phosphoserine
+P0CX70	YDR365W-A	TY1A-DR6	416	Phosphoserine
+P14680	YJL141C	YAK1	38	Phosphoserine
+P14680	YJL141C	YAK1	115	Phosphoserine
+P14680	YJL141C	YAK1	118	Phosphoserine
+P14680	YJL141C	YAK1	127	Phosphoserine
+P14680	YJL141C	YAK1	206	Phosphoserine
+P14680	YJL141C	YAK1	240	Phosphoserine
+P14680	YJL141C	YAK1	245	Phosphoserine
+P14680	YJL141C	YAK1	247	Phosphoserine
+P14680	YJL141C	YAK1	288	Phosphothreonine
+P14680	YJL141C	YAK1	295	Phosphoserine
+P14680	YJL141C	YAK1	530	Phosphotyrosine
+P46683	YPL239W	YAR1	78	Phosphoserine
+P40917	YOR028C	CIN5	85	Phosphoserine
+P40917	YOR028C	CIN5	89	Phosphoserine
+P40917	YOR028C	CIN5	196	Phosphoserine
+Q03612	YER138C	TY1B-ER1	416	Phosphoserine
diff --git a/test_files/PTMs.txt b/test_files/PTMs.txt
new file mode 100644
index 0000000..51e681e
--- /dev/null
+++ b/test_files/PTMs.txt
@@ -0,0 +1,9881 @@
+P12688	57	Phosphothreonine
+P12688	61	Phosphoserine
+P12688	64	Phosphoserine
+P12688	71	Phosphoserine
+P12688	170	Phosphoserine
+P12688	502	Phosphothreonine
+P12688	504	Phosphothreonine%3B
+P12688	644	Phosphoserine
+P12688	653	Phosphoserine
+P12688	662	Phosphothreonine%3B
+P12688	671	Phosphoserine
+P25491	406	Cysteine
+P25491	406	S-farnesyl
+P25491	198	Glycyl
+P16521	2	N-acetylserine
+P16521	187	N6%2CN6%2CN6-trimethyllysine
+P16521	196	N6%2CN6%2CN6-trimethyllysine
+P16521	642	Phosphoserine
+P16521	789	N6%2CN6%2CN6-trimethyllysine
+P16521	972	Phosphothreonine
+P16521	974	Phosphoserine
+P16521	1039	Phosphoserine
+P16521	1040	Phosphoserine
+P16521	350	Glycyl
+P16521	636	Glycyl
+P11484	2	N-acetylalanine
+P11484	47	Phosphothreonine
+P11484	431	Phosphothreonine
+P39940	258	Glycyl
+Q06224	517	Phosphoserine%3B
+P02829	657	Phosphoserine
+P10591	2	N-acetylserine
+P10591	62	Phosphoserine
+P10591	551	Phosphoserine
+P10591	603	Phosphoserine
+P10591	556	Glycyl
+P41800	6	N-linked
+P41800	50	N-linked
+P41800	55	N-linked
+P41800	59	N-linked
+P00546	2	N-acetylserine
+P00546	19	Phosphotyrosine
+P00546	169	Phosphothreonine
+P15108	653	Phosphoserine
+P31539	1	N-acetylmethionine
+P31539	206	Phosphoserine
+P31539	306	Phosphoserine
+P31539	499	Phosphothreonine
+P31539	535	Phosphoserine
+P31539	442	Glycyl
+P31539	620	Glycyl
+P25623	264	Phosphoserine
+P25623	331	Phosphoserine
+P25623	416	Phosphothreonine
+P25623	496	Phosphoserine
+P25623	500	Phosphoserine
+P25623	577	Phosphothreonine
+P25623	256	Glycyl
+P08539	2	N-myristoyl
+P08539	3	S-palmitoyl
+P08539	165	Glycyl
+P15442	761	Phosphoserine
+P15442	882	Phosphothreonine%3B
+P15442	887	Phosphothreonine%3B
+P10592	2	N-acetylserine
+P10592	20	Phosphoserine
+P10592	551	Phosphoserine
+P10592	603	Phosphoserine
+P10592	556	Glycyl
+P06782	210	Phosphothreonine%3B
+P06782	413	Phosphoserine
+P06782	487	Phosphoserine
+P06782	632	Phosphoserine
+P06782	461	Glycyl
+P06782	549	Glycyl
+P22147	1506	Phosphothreonine
+P22147	1510	Phosphoserine
+P32598	1	N-acetylmethionine
+P32598	22	Glycyl
+P32598	47	Glycyl
+P35202	2	N-acetylserine
+P16120	124	N6-(pyridoxal
+P16120	467	Phosphoserine
+P40328	255	Phosphoserine
+P39077	1	N-acetylmethionine
+P39077	257	Phosphoserine
+P35691	9	Phosphoserine
+P35691	15	Phosphoserine
+P29056	381	Phosphoserine
+P29056	384	Phosphoserine
+P32318	205	2%2C3-didehydroalanine
+Q08144	109	Phosphoserine
+P07273	116	Phosphoserine
+P00927	109	N6-(pyridoxal
+P41338	2	N-acetylserine
+O74700	1	N-acetylmethionine
+Q12218	465	GPI-anchor
+Q12218	327	N-linked
+Q12218	348	N-linked
+Q12218	368	N-linked
+Q12218	403	N-linked
+Q12218	404	N-linked
+Q05998	560	Phosphoserine
+P40040	22	Phosphoserine
+P40040	58	Phosphoserine
+P40040	68	Phosphoserine
+P27654	186	GPI-anchor
+P10863	233	GPI-anchor
+P32802	61	N-linked
+P32802	282	N-linked
+Q03290	157	Phosphoserine
+Q03290	258	Phosphothreonine
+P46678	49	Phosphoserine
+P46678	178	Phosphoserine
+Q12415	365	Phosphoserine
+P42883	62	N6-(pyridoxal
+P40340	2	N-acetylalanine
+P40340	11	Phosphoserine
+P40340	17	Phosphoserine
+P40340	94	Phosphoserine
+P40340	212	Phosphothreonine
+P40340	229	Phosphothreonine
+P40340	241	Phosphoserine
+P40340	259	Phosphoserine
+P40340	285	Phosphoserine
+P40340	367	Phosphoserine
+P40340	369	Phosphoserine
+P40340	370	Phosphoserine
+P40340	735	Phosphoserine
+P40340	1142	Phosphoserine
+P40340	1256	Phosphoserine
+Q08921	52	Phosphothreonine
+Q08921	82	Phosphothreonine
+Q08921	84	Phosphoserine
+Q08921	104	Phosphoserine
+Q08921	107	Phosphoserine
+Q08921	115	Phosphoserine
+Q08921	144	Phosphoserine
+Q08921	203	Phosphoserine
+Q08921	215	Phosphoserine
+Q08921	290	Phosphoserine
+Q08921	397	Phosphoserine
+Q08921	575	Phosphoserine
+Q08921	707	Phosphoserine
+P32776	150	Phosphothreonine
+P33339	311	Phosphoserine
+Q08686	201	Phosphoserine
+Q08686	264	Phosphoserine
+P33315	286	Phosphoserine
+P33315	648	Glycyl
+Q12239	114	N-linked
+P36165	55	Phosphoserine
+P36165	737	Phosphoserine
+P36165	749	Phosphoserine
+P36165	751	Phosphoserine
+P36165	836	Phosphoserine
+P47183	62	N6-(pyridoxal
+P43534	62	N6-(pyridoxal
+P89886	1	N-acetylmethionine
+Q12049	1	N-acetylmethionine
+P40462	2	N-acetylserine
+Q12513	24	Phosphoserine
+Q12513	68	Phosphoserine
+P53840	626	Phosphoserine
+P53840	654	Phosphoserine
+P53840	1056	Phosphoserine
+P53840	1058	Phosphoserine
+P53840	1213	Phosphoserine
+P40310	119	Phosphoserine
+Q03280	1890	Phosphoserine
+Q03280	2096	Phosphothreonine
+Q03280	2119	Phosphoserine
+Q03280	2376	Phosphoserine
+Q03280	2406	Phosphoserine
+Q03280	2418	Phosphoserine
+P35180	172	Phosphoserine
+P38825	55	Phosphoserine
+P32830	2	N-acetylserine
+P33890	231	GPI-anchor
+Q08422	2	N-acetylserine
+Q08422	43	Phosphoserine
+Q08422	54	Phosphoserine
+P04786	14	Phosphoserine
+P04786	15	Phosphoserine
+P04786	24	Phosphoserine
+P04786	49	Phosphoserine
+P04786	76	Phosphoserine
+P06786	1086	Phosphothreonine%3B
+P06786	1087	Phosphoserine%3B
+P06786	1252	Phosphoserine
+P06786	1258	Phosphothreonine%3B
+P06786	1266	Phosphoserine%3B
+P06786	1269	Phosphoserine%3B
+P06786	1272	Phosphoserine%3B
+P06786	1353	Phosphoserine%3B
+P06786	1356	Phosphoserine%3B
+P06786	1408	Phosphoserine%3B
+P06786	1423	Phosphoserine%3B
+Q06177	28	Phosphoserine
+Q06177	79	Phosphoserine
+P49334	44	Phosphoserine
+P49334	46	Phosphoserine
+P38288	236	N-linked
+P38288	417	N-linked
+P12685	15	Phosphoserine
+P12685	414	Phosphoserine
+P12685	534	Phosphoserine
+P12685	100	N-linked
+P12685	169	N-linked
+P12685	222	N-linked
+P12685	227	N-linked
+P12685	251	N-linked
+P12685	369	N-linked
+P12685	383	N-linked
+P12685	497	N-linked
+P12685	501	N-linked
+P12685	532	N-linked
+P12685	580	N-linked
+P12685	677	N-linked
+P12685	919	N-linked
+P12685	1030	N-linked
+P12685	1135	N-linked
+Q12400	16	Phosphothreonine
+Q12400	283	Phosphoserine
+Q02648	107	Phosphoserine
+P32643	2	N-acetylserine
+P32600	10	Phosphothreonine
+P17536	195	Phosphoserine
+P17536	39	Glycyl
+P17536	59	Glycyl
+P17536	187	Glycyl
+P53283	50	Phosphoserine
+Q12256	589	Phosphothreonine
+Q12256	606	Phosphothreonine
+Q12256	608	Phosphothreonine
+Q12256	633	Phosphoserine
+Q12256	646	Phosphoserine
+Q05024	113	Phosphoserine
+Q05024	225	Phosphoserine
+Q05024	201	Glycyl
+Q05024	215	Glycyl
+P33753	92	Phosphoserine
+P33753	93	Phosphoserine
+P22217	54	Glycyl
+P22217	66	Glycyl
+P22217	96	Glycyl
+P34760	174	Phosphothreonine
+P34760	14	Glycyl
+P34760	89	Glycyl
+P34760	132	Glycyl
+P40061	19	Phosphoserine
+P40061	81	Phosphoserine
+P40061	84	Phosphoserine
+P40061	87	Phosphoserine
+P40061	141	Phosphoserine
+P40552	245	GPI-anchor
+P40552	234	N-linked
+Q12000	301	Phosphoserine
+Q06266	40	Phosphoserine
+Q06266	100	Phosphoserine
+Q07824	19	Phosphoserine%3B
+Q07824	52	Phosphothreonine%3B
+Q07824	72	Phosphoserine
+Q07824	76	Phosphoserine
+Q07824	89	Phosphothreonine
+Q07824	91	Phosphoserine
+Q07824	342	Phosphoserine%3B
+Q12199	55	Phosphothreonine
+P23254	286	Phosphoserine
+P23254	335	Phosphoserine
+P23254	402	Phosphoserine
+P23254	492	Phosphoserine
+P23254	647	Glycyl
+Q03322	31	Phosphothreonine%3B
+Q03322	205	S-palmitoyl
+Q03322	206	S-palmitoyl
+Q03322	183	Glycyl
+P53322	27	Phosphoserine
+P53322	283	Glycyl
+Q08919	139	N-linked
+Q08919	213	N-linked
+Q08919	529	N-linked
+Q03774	93	Phosphoserine
+P32893	393	Phosphoserine
+P32893	398	Phosphoserine
+Q02208	397	Phosphoserine
+Q02208	405	Phosphothreonine
+P07213	174	Phosphoserine
+P48560	80	GPI-anchor
+P48560	69	N-linked
+P00942	4	Phosphothreonine
+P00942	71	Phosphoserine
+P00942	215	Phosphoserine
+P00942	223	Glycyl
+P40414	55	Phosphoserine
+P40414	116	Phosphoserine
+P40414	157	Phosphoserine
+Q06451	55	Phosphoserine
+Q06451	98	Phosphothreonine
+Q06451	101	Phosphoserine
+Q06451	132	Phosphoserine
+P36029	569	Phosphoserine
+Q04183	379	Phosphoserine
+Q04183	387	Phosphoserine
+P38427	49	Phosphoserine
+P38427	53	Phosphoserine
+P38427	56	Phosphoserine
+P38427	71	Phosphoserine
+P38427	77	Phosphoserine
+P38427	135	Phosphoserine
+P38427	147	Phosphoserine
+P38427	161	Phosphoserine
+P38427	229	Phosphoserine
+P38427	251	Phosphothreonine
+P38427	303	Phosphoserine
+P38427	815	Phosphothreonine
+P35172	52	Phosphoserine
+P35172	53	Phosphoserine
+P35172	88	Phosphothreonine
+P35172	112	Phosphoserine
+P34219	280	Phosphoserine
+P34219	333	Phosphoserine
+P34219	341	Phosphoserine
+P34219	366	Phosphoserine
+P33448	1	N-acetylmethionine
+P38811	2	N-acetylserine
+P38811	172	Phosphoserine
+P38811	542	Phosphoserine
+Q08693	228	N-linked
+Q08693	669	N-linked
+Q08693	736	N-linked
+P48561	596	Phosphoserine
+P48561	602	Phosphoserine
+P28584	216	N-linked
+P28584	233	N-linked
+P28584	265	N-linked
+P33122	104	Phosphoserine
+P33122	237	Phosphothreonine
+P21734	93	Glycyl
+P33296	139	Phosphoserine
+P33296	178	Phosphothreonine
+P32571	443	Phosphoserine
+P19812	296	Phosphoserine
+P19812	300	Phosphoserine
+P19812	1938	Phosphoserine
+Q07963	1218	Phosphoserine
+Q07963	1222	Phosphoserine
+Q07963	709	Glycyl
+Q06682	139	Phosphoserine
+P29509	303	Phosphoserine
+P38962	63	N-linked
+P38962	86	N-linked
+P38962	185	N-linked
+P22803	62	Phosphoserine
+P22803	67	Glycyl
+P22803	97	Glycyl
+Q12094	286	Phosphoserine
+Q12094	289	Phosphoserine
+Q08747	218	Phosphoserine
+Q08747	220	Phosphoserine
+Q08747	223	Phosphoserine
+P14682	186	Phosphoserine
+P14682	282	Phosphoserine
+P14682	292	Phosphoserine
+P40032	607	Phosphoserine
+P38426	148	Phosphoserine
+P38426	150	Phosphoserine
+P38426	181	Phosphoserine
+P38426	265	Phosphothreonine
+P38426	267	Phosphoserine
+P38426	273	Phosphoserine
+P38426	960	Phosphoserine
+P46959	302	Phosphoserine
+Q12009	7	Phosphoserine%3B
+Q12009	59	Phosphoserine
+P53250	167	Phosphoserine
+P53250	172	Phosphoserine
+P00899	81	Phosphoserine
+P00899	223	Phosphothreonine
+P00937	2	Phosphoserine
+P00931	384	N6-(pyridoxal
+P00931	540	Phosphoserine
+P00931	683	Phosphoserine
+Q04767	146	Phosphothreonine
+Q04767	153	Phosphothreonine
+Q04767	22	N-linked
+Q99394	2	N-acetylserine
+Q04120	174	Phosphothreonine
+Q04120	14	Glycyl
+Q04120	89	Glycyl
+Q04120	132	Glycyl
+P36097	817	Phosphoserine
+P16649	439	Phosphoserine
+P32356	2	N-acetylserine
+P32356	20	Phosphoserine
+P32356	21	Phosphoserine
+P32356	23	Phosphoserine
+P32356	58	Phosphothreonine
+P32356	60	Phosphoserine
+P32356	66	Phosphoserine
+P32356	83	Phosphoserine
+P53044	354	Phosphoserine
+P33202	87	Phosphothreonine
+P33202	349	Glycyl
+Q02724	2	N-acetylserine
+Q02724	21	Phosphoserine
+Q02724	25	Phosphoserine
+Q02724	179	Phosphothreonine
+Q02724	264	Phosphoserine
+P28274	422	Glycyl
+P40362	182	Phosphoserine
+P40362	184	Phosphoserine
+P40498	53	Phosphoserine
+P40498	63	Phosphoserine
+P40498	196	Phosphoserine
+P16140	4	Phosphoserine
+P16140	137	Phosphoserine
+P16140	503	Phosphoserine
+P16140	504	Phosphoserine
+P16140	511	Phosphoserine%3B
+P16140	515	Phosphoserine
+P16140	14	Glycyl
+P16140	508	Glycyl
+P38358	420	N-linked
+Q04602	62	Phosphoserine
+Q04602	99	Phosphoserine
+Q04602	106	Phosphoserine
+Q04602	160	Phosphoserine
+Q04602	192	Phosphoserine
+Q04602	480	N-linked
+Q04602	553	N-linked
+P39538	84	Phosphoserine
+P39538	1160	Phosphoserine
+P47049	369	Phosphoserine
+P40554	99	1-thioglycine
+P40554	99	Glycyl
+Q04500	34	Phosphoserine
+Q04500	35	Phosphoserine
+Q04500	151	Phosphoserine
+Q04500	423	Phosphoserine
+Q04500	424	Phosphoserine
+Q04500	488	Phosphoserine
+Q04500	500	Phosphoserine
+Q04500	562	Phosphoserine
+Q04500	668	Phosphoserine
+Q04500	738	Phosphoserine
+Q12339	182	Phosphoserine
+P43123	218	Phosphoserine
+P43123	461	Phosphoserine
+P52490	92	Glycyl
+Q02159	89	Glycyl
+Q08562	121	Phosphoserine
+P25386	1770	Phosphoserine
+P42945	2	N-acetylserine
+Q06078	2	N-acetylserine
+Q06078	772	Phosphoserine
+P53254	10	Phosphoserine
+P53254	58	Phosphoserine
+P53254	60	Phosphothreonine
+P53254	64	Phosphoserine
+P53276	95	Phosphothreonine
+P53276	148	Phosphoserine
+P53276	150	Phosphoserine
+P21373	499	Phosphoserine
+P21373	503	Phosphoserine
+Q01476	907	Phosphoserine
+P43593	389	Phosphothreonine
+P43593	470	Phosphoserine
+P38882	547	Phosphoserine
+P38882	564	Phosphoserine
+P25591	2	N-acetylalanine
+P25591	119	Phosphoserine
+P25591	149	Phosphothreonine
+P25591	178	Phosphoserine
+P25591	248	Phosphothreonine
+P25591	269	Phosphoserine
+P17255	2	N-acetylalanine
+P17255	131	Phosphothreonine
+P17255	858	Phosphoserine
+P17255	928	Phosphoserine
+P06104	120	Phosphoserine%3B
+P38349	388	Phosphoserine
+P38349	19	Glycyl
+P53177	26	Phosphoserine
+P53177	238	Phosphoserine
+P22515	2	N-acetylserine
+P22515	265	Phosphoserine
+P22515	914	Phosphoserine
+P22515	595	Glycyl
+P22515	608	Glycyl
+P52491	1	N-acetylmethionine
+P15732	12	Phosphoserine
+P15732	91	Glycyl
+P38187	198	Phosphoserine
+P25037	530	Phosphoserine
+P25037	531	Phosphoserine
+P25037	555	Phosphoserine
+P25037	618	Phosphoserine
+P25037	638	Phosphoserine
+P25037	652	Phosphothreonine
+P25037	653	Phosphoserine
+P25037	654	Phosphoserine
+P25037	670	Phosphoserine
+P25037	755	Phosphoserine
+P32861	2	N-acetylserine
+P32861	17	Phosphoserine
+P32861	19	Phosphothreonine
+P32861	21	Phosphoserine
+P32861	79	Phosphoserine
+P32861	369	Omega-N-methylarginine
+Q08960	496	Glycyl
+P38820	1	N-acetylmethionine
+P38820	326	Phosphoserine
+P15731	12	Phosphoserine
+P15731	91	Glycyl
+P34223	128	Phosphoserine
+P34223	210	Phosphoserine
+P34223	224	Phosphoserine
+P34223	315	Phosphoserine
+P34223	321	Phosphoserine
+P34223	322	Phosphoserine
+P34223	331	Phosphothreonine
+P34223	241	Glycyl
+Q04511	511	Phosphoserine
+Q04511	514	Phosphothreonine
+P40537	788	Phosphoserine
+P40537	903	Phosphoserine
+P40537	983	Phosphoserine
+P40537	984	Phosphoserine
+Q12151	122	Phosphothreonine
+Q12151	519	Phosphoserine
+P50623	2	N-acetylserine
+P0CG63	76	Glycyl
+Q03327	1	N-acetylmethionine
+P39547	11	Glycyl
+P39547	218	Glycyl
+P18562	82	Phosphoserine
+P27515	17	Phosphoserine
+P27515	276	Phosphoserine
+P32366	1	N-acetylmethionine
+Q06708	767	Phosphoserine
+Q06708	805	Phosphoserine
+Q06708	867	Phosphoserine
+Q99385	1	N-acetylmethionine
+Q99385	13	Phosphoserine
+P53058	26	N-linked
+P53058	48	N-linked
+P53058	91	N-linked
+P53058	139	N-linked
+P53058	152	N-linked
+Q08926	140	Phosphoserine
+Q08926	185	Phosphoserine
+Q08926	205	Phosphoserine
+P39001	114	Phosphoserine
+P39001	141	Phosphoserine
+P39001	150	Phosphoserine
+P39001	228	Phosphoserine
+P39001	316	Phosphoserine
+P39001	318	Phosphoserine
+P39001	645	Phosphoserine
+P23202	2	N-acetylmethionine
+Q03714	374	Phosphoserine
+Q03714	376	Phosphoserine
+Q03714	379	Phosphoserine
+P36172	70	N-linked
+P36172	423	N-linked
+P04840	109	Phosphoserine
+P04840	117	Phosphothreonine
+P40157	170	Phosphoserine
+P40157	195	Phosphoserine
+P40157	196	Phosphoserine
+P40157	222	Phosphoserine
+P40157	486	Phosphothreonine
+Q06685	31	Phosphoserine
+Q06685	54	Phosphoserine
+Q06685	77	Phosphoserine
+Q06685	895	Phosphoserine
+Q06685	1107	Phosphoserine
+P39968	11	Phosphoserine
+P39968	16	Phosphoserine
+P39968	2	N-myristoyl
+P39968	4	S-palmitoyl
+P39968	5	S-palmitoyl
+P39968	7	S-palmitoyl
+P39968	77	Glycyl
+P39968	515	Glycyl
+Q05934	21	N-linked
+Q05934	242	N-linked
+Q05934	291	N-linked
+Q05934	540	N-linked
+Q05934	645	N-linked
+Q05934	649	N-linked
+Q05934	652	N-linked
+Q05934	662	N-linked
+Q05934	669	N-linked
+Q05934	673	N-linked
+Q05934	688	N-linked
+Q05934	722	N-linked
+P23642	25	Phosphoserine
+P23642	215	N-linked
+P23642	251	N-linked
+P48836	2	N-acetylserine
+P32319	96	N-linked
+P32319	170	N-linked
+P32319	447	N-linked
+P32319	793	N-linked
+P32319	1010	N-linked
+P32319	1303	N-linked
+P32913	544	Phosphoserine
+Q04272	2	N-myristoyl
+P39702	1	N-acetylmethionine
+P38329	34	Phosphoserine
+P38329	654	Phosphoserine
+P38329	915	Phosphoserine
+P38329	918	Phosphoserine
+P40522	409	Phosphoserine
+Q08438	90	Phosphothreonine
+P53285	74	N-linked
+P53285	145	N-linked
+Q06525	150	Phosphoserine
+Q12132	162	Phosphoserine
+Q12132	163	Phosphoserine
+P53950	164	Phosphoserine
+P53950	1020	N-linked
+P53950	1099	N-linked
+P47161	55	N-linked
+P47161	237	N-linked
+P47161	568	N-linked
+P47161	599	N-linked
+P47161	670	N-linked
+P37370	519	Phosphoserine
+P37370	762	Phosphoserine
+P37370	109	N-linked
+P37370	212	N-linked
+P37370	337	N-linked
+P37370	383	N-linked
+P37370	784	N-linked
+P37370	796	N-linked
+Q03631	128	Phosphothreonine
+P31412	2	N-acetylalanine
+P22203	2	N-acetylserine
+Q04301	123	N-linked
+Q04301	324	N-linked
+Q04301	504	N-linked
+P25594	195	N-linked
+P53262	69	N-linked
+P53262	104	N-linked
+P53262	172	N-linked
+P32563	2	N-acetylalanine
+P38959	26	Phosphoserine
+P38959	53	Phosphoserine
+Q12071	69	Phosphoserine
+Q12071	72	Phosphoserine
+Q12071	74	Phosphothreonine
+P47111	137	Phosphoserine
+Q12016	1	N-acetylmethionine
+Q12016	8	Phosphoserine
+Q12016	52	N-linked
+Q06385	14	Phosphoserine
+Q06385	19	Phosphoserine
+Q07655	22	Phosphoserine
+Q07655	206	Phosphoserine
+Q07655	258	Phosphoserine
+Q07655	283	Phosphoserine
+P42839	26	Phosphothreonine
+P42839	32	Phosphoserine
+P42839	33	Phosphothreonine
+P42839	110	Phosphoserine
+P42839	118	Phosphothreonine
+P42839	121	Phosphoserine
+P42839	361	N-linked
+P39904	602	Phosphoserine
+P54787	375	Phosphoserine
+Q06263	183	Phosphoserine
+Q06263	195	Phosphothreonine
+Q06263	233	Phosphoserine
+P47165	79	Phosphoserine
+P53076	2	N-acetylserine
+P53076	147	Phosphoserine
+P53076	246	Phosphoserine
+P53076	248	Phosphoserine
+P53076	277	Phosphoserine
+P22219	2	N-myristoyl
+P21576	579	Phosphoserine
+P21576	599	Phosphoserine
+Q04338	2	N-acetylserine
+Q04338	110	Phosphoserine
+Q04338	149	Phosphoserine
+P40438	479	N-linked
+P40438	769	N-linked
+P40438	986	N-linked
+P40890	479	N-linked
+P40890	769	N-linked
+P40890	986	N-linked
+P34761	231	Phosphoserine
+P40463	53	Phosphoserine
+P40463	61	Phosphoserine
+P40463	102	Phosphoserine
+P40463	172	Phosphoserine
+P40463	299	Phosphoserine
+P40463	301	Phosphoserine
+P40463	303	Phosphoserine
+P40463	325	Phosphoserine
+Q07878	1364	Phosphoserine
+Q07878	1382	Phosphoserine
+Q07878	1715	Phosphoserine
+Q07878	1729	Phosphoserine
+Q07878	1731	Phosphoserine
+Q03390	12	Phosphoserine
+P53853	3	Phosphoserine
+Q12215	84	N-linked
+Q12215	367	N-linked
+Q12215	370	N-linked
+P38739	340	N-linked
+P38739	386	N-linked
+P38739	389	N-linked
+P38739	398	N-linked
+P38739	479	N-linked
+P38739	553	N-linked
+P38739	583	N-linked
+P43582	75	Phosphoserine
+P43582	78	Phosphothreonine
+P43582	50	Glycyl
+P43582	60	Glycyl
+P53241	32	Phosphoserine
+P53241	33	Phosphoserine
+P53241	43	Phosphoserine
+P40547	226	Phosphoserine
+P38735	11	N-linked
+P38735	370	N-linked
+P20795	626	Phosphoserine
+P34110	846	Phosphoserine
+P34110	848	Phosphoserine
+P34110	868	Phosphoserine
+Q02725	43	Phosphoserine
+Q02725	45	Phosphoserine
+Q02725	50	Phosphoserine
+Q02725	183	Phosphothreonine
+Q02725	195	Phosphoserine
+Q02725	198	Phosphoserine
+Q02725	270	Phosphoserine
+Q02725	274	Phosphoserine
+Q02725	589	Phosphoserine
+Q02725	592	Phosphoserine
+Q02725	621	Phosphoserine
+Q02725	622	Phosphoserine
+P47075	75	Glycyl
+Q12416	47	Phosphothreonine
+Q12416	57	Phosphothreonine
+Q12416	59	Phosphoserine
+Q12416	62	Phosphoserine
+Q12416	88	Phosphoserine
+Q12416	113	Phosphoserine
+Q12416	115	Phosphoserine
+Q12416	154	Phosphoserine
+Q12416	156	Phosphoserine
+Q12416	161	Phosphoserine
+Q12416	262	Phosphoserine
+Q12416	288	Phosphoserine
+Q12416	290	Phosphothreonine
+Q12363	187	Phosphothreonine
+Q12363	200	Phosphoserine
+Q12363	370	Phosphothreonine
+Q12363	406	Phosphothreonine
+P36095	203	Glycyl
+P40343	157	Phosphoserine
+P40343	495	Phosphoserine
+P40343	613	Phosphoserine
+P40343	294	Glycyl
+P36116	2	N-acetylalanine
+Q03388	425	Phosphoserine
+P40046	2	N-acetylserine
+P43585	182	Phosphoserine
+P43585	187	Phosphoserine
+P43585	196	Phosphoserine
+P43585	264	Phosphoserine
+P43585	583	Phosphoserine
+P43585	615	Phosphoserine
+P43585	616	Phosphoserine
+P43585	620	Phosphothreonine
+P43585	626	Phosphoserine
+P43585	657	Phosphoserine
+P53832	402	Phosphothreonine
+P53832	455	Phosphoserine
+P53832	458	Phosphoserine
+P42826	244	Phosphoserine
+P33301	349	Phosphoserine
+P33301	533	Phosphoserine
+P33301	534	Phosphoserine
+P33301	553	Phosphoserine
+P33301	555	Phosphothreonine
+Q02792	574	Phosphoserine
+P30822	1080	Phosphoserine
+P36017	188	Phosphoserine
+P36017	210	Cysteine
+P36017	208	S-geranylgeranyl
+P36017	210	S-geranylgeranyl
+Q03897	759	Phosphoserine
+P38216	2	N-acetylserine
+P38216	32	Glycyl
+P38239	2	N-acetylserine
+P38243	182	Phosphoserine
+P38243	184	Phosphothreonine
+P38243	186	Phosphoserine
+P32386	936	Phosphoserine
+P32386	940	Phosphoserine
+P32386	955	Phosphoserine
+P32386	6	N-linked
+P32386	97	N-linked
+P25349	244	Cysteine
+P25349	243	S-palmitoyl
+P25349	244	S-farnesyl
+P25351	313	Phosphoserine
+P25351	603	Phosphoserine
+P25639	219	Phosphoserine
+P25639	87	N-linked
+P25639	98	N-linked
+P25639	250	Glycyl
+Q12489	2	N-acetylserine
+Q12489	13	Glycyl
+Q03193	229	Phosphoserine
+Q03193	251	N-linked
+Q03193	259	N-linked
+Q03780	1	N-acetylmethionine
+Q03780	63	Phosphoserine
+Q03780	254	Phosphoserine
+Q03780	313	Phosphoserine
+Q03780	342	Phosphoserine
+Q03780	345	Phosphoserine
+Q03780	390	Phosphoserine
+Q03780	477	Phosphoserine
+Q03780	492	Phosphoserine
+Q03780	546	Phosphoserine
+Q03780	683	Phosphoserine
+Q03780	699	Phosphoserine
+P34225	290	Phosphothreonine
+P34225	293	Phosphoserine
+P34225	299	Phosphoserine
+P43590	50	Glycyl
+P53273	42	Phosphoserine
+P53273	127	Phosphoserine
+P53273	130	Phosphothreonine
+P53273	140	Phosphoserine
+P53273	144	Phosphoserine
+P53273	149	Phosphoserine
+P53273	152	Phosphoserine
+P53273	153	Phosphoserine
+P53273	842	Phosphoserine
+P53273	847	Phosphothreonine
+P48236	78	Phosphoserine
+P38750	305	Phosphothreonine
+P38750	546	Phosphoserine
+P38750	588	Phosphothreonine
+P38708	149	Phosphoserine
+P38708	170	Phosphothreonine
+P38708	655	Phosphoserine
+P38716	198	N6-(pyridoxal
+P34231	675	Phosphoserine
+P34231	678	Phosphoserine
+P34231	61	N-linked
+P34231	84	N-linked
+P34231	115	N-linked
+P34231	154	N-linked
+P34231	176	N-linked
+P34231	197	N-linked
+P34231	207	N-linked
+P34231	228	N-linked
+P34231	241	N-linked
+P34231	267	N-linked
+P34231	293	N-linked
+P34231	299	N-linked
+P34231	312	N-linked
+P34231	335	N-linked
+P34231	351	N-linked
+P34231	373	N-linked
+P34231	389	N-linked
+P34231	519	N-linked
+P34231	709	N-linked
+P34231	714	N-linked
+P34231	724	N-linked
+P34231	697	Glycyl
+Q07988	203	GPI-anchor
+Q07988	148	N-linked
+Q07988	181	N-linked
+Q07988	191	N-linked
+Q05131	425	Phosphoserine
+Q03177	528	Phosphoserine
+Q03177	771	Phosphothreonine
+P53964	270	N-linked
+Q99247	668	Phosphoserine
+Q99247	693	Phosphothreonine
+Q92393	416	Phosphoserine
+Q08844	28	N-linked
+Q08844	43	N-linked
+Q08844	87	N-linked
+Q08844	103	N-linked
+P53049	10	Phosphoserine
+P53049	24	Phosphoserine
+P53049	53	Phosphothreonine
+P53049	661	N-linked
+P53049	759	N-linked
+P53049	799	N-linked
+Q12079	155	N-linked
+Q12079	265	N-linked
+Q02864	21	Phosphoserine
+Q06537	27	N-linked
+P18961	63	Phosphothreonine
+P18961	66	Phosphothreonine
+P18961	72	Phosphoserine
+P18961	499	Phosphothreonine
+P18961	501	Phosphothreonine%3B
+P18961	641	Phosphoserine%3B
+P18961	650	Phosphoserine
+P18961	659	Phosphothreonine%3B
+P18961	669	Phosphoserine
+P32939	208	Cysteine
+P32939	206	S-geranylgeranyl
+P32939	208	S-geranylgeranyl
+P32939	147	Glycyl
+P36036	1	N-acetylmethionine
+P38079	293	Phosphoserine
+P38079	341	Phosphothreonine
+P38079	343	Phosphoserine
+P38079	286	Glycyl
+Q2V2Q2	55	GPI-anchor
+Q2V2Q2	25	N-linked
+Q2V2Q2	30	N-linked
+Q2V2Q2	35	N-linked
+Q2V2Q2	40	N-linked
+P39109	251	Phosphoserine
+P39109	873	Phosphoserine
+P39109	903	Phosphoserine
+P39109	908	Phosphoserine
+P39109	911	Phosphothreonine
+P39109	914	Phosphoserine
+Q12316	416	Phosphoserine
+Q12222	211	Phosphoserine
+P38733	111	N-linked
+Q99219	2	N-acetylserine
+P53845	2	N-acetylserine
+P40440	87	N-linked
+P47098	416	Phosphoserine
+P47072	514	Phosphoserine
+P36015	158	Phosphothreonine
+P36015	197	Cysteine
+P36015	196	S-palmitoyl
+P36015	197	S-farnesyl
+P53925	22	Phosphoserine
+P53925	56	Phosphoserine
+P53925	63	Phosphoserine
+P53925	244	Phosphoserine
+Q08234	41	N-linked
+Q08234	86	N-linked
+Q08234	101	N-linked
+Q08234	151	N-linked
+Q08234	341	N-linked
+Q08234	349	N-linked
+Q08234	371	N-linked
+Q08234	528	N-linked
+Q08234	983	N-linked
+Q12275	99	Phosphoserine
+Q12275	751	Phosphoserine
+Q12275	28	N-linked
+Q12275	71	N-linked
+Q12275	98	N-linked
+Q12275	128	N-linked
+Q12275	151	N-linked
+Q12275	209	N-linked
+Q12275	288	N-linked
+Q12275	328	N-linked
+Q12275	575	N-linked
+Q12275	644	N-linked
+Q12275	730	N-linked
+Q12275	881	N-linked
+Q12275	917	N-linked
+Q12275	995	N-linked
+Q12275	1009	N-linked
+Q12275	1198	N-linked
+Q12275	1301	N-linked
+Q12275	1302	N-linked
+Q12275	1447	N-linked
+Q12275	1472	N-linked
+Q12275	1488	N-linked
+Q12275	1565	N-linked
+Q12275	1597	N-linked
+Q12275	1634	N-linked
+Q12282	212	GPI-anchor
+Q12282	155	N-linked
+Q12282	160	N-linked
+Q12282	203	N-linked
+Q12282	212	N-linked
+Q06328	136	Phosphoserine
+P40583	515	GPI-anchor
+P40583	57	N-linked
+P40583	149	N-linked
+P40583	156	N-linked
+P40583	161	N-linked
+P40583	183	N-linked
+P40583	195	N-linked
+P40583	311	N-linked
+P40583	363	N-linked
+P40583	375	N-linked
+P40583	379	N-linked
+P40583	472	N-linked
+P48559	415	S-geranylgeranyl
+P48559	416	S-geranylgeranyl
+P51996	2	N-acetylserine
+P51996	221	S-geranylgeranyl
+P51996	222	S-geranylgeranyl
+P40517	31	Phosphothreonine
+P40517	179	Phosphoserine
+P50111	229	Phosphoserine
+Q07555	267	Phosphoserine
+P0CX65	416	Phosphoserine
+Q12301	225	Phosphoserine
+Q99315	2	N-acetylserine
+P53278	286	Phosphoserine
+P53278	343	Phosphoserine
+P53278	347	Phosphoserine
+P53278	809	Phosphothreonine
+P38809	69	Phosphoserine
+P38809	76	Phosphothreonine
+P38809	189	Phosphothreonine
+P38809	288	Phosphoserine
+P38809	294	Phosphoserine
+P38809	359	Phosphoserine
+P38809	78	Glycyl
+P38809	187	Glycyl
+P38809	242	Glycyl
+P38841	41	Phosphoserine
+P40566	594	Phosphothreonine
+P47100	416	Phosphoserine
+P47139	39	Phosphoserine
+Q07895	68	N-linked
+Q07895	112	N-linked
+Q07895	152	N-linked
+Q07895	200	N-linked
+Q07895	291	N-linked
+Q07895	333	N-linked
+Q07895	450	N-linked
+Q07895	521	N-linked
+Q07895	542	N-linked
+Q07895	569	N-linked
+Q07895	663	N-linked
+Q07895	679	N-linked
+Q07895	688	N-linked
+Q07834	762	Phosphoserine
+Q12110	127	Phosphoserine
+P0CX68	416	Phosphoserine
+Q05948	22	Glycyl
+Q06146	2	N-acetylvaline
+Q06146	44	Phosphothreonine
+Q06146	49	Phosphoserine
+Q06146	69	Phosphoserine
+Q06146	121	Phosphoserine
+Q06146	126	Phosphoserine
+Q06146	129	Phosphoserine
+Q06146	137	Phosphoserine
+Q06146	139	Phosphoserine
+Q06146	159	Phosphothreonine
+Q06146	238	Phosphoserine
+Q06146	240	Phosphoserine
+Q06146	242	Phosphoserine
+Q06146	270	Phosphoserine
+Q06137	6	Phosphoserine
+P53751	35	N-linked
+P53751	336	N-linked
+P53751	553	N-linked
+P53751	846	N-linked
+P53751	985	N-linked
+P53962	351	Phosphoserine
+P0CX59	416	Phosphoserine
+Q06839	310	Phosphoserine
+Q06839	451	Phosphoserine
+P0C2I9	416	Phosphoserine
+P0C2J1	416	Phosphoserine
+Q12523	47	Phosphoserine
+Q12523	65	Phosphoserine
+P43587	2	N-acetylserine
+P43587	22	Phosphoserine
+P43587	133	Phosphoserine
+P36019	220	Cysteine
+P36019	218	S-geranylgeranyl
+P36019	220	S-geranylgeranyl
+P0CX57	416	Phosphoserine
+P38749	135	Phosphoserine
+O43137	22	Phosphoserine
+Q12217	416	Phosphoserine
+Q12193	416	Phosphoserine
+P38355	199	Phosphothreonine
+P38355	234	Phosphoserine
+P38142	63	N-linked
+Q8J0M4	71	Phosphoserine
+Q8J0M4	74	Phosphoserine
+Q8J0M4	86	Glycyl
+Q12235	500	Phosphoserine
+Q12235	501	Phosphoserine
+Q12235	146	N-linked
+Q03855	416	Phosphoserine
+Q12407	90	Phosphoserine
+P0CX66	416	Phosphoserine
+P40028	730	Phosphoserine
+P40028	731	Phosphoserine
+Q12141	416	Phosphoserine
+P53274	106	Phosphoserine
+P53316	29	Phosphoserine
+P53316	433	Phosphoserine
+P53316	435	Phosphoserine
+P53316	482	Phosphoserine
+P53316	485	Phosphoserine
+P53316	486	Phosphothreonine
+P53316	501	Phosphoserine
+P53110	1	N-acetylmethionine
+P38833	96	Phosphoserine
+P38870	2	N-acetylserine
+P36134	17	Glycyl
+P0CX72	416	Phosphoserine
+Q3E760	4	N-linked
+P53740	78	N-linked
+P53740	123	N-linked
+P53740	187	N-linked
+P53740	202	N-linked
+P53740	213	N-linked
+P53740	240	N-linked
+P53740	291	N-linked
+Q08560	14	N-linked
+Q08560	15	N-linked
+Q12441	416	Phosphoserine
+Q99231	416	Phosphoserine
+Q03362	10	N-linked
+Q03362	70	N-linked
+Q03362	74	N-linked
+P0CX71	416	Phosphoserine
+P43562	52	N-linked
+P43562	374	N-linked
+P53249	59	N-linked
+P53249	98	N-linked
+P53249	126	N-linked
+P53249	171	N-linked
+P53249	221	N-linked
+P53249	230	N-linked
+P53249	262	N-linked
+P38887	305	N-linked
+P38887	497	N-linked
+P38887	577	N-linked
+P0CF21	39	N6-(pyridoxal
+P40520	68	N-linked
+P40520	84	N-linked
+P0C2I7	416	Phosphoserine
+Q12402	2	N-acetylserine
+Q02831	59	Phosphoserine
+Q02831	95	Phosphoserine
+Q6Q5H1	416	Phosphoserine
+Q99395	68	Phosphoserine
+Q07688	64	Phosphohistidine
+P40049	65	N-linked
+P40049	86	N-linked
+P40049	93	N-linked
+P40049	220	N-linked
+P40049	231	N-linked
+P43564	435	Phosphoserine
+P43564	1037	Phosphoserine
+P53066	1	N-acetylmethionine
+P53066	172	Phosphoserine
+P0CX19	184	GPI-anchor
+P0CX19	28	N-linked
+P0CX19	138	N-linked
+P38745	497	Phosphoserine
+P38745	152	N-linked
+P38745	253	N-linked
+Q04116	315	Phosphoserine
+P40543	107	Phosphoserine
+P40543	172	Phosphoserine
+P40508	230	Phosphoserine
+P40017	2	N-acetylserine
+P40017	783	Phosphoserine
+Q3E776	114	N-linked
+P42937	1	N-acetylmethionine
+Q3E7B7	37	Phosphoserine
+P0CX67	416	Phosphoserine
+P53139	2	N-myristoyl
+P53139	4	S-palmitoyl
+P0CX74	416	Phosphoserine
+P47121	15	N-linked
+P40361	9	Phosphoserine
+P40361	41	Phosphoserine
+P40361	178	Phosphoserine
+P40361	180	Phosphoserine
+P36138	21	Glycyl
+P40544	184	N-linked
+P40544	274	N-linked
+P40544	285	N-linked
+P0C2I3	416	Phosphoserine
+P40095	63	N-linked
+P40095	123	N-linked
+P40095	236	N-linked
+P40095	437	N-linked
+P40095	442	N-linked
+P40095	498	N-linked
+P40095	535	N-linked
+P40095	541	N-linked
+Q12085	416	Phosphoserine
+Q12485	416	Phosphoserine
+Q12269	416	Phosphoserine
+P40442	28	N-linked
+P40442	35	N-linked
+P40442	468	N-linked
+P40442	664	N-linked
+P36114	196	Phosphothreonine
+P36114	246	Phosphoserine
+P36114	377	Phosphoserine
+P36114	380	Phosphoserine
+P0C2I6	416	Phosphoserine
+Q06251	1	N-acetylmethionine
+Q06251	31	Phosphoserine
+Q06251	34	Phosphoserine
+Q06251	84	Phosphoserine
+Q06251	235	Phosphothreonine
+Q05777	232	GPI-anchor
+Q05777	229	N-linked
+P0CX76	416	Phosphoserine
+Q04835	40	Glycyl
+Q03730	93	Phosphoserine
+Q03161	88	Phosphoserine
+P53826	99	N-linked
+P53826	106	N-linked
+P53947	148	Phosphoserine
+P53947	256	Phosphoserine
+P53947	276	Phosphoserine
+P38806	183	Phosphoserine
+P38806	185	Phosphothreonine
+P38806	188	Phosphoserine
+P53862	118	N-linked
+Q08206	1	N-acetylmethionine
+P0CX73	416	Phosphoserine
+P0CX58	416	Phosphoserine
+Q06522	95	N-linked
+Q12152	456	Phosphoserine
+Q12152	533	Phosphoserine
+P32618	154	Phosphothreonine
+P32618	501	Phosphoserine
+P32618	520	Phosphoserine
+P32618	802	Phosphoserine
+P32618	842	Phosphoserine
+P32618	895	Phosphoserine
+Q07950	73	Phosphoserine
+Q07950	107	Phosphoserine
+P43597	180	Phosphoserine
+P43597	462	Phosphoserine
+P43597	523	Phosphoserine
+P43597	861	Phosphothreonine
+P43597	975	Phosphoserine
+P43597	1037	Phosphoserine
+P43597	1046	Phosphoserine
+P53120	1167	Phosphoserine
+P53120	1191	Phosphotyrosine
+P53120	1198	Phosphoserine
+P53120	1199	Phosphoserine
+P25637	187	Glycyl
+P40483	361	Phosphoserine
+P40483	245	Glycyl
+P40483	478	Glycyl
+P40483	518	Glycyl
+P40483	579	Glycyl
+P40483	590	Glycyl
+P40483	596	Glycyl
+P53108	60	Phosphoserine
+P47078	33	N-linked
+P36119	426	Phosphoserine
+P36119	431	Phosphoserine
+P36119	434	Phosphoserine
+P36119	457	Phosphoserine
+P36119	509	Glycyl
+Q06698	9	Phosphoserine
+Q06698	816	Phosphoserine
+Q03434	416	Phosphoserine
+Q04336	299	Phosphoserine
+Q04336	984	Phosphoserine
+Q04336	1013	Phosphothreonine
+Q04336	1081	Phosphoserine
+Q03559	11	Phosphoserine
+Q03559	23	Phosphoserine
+Q03559	26	Glycyl
+Q03559	32	Glycyl
+Q04869	2	Phosphoserine
+P39523	1	N-acetylmethionine
+P39523	553	Phosphoserine
+P39523	586	Phosphoserine
+P39523	619	Phosphoserine
+P39523	649	Phosphoserine
+P39523	681	Phosphoserine
+P39523	766	Phosphoserine
+P39523	771	Phosphoserine
+Q03795	237	Phosphoserine
+Q05016	260	Phosphoserine
+Q03759	2	N-acetylserine
+P53723	2	N-acetylserine
+P53723	44	N-linked
+P53723	98	N-linked
+Q08910	26	N-linked
+Q08910	48	N-linked
+Q08910	91	N-linked
+Q08910	139	N-linked
+Q08910	152	N-linked
+Q08910	183	N-linked
+Q08157	224	Phosphoserine
+Q08157	232	Phosphoserine
+Q08157	363	Phosphoserine
+P38070	90	Phosphoserine
+P38070	105	Phosphoserine
+P38070	107	Phosphothreonine
+P38070	321	Phosphoserine%3B
+P38070	490	Phosphothreonine%3B
+P38070	513	Phosphoserine%3B
+P53057	57	N-linked
+P38815	65	Phosphoserine
+P38815	66	Phosphoserine
+Q99260	215	Cysteine
+Q99260	213	S-geranylgeranyl
+Q99260	215	S-geranylgeranyl
+P31111	481	Phosphoserine
+P40021	275	Phosphoserine
+P40021	354	Phosphoserine
+P40021	403	Phosphoserine
+P40021	407	Phosphoserine
+P40021	632	Phosphoserine
+P40021	676	Phosphoserine
+Q12512	28	N-linked
+Q12512	57	N-linked
+Q12512	98	N-linked
+Q12512	217	N-linked
+Q06325	26	N-linked
+Q06325	59	N-linked
+Q06325	106	N-linked
+Q06325	131	N-linked
+Q06325	140	N-linked
+Q06325	143	N-linked
+Q06325	148	N-linked
+Q06325	175	N-linked
+Q06325	308	N-linked
+Q06325	391	N-linked
+Q06325	455	N-linked
+Q06325	478	N-linked
+Q06325	484	N-linked
+Q06325	549	N-linked
+Q06325	552	N-linked
+P38146	199	Cysteine
+P38146	197	S-geranylgeranyl
+P38146	199	S-geranylgeranyl
+P38555	2	N-acetylserine
+P38555	222	S-geranylgeranyl
+P38555	223	S-geranylgeranyl
+P36018	139	Phosphoserine
+P36018	142	Phosphoserine
+P36018	232	S-geranylgeranyl
+P36018	233	S-geranylgeranyl
+P36018	151	Glycyl
+P38280	159	Phosphoserine
+P38280	160	Phosphoserine
+Q12324	636	Phosphothreonine
+P53303	23	Phosphoserine
+P53303	407	Phosphothreonine
+P0C2I5	416	Phosphoserine
+Q06689	654	Phosphoserine
+Q06689	665	Phosphoserine
+Q06689	49	N-linked
+Q06689	72	N-linked
+Q06689	103	N-linked
+Q06689	142	N-linked
+Q06689	160	N-linked
+Q06689	194	N-linked
+Q06689	215	N-linked
+Q06689	228	N-linked
+Q06689	252	N-linked
+Q06689	286	N-linked
+Q06689	299	N-linked
+Q06689	318	N-linked
+Q06689	322	N-linked
+Q06689	358	N-linked
+Q06689	375	N-linked
+Q06689	405	N-linked
+Q06689	429	N-linked
+Q06689	468	N-linked
+Q06689	671	Glycyl
+Q04461	17	Phosphoserine
+Q04461	23	Phosphoserine
+Q04461	237	Phosphoserine
+Q04461	249	Phosphoserine
+Q04461	254	Phosphothreonine
+Q04471	338	Phosphoserine
+Q04670	416	Phosphoserine
+Q03823	76	Phosphoserine
+Q03823	79	Phosphoserine
+Q03231	47	Phosphoserine
+Q04867	190	Phosphoserine
+Q03208	72	Phosphoserine
+Q04773	1	N-acetylmethionine
+Q04773	121	Phosphoserine
+Q04773	126	Phosphoserine
+Q12470	416	Phosphoserine
+P53719	136	Phosphoserine
+P40159	2	N-acetylserine
+P40159	53	Phosphoserine
+P40159	70	Phosphoserine
+Q92392	416	Phosphoserine
+Q12015	11	N-linked
+Q12015	41	N-linked
+Q12015	77	N-linked
+Q12015	99	N-linked
+Q12015	145	N-linked
+Q08743	19	N-linked
+Q08743	121	N-linked
+Q08912	68	N-linked
+Q08912	150	N-linked
+Q08912	219	N-linked
+Q08912	366	N-linked
+Q08912	441	N-linked
+Q08912	447	N-linked
+Q08912	464	N-linked
+Q08912	528	N-linked
+Q12160	36	N-linked
+Q06116	2254	Phosphoserine
+Q06116	2278	Phosphoserine
+Q06116	191	N-linked
+Q06116	210	N-linked
+Q06116	311	N-linked
+Q06116	452	N-linked
+Q06116	468	N-linked
+Q06116	605	N-linked
+Q06116	638	N-linked
+Q06116	663	N-linked
+Q06116	698	N-linked
+Q06116	789	N-linked
+Q06116	835	N-linked
+Q06116	981	N-linked
+Q06116	1255	N-linked
+Q06116	1404	N-linked
+Q06116	1476	N-linked
+Q06116	1978	N-linked
+Q06116	2189	N-linked
+Q06116	2279	N-linked
+P0CX60	416	Phosphoserine
+Q06523	47	Phosphoserine
+Q12159	2	N-acetylserine
+Q12159	8	Phosphoserine
+Q12159	100	Phosphoserine
+P53107	272	Phosphothreonine
+Q12436	148	Phosphoserine
+Q12436	149	Phosphoserine
+Q12436	162	Phosphoserine
+Q12436	170	Phosphoserine
+Q12436	188	Phosphothreonine
+P32527	50	Phosphoserine
+P40523	559	Phosphoserine
+P47114	291	Phosphoserine
+P47114	319	Phosphoserine
+P46992	368	GPI-anchor
+P46992	51	N-linked
+P46992	99	N-linked
+P46992	122	N-linked
+P46992	146	N-linked
+P46992	174	N-linked
+P46992	219	N-linked
+P46992	249	N-linked
+P46992	267	N-linked
+P46992	300	N-linked
+P46992	328	N-linked
+P46992	346	N-linked
+P47087	176	Phosphoserine
+Q07990	139	GPI-anchor
+Q07990	77	N-linked
+Q07990	104	N-linked
+Q07990	120	N-linked
+P0CX75	416	Phosphoserine
+Q99296	82	Phosphoserine
+Q99296	89	Phosphoserine
+Q99296	483	Phosphoserine
+Q99296	651	Phosphoserine
+Q05854	1143	Phosphoserine
+Q04706	416	Phosphoserine
+Q3E842	45	N-linked
+P0CX69	416	Phosphoserine
+Q03219	263	Phosphoserine
+Q03649	82	Glycyl
+Q03697	209	Phosphoserine
+Q03697	99	N-linked
+Q12273	416	Phosphoserine
+Q3E752	24	Phosphoserine
+Q3E752	32	Phosphoserine
+Q06833	640	Phosphoserine
+Q06833	669	Phosphoserine
+Q06833	717	Phosphoserine
+Q06833	720	Phosphoserine
+Q06833	723	Phosphoserine
+Q06833	228	N-linked
+Q06833	263	N-linked
+Q06833	279	N-linked
+Q06833	300	N-linked
+Q06833	391	N-linked
+Q06833	528	N-linked
+Q06833	529	N-linked
+Q06833	595	N-linked
+Q06833	620	N-linked
+Q06833	700	N-linked
+Q06833	718	N-linked
+Q06616	158	Phosphoserine
+Q06616	170	Phosphoserine
+Q06616	175	Phosphoserine
+Q12697	1	N-acetylmethionine
+Q12697	95	Phosphothreonine
+Q12697	108	Phosphoserine
+Q12697	1117	Phosphoserine
+Q12697	1120	Phosphoserine
+Q12303	483	GPI-anchor
+Q12303	75	N-linked
+Q12303	120	N-linked
+Q12303	160	N-linked
+Q12303	163	N-linked
+Q12303	275	N-linked
+Q12303	309	N-linked
+Q12303	328	N-linked
+Q12303	367	N-linked
+Q12303	422	N-linked
+Q12303	445	N-linked
+Q12303	462	N-linked
+P41920	60	Phosphoserine
+Q08245	2	N-acetylserine
+Q08245	2	Phosphoserine
+Q08245	25	Phosphoserine
+Q08245	40	Phosphoserine
+Q08245	49	Phosphothreonine
+Q08245	18	Glycyl
+Q08245	23	Glycyl
+Q08245	29	Glycyl
+Q08245	34	Glycyl
+Q08245	45	Glycyl
+Q08245	57	Glycyl
+Q08245	82	Glycyl
+P53752	157	N-linked
+P53975	270	N-linked
+Q3E824	44	N-linked
+P32329	548	GPI-anchor
+P32329	95	N-linked
+P32329	203	N-linked
+P32329	232	N-linked
+P32329	242	N-linked
+P32329	245	N-linked
+P32329	299	N-linked
+P32329	358	N-linked
+P32329	480	N-linked
+P32329	522	N-linked
+P32329	532	N-linked
+P01123	1	N-acetylmethionine
+P01123	172	Phosphoserine
+P01123	174	Phosphoserine
+P01123	23	S-palmitoyl
+P01123	123	S-palmitoyl
+P01123	205	S-geranylgeranyl
+P01123	206	S-geranylgeranyl
+P01123	144	Glycyl
+P47043	156	Phosphoserine
+P47043	166	Phosphoserine
+P47043	515	Phosphoserine
+P54786	50	Phosphoserine
+Q12025	47	N-linked
+P38966	238	Phosphoserine
+P38966	241	Phosphoserine
+P38966	316	Phosphoserine
+P38966	324	Phosphoserine
+P38966	327	Phosphoserine
+P38966	609	Phosphoserine
+P38966	612	Phosphoserine
+P38966	668	Phosphoserine
+P38966	760	Phosphoserine
+Q12121	329	Phosphoserine
+P40022	1	N-acetylmethionine
+P35723	190	Glycyl
+Q12173	2	N-acetylserine
+P50089	215	Phosphoserine
+P50089	667	Phosphoserine
+P53183	339	Phosphoserine
+P53133	223	Phosphoserine
+P38616	40	N-linked
+P38616	50	N-linked
+P38616	53	N-linked
+P38616	58	N-linked
+P38616	61	N-linked
+P38616	65	N-linked
+P38616	87	N-linked
+P38616	94	N-linked
+P38616	100	N-linked
+P38616	106	N-linked
+P38616	118	N-linked
+P38616	172	N-linked
+P38616	239	N-linked
+P38616	286	N-linked
+P38829	2	N-acetylserine
+P40449	16	Glycyl
+P40449	35	Glycyl
+P47099	416	Phosphoserine
+P47115	221	Phosphoserine
+P0C2I8	416	Phosphoserine
+Q06247	24	Phosphothreonine
+Q06247	27	Phosphoserine
+Q06247	115	N-linked
+Q06247	141	N-linked
+Q06247	169	N-linked
+Q06247	407	N-linked
+Q06247	425	N-linked
+Q06247	449	N-linked
+Q06247	453	N-linked
+Q06247	527	N-linked
+Q06247	580	N-linked
+Q08989	40	N-linked
+Q08989	68	N-linked
+Q08989	150	N-linked
+Q08989	220	N-linked
+Q08989	304	N-linked
+Q08989	367	N-linked
+Q08989	442	N-linked
+Q08989	448	N-linked
+Q08816	69	Phosphotyrosine
+Q08816	105	Phosphoserine
+Q08816	108	Phosphoserine
+Q08816	342	Phosphoserine
+Q12414	416	Phosphoserine
+Q12010	9	N-linked
+Q12010	189	N-linked
+Q12010	275	N-linked
+P32793	301	Phosphoserine
+P32793	311	Phosphoserine
+P26725	77	N-linked
+P26725	82	N-linked
+P26725	92	N-linked
+P26725	167	N-linked
+P26725	414	N-linked
+P53735	16	Phosphoserine
+P53735	131	Phosphoserine
+P53735	498	Phosphoserine
+P20107	387	Phosphoserine
+P20107	393	Phosphoserine
+P20107	397	Phosphoserine
+P20107	357	Glycyl
+P34240	178	Phosphoserine
+P34240	188	Phosphoserine
+Q06681	13	Phosphoserine
+Q06681	411	Phosphoserine
+Q06681	596	Phosphoserine
+Q06681	1032	Phosphoserine
+Q06681	1306	N-linked
+Q06681	1373	N-linked
+Q06681	1430	N-linked
+P15891	2	N-acetylalanine
+P15891	165	Phosphothreonine
+P15891	167	Phosphoserine
+P15891	169	Phosphoserine
+P15891	181	Phosphothreonine
+P15891	183	Phosphoserine
+P15891	313	Phosphoserine
+P15891	365	Phosphoserine
+P15891	389	Phosphoserine
+P15891	458	Phosphoserine
+P15891	481	Phosphoserine
+P15891	464	Glycyl
+P32316	2	N-acetylthreonine
+P32316	350	Phosphoserine
+Q00362	124	Phosphoserine
+P47096	176	Phosphoserine
+P32357	253	Phosphoserine
+P32357	274	Phosphothreonine
+P32357	328	Phosphotyrosine
+P32357	331	Phosphoserine
+P32357	345	Phosphothreonine
+P07248	54	Phosphoserine
+P07248	188	Phosphothreonine
+P07248	193	Phosphothreonine
+P07248	230	Phosphoserine%3B
+P07248	258	Phosphoserine
+P07248	259	Phosphothreonine
+P07248	299	Phosphoserine
+P07248	323	Phosphoserine
+P07248	325	Phosphoserine
+P07248	327	Phosphothreonine
+P38903	242	Phosphothreonine
+P38903	257	Phosphothreonine
+P47129	44	Phosphoserine
+P47129	71	Phosphoserine
+P47129	74	Phosphoserine
+P47129	78	Phosphoserine
+P47129	165	Phosphoserine
+P47129	288	Phosphoserine
+P14164	189	Phosphothreonine
+P14164	193	Phosphoserine
+P14164	467	Phosphoserine
+P14164	554	Phosphoserine
+P14164	618	Phosphoserine
+P14164	624	Phosphoserine%3B
+P14164	720	Phosphoserine%3B
+P14164	18	Glycyl
+P40535	171	Phosphoserine
+P40535	179	Phosphoserine
+P40535	399	Phosphoserine
+P40535	557	Phosphoserine
+P40535	559	Phosphothreonine
+P31787	51	Glycyl
+P31787	72	Glycyl
+P32323	699	GPI-anchor
+Q12471	55	Glycyl
+P23542	2	N-acetylserine
+P23542	255	N6-(pyridoxal
+P23542	389	Phosphoserine
+Q07622	184	Glycyl
+Q07622	191	Glycyl
+Q03771	2	N-acetylserine
+P21192	80	Phosphoserine
+P21192	122	Phosphoserine
+P21192	247	Phosphoserine
+P21192	249	Phosphoserine
+P21192	253	Phosphoserine
+P21192	259	Phosphothreonine
+P21192	385	Phosphoserine
+P21192	392	Phosphoserine
+P21192	483	Phosphoserine
+P21192	486	Phosphothreonine
+P21192	501	Phosphothreonine
+P21192	564	Phosphoserine
+P21192	709	Phosphoserine
+P21192	714	Phosphoserine
+P28240	53	Phosphothreonine
+P38720	50	Phosphoserine
+Q01802	286	N6-(pyridoxal
+Q08641	93	Phosphoserine
+Q08641	150	Phosphothreonine
+Q08641	321	Phosphoserine
+Q08641	326	Phosphoserine
+Q08641	347	Phosphothreonine
+P40433	92	Phosphoserine
+P40433	157	Phosphothreonine
+P40433	644	Phosphoserine
+P40433	652	Phosphoserine
+P40433	659	Phosphoserine
+P40433	667	Phosphoserine
+Q00955	2	N-acetylserine
+Q00955	2	Phosphoserine
+Q00955	735	N6-biotinyllysine
+Q00955	790	Phosphoserine
+Q00955	1148	Phosphoserine
+Q00955	1157	Phosphoserine
+Q00955	1162	Phosphoserine
+P40529	2	N-acetylserine
+P40529	180	Phosphoserine
+P40529	183	Phosphoserine
+P40529	207	Phosphoserine
+P46680	2	N-acetylserine
+P52893	77	Phosphoserine
+P52893	412	N6-(pyridoxal
+P38065	727	Phosphothreonine
+P38065	733	Phosphoserine
+P53886	1462	Phosphoserine
+P36154	78	Phosphoserine
+P46367	96	Phosphoserine
+P46367	216	Phosphothreonine
+P46367	500	Phosphoserine
+P40350	83	N-linked
+P40350	119	N-linked
+P43633	76	Phosphoserine
+P43633	79	Phosphoserine
+Q08269	2	N-acetylserine
+Q08269	77	Phosphotyrosine
+Q08269	85	Phosphoserine
+Q08269	185	Phosphoserine
+Q08269	188	Phosphoserine
+Q08269	220	Phosphoserine
+Q08269	221	Phosphoserine
+Q08269	236	Phosphoserine
+Q08269	242	Phosphothreonine
+Q08269	850	Phosphoserine
+P14904	356	Phosphoserine
+P14904	107	N-linked
+P14904	110	N-linked
+P14904	448	N-linked
+P60010	1	N-acetylmethionine
+P60010	191	Glycyl
+P25371	659	Phosphoserine
+P25371	702	Phosphoserine
+P25371	50	N-linked
+P25371	114	N-linked
+P25371	165	N-linked
+P25371	221	N-linked
+P25371	935	N-linked
+P33304	472	Phosphoserine
+P33304	526	Phosphoserine
+P43636	170	N-linked
+P43636	303	N-linked
+P43636	371	N-linked
+P43636	400	N-linked
+P47029	155	Phosphoserine
+P47029	162	Phosphoserine
+P47029	213	Phosphoserine
+P47029	586	Phosphoserine
+P47029	826	Phosphoserine
+P47029	838	Phosphoserine
+P47029	900	Phosphoserine
+P47029	1022	Phosphoserine
+P47029	1023	Phosphoserine
+P40502	2	N-acetylserine
+P40563	18	Phosphothreonine
+P40563	36	Phosphoserine
+P40563	58	Phosphothreonine
+P40563	70	Phosphoserine
+P40563	85	Phosphothreonine
+P40563	104	Phosphoserine
+P40563	183	Phosphoserine
+P40563	206	Phosphoserine
+P40563	231	Phosphoserine
+P40563	277	Phosphothreonine
+P40563	284	Phosphoserine
+P40563	324	Phosphoserine
+P40563	552	Phosphothreonine
+P40563	576	Phosphoserine
+P40563	620	Phosphoserine
+P40563	623	Phosphoserine
+P40563	625	Phosphoserine
+P40563	627	Phosphoserine
+P40563	667	Phosphoserine
+P40563	671	Phosphoserine
+P40563	675	Phosphoserine
+P40563	678	Phosphoserine
+P16550	60	Phosphothreonine
+P00330	2	N-acetylserine
+P00330	213	Phosphoserine
+P00330	223	Phosphothreonine
+P00330	279	Phosphoserine
+P00330	316	Phosphoserine
+P00330	226	Glycyl
+P00330	234	Glycyl
+P00330	287	Glycyl
+P00330	319	Glycyl
+P00331	2	N-acetylserine
+P00331	213	Phosphoserine
+P00331	223	Phosphothreonine
+P00331	279	Phosphoserine
+P00331	316	Phosphoserine
+P00331	226	Glycyl
+P00331	234	Glycyl
+P00331	287	Glycyl
+P00331	319	Glycyl
+Q04894	131	Phosphoserine
+Q04894	315	Phosphoserine
+Q04894	359	Phosphoserine
+P38266	57	Phosphoserine
+P38266	58	Phosphoserine
+P38266	64	Phosphoserine
+P38266	476	Phosphoserine
+P38266	729	Phosphothreonine
+P38266	861	Phosphothreonine
+Q99299	25	Phosphoserine
+P53954	262	N-linked
+P53954	393	N-linked
+P53954	480	N-linked
+P53954	490	N-linked
+P38313	41	Phosphoserine
+P38313	45	Phosphoserine
+P38313	53	Phosphoserine
+P38313	59	Phosphoserine
+P38313	101	Phosphoserine
+P52910	679	Phosphoserine
+P52910	506	Glycyl
+P25376	6	Phosphoserine
+P25376	633	S-palmitoyl
+P25376	11	Glycyl
+P10869	333	Phosphothreonine
+Q08548	513	Phosphoserine
+Q08548	605	Phosphoserine
+Q08548	610	Phosphoserine
+Q08548	615	Phosphoserine
+P36117	220	Phosphoserine
+P38113	226	Phosphothreonine
+P38113	282	Phosphoserine
+P38113	319	Phosphoserine
+P38113	229	Glycyl
+P38113	237	Glycyl
+P38113	290	Glycyl
+Q12013	534	N-linked
+P52892	327	N6-(pyridoxal
+P14540	11	Phosphothreonine
+P14540	56	Phosphoserine
+P14540	63	Phosphoserine
+P14540	76	Phosphoserine
+P14540	83	Phosphoserine
+P14540	96	Phosphoserine
+P14540	147	Phosphoserine
+P14540	150	Phosphothreonine
+P14540	179	Phosphothreonine
+P14540	268	Phosphoserine
+P14540	290	Phosphothreonine
+P14540	310	Phosphotyrosine
+P14540	313	Phosphoserine
+P14540	27	Glycyl
+P14540	73	Glycyl
+P14540	85	Glycyl
+P14540	308	Glycyl
+P50076	31	N-linked
+P50076	278	N-linked
+P50076	372	N-linked
+P32375	157	N6-carboxylysine
+P54783	56	Pros-8alpha-FAD
+P38971	39	Phosphothreonine
+Q08981	48	Phosphoserine
+Q08981	161	Phosphothreonine
+Q08981	202	Phosphoserine
+P32463	82	O-(pantetheine
+P25377	132	Phosphoserine
+P25377	316	Phosphoserine
+P32781	22	O-linked
+P32781	30	O-linked
+P32781	32	O-linked
+P32781	39	O-linked
+P32781	63	O-linked
+P32781	66	O-linked
+P32781	75	O-linked
+P38628	67	Phosphoserine
+P43567	201	N6-(pyridoxal
+Q12476	31	Phosphoserine
+Q12476	49	Phosphoserine
+P19414	391	Phosphoserine
+P19414	409	Phosphothreonine
+P19414	556	Phosphoserine
+Q03233	79	Phosphoserine
+Q12433	282	Phosphoserine
+Q12433	505	Phosphoserine
+P38013	2	N-acetylserine
+P38013	28	Phosphoserine
+P38013	59	Phosphoserine
+P38013	116	Phosphoserine
+P38013	32	Glycyl
+P38013	48	Glycyl
+P38013	113	Glycyl
+Q12156	2	N-acetylserine
+Q12156	137	Phosphoserine
+P40507	37	Phosphoserine
+P39010	51	Phosphoserine
+P39010	57	Phosphoserine
+P38840	90	Phosphoserine
+P38840	92	Phosphoserine
+P80428	349	Phosphoserine
+P40467	166	Phosphoserine%3B
+P40467	186	Phosphoserine
+P40467	963	Phosphoserine
+P34233	56	Phosphoserine
+P34233	465	Phosphoserine
+P49435	68	Phosphoserine
+P18544	276	N6-(pyridoxal
+P53974	478	Phosphoserine
+P53974	522	Phosphoserine
+P53974	535	Phosphoserine
+P38116	2	N-myristoyl
+P40994	2	N-myristoyl
+P53090	100	Phosphoserine
+P32449	2	N-acetylserine
+P53946	7	Phosphoserine
+P53946	24	Phosphothreonine
+P53946	383	Phosphoserine
+P53946	12	Glycyl
+Q12386	65	Phosphoserine
+Q12386	70	Phosphoserine
+P53731	155	Phosphothreonine
+P53731	324	Phosphoserine
+P38986	350	Phosphoserine
+P40024	43	Phosphoserine
+P40024	65	Phosphoserine
+P40024	196	Phosphoserine
+P40024	446	Phosphothreonine
+P11076	2	N-myristoyl
+P11076	127	Glycyl
+P00812	1	N-acetylmethionine
+P00812	16	Phosphoserine
+P00812	77	Phosphothreonine
+P00812	270	Phosphothreonine
+P15274	19	Phosphoserine
+P15274	58	Phosphoserine
+P15274	61	Phosphoserine
+P15274	138	Phosphoserine
+Q08951	2	N-acetylthreonine
+Q08951	700	Phosphoserine
+Q08951	727	Phosphoserine
+Q08951	767	Phosphothreonine
+Q08951	770	Phosphoserine
+Q08951	773	Phosphoserine
+Q08951	798	Phosphoserine
+Q08951	888	Phosphoserine
+Q08951	918	Phosphoserine
+P36973	2	N-acetylserine
+P25628	21	Phosphoserine
+P25628	45	Phosphoserine
+P36090	511	S-palmitoyl
+P36090	516	S-palmitoyl
+P46682	693	Phosphoserine
+P46682	698	Phosphoserine
+P46682	724	Phosphoserine
+P46682	726	Phosphoserine
+P04076	27	Phosphoserine
+P38832	137	GPI-anchor
+P37302	85	N-linked
+P37302	96	N-linked
+P37302	115	N-linked
+P37302	150	N-linked
+P37302	162	N-linked
+P37302	371	N-linked
+P37302	427	N-linked
+P37302	480	N-linked
+P22936	356	Phosphoserine
+Q06408	588	Glycyl
+P38080	2	N-acetylserine
+P38080	10	Phosphoserine
+P38080	407	Phosphoserine
+P38080	471	Phosphothreonine
+P38080	504	Phosphoserine
+P38080	541	Phosphoserine
+P38080	574	Phosphoserine
+P38080	801	Phosphoserine
+P38080	846	Phosphoserine
+P38080	953	Phosphoserine
+P38080	960	Phosphoserine
+P38080	1048	Phosphoserine
+P38080	1072	Phosphoserine
+P38080	1008	Glycyl
+P38080	1046	Glycyl
+P54115	3	Glycyl
+P54115	142	Glycyl
+P54115	196	Glycyl
+P16661	88	N-linked
+P16661	199	N-linked
+P16661	425	N-linked
+P19880	9	Phosphoserine
+P19880	14	Phosphoserine
+P19880	17	Phosphoserine
+P19880	165	Phosphothreonine
+P19880	204	Phosphoserine
+P19880	372	Phosphoserine
+P19880	528	Phosphoserine
+P27351	649	Phosphoserine
+P27351	652	Phosphothreonine
+P27351	683	Phosphoserine
+Q99186	179	Phosphoserine
+Q99186	180	Phosphoserine
+Q99186	181	Phosphoserine
+P38115	151	Phosphothreonine
+P53309	449	Phosphothreonine
+P53309	282	Glycyl
+P13586	2	N-acetylserine
+P13586	227	Phosphoserine
+Q12675	70	Phosphothreonine
+Q12675	85	Phosphoserine
+Q12675	389	Phosphoserine
+Q12675	392	Phosphoserine
+Q12675	396	Phosphoserine
+Q12675	403	Phosphoserine
+Q12675	406	Phosphotyrosine
+Q12675	782	Phosphothreonine
+Q12675	1542	Phosphoserine
+Q12675	1592	Phosphoserine
+Q12675	938	Glycyl
+P40527	102	Phosphoserine
+P40527	551	Phosphoserine
+P38316	186	Glycyl
+Q06628	344	Phosphoserine%3B
+Q06628	348	Phosphoserine%3B
+Q06628	355	Phosphoserine
+Q06628	437	Phosphoserine%3B
+Q06628	438	Phosphoserine%3B
+Q06628	461	Phosphoserine
+Q06628	496	Phosphoserine%3B
+Q06628	535	Phosphoserine%3B
+Q06628	541	Phosphoserine%3B
+Q06628	554	Phosphoserine
+Q06628	581	Phosphoserine%3B
+Q06628	646	Phosphoserine%3B
+Q06628	649	Phosphoserine%3B
+P21306	52	Phosphothreonine
+P00830	112	Phosphothreonine
+P00830	237	Phosphothreonine
+P00830	373	Phosphoserine
+P05626	144	Phosphoserine
+Q07528	2	N-acetylserine
+Q07528	361	Phosphoserine
+Q07528	363	Phosphoserine
+P48016	28	N-linked
+P48016	32	N-linked
+P48016	98	N-linked
+P48016	207	N-linked
+P48016	238	N-linked
+P48016	247	N-linked
+P48016	255	N-linked
+P48016	259	N-linked
+P48016	325	N-linked
+P48016	370	N-linked
+P48016	376	N-linked
+P48016	488	N-linked
+P48016	539	N-linked
+P48016	568	N-linked
+P48016	628	N-linked
+P48016	638	N-linked
+P48016	696	N-linked
+P48016	705	N-linked
+P48016	879	N-linked
+P48016	897	N-linked
+P48016	910	N-linked
+P48016	972	N-linked
+P48016	990	N-linked
+P48016	1031	N-linked
+P48016	1049	N-linked
+P48016	1064	N-linked
+P48016	1147	N-linked
+P48016	1157	N-linked
+Q12233	1	N-acetylmethionine
+Q12233	3	Phosphoserine
+Q12233	62	Phosphoserine
+Q12500	519	Phosphoserine
+Q12500	524	Phosphoserine
+Q05933	29	Glycyl
+P0CX79	29	N-linked
+P0CX79	93	N-linked
+P0CX79	239	N-linked
+P25641	173	N-linked
+P25641	202	N-linked
+P25641	208	N-linked
+P35193	136	Phosphoserine
+P35193	141	Phosphoserine
+P35193	243	Phosphoserine
+P35193	213	Glycyl
+P35193	216	Glycyl
+P53104	34	Phosphoserine
+P53104	129	Phosphothreonine
+P53104	226	Phosphothreonine%3B
+P53104	304	Phosphoserine
+P53104	365	Phosphoserine
+P53104	390	Phosphoserine
+P53104	508	Phosphoserine%3B
+P53104	515	Phosphoserine%3B
+P53104	533	Phosphoserine
+P53104	551	Phosphoserine
+P53104	552	Phosphoserine
+P53104	590	Phosphothreonine
+P53104	621	Phosphoserine
+P53104	635	Phosphoserine
+P53104	638	Phosphoserine
+P53104	647	Phosphoserine
+P53104	677	Phosphoserine
+P53104	680	Phosphoserine
+P53104	683	Phosphoserine
+P53104	769	Phosphoserine
+P53104	783	Phosphoserine
+P53867	488	Phosphoserine
+Q12380	149	Glycyl
+Q12092	106	Phosphoserine
+Q12092	187	Phosphoserine
+Q12092	188	Phosphoserine
+P40458	114	Phosphoserine
+P40458	119	Phosphoserine
+P38182	116	Phosphatidylethanolamine
+P32453	109	Phosphoserine
+P40851	262	Phosphoserine
+Q06541	296	N-linked
+P46993	121	Phosphoserine
+P46993	123	Phosphoserine
+P46993	125	Phosphoserine
+P46993	153	Phosphothreonine
+P54074	2	N-linked
+P54074	19	N-linked
+P54074	29	N-linked
+P48361	344	Phosphoserine
+P48361	793	Phosphoserine
+P48361	808	Phosphothreonine
+P48361	944	Phosphoserine
+P48361	969	Phosphoserine
+P48361	1017	Phosphothreonine
+P48361	1070	Phosphoserine
+P48361	1095	Phosphoserine
+P48361	1098	Phosphoserine
+P32660	53	Phosphoserine
+P32660	70	Phosphothreonine
+P32660	81	Phosphoserine
+P32660	85	Phosphothreonine
+P32660	92	Phosphoserine
+P32660	94	Phosphothreonine
+P32660	104	Phosphoserine
+P32660	109	Phosphothreonine
+P32660	351	Phosphoserine
+P32660	354	Phosphoserine
+P32660	358	Phosphoserine
+P32660	365	Phosphoserine
+P32660	368	Phosphotyrosine
+P32660	1506	Phosphoserine
+P32660	1551	Phosphothreonine
+P32660	1552	Phosphoserine
+P32660	1563	Phosphoserine
+P32660	895	Glycyl
+Q12674	627	Phosphoserine
+P30902	2	N-acetylserine
+P40518	142	Phosphothreonine
+Q06598	201	N-linked
+Q06598	365	N-linked
+P35734	26	Phosphoserine
+P35734	118	Phosphoserine
+P35734	134	Phosphoserine
+P35734	140	Phosphothreonine
+P35734	155	Phosphoserine
+P35734	156	Phosphoserine
+P35734	200	Phosphoserine%3B
+P35734	216	Phosphoserine
+P35734	250	Phosphoserine%3B
+P53855	236	Phosphoserine
+Q05789	2	N-acetylserine
+P36107	392	Phosphoserine
+P36107	395	Phosphoserine
+P36107	132	N-linked
+P36062	59	Phosphoserine
+P36062	119	Phosphoserine
+P36062	121	Phosphoserine
+P36062	165	Phosphoserine
+P53629	175	Phosphoserine
+P53629	176	Phosphoserine
+P19146	2	N-myristoyl
+P19146	127	Glycyl
+P49089	265	Phosphoserine
+P49089	509	Phosphoserine
+P43601	354	Phosphoserine
+Q02887	213	Phosphothreonine
+Q02887	237	Phosphoserine
+P25568	278	Phosphoserine
+Q06485	127	Phosphoserine
+Q06485	129	Phosphoserine
+P40344	19	N6-acetyllysine%3B
+P40344	48	N6-acetyllysine%3B
+P32907	2	N-acetylserine
+P32907	2	Phosphoserine
+P32907	7	Phosphoserine
+P32907	21	Phosphoserine
+P32907	22	Phosphoserine
+P32907	28	Phosphoserine
+P32907	40	Phosphoserine
+P32454	381	N-linked
+P32454	713	N-linked
+P32381	1	N-acetylmethionine
+P53244	364	Glycyl
+P53983	24	N-linked
+P53983	34	N-linked
+P53983	46	N-linked
+P53983	66	N-linked
+P0CZ17	29	N-linked
+P0CZ17	93	N-linked
+P0CZ17	239	N-linked
+P39524	102	Phosphoserine
+P39986	324	Phosphoserine
+P39986	936	Phosphoserine
+Q01217	359	Phosphoserine
+Q02804	1	N-acetylmethionine
+Q02804	50	Glycyl
+P28777	2	N-acetylserine
+P18634	118	Glycyl
+P50275	17	Phosphoserine
+P0CX77	29	N-linked
+P0CX77	93	N-linked
+P0CX77	239	N-linked
+P0CX78	29	N-linked
+P0CX78	93	N-linked
+P0CX78	239	N-linked
+Q06321	76	Phosphoserine
+Q06321	693	Phosphoserine
+Q12142	143	Phosphoserine
+Q12142	144	Phosphoserine
+Q12142	787	Phosphoserine
+Q12359	4	Phosphoserine
+P61829	1	N-formylmethionine
+P35817	270	Phosphoserine
+P35817	429	Phosphoserine
+P35817	615	Phosphoserine
+P35817	659	Phosphoserine
+P39714	63	Phosphoserine
+P07251	57	Phosphoserine
+P07251	178	Phosphoserine
+P13090	394	N-linked
+P13090	471	N-linked
+Q01389	407	Phosphothreonine
+Q01389	411	Phosphoserine
+Q01389	491	Phosphoserine
+Q01389	747	Phosphoserine
+Q01389	816	Phosphoserine
+Q01389	1058	Phosphoserine
+Q01389	1061	Phosphoserine
+Q01389	1134	Phosphoserine%3B
+P39713	63	Phosphoserine
+Q08347	1	N-acetylmethionine
+P81449	2	N-acetylserine
+P41815	14	Phosphoserine
+P41815	79	Phosphoserine
+P47068	103	Phosphoserine
+P47068	158	Phosphoserine
+P47068	166	Phosphoserine
+P47068	565	Phosphoserine
+P47068	621	Phosphoserine
+P47068	631	Phosphoserine
+P47068	634	Phosphoserine
+P47068	636	Phosphothreonine
+P47068	638	Phosphoserine
+P47068	647	Phosphoserine
+P47068	850	Phosphothreonine
+P47068	889	Phosphoserine
+P47068	894	Phosphothreonine
+P47068	895	Phosphothreonine
+P47068	1012	Glycyl
+Q08236	1	N-acetylmethionine
+Q08236	140	Phosphoserine
+Q08236	144	Phosphoserine
+Q08236	400	Phosphoserine
+Q08236	509	Phosphoserine
+Q08236	510	Phosphothreonine
+Q08236	552	Phosphoserine
+P47082	8	Phosphoserine
+P47082	15	Phosphoserine
+P47082	35	Phosphoserine
+P47082	181	Phosphothreonine
+P47082	187	Phosphoserine
+P38084	3	Phosphoserine
+P38084	15	Phosphothreonine
+P38084	16	Phosphoserine
+P38084	19	Phosphoserine
+P38084	21	Phosphoserine
+P38084	24	Phosphoserine
+P38084	76	Phosphoserine
+P38084	84	Phosphoserine
+P39960	129	Phosphoserine
+P39960	283	Phosphoserine
+P39960	1012	Phosphoserine
+P39960	1016	Phosphoserine
+P39960	1038	Phosphothreonine
+P39960	1046	Phosphoserine
+P39960	1054	Phosphoserine
+P39960	1128	Phosphoserine
+P39960	27	Glycyl
+P36149	80	S-palmitoyl
+P47134	477	Phosphoserine
+P47134	508	Phosphoserine
+P47134	552	Phosphoserine
+P47134	587	Phosphoserine
+P47134	751	Phosphoserine
+P47134	765	Phosphoserine
+P47041	58	Phosphotyrosine
+P47041	59	Phosphoserine
+P47041	139	Phosphoserine
+P47041	144	Phosphoserine
+Q08235	285	Phosphoserine
+Q05611	177	Phosphoserine
+Q08280	37	Phosphoserine
+Q08280	41	Phosphoserine
+Q08280	49	N-linked
+P47176	202	N6-(pyridoxal
+P15703	202	N-linked
+P15703	284	N-linked
+P50277	314	N6-(pyridoxal
+Q08965	438	Phosphoserine
+Q08965	478	Phosphoserine
+Q08965	492	Phosphoserine
+Q08965	504	Phosphothreonine
+Q08965	516	Phosphothreonine
+Q08965	518	Phosphoserine
+Q08965	523	Phosphoserine
+Q08965	574	Phosphoserine
+Q08965	578	Phosphoserine
+P47039	271	N6-(pyridoxal
+P40450	621	Phosphoserine
+P40450	751	Phosphoserine
+Q07660	830	N-linked
+P53755	111	Phosphoserine
+P53755	350	Phosphoserine
+Q06604	46	Phosphoserine
+Q06604	79	Phosphoserine
+Q06604	88	Phosphoserine
+Q06604	185	Phosphoserine
+Q06604	220	Phosphoserine
+Q06604	309	Phosphoserine
+Q06604	320	Phosphoserine
+P50944	88	Phosphoserine
+P50944	130	Phosphoserine
+P50944	165	Phosphoserine
+P41696	61	Phosphoserine
+P41696	286	Phosphoserine
+P41696	325	Phosphoserine
+Q12365	29	Phosphoserine
+Q12365	73	Phosphoserine
+Q12365	115	Phosphoserine
+P38928	642	Phosphoserine
+P38928	673	Phosphoserine
+P38928	676	Phosphoserine
+P38928	41	N-linked
+P38928	50	N-linked
+P38928	96	N-linked
+P38928	117	N-linked
+P38928	163	N-linked
+P38928	260	N-linked
+P38928	266	N-linked
+P38928	304	N-linked
+P38928	324	N-linked
+P38928	359	N-linked
+P38928	382	N-linked
+P38928	389	N-linked
+P38928	403	N-linked
+P38928	447	N-linked
+P38928	451	N-linked
+P38928	495	N-linked
+P33306	334	Phosphoserine
+P33306	757	Phosphoserine
+P33306	761	Phosphoserine
+Q07442	264	Phosphoserine
+P53858	43	Phosphoserine
+P53858	133	Phosphoserine
+P53858	281	Phosphoserine
+P53858	364	Phosphoserine
+P53858	394	Phosphoserine
+P53858	410	Phosphothreonine
+P53858	476	Phosphoserine
+P53858	500	Phosphoserine
+P53858	503	Phosphoserine
+P53858	618	Phosphoserine
+P53858	703	Phosphothreonine
+P53858	746	Phosphoserine
+P53858	825	Phosphoserine
+Q06338	205	Phosphothreonine
+Q06338	209	Phosphothreonine
+P47113	317	Phosphoserine
+P40013	2	N-acetylserine
+P40013	157	Phosphoserine
+P29366	1	N-acetylmethionine
+P29366	47	Phosphoserine
+P29366	255	Phosphoserine
+P29366	258	Phosphoserine
+P29366	458	Phosphoserine
+P29366	461	Phosphoserine
+P38813	24	N-linked
+P38813	144	N-linked
+P43583	11	Phosphoserine
+P43583	29	Phosphoserine
+P43583	56	Phosphoserine
+P43583	62	Phosphoserine
+P43583	64	Phosphothreonine
+P43583	66	Phosphothreonine
+P43583	1041	Phosphoserine
+Q04347	257	Phosphothreonine
+Q04347	367	Phosphoserine
+Q04347	371	Phosphothreonine
+Q04347	375	Phosphoserine
+P33314	2	N-acetylserine
+P33314	854	Phosphoserine
+P47136	10	Phosphoserine
+P47136	78	Phosphoserine
+P47136	81	Phosphoserine
+P47136	91	Phosphoserine
+P47136	96	Phosphoserine
+P47136	167	Phosphoserine
+P47136	365	Phosphothreonine
+P47136	367	Phosphoserine
+P47136	511	Phosphoserine
+P47136	616	Phosphoserine
+P47136	805	Phosphoserine
+P47136	811	Phosphoserine
+P41697	12	Phosphothreonine
+P41697	233	Phosphoserine
+P41697	327	Phosphoserine
+P41697	342	Phosphoserine
+P38822	327	Phosphoserine
+P38822	463	Phosphoserine
+P38822	472	Phosphoserine
+P38822	476	Phosphoserine
+Q04749	315	Phosphoserine
+Q04749	350	Phosphoserine
+P40074	344	Phosphoserine
+P12630	84	N-linked
+P12630	90	N-linked
+P12630	268	N-linked
+P12630	308	N-linked
+P12630	366	N-linked
+P12630	398	N-linked
+P12630	468	N-linked
+P12630	503	N-linked
+P12630	551	N-linked
+Q12186	93	Phosphoserine
+Q12186	95	Phosphoserine
+Q12186	100	Phosphotyrosine
+Q12186	382	Phosphoserine
+P38891	219	N6-(pyridoxal
+P38891	315	Phosphothreonine
+P38772	330	Phosphoserine
+P32873	254	Phosphoserine
+Q06631	41	Phosphoserine
+Q06631	44	Phosphoserine
+Q06631	366	Phosphoserine
+Q06631	372	Phosphoserine
+Q06631	379	Phosphoserine
+P11709	95	Phosphoserine
+P11709	110	Phosphoserine
+Q08492	16	Phosphoserine
+Q08492	45	Phosphoserine
+Q08492	65	Phosphoserine
+Q08492	144	Phosphoserine
+Q05949	24	Phosphoserine
+P0C155	54	N-linked
+P0C155	76	N-linked
+P0C155	335	N-linked
+P0C155	428	N-linked
+P0C155	17	Glycyl
+P27614	88	N-linked
+P27614	176	N-linked
+P27614	228	N-linked
+P27614	381	N-linked
+P27614	525	N-linked
+P27614	8	Glycyl
+P00729	124	N-linked
+P00729	198	N-linked
+P00729	279	N-linked
+P00729	479	N-linked
+P34730	2	N-acetylserine
+P38041	104	Phosphoserine
+P38041	106	Phosphoserine
+P38041	128	Phosphoserine
+P38041	151	Phosphothreonine
+P38041	158	Phosphothreonine
+P38041	209	Phosphoserine
+P38041	393	Phosphoserine
+P38041	412	Phosphoserine
+P38041	525	Phosphoserine
+P38041	528	Phosphoserine
+P38041	589	Phosphoserine
+P38041	590	Phosphoserine
+P38041	593	Phosphoserine
+P38041	644	Phosphoserine
+P38041	655	Phosphoserine
+P38041	735	Phosphoserine
+P38041	919	Phosphothreonine
+P53836	491	Phosphoserine
+P53836	510	Phosphoserine
+P53836	518	Phosphoserine
+P53836	538	Phosphoserine
+P53836	556	Phosphoserine
+P53836	871	Phosphoserine
+P53836	885	Phosphoserine
+P39101	132	Glycyl
+P17555	454	Phosphoserine
+P06787	82	Phosphoserine
+P06787	102	Phosphoserine
+P27825	25	N-linked
+P27825	104	N-linked
+P27825	296	N-linked
+P27825	416	N-linked
+P27825	425	N-linked
+P04817	54	Phosphoserine
+P04817	66	Phosphoserine
+P28495	2	N-acetylserine
+P28495	17	Phosphoserine
+P34237	364	Phosphoserine
+P34237	450	Phosphoserine
+P34237	453	Phosphoserine
+P34237	555	Phosphoserine
+P15202	2	N-acetylserine
+Q06071	33	Phosphoserine
+P29311	2	N-acetylserine
+P29311	89	Phosphoserine
+P29311	76	Glycyl
+P48582	740	Phosphoserine
+P32639	403	Phosphoserine
+P25558	766	Phosphoserine
+P25558	1045	Phosphothreonine
+P25558	1063	Phosphoserine
+P25558	1075	Phosphoserine
+P25558	1134	Phosphoserine
+P25558	1149	Phosphoserine
+P25558	1157	Phosphothreonine
+P25558	1160	Phosphoserine
+P25558	1228	Phosphoserine
+P25558	1254	Phosphoserine
+P25558	1257	Phosphoserine
+P25558	1390	Phosphoserine
+P25558	1412	Phosphoserine
+P25558	1429	Phosphothreonine
+P25558	1440	Phosphothreonine
+P25558	1443	Phosphoserine
+P25558	1501	Phosphoserine
+P25558	1549	Phosphoserine
+P25558	1589	Phosphoserine
+P25558	1614	Phosphoserine
+P25558	792	Glycyl
+P25558	963	Glycyl
+Q12191	2	N-acetylserine
+Q12191	87	Phosphoserine
+Q12191	170	Phosphoserine
+Q12191	292	Phosphothreonine
+Q03758	22	Phosphothreonine
+Q03758	557	Phosphoserine
+P12962	78	Phosphoserine
+P12962	91	Phosphoserine
+P12962	99	Phosphothreonine
+P12962	101	Phosphothreonine
+P12962	102	Phosphothreonine
+P12962	154	Phosphoserine
+P53890	70	Phosphoserine
+P53890	179	Phosphoserine
+P53890	194	Phosphoserine
+P53890	257	Phosphothreonine
+P53890	270	Phosphoserine
+P53890	273	Phosphoserine
+P53890	274	Phosphothreonine
+P53890	332	Phosphoserine
+P53890	340	Phosphoserine
+P53890	344	Phosphotyrosine
+P53890	346	Phosphoserine
+P53890	350	Phosphoserine
+P39969	18	Phosphoserine
+P39969	24	Phosphoserine
+P39969	28	Phosphoserine
+P39969	450	Phosphoserine
+P39969	519	Phosphoserine
+P39969	523	Phosphoserine
+P39969	546	Phosphoserine
+P39969	652	Phosphoserine
+P43132	227	Phosphoserine
+P38356	312	Glycyl
+P43573	580	Phosphoserine
+P53323	187	Phosphoserine%3B
+P53323	189	Phosphoserine%3B
+P41698	92	N-linked
+P41698	110	N-linked
+P41698	211	N-linked
+P41698	240	N-linked
+P41698	271	N-linked
+P41698	333	N-linked
+P41698	396	N-linked
+P41698	423	N-linked
+P53226	112	Phosphoserine
+P53226	189	Phosphoserine
+P53226	83	N-linked
+P53226	139	N-linked
+P53226	142	N-linked
+P53226	221	N-linked
+P53226	259	N-linked
+P53226	263	N-linked
+P53226	289	N-linked
+P53226	299	N-linked
+P53226	340	N-linked
+P48524	58	Phosphoserine
+P48524	70	Phosphoserine
+P07245	176	Phosphoserine
+P07245	318	Phosphothreonine
+P07245	322	Phosphoserine
+P36076	42	Phosphoserine
+P36076	116	Phosphoserine
+P36076	121	Phosphoserine
+P36076	124	Phosphoserine
+P36076	264	Phosphoserine
+P13517	2	N-acetylserine
+P13517	85	Phosphoserine
+P13517	92	Phosphoserine
+Q02948	142	Phosphothreonine
+P38934	260	Phosphoserine
+P38934	336	Phosphothreonine
+P38934	369	Phosphoserine
+Q06150	383	Phosphoserine
+P53741	187	Phosphoserine
+P53741	282	Phosphoserine
+P53741	336	Phosphothreonine
+P53741	340	Phosphoserine
+P53741	398	Phosphoserine
+P43571	19	N-linked
+P43571	295	N-linked
+P43571	302	N-linked
+P43571	447	N-linked
+P43571	456	N-linked
+P43571	485	N-linked
+P43571	565	N-linked
+P43571	651	N-linked
+P43571	668	N-linked
+P43571	694	N-linked
+P43571	918	N-linked
+P41832	311	Phosphoserine
+P41832	325	Phosphoserine
+P41832	1085	Phosphoserine
+P41832	1170	Phosphoserine
+P41832	1338	Phosphoserine
+P41832	1344	Phosphoserine
+P41832	1918	Phosphothreonine
+P25385	1	N-acetylmethionine
+P14772	645	Phosphoserine
+P14772	885	Phosphoserine
+P14772	889	Phosphothreonine
+P14772	893	Phosphoserine
+P14772	895	Phosphoserine
+P14772	916	Phosphothreonine
+P14772	927	Phosphoserine
+P14772	931	Phosphoserine
+P14772	934	Phosphothreonine
+P14772	1011	N-linked
+P23293	240	Phosphothreonine%3B
+P23293	400	Phosphoserine
+P23293	405	Phosphothreonine
+P23293	417	Phosphoserine
+P23293	634	Phosphoserine
+P36106	177	Phosphoserine
+P32797	306	Phosphoserine
+P32797	308	Phosphothreonine
+P32797	333	Phosphoserine
+P25656	199	N-linked
+P25656	216	N-linked
+P25656	237	N-linked
+P25656	288	N-linked
+P25656	329	N-linked
+P09119	368	Phosphothreonine
+P53197	213	Phosphoserine
+Q12453	754	Phosphoserine
+P07267	144	N-linked
+P07267	345	N-linked
+P32582	53	N6-(pyridoxal
+P32582	134	Phosphoserine
+P32582	350	Phosphoserine
+P32582	424	Phosphoserine
+Q06703	142	N-linked
+Q06703	181	N-linked
+Q06703	199	N-linked
+Q06703	246	N-linked
+Q06703	263	N-linked
+P27636	561	Phosphoserine
+P27636	567	Phosphoserine
+P27636	870	Phosphothreonine
+P04821	151	Phosphoserine
+P04821	154	Phosphoserine
+P04821	423	Phosphoserine
+P04821	580	Phosphoserine
+P04821	596	Phosphoserine
+P04821	632	Phosphoserine
+P04821	635	Phosphothreonine
+P04821	649	Phosphoserine
+P25694	472	Phosphoserine
+P25694	519	Phosphoserine
+P25694	735	Phosphothreonine
+P25694	770	Phosphoserine
+P25694	305	Glycyl
+P25694	322	Glycyl
+P25694	346	Glycyl
+P25694	522	Glycyl
+P25694	539	Glycyl
+P25694	594	Glycyl
+P25694	673	Glycyl
+P40969	575	Phosphoserine
+P53894	109	Phosphothreonine
+P24869	2	N-acetylserine
+P80235	517	Phosphoserine
+P25296	2	N-myristoyl
+P07253	2	N-acetylserine
+P07253	97	Phosphothreonine
+P31384	33	Phosphothreonine
+P31384	278	Phosphoserine
+P31384	285	Phosphothreonine
+Q12127	112	GPI-anchor
+Q12127	21	N-linked
+Q12127	23	O-linked
+Q12127	24	O-linked
+Q12127	26	O-linked
+Q12127	28	O-linked
+Q12127	31	O-linked
+Q12127	32	O-linked
+Q12127	33	O-linked
+Q12127	36	O-linked
+Q12127	38	O-linked
+Q12127	39	O-linked
+Q12127	46	O-linked
+Q12127	48	O-linked
+Q12127	81	N-linked
+Q12127	97	N-linked
+Q12127	80	Glycyl
+P32457	2	N-acetylserine
+P32457	2	Phosphoserine
+P32457	9	Phosphoserine
+P32457	47	Phosphothreonine
+P32457	60	Phosphoserine
+P32457	77	Phosphoserine
+P32457	175	Phosphoserine
+P32457	468	Phosphothreonine
+P32457	509	Phosphoserine
+P32457	4	Glycyl
+P32457	11	Glycyl
+P32457	30	Glycyl
+P32457	63	Glycyl
+P32457	287	Glycyl
+Q06697	114	Phosphoserine
+Q06697	150	Phosphoserine
+P17106	1	N-acetylmethionine
+P17106	45	Phosphoserine%3B
+P17106	48	Phosphoserine
+P17106	84	Phosphoserine
+P17106	138	Phosphothreonine
+Q06702	26	N-linked
+Q06702	50	N-linked
+Q06702	68	N-linked
+Q06702	189	N-linked
+P25342	1	N-acetylmethionine
+P25342	216	Phosphothreonine
+P32468	2	N-acetylserine
+P16522	59	Phosphoserine%3B
+P06704	130	Phosphothreonine
+P25356	1667	Glycyl
+P27637	2	N-acetylserine
+P27637	159	Phosphotyrosine
+P27637	160	Phosphoserine
+P27637	162	Phosphoserine
+P27637	177	Phosphothreonine
+P27637	212	Phosphoserine
+P27637	222	Phosphoserine
+P27637	376	Phosphoserine
+P27637	378	Phosphoserine
+P27637	401	Phosphoserine
+P27637	507	Phosphoserine
+P27637	655	Phosphoserine
+P27637	658	Phosphoserine
+P27637	670	Phosphoserine
+P32504	566	Phosphoserine
+P32504	706	Phosphotyrosine
+P33322	47	Phosphoserine
+P33322	378	Phosphothreonine
+P33322	9	Glycyl
+P33322	267	Glycyl
+P50077	284	Phosphoserine
+P00431	220	Phosphotyrosine
+Q7LHD1	115	GPI-anchor
+Q7LHD1	21	N-linked
+Q7LHD1	82	N-linked
+P19073	188	Cysteine
+P19073	188	S-geranylgeranyl
+P32458	2	N-acetylserine
+P32458	2	Phosphoserine
+P32458	305	Phosphoserine
+P32458	327	Phosphothreonine
+P32458	412	Glycyl
+P14724	12	Phosphoserine
+P06101	14	Phosphoserine
+P06101	17	Phosphoserine
+P06101	367	Phosphoserine
+P06101	466	Phosphoserine
+P06101	484	Phosphoserine
+Q12018	760	Glycyl
+P38910	2	N-acetylserine
+P38910	31	Phosphoserine
+P47818	29	Phosphoserine
+P47818	53	Phosphoserine
+P47818	68	Phosphoserine
+P47818	71	Phosphoserine
+P47818	83	Phosphoserine
+O13547	217	GPI-anchor
+O13547	87	N-linked
+O13547	161	Glycyl
+Q00684	467	Phosphoserine
+O13297	2	N-acetylserine
+O13297	15	Phosphoserine
+O13297	124	Phosphoserine
+P29029	553	N-linked
+Q12114	305	Phosphothreonine
+Q12114	338	Phosphoserine
+Q12114	362	Phosphoserine
+Q12114	365	Phosphoserine
+Q12114	383	Phosphoserine
+Q12114	384	Phosphoserine
+Q12114	573	Phosphoserine
+Q12114	579	Phosphoserine
+Q12114	590	Phosphoserine
+Q12114	584	Glycyl
+P43634	164	Phosphoserine
+P43634	166	Phosphoserine
+P22516	86	Phosphoserine
+P22516	172	Phosphoserine
+Q08032	453	Phosphothreonine
+P07834	104	Phosphoserine
+P32562	23	Phosphothreonine
+P32562	419	Phosphoserine
+P40558	291	Phosphoserine
+P53280	1042	Phosphoserine
+P08004	34	Phosphoserine
+P08004	35	Phosphoserine
+P08004	270	Phosphoserine
+P08004	299	Phosphoserine
+P08004	318	Phosphoserine
+P08004	328	Phosphothreonine
+P08004	358	Phosphoserine
+P14180	40	Phosphoserine
+P14180	82	Phosphoserine
+P14180	86	Phosphoserine
+P14180	100	Phosphoserine
+P14180	133	Phosphoserine
+P14180	217	Phosphoserine
+P14180	22	N-linked
+P14180	197	N-linked
+P14180	447	N-linked
+P32657	36	Phosphoserine
+P32657	72	Phosphoserine
+P32657	987	Phosphoserine
+P32657	989	Phosphoserine
+P32657	1336	Phosphoserine
+P32657	1364	Phosphoserine
+P32657	1372	Phosphoserine
+P32657	1144	Glycyl
+Q06350	147	N-linked
+Q06350	228	N-linked
+Q06350	456	N-linked
+Q06350	472	N-linked
+P05374	2	N-acetylserine
+P29465	537	Phosphoserine
+P29465	538	Phosphothreonine
+P29465	82	N-linked
+P29465	114	N-linked
+P29465	152	N-linked
+P29465	163	N-linked
+P29465	303	N-linked
+P29465	332	N-linked
+P29465	371	N-linked
+P29465	136	Glycyl
+P40019	2	N-acetylserine
+P40019	68	Phosphoserine
+P40019	70	Phosphoserine
+Q07897	59	Phosphoserine
+P27895	972	Phosphoserine
+P48562	29	Phosphoserine
+P48562	46	Phosphoserine
+P48562	351	Phosphoserine
+P48562	367	Phosphoserine
+P48562	425	Phosphoserine
+P22137	1107	Glycyl
+Q06156	464	Phosphoserine
+Q06156	475	Phosphoserine
+P53079	1	N-acetylmethionine
+P53079	305	Phosphoserine
+Q12510	64	Phosphoserine
+Q12510	69	Phosphothreonine
+Q12510	224	Phosphoserine
+Q06680	198	Phosphoserine
+Q06680	933	Phosphoserine
+Q06680	981	Phosphoserine
+Q06680	1008	Phosphoserine
+P47001	68	O-linked
+P47001	78	O-linked
+P47001	105	O-linked
+P47001	106	O-linked
+P47001	107	O-linked
+P47001	109	O-linked
+P47001	111	O-linked
+P47001	112	O-linked
+P47001	113	O-linked
+P47001	114	N-linked
+P47001	116	O-linked
+P47001	117	O-linked
+P47001	118	O-linked
+Q03690	1247	Phosphoserine
+P53865	17	Phosphoserine
+P53865	20	Phosphoserine
+P53865	72	Phosphoserine
+P53865	85	Phosphoserine
+P53865	89	Phosphoserine
+P53865	151	Phosphoserine
+P41810	181	Phosphoserine
+P41810	540	Phosphoserine
+Q01519	82	Phosphoserine
+Q03048	4	Phosphoserine
+P00401	245	1'-histidyl-3'-tyrosine
+P38287	354	Phosphoserine
+P43639	2	N-acetylserine
+P43639	2	Phosphoserine
+P46946	143	Phosphoserine
+P46946	267	Phosphoserine%3B
+P32074	638	Phosphothreonine
+P32074	643	Phosphoserine
+P32074	653	Phosphoserine
+P32074	647	Glycyl
+P32798	225	Phosphoserine
+P32798	301	Glycyl
+P04037	55	Phosphothreonine
+P10614	458	Phosphoserine
+P10614	116	Glycyl
+P10614	353	Glycyl
+P10614	454	Glycyl
+P08679	21	Phosphoserine
+P08679	218	Glycyl
+P08679	239	Glycyl
+P08679	354	Glycyl
+P08679	385	Glycyl
+P17891	49	Phosphothreonine
+P17891	52	Phosphoserine
+P41811	326	Phosphoserine
+P38170	245	Phosphoserine
+P38170	548	Phosphoserine
+P43621	277	Phosphothreonine
+Q06705	2	N-acetylserine
+Q06705	2	Phosphoserine
+Q03957	14	Phosphoserine%3B
+Q03957	338	Phosphothreonine
+P40094	507	Phosphoserine
+P40094	647	Phosphoserine
+Q06440	441	Phosphoserine
+Q06440	454	Phosphoserine
+Q06440	456	Phosphoserine
+Q06440	517	Phosphothreonine
+Q06440	529	Phosphothreonine
+Q06440	573	Phosphoserine
+Q06440	579	Phosphoserine
+Q12150	82	N-linked
+Q12150	117	N-linked
+Q12150	144	N-linked
+Q12150	271	N-linked
+Q12150	478	N-linked
+Q12150	530	N-linked
+Q12150	816	N-linked
+Q12150	821	N-linked
+Q12150	839	N-linked
+Q12150	892	N-linked
+Q12150	1309	N-linked
+Q12150	1368	N-linked
+Q12150	1453	N-linked
+Q12150	1785	N-linked
+Q12150	1921	N-linked
+Q12150	2130	N-linked
+Q12150	2146	N-linked
+Q12150	2280	N-linked
+Q12150	2337	N-linked
+Q12150	2520	N-linked
+Q12150	2578	N-linked
+Q12150	2719	N-linked
+Q12150	2869	N-linked
+Q12748	2	N-acetylserine
+Q08923	174	Phosphothreonine
+Q08923	175	Phosphoserine
+Q08923	177	Phosphothreonine
+Q08923	216	Phosphoserine
+Q08923	267	Phosphoserine
+Q12734	23	Phosphoserine
+Q12734	46	Phosphoserine
+Q12734	127	Phosphoserine
+Q12734	327	Phosphoserine
+Q12734	987	Phosphoserine
+Q12734	841	Glycyl
+P25618	419	N-linked
+P25618	490	N-linked
+P25618	767	N-linked
+P25618	792	N-linked
+P25618	825	N-linked
+Q04632	410	Phosphoserine
+P38845	153	Phosphoserine
+P38845	156	Phosphoserine
+P38845	182	Phosphothreonine
+P38845	271	Phosphoserine
+P38845	295	Phosphothreonine
+P38845	319	Phosphoserine
+P38845	343	Phosphoserine
+P38845	366	Phosphothreonine
+P38845	394	Phosphoserine
+P38845	440	Phosphoserine
+P43497	71	GPI-anchor
+P53968	170	Phosphothreonine
+P53968	175	Phosphoserine
+P53968	245	Phosphoserine
+P53968	385	Phosphoserine
+P14306	1	N-acetylmethionine
+P53301	482	GPI-anchor
+P53301	117	N-linked
+P53301	177	N-linked
+P53301	201	N-linked
+Q06538	171	N-linked
+P35206	35	N-linked
+P35206	49	N-linked
+P25355	433	Phosphothreonine
+P25355	559	Phosphoserine
+P53923	489	Phosphoserine
+P53830	163	Phosphoserine
+P00044	78	N6%2CN6%2CN6-trimethyllysine%3B
+P00044	79	N6%2CN6%2CN6-trimethyllysine
+P32898	920	Phosphoserine
+P32623	445	GPI-anchor
+P32623	28	N-linked
+P32623	96	N-linked
+P32623	190	N-linked
+P32623	196	N-linked
+P32623	233	N-linked
+P32623	237	N-linked
+P32623	261	N-linked
+P32623	297	N-linked
+P32623	310	N-linked
+P49573	344	Phosphoserine
+P49573	349	Phosphoserine
+P49573	356	Phosphothreonine
+P49573	369	Phosphoserine
+P49573	113	N-linked
+P49573	148	N-linked
+P49573	345	Glycyl
+P89105	1015	Phosphoserine
+P89105	1017	Phosphoserine
+Q04201	48	Phosphoserine
+Q04201	37	Glycyl
+Q08412	21	Phosphoserine
+Q08412	36	Phosphoserine
+Q08412	70	Phosphothreonine
+Q08412	91	Phosphoserine
+Q08412	167	Phosphothreonine
+Q08412	220	Phosphoserine
+Q08412	309	Phosphoserine
+Q08412	318	Phosphoserine
+Q08412	346	Phosphothreonine
+Q08412	348	Phosphoserine
+Q08412	352	Phosphothreonine
+Q08412	364	Phosphothreonine
+Q08412	367	Phosphothreonine
+Q08412	407	Phosphoserine
+Q08412	15	Glycyl
+Q08412	59	Glycyl
+Q08412	76	Glycyl
+Q08412	156	Glycyl
+Q08412	354	Glycyl
+Q08412	396	Glycyl
+P47050	791	Glycyl
+P53854	129	Phosphoserine
+Q12046	335	Phosphoserine
+Q12046	336	Phosphoserine
+P53008	42	N-linked
+P53008	122	N-linked
+P53008	135	N-linked
+P53008	787	N-linked
+P28319	217	GPI-anchor
+Q08226	704	Phosphoserine
+P53859	94	Phosphoserine
+P21657	833	Phosphoserine
+P47179	1137	GPI-anchor
+P22204	17	Phosphoserine
+P22204	20	Phosphoserine
+P22204	74	Phosphoserine
+P22204	374	Phosphoserine%3B
+P22204	544	Phosphothreonine%3B
+P24309	269	Phosphoserine
+P36091	428	GPI-anchor
+P36091	34	N-linked
+P36091	84	N-linked
+P36091	109	N-linked
+P36091	133	N-linked
+P36091	203	N-linked
+P36091	225	N-linked
+P36091	240	N-linked
+P36091	265	N-linked
+P36091	281	N-linked
+P36091	337	N-linked
+P36091	362	N-linked
+P36091	420	N-linked
+P53899	273	Phosphoserine
+P08678	2	N-acetylserine
+P08678	376	Phosphothreonine
+P08678	389	Phosphothreonine
+P08678	433	Phosphoserine
+P08678	487	Phosphoserine
+P08678	497	Phosphoserine
+P08678	562	Phosphoserine
+P53206	86	N6-(pyridoxal
+P47178	275	GPI-anchor
+P18962	63	N-linked
+P18962	79	N-linked
+P18962	110	N-linked
+P18962	139	N-linked
+P18962	372	N-linked
+P18962	392	N-linked
+P18962	421	N-linked
+P18962	738	N-linked
+Q12123	341	Phosphoserine
+P46963	35	Phosphothreonine
+P53137	377	Phosphoserine
+Q12389	101	Phosphoserine
+Q12389	398	Phosphoserine
+Q12389	400	Phosphoserine
+P24783	88	Phosphoserine
+P24783	90	Phosphoserine
+P24783	474	Glycyl
+P20449	86	Phosphoserine
+P20449	93	Phosphoserine
+P20449	162	Phosphoserine
+P53734	73	Phosphoserine
+P53734	77	Phosphoserine
+P53734	78	Phosphoserine
+P21182	88	Pyruvic
+P08432	116	N6-(pyridoxal
+P06634	2	N-acetylalanine
+P06634	62	Dimethylated
+P06634	215	Phosphoserine
+P06634	218	Phosphoserine
+P06634	263	Phosphoserine
+P06634	535	Phosphoserine
+P06634	539	Phosphoserine
+P06634	543	Phosphoserine
+P06634	572	Phosphoserine
+P06634	576	Phosphoserine
+P06634	598	Phosphoserine
+P06634	158	Glycyl
+P38307	1	N-acetylmethionine
+Q01454	377	Phosphoserine
+Q01454	379	Phosphoserine
+Q01454	398	Phosphoserine
+Q01454	401	Phosphothreonine
+Q01454	411	Phosphothreonine
+Q01454	463	Phosphoserine
+P53769	33	Phosphoserine
+P53769	105	Phosphoserine
+P35176	139	N-linked
+P14832	2	N-acetylserine
+P14832	71	Phosphothreonine
+P14832	142	Phosphoserine
+P14832	145	Phosphoserine
+P14832	29	Glycyl
+P14832	42	Glycyl
+P14832	123	Glycyl
+P14832	139	Glycyl
+P14832	151	Glycyl
+P14832	158	Glycyl
+P31373	204	N6-(pyridoxal
+P31373	362	Phosphoserine
+Q12248	91	Phosphoserine
+P25334	166	N-linked
+P06106	44	Phosphoserine
+P06106	209	N6-(pyridoxal
+P06106	160	Glycyl
+Q99288	248	Phosphoserine
+Q05080	337	Phosphoserine
+Q05080	366	Phosphoserine
+Q05080	421	Phosphoserine
+P20448	692	Phosphoserine
+P20448	710	Phosphoserine
+P20448	714	Phosphoserine
+P20448	743	Phosphoserine
+P40087	171	Glycyl
+P40087	257	Glycyl
+P69851	1	N-acetylmethionine
+P32328	17	Phosphoserine
+P32328	366	Phosphoserine
+P32328	536	Phosphothreonine
+P53550	116	Phosphoserine
+P53550	439	Phosphoserine
+P53550	677	Phosphothreonine
+P53550	679	Phosphoserine
+P53550	682	Phosphoserine
+P53550	751	Phosphoserine
+P53550	771	Phosphoserine
+P53550	773	Phosphoserine
+P53550	778	Phosphoserine
+P18899	183	Phosphoserine
+P18899	191	Phosphoserine
+P18899	314	Phosphoserine
+P18899	322	Phosphoserine
+P31385	56	Phosphoserine
+P31385	120	Phosphoserine
+P31385	370	Phosphoserine
+P14922	429	Phosphoserine
+P14922	475	Phosphothreonine
+P14922	710	Phosphoserine
+P14922	741	Phosphoserine
+P14922	768	Phosphoserine
+P14922	815	Phosphoserine
+P14922	817	Phosphoserine
+P14922	866	Phosphoserine
+P14922	943	Phosphoserine
+Q07533	209	Phosphoserine
+Q07533	292	Phosphoserine
+Q07533	313	Phosphoserine
+Q07533	354	Phosphoserine
+Q07533	391	Phosphothreonine
+P36162	1	N-acetylmethionine
+P53267	2	N-acetylserine
+P53267	20	Phosphoserine%3B
+P53267	31	Phosphoserine
+P53267	257	Phosphoserine%3B
+P53267	265	Phosphoserine%3B
+P53267	292	Phosphoserine%3B
+P53202	688	Glycyl
+Q02554	104	Phosphothreonine
+Q02554	112	Phosphothreonine
+Q02554	114	Phosphoserine
+P54838	2	N-acetylserine
+P54838	2	Phosphoserine
+P54838	5	Phosphoserine
+P54838	365	Phosphoserine
+P54838	512	Phosphoserine
+Q12382	44	Phosphoserine
+Q12382	45	Phosphoserine
+Q12382	46	Phosphoserine
+Q12382	11	N-linked
+Q12382	197	N-linked
+Q12382	270	N-linked
+P54861	629	Phosphoserine
+P40059	245	Phosphoserine
+P40059	247	Phosphoserine
+P40059	487	Phosphoserine
+P40059	489	Phosphothreonine
+P40059	491	Phosphoserine
+P32469	172	Phosphoserine
+P32469	298	Phosphoserine
+P32892	208	Phosphoserine
+P23501	62	N-linked
+P07262	2	N-acetylserine
+P07262	325	Glycyl
+P07262	371	Glycyl
+P07262	433	Glycyl
+Q08496	393	Phosphoserine
+P04819	58	Phosphoserine
+P04819	75	Phosphoserine
+P04819	119	Phosphoserine
+P04819	123	Phosphoserine
+Q03921	244	Phosphoserine
+P46957	1	N-acetylmethionine
+P46957	20	Phosphoserine
+P36152	206	Phosphoserine
+Q04792	318	N6-(pyridoxal
+P35732	260	Phosphoserine
+P35732	273	Phosphoserine
+P35732	307	Phosphoserine
+P35732	338	Phosphothreonine
+P35732	646	Phosphoserine
+P32330	716	Phosphoserine
+P39708	326	Glycyl
+P39708	372	Glycyl
+P39708	436	Glycyl
+Q04603	183	Phosphoserine%3B
+Q04217	181	Phosphoserine
+P40318	1	N-acetylmethionine
+P47110	223	Phosphothreonine
+P47110	230	Phosphoserine
+P53255	242	Phosphoserine
+P32325	59	Phosphoserine
+P32325	84	Phosphoserine
+P32325	235	Phosphoserine
+P32325	623	Phosphoserine
+Q03373	34	Phosphoserine
+Q03373	225	Phosphoserine
+Q03373	266	Phosphoserine
+Q03373	270	Phosphoserine
+P40366	17	Phosphoserine
+Q06819	2	N-acetylalanine
+P39976	17	Glycyl
+P31116	290	Glycyl
+P36037	332	Phosphoserine
+Q12395	12	Phosphoserine
+Q06151	2	N-acetylserine
+Q06151	60	Phosphoserine
+Q06151	66	Phosphothreonine
+Q06151	66	Phosphothreonine%3B
+Q06151	70	Phosphotyrosine
+Q06151	120	Phosphothreonine
+P89113	24	N-linked
+P89113	27	N-linked
+P69771	5	Phosphoserine
+P38823	150	Glycyl
+P38823	204	Glycyl
+P38823	217	Glycyl
+P38823	237	Glycyl
+P38823	240	Glycyl
+P38823	260	Glycyl
+P38823	300	Glycyl
+P38823	306	Glycyl
+P38823	313	Glycyl
+P38823	317	Glycyl
+Q08949	436	Phosphoserine
+Q05031	437	GPI-anchor
+Q05031	89	N-linked
+Q05031	114	N-linked
+Q05031	138	N-linked
+Q05031	208	N-linked
+Q05031	231	N-linked
+Q05031	245	N-linked
+Q05031	270	N-linked
+Q05031	273	N-linked
+Q05031	417	N-linked
+Q08650	17	Phosphoserine
+P13663	13	Phosphothreonine
+P13663	318	Phosphoserine
+P13663	323	Phosphoserine
+Q03063	45	Phosphoserine
+Q03063	126	Phosphoserine
+Q03063	142	Phosphoserine
+Q03063	272	Phosphoserine
+Q03063	275	Phosphoserine
+Q03063	330	Phosphoserine
+Q03063	379	Phosphothreonine
+Q03063	395	Phosphoserine
+Q03063	428	Phosphoserine
+P53388	22	Phosphoserine
+P53388	76	Glycyl
+P53924	206	Phosphoserine
+P53924	211	Glycyl
+P53924	256	Glycyl
+P53924	258	Glycyl
+P53924	288	Glycyl
+P53924	310	Glycyl
+P53924	333	Glycyl
+P53924	343	Glycyl
+P53924	346	Glycyl
+P53924	366	Glycyl
+P53924	406	Glycyl
+P53924	412	Glycyl
+P53924	423	Glycyl
+P38859	4	Phosphothreonine
+P38859	17	Phosphoserine%3B
+P38859	237	Phosphoserine%3B
+P38859	962	Phosphothreonine
+P02994	2	N%2CN%2CN-trimethylglycine%3B
+P02994	3	N6%2CN6-dimethyllysine%3B
+P02994	3	N6-methyllysine%3B
+P02994	18	Phosphoserine
+P02994	30	N6-methyllysine%3B
+P02994	72	Phosphothreonine
+P02994	79	N6%2CN6%2CN6-trimethyllysine%3B
+P02994	82	Phosphothreonine
+P02994	163	Phosphoserine
+P02994	259	Phosphothreonine
+P02994	289	Phosphoserine
+P02994	316	N6%2CN6-dimethyllysine%3B
+P02994	316	N6-methyllysine%3B
+P02994	390	N6-methyllysine%3B
+P02994	414	Phosphoserine
+P02994	430	Phosphothreonine
+P02994	458	Lysine
+P02994	224	Glycyl
+P02994	242	Glycyl
+P02994	253	Glycyl
+P02994	271	Glycyl
+P02994	393	Glycyl
+P02994	437	Glycyl
+Q03653	227	Phosphoserine
+Q03653	231	Phosphothreonine
+Q03653	564	Phosphoserine
+Q03653	625	Phosphoserine
+Q03653	632	Phosphoserine
+Q03653	643	Phosphoserine
+Q03653	675	Phosphoserine
+Q03653	687	Phosphothreonine
+Q03653	690	Phosphothreonine
+Q03653	735	Phosphoserine
+Q03653	771	Phosphoserine
+Q03653	774	Phosphoserine
+P09032	296	Phosphoserine
+P09032	300	Phosphoserine
+P09032	306	Phosphothreonine
+P38121	126	Phosphoserine
+P13382	2	N-acetylserine
+P13382	31	Phosphoserine
+P13382	82	Phosphoserine
+P13382	83	Phosphoserine
+P13382	84	Phosphoserine
+P13382	169	Phosphoserine
+P13382	170	Phosphoserine
+P13382	172	Phosphothreonine
+P13382	240	Phosphoserine
+P13382	274	Phosphoserine
+P13382	309	Phosphothreonine
+P13382	313	Phosphothreonine
+Q05521	285	Phosphoserine
+Q08729	395	Phosphoserine
+P48510	13	Glycyl
+P48510	76	Glycyl
+P40568	250	Phosphoserine
+P36049	104	Phosphoserine
+P36049	177	Phosphoserine
+P36049	183	Phosphoserine
+Q99252	291	Phosphoserine
+Q99252	338	Phosphoserine
+P53168	2	N-acetylserine
+P36041	30	Phosphoserine
+P36041	281	Phosphoserine
+P36041	282	Phosphoserine
+P36041	327	Phosphoserine
+P36041	344	Phosphoserine
+P36041	387	Phosphoserine
+P42835	1020	GPI-anchor
+P42835	65	N-linked
+P42835	103	N-linked
+P42835	161	N-linked
+P42835	175	N-linked
+P42835	249	N-linked
+P42835	332	N-linked
+P42835	401	N-linked
+P42835	435	N-linked
+P42835	465	N-linked
+P42835	485	N-linked
+P42835	506	N-linked
+P42835	526	N-linked
+P42835	544	N-linked
+P42835	556	N-linked
+P42835	635	N-linked
+P42835	636	N-linked
+P42835	657	N-linked
+P42835	709	N-linked
+P42835	756	N-linked
+P47120	2	N-acetylserine
+P47120	126	Phosphoserine
+P47120	187	Phosphothreonine
+P47120	281	Phosphoserine
+P27344	186	Phosphoserine
+P27344	188	Phosphoserine
+P27344	189	Phosphoserine
+P40487	44	Phosphoserine
+P47013	16	Phosphothreonine
+P47013	18	Phosphoserine
+P38844	308	GPI-anchor
+P43616	451	Phosphoserine
+P32528	803	Phosphoserine
+P32528	1798	N6-biotinyllysine
+P53759	2	N-acetylthreonine
+P53063	198	Phosphoserine
+Q06337	841	Phosphoserine
+Q06337	971	Phosphothreonine
+P53911	200	Phosphoserine
+P53911	225	Phosphoserine
+Q03212	519	Phosphoserine
+Q03212	538	Phosphoserine
+Q03212	110	N-linked
+Q03212	203	N-linked
+Q03212	210	N-linked
+Q03212	256	N-linked
+Q03212	295	N-linked
+P38167	18	Phosphoserine
+P38167	115	Phosphoserine
+P38167	140	Phosphoserine
+P38167	286	Phosphoserine
+P38167	527	Phosphoserine
+P38167	550	Phosphoserine
+P38167	775	Phosphoserine
+P38167	1035	Phosphoserine
+P38167	191	Glycyl
+P38167	577	Glycyl
+P38167	651	Glycyl
+P38167	712	Glycyl
+P38167	794	Glycyl
+P38167	807	Glycyl
+P38167	1024	Glycyl
+P38737	2	N-acetylserine
+P38737	1692	Phosphoserine
+P53235	564	Phosphoserine
+P53235	567	Phosphoserine
+P53235	572	Phosphoserine
+P32497	98	Phosphoserine
+P32497	99	Phosphoserine
+P32497	103	Phosphoserine
+Q12050	6	Phosphoserine
+P25574	73	N-linked
+P25574	106	N-linked
+P25574	192	N-linked
+P25574	202	N-linked
+P25574	420	N-linked
+P25574	443	N-linked
+P25574	574	N-linked
+P25574	578	N-linked
+P40077	553	Glycyl
+Q12432	201	Phosphoserine
+P32471	2	N-acetylalanine
+P32471	31	Phosphoserine
+P32471	86	Phosphoserine
+P32471	13	Glycyl
+P29547	2	N-acetylserine
+P29547	32	Phosphothreonine
+P32324	509	N6%2CN6%2CN6-trimethyllysine%3B
+P32324	509	N6%2CN6-dimethyllysine%3B
+P32324	509	N6-methyllysine%3B
+P32324	579	Phosphoserine
+P32324	613	N6%2CN6-dimethyllysine%3B
+P32324	613	N6-methyllysine%3B
+P32324	699	Diphthamide
+P32324	713	Phosphothreonine
+P32324	763	Phosphothreonine
+P32324	841	Glycyl
+P47163	177	Phosphothreonine
+P24482	122	Phosphoserine
+P24482	141	Phosphoserine%3B
+P24482	613	Phosphoserine
+P39985	789	Phosphoserine
+Q06673	635	Phosphoserine
+Q06673	1065	Phosphoserine
+P38728	45	N-linked
+Q05902	119	N-linked
+Q05902	191	N-linked
+Q05902	270	N-linked
+Q05902	298	N-linked
+Q05902	454	N-linked
+Q05902	517	N-linked
+P47138	2	N-acetylserine
+P14020	2	N-acetylserine
+P14020	141	Phosphoserine%3B
+P15436	30	Phosphoserine
+P15436	37	Phosphoserine
+P39009	10	Phosphoserine
+P39009	139	Phosphoserine
+P39009	380	Phosphothreonine
+Q04067	2	N-acetylserine
+Q04067	131	Phosphoserine
+Q03764	23	Phosphoserine
+Q02884	222	Phosphoserine
+Q04409	2	N-acetylserine
+Q04409	2	Phosphoserine
+Q04409	470	Phosphoserine
+P38333	172	Phosphoserine%3B
+P38333	190	Phosphoserine
+P38333	404	Phosphoserine
+P54781	164	Glycyl
+P54781	198	Glycyl
+P53080	2	N-acetylserine
+P53080	82	Phosphoserine
+P39998	257	Phosphoserine
+P39998	261	Phosphoserine
+P14741	2	N-acetylserine
+P14741	291	Phosphothreonine
+P32501	478	Phosphoserine
+P32501	481	Phosphoserine
+P32501	507	Phosphoserine
+P32501	525	Phosphoserine
+P32501	538	Phosphoserine
+P32501	707	Phosphoserine
+Q05775	75	Phosphothreonine
+Q05775	92	Phosphoserine
+P36053	55	Phosphoserine
+P36053	117	Phosphoserine
+P36053	124	Phosphoserine
+P36053	142	Phosphoserine
+P25358	334	Phosphothreonine
+P25358	336	Phosphoserine
+P25358	338	Phosphoserine
+P25358	32	N-linked
+P39013	276	Phosphoserine
+Q05785	165	Phosphothreonine
+Q05785	167	Phosphoserine
+Q05785	430	Phosphothreonine
+Q05785	434	Phosphoserine
+Q05785	450	Phosphothreonine
+Q05785	468	Phosphothreonine
+Q05785	470	Phosphothreonine
+Q05785	426	Glycyl
+Q12003	13	S-palmitoyl
+Q12003	14	S-palmitoyl
+Q12003	15	S-palmitoyl
+O13529	2	N-linked
+O13529	132	N-linked
+O13529	137	N-linked
+P39715	188	Phosphoserine
+P34216	238	Phosphothreonine
+P34216	241	Phosphoserine
+P34216	244	Phosphoserine
+P34216	245	Phosphothreonine
+P34216	248	Phosphoserine
+P34216	249	Phosphoserine
+P34216	251	Phosphothreonine
+P34216	265	Phosphoserine
+P34216	419	Phosphoserine
+P34216	450	Phosphothreonine
+P34216	477	Phosphothreonine
+P34216	487	Phosphothreonine
+P34216	495	Phosphoserine
+P34216	848	Phosphoserine
+P34216	931	Phosphoserine
+P34216	950	Phosphoserine
+P34216	964	Phosphoserine
+P34216	1008	Phosphoserine
+P34216	1012	Phosphoserine
+P34216	1020	Phosphoserine
+P34216	1046	Phosphothreonine
+P34216	1069	Phosphoserine
+P34216	1087	Phosphoserine
+P34216	1093	Phosphoserine
+P34216	1095	Phosphoserine
+P34216	1096	Phosphoserine
+P34216	1100	Phosphoserine
+P34216	1111	Phosphothreonine
+P34216	1181	Phosphoserine
+P34216	1187	Phosphoserine
+P34216	1307	Phosphothreonine
+P34216	1343	Phosphoserine
+P34216	674	Glycyl
+P34216	1329	Glycyl
+P36008	2	N-acetylserine
+P53978	2	N-acetylserine
+P53978	187	N6%2CN6%2CN6-trimethyllysine
+P53978	196	N6%2CN6%2CN6-trimethyllysine
+P53978	789	N6%2CN6%2CN6-trimethyllysine
+P53978	972	Phosphothreonine
+P53978	974	Phosphoserine
+P53978	1039	Phosphoserine
+P53978	1040	Phosphoserine
+P12754	2	N-acetylserine
+P12754	106	Phosphoserine
+P12754	121	Phosphothreonine
+P32801	152	Phosphoserine
+P32801	516	Phosphoserine
+P32801	519	Phosphoserine
+P32476	284	Glycyl
+P32476	289	Glycyl
+P32476	311	Glycyl
+P38819	171	N-linked
+Q08649	17	Phosphoserine
+Q08649	262	N6-acetyllysine%3B
+Q06340	90	Phosphoserine
+Q06340	125	Phosphoserine
+Q06340	126	Phosphoserine
+Q06344	86	Phosphoserine
+Q06344	220	Phosphothreonine
+Q06344	223	Phosphoserine
+Q06344	225	Phosphoserine
+Q06344	367	Phosphoserine
+Q06344	369	Phosphoserine
+Q06344	372	Phosphoserine
+Q06344	542	Phosphothreonine
+P22696	161	Phosphoserine
+P32474	159	N-linked
+P32474	174	N-linked
+P32474	207	N-linked
+P32474	293	N-linked
+P32474	462	N-linked
+Q02908	453	Glycyl
+P00925	138	Phosphoserine
+P00925	188	Phosphoserine
+P00925	313	Phosphothreonine
+P00925	324	Phosphothreonine
+P00925	60	Glycyl
+P00925	243	Glycyl
+P00925	358	Glycyl
+Q12518	160	Phosphothreonine
+Q12518	163	Phosphoserine
+Q12518	180	Phosphothreonine
+Q12518	328	Phosphoserine
+Q12518	364	Phosphothreonine
+Q12518	366	Phosphothreonine
+Q12518	384	Phosphothreonine
+Q12518	386	Phosphothreonine
+Q12518	388	Phosphothreonine
+Q12518	395	Phosphothreonine%3B
+Q12518	415	Phosphothreonine%3B
+Q12518	357	Glycyl
+P47160	2	N-acetylserine
+P47160	196	Phosphoserine
+P47160	198	Phosphoserine
+P47160	203	Phosphoserine
+P47160	212	Phosphoserine
+P47160	223	Phosphoserine
+Q03769	1	N-acetylmethionine
+Q03769	322	Phosphoserine
+Q03769	324	Phosphoserine
+Q03769	363	Phosphoserine
+Q03769	368	Phosphothreonine
+Q03769	394	Phosphoserine
+Q03769	401	Phosphoserine
+Q08651	282	N-linked
+P25087	2	N-acetylserine
+P25087	99	Phosphoserine
+P40456	170	Phosphoserine
+P40456	190	Phosphoserine
+Q07872	195	Phosphoserine
+P40557	85	N-linked
+P40557	264	N-linked
+P40557	299	N-linked
+P40557	370	N-linked
+P38604	2	N-acetylthreonine
+P38836	41	N-linked
+P38836	295	N-linked
+Q05958	431	Phosphoserine
+Q05958	445	Phosphoserine
+Q05958	464	Phosphoserine
+P32644	227	Phosphoserine
+P32644	392	Phosphoserine
+P32644	465	Phosphothreonine
+P38248	339	Phosphoserine
+P38248	406	GPI-anchor
+P38248	21	N-linked
+P38248	56	N-linked
+P38248	82	N-linked
+P38248	196	N-linked
+P38248	209	N-linked
+P38248	227	N-linked
+P38248	234	N-linked
+P38248	241	N-linked
+P38248	267	N-linked
+P38248	279	N-linked
+P38248	304	N-linked
+P38248	328	N-linked
+P38248	389	N-linked
+P43605	223	N6-acetyllysine%3B
+P38249	508	Phosphoserine
+P38249	691	Phosphoserine
+P38249	935	Phosphothreonine
+P40217	302	Phosphoserine
+Q05050	2	N-acetylserine
+Q05050	2	Phosphoserine
+Q05050	88	Phosphoserine
+Q05050	130	Phosphoserine
+Q05050	182	Phosphoserine
+Q05050	401	Phosphoserine
+Q05050	584	Phosphoserine
+Q05050	710	Phosphoserine
+Q05050	720	Phosphothreonine
+Q05050	763	Phosphoserine
+Q05050	775	Phosphoserine
+Q05050	816	Phosphoserine
+Q05050	828	Phosphoserine
+Q05050	829	Phosphoserine
+Q05050	838	Phosphoserine
+P40319	2	N-linked
+P40319	20	N-linked
+P40319	66	N-linked
+P53861	235	Phosphoserine
+P53861	278	Phosphoserine
+P53753	138	N-linked
+P53753	186	N-linked
+P53753	223	N-linked
+P53753	259	N-linked
+P53753	280	N-linked
+P53753	303	N-linked
+P53753	307	N-linked
+P53753	393	N-linked
+P53753	533	N-linked
+P53753	886	N-linked
+P06103	61	Phosphoserine
+P06103	67	Phosphotyrosine
+P06103	669	Phosphoserine
+P00924	119	Phosphoserine
+P00924	138	Phosphoserine
+P00924	188	Phosphoserine
+P00924	313	Phosphothreonine
+P00924	324	Phosphothreonine
+P00924	60	Glycyl
+P00924	243	Glycyl
+P00924	358	Glycyl
+P32353	324	Glycyl
+P32353	344	Glycyl
+Q03071	2	N-acetylserine
+Q03071	2	Phosphoserine
+P53938	103	N-linked
+P53938	104	N-linked
+Q12452	345	Phosphothreonine
+P38748	376	Phosphoserine
+P38748	369	Glycyl
+P38748	410	Glycyl
+P38748	450	Glycyl
+P38071	339	Phosphoserine
+P23776	165	N-linked
+P23776	325	N-linked
+P52911	50	N-linked
+P52911	77	N-linked
+P52911	86	N-linked
+P52911	90	N-linked
+P52911	106	N-linked
+P52911	157	N-linked
+P52911	220	N-linked
+P52911	281	N-linked
+P52911	285	N-linked
+P52911	310	N-linked
+P52911	317	N-linked
+P52911	322	N-linked
+P52911	401	N-linked
+P52911	480	N-linked
+P52911	539	N-linked
+Q04660	23	Phosphoserine
+Q04660	72	Phosphoserine
+Q04660	76	Phosphoserine
+Q04660	146	Phosphoserine
+Q04660	149	Phosphoserine
+Q04660	418	Phosphoserine
+Q04660	127	Glycyl
+P05453	2	N-acetylserine
+P05453	571	Phosphoserine
+P19097	50	Phosphoserine
+P19097	180	O-(pantetheine
+P19097	523	Phosphoserine
+P19097	958	Phosphoserine
+P19097	1440	Phosphoserine
+P19097	37	Glycyl
+P53917	18	Phosphoserine
+P53917	81	Phosphoserine
+P53917	524	Phosphoserine
+P53917	527	Phosphoserine
+P53917	528	Phosphoserine
+P21268	87	Phosphoserine%3B
+P21268	110	Phosphoserine
+P21268	114	Phosphoserine
+P21268	306	Phosphothreonine
+P15646	16	Asymmetric
+P15646	16	Omega-N-methylarginine%3B
+P15646	22	Omega-N-methylarginine%3B
+P15646	30	Asymmetric
+P15646	34	Asymmetric
+P15646	34	Omega-N-methylarginine%3B
+P15646	40	Omega-N-methylarginine%3B
+P15646	48	Asymmetric
+P15646	52	Asymmetric
+P15646	52	Omega-N-methylarginine%3B
+P15646	58	Omega-N-methylarginine%3B
+P15646	70	Asymmetric
+P15646	70	Omega-N-methylarginine%3B
+P15646	73	Asymmetric
+P15646	73	Omega-N-methylarginine%3B
+P15646	81	Asymmetric
+P15646	81	Omega-N-methylarginine%3B
+P15646	150	Glycyl
+P40988	48	Phosphoserine
+P40988	50	Phosphoserine
+P40988	39	Glycyl
+P53918	57	Phosphoserine
+P53918	112	Phosphoserine
+P53918	172	Phosphoserine
+P53918	637	Phosphoserine
+P53918	230	N-linked
+P53918	471	N-linked
+P53918	492	N-linked
+P38224	288	Phosphoserine
+P38224	293	Phosphothreonine
+P38224	296	Phosphoserine
+P40020	81	Phosphoserine
+P40020	172	Phosphoserine
+P40020	225	Phosphoserine
+Q08906	130	GPI-anchor
+Q08906	92	N-linked
+P12385	182	N5-methylglutamine
+P12385	421	Phosphoserine
+P12385	331	Glycyl
+Q03103	21	N-linked
+Q03103	35	N-linked
+Q03103	53	N-linked
+Q03103	130	N-linked
+Q03103	342	N-linked
+Q03103	425	N-linked
+Q03103	458	N-linked
+Q03103	468	N-linked
+Q03103	491	N-linked
+P17261	177	N-linked
+Q03661	500	Phosphothreonine
+Q03661	532	Phosphoserine
+Q03661	579	Phosphoserine
+Q03661	583	Phosphoserine
+Q03661	608	Phosphoserine
+Q03661	662	Phosphoserine
+Q03661	865	Phosphoserine
+Q03661	866	Phosphoserine
+Q03661	888	Phosphoserine
+Q03661	911	Phosphoserine
+Q03661	937	Phosphoserine
+Q03661	1092	Phosphoserine
+Q03661	1096	Phosphoserine
+Q03661	1098	Phosphoserine
+Q03661	1166	Phosphoserine
+Q03661	1176	Phosphoserine
+Q03661	1178	Phosphoserine
+Q03661	1214	Phosphoserine
+Q03661	1254	Phosphoserine
+Q03661	1290	Phosphoserine
+Q03661	1326	Phosphoserine
+Q03661	1332	Phosphoserine
+Q03661	1403	Phosphoserine
+Q03661	1409	Phosphoserine
+Q03661	1450	Phosphoserine
+Q03661	1454	Phosphoserine
+Q03661	1539	Phosphoserine
+Q03661	1590	Phosphoserine
+Q03661	1591	Phosphoserine
+P53743	7	Phosphoserine
+P53743	13	Phosphoserine
+P53743	14	Phosphoserine
+P42940	2	N-acetylserine
+Q08421	30	Phosphoserine
+P39875	372	Phosphoserine
+P38261	58	Phosphothreonine
+P38261	139	Phosphoserine
+P38261	482	Phosphoserine
+P38261	219	Glycyl
+P09201	12	Phosphoserine
+P34756	2	N-acetylserine
+P34756	186	Phosphoserine
+P34756	1627	Phosphoserine
+P34756	1630	Phosphoserine
+P34756	1938	Phosphoserine
+P34756	1953	Phosphothreonine
+P32604	435	Phosphoserine
+P32604	446	Phosphoserine
+Q04952	844	N-linked
+Q04952	874	N-linked
+Q04952	955	N-linked
+Q04952	1002	N-linked
+Q04952	1170	N-linked
+Q04952	1360	N-linked
+Q04952	1579	N-linked
+Q04952	1761	N-linked
+P36170	1146	GPI-anchor
+P36170	122	N-linked
+P36170	157	N-linked
+P36170	279	N-linked
+P36170	389	N-linked
+P36170	452	N-linked
+P36170	515	N-linked
+P36170	578	N-linked
+P36170	656	N-linked
+P36170	686	N-linked
+P36170	879	N-linked
+P36170	1092	N-linked
+P36170	1099	N-linked
+P08640	1346	GPI-anchor
+P08640	817	N-linked
+P08640	874	N-linked
+P32768	1514	GPI-anchor
+P32768	135	N-linked
+P32768	187	N-linked
+P32768	262	N-linked
+P32768	329	N-linked
+P32768	374	N-linked
+P32768	419	N-linked
+P32768	464	N-linked
+P32768	509	N-linked
+P32768	554	N-linked
+P32768	599	N-linked
+P32768	644	N-linked
+P32768	689	N-linked
+P32768	734	N-linked
+P32768	1114	N-linked
+Q05040	115	Phosphoserine
+Q05040	132	Phosphothreonine
+Q08907	182	GPI-anchor
+P53971	951	Phosphothreonine
+P53971	958	Phosphoserine
+Q03254	701	Phosphoserine
+Q03254	718	Phosphoserine
+Q03254	720	Phosphoserine
+Q03254	74	Glycyl
+Q12119	46	Phosphothreonine
+P17064	18	Phosphoserine
+P17064	16	Glycyl
+P39676	22	Phosphothreonine
+P07149	1	N-acetylmethionine
+P07149	733	Phosphothreonine
+P07149	1121	Phosphoserine
+P07149	1364	Glycyl
+P40039	43	Phosphoserine
+P40039	46	Phosphothreonine
+Q08991	109	N-linked
+Q08991	117	N-linked
+Q08991	235	N-linked
+P25653	1588	GPI-anchor
+P25653	29	N-linked
+P25653	231	N-linked
+P25653	298	N-linked
+P25653	347	N-linked
+P25653	386	N-linked
+P25653	426	N-linked
+P25653	495	N-linked
+P25653	535	N-linked
+P25653	661	N-linked
+P25653	674	N-linked
+P25653	713	N-linked
+P25653	889	N-linked
+P25653	907	N-linked
+P25653	1079	N-linked
+P25653	1400	N-linked
+P42837	829	Phosphoserine
+P38911	2	N-acetylserine
+P38911	80	Phosphoserine
+P38911	81	Phosphoserine
+P38911	89	Phosphothreonine
+P38911	184	Phosphotyrosine%3B
+P38911	186	Phosphoserine%3B
+P20081	2	N-acetylserine
+P20081	51	Phosphoserine
+P38631	269	Phosphothreonine
+P38631	272	Phosphothreonine
+P38631	259	Glycyl
+P38631	275	Glycyl
+P38631	386	Glycyl
+P38631	910	Glycyl
+P38631	915	Glycyl
+P38631	1539	Glycyl
+P38631	1547	Glycyl
+Q07825	69	Phosphoserine
+Q07825	92	Phosphoserine
+Q07825	95	Phosphoserine
+P32791	69	N-linked
+P32791	100	N-linked
+P32791	124	N-linked
+P53746	51	N-linked
+P53746	80	N-linked
+P53746	101	N-linked
+P53746	113	N-linked
+P53746	127	N-linked
+P53746	135	N-linked
+P08417	428	Phosphothreonine
+P28003	194	Phosphothreonine
+P28003	207	Phosphoserine
+P28003	211	Phosphoserine
+P11412	2	N-acetylserine
+P11412	142	Phosphoserine
+P11412	145	Phosphotyrosine
+P04385	381	Phosphoserine
+P04386	694	Phosphotyrosine
+P04386	696	Phosphoserine
+P04386	699	Phosphoserine
+P04386	703	Phosphoserine
+P04386	712	Phosphoserine
+Q04739	12	Phosphoserine
+Q04739	21	Phosphoserine
+Q04739	44	Phosphoserine
+Q04739	135	Phosphoserine
+Q04739	276	Phosphoserine
+Q04739	279	Phosphoserine
+P39719	28	N-linked
+P39719	65	N-linked
+P39719	81	N-linked
+P39719	156	N-linked
+P39719	323	N-linked
+P36033	85	N-linked
+P36033	108	N-linked
+P36033	120	N-linked
+P36033	134	N-linked
+P36033	341	N-linked
+Q12473	89	N-linked
+Q12473	112	N-linked
+Q12473	124	N-linked
+P12709	2	N-acetylserine
+P12709	53	Phosphothreonine
+P12709	220	Phosphothreonine
+P17649	326	N6-(pyridoxal
+P38225	184	N-linked
+P38225	289	N-linked
+P38225	534	N-linked
+P38225	591	N-linked
+P38993	27	N-linked
+P38993	74	N-linked
+P38993	77	N-linked
+P38993	88	N-linked
+P38993	113	N-linked
+P38993	194	N-linked
+P38993	198	N-linked
+P38993	244	N-linked
+P38993	265	N-linked
+P38993	292	N-linked
+P38993	300	N-linked
+P38993	359	N-linked
+P38993	381	N-linked
+Q08913	109	N-linked
+Q08913	117	N-linked
+Q08913	235	N-linked
+P39521	44	Phosphoserine
+P39521	228	Phosphoserine
+P39521	230	Phosphothreonine
+P39521	247	Phosphothreonine
+P39521	264	Phosphoserine
+P53121	616	Phosphoserine
+P53121	635	Phosphoserine
+P53121	779	Phosphoserine
+P53121	782	Phosphoserine
+P53121	149	N-linked
+P53121	321	N-linked
+P53121	547	N-linked
+Q08967	610	Phosphoserine
+Q08967	626	Phosphothreonine
+Q08967	771	Phosphoserine
+Q08967	774	Phosphoserine
+Q08967	143	N-linked
+Q08967	281	N-linked
+P53739	140	Phosphoserine
+P53739	144	Phosphoserine
+P53739	171	Phosphoserine
+P53739	175	Phosphoserine
+P53739	185	Phosphoserine
+P53739	300	Phosphoserine
+P53739	414	Phosphoserine
+P53739	462	Phosphoserine
+P23900	150	Phosphoserine
+P23900	168	Phosphothreonine
+P23900	209	Phosphoserine
+P23900	212	Phosphoserine
+P38310	449	Phosphoserine
+P38310	453	Phosphoserine
+P00358	302	Phosphoserine
+P00358	46	Glycyl
+P00358	63	Glycyl
+P00359	302	Phosphoserine
+P00359	46	Glycyl
+P00359	63	Glycyl
+P38260	12	Phosphoserine
+P43561	24	N-linked
+P43561	86	N-linked
+P43561	115	N-linked
+P43561	196	N-linked
+P43561	200	N-linked
+P43561	246	N-linked
+P43561	295	N-linked
+P43561	364	N-linked
+P43561	455	N-linked
+P41813	708	Phosphoserine
+P41813	832	Phosphoserine
+P41813	833	Phosphoserine
+P40989	288	Phosphothreonine
+P40989	291	Phosphothreonine
+P40989	278	Glycyl
+P40989	405	Glycyl
+P40989	929	Glycyl
+P40989	934	Glycyl
+P40989	1558	Glycyl
+P40989	1566	Glycyl
+Q08905	85	N-linked
+Q08905	108	N-linked
+Q08905	120	N-linked
+Q08905	134	N-linked
+Q08908	117	N-linked
+Q12209	371	N-linked
+Q12209	383	N-linked
+Q12209	384	N-linked
+Q03002	441	Phosphoserine
+Q03898	54	Phosphoserine
+Q03898	68	Phosphothreonine
+Q03898	74	Phosphoserine
+Q03898	88	Phosphoserine
+Q04433	506	GPI-anchor
+Q04433	412	N-linked
+Q04433	464	N-linked
+Q04433	503	N-linked
+P39712	1299	GPI-anchor
+P39712	135	N-linked
+P39712	187	N-linked
+P39712	203	N-linked
+P39712	257	N-linked
+P39712	262	N-linked
+P39712	270	N-linked
+P39712	329	N-linked
+P39712	419	N-linked
+P39712	464	N-linked
+P39712	509	N-linked
+P39712	554	N-linked
+P39712	599	N-linked
+P39712	644	N-linked
+P39712	689	N-linked
+P39712	734	N-linked
+P39712	888	N-linked
+Q07651	230	Phosphoserine
+Q07651	232	Phosphoserine
+Q07651	235	Phosphothreonine
+Q07651	73	N-linked
+P31380	232	Phosphoserine
+P31380	369	Phosphoserine
+P31380	451	Phosphoserine
+Q12035	1	N-acetylmethionine
+Q06205	80	Phosphoserine
+Q06205	82	Phosphoserine
+Q04991	238	Phosphoserine
+Q04991	249	Phosphoserine
+Q04991	269	Phosphoserine
+P53848	2	N-acetylserine
+P53848	286	Phosphoserine
+P38894	1052	GPI-anchor
+P38894	135	N-linked
+P38894	187	N-linked
+P38894	203	N-linked
+P38894	262	N-linked
+P38894	663	N-linked
+P38894	749	N-linked
+Q12029	2	N-acetylalanine
+P16892	180	Phosphothreonine
+P16892	182	Phosphotyrosine
+P16892	345	Glycyl
+P53913	2	N-acetylserine
+P45976	50	Phosphoserine
+P04397	562	Phosphoserine
+P13181	32	Phosphoserine
+P13181	35	Phosphoserine
+P13181	39	Phosphoserine
+P13181	48	Phosphoserine
+P13181	50	Phosphoserine
+P13181	53	Phosphoserine
+P13181	55	Phosphoserine
+P13045	1	N-acetylmethionine
+P43574	167	Phosphoserine
+P43574	262	Phosphoserine
+P43574	270	Phosphoserine
+P43574	369	Phosphothreonine
+P43574	399	Phosphoserine
+P43574	418	Phosphoserine
+P39012	87	N-linked
+P28006	415	Phosphoserine
+P28006	424	Phosphoserine
+P40056	2	N-acetylserine
+P40056	45	Phosphoserine
+P40056	173	N-linked
+P40056	196	N-linked
+P14742	253	Phosphoserine
+P14742	334	Phosphothreonine
+P14742	336	Phosphoserine
+P40036	51	Phosphoserine
+P40036	52	Phosphothreonine
+P40036	155	Phosphoserine
+P40036	221	Phosphoserine
+P40036	238	Phosphoserine
+P39732	497	Phosphoserine
+P39732	501	Phosphoserine
+P39732	609	Phosphoserine
+P25346	80	N-linked
+P36143	230	O-linked
+P36143	598	O-linked
+Q05670	20	Phosphothreonine
+Q05670	67	Phosphoserine
+Q05670	72	Phosphoserine
+Q05670	84	Phosphoserine
+Q05670	88	Phosphothreonine
+Q05670	100	Phosphoserine
+Q05670	106	Phosphoserine
+Q08559	91	N-linked
+P46949	92	Phosphoserine
+P46949	100	Phosphoserine
+P46949	134	Phosphoserine
+P46949	163	Phosphoserine
+P46949	180	Phosphoserine
+P46949	182	Phosphoserine
+P46949	237	Phosphoserine
+P46949	238	Phosphoserine
+P46949	532	Phosphoserine
+P08431	27	Phosphoserine
+P04387	1	N-acetylmethionine
+P25555	130	Phosphothreonine
+P51601	15	Phosphothreonine
+P51601	23	Phosphoserine
+P43535	2	N-acetylalanine
+Q04839	87	Phosphoserine
+Q04839	106	Phosphoserine
+Q04839	111	Phosphoserine
+P22146	528	GPI-anchor
+P22146	40	N-linked
+P22146	57	N-linked
+P22146	95	N-linked
+P22146	149	N-linked
+P22146	165	N-linked
+P22146	253	N-linked
+P22146	283	N-linked
+P22146	321	N-linked
+P22146	409	N-linked
+P22146	495	N-linked
+Q06135	531	GPI-anchor
+Q06135	498	N-linked
+P39993	46	Phosphoserine
+P39993	284	Phosphoserine
+Q06648	254	Phosphoserine
+Q06648	258	Phosphoserine
+Q06648	337	Phosphoserine
+Q06648	345	Phosphoserine
+Q06648	367	Phosphoserine
+Q03833	70	Phosphoserine
+Q03833	343	Phosphoserine
+Q03833	690	Phosphoserine
+Q03833	694	Phosphoserine
+Q03833	696	Phosphoserine
+Q03833	734	Phosphoserine
+Q03833	747	Phosphoserine
+P38196	54	Phosphothreonine
+P38196	56	Phosphoserine
+P38196	635	Glycyl
+P11710	178	Phosphothreonine
+P11710	190	Phosphoserine
+P11710	256	Phosphoserine
+P11710	281	Phosphothreonine
+P11710	424	Phosphothreonine
+P38297	398	Glycyl
+P38297	464	Glycyl
+P18852	107	Cysteine
+P18852	106	S-palmitoyl
+P18852	107	S-farnesyl
+P47102	49	Phosphoserine
+Q04233	165	Phosphoserine
+Q04233	304	Phosphoserine
+Q04233	616	Phosphoserine
+Q04233	622	Phosphoserine
+Q04233	707	Phosphoserine
+Q04233	720	Phosphoserine
+P32614	66	Phosphoserine
+P31381	45	Phosphoserine
+P31381	58	Phosphoserine
+P19145	76	Glycyl
+P28007	4	Asymmetric
+P28007	8	Asymmetric
+P28007	11	Asymmetric
+P28007	15	Asymmetric
+P28007	19	Asymmetric
+P28007	147	Asymmetric
+P28007	154	Asymmetric
+P28007	158	Asymmetric
+P28007	162	Asymmetric
+P28007	165	Asymmetric
+P28007	171	Asymmetric
+P28007	174	Asymmetric
+P28007	180	Asymmetric
+P28007	184	Asymmetric
+P28007	189	Asymmetric
+P28007	193	Asymmetric
+P28007	197	Asymmetric
+P28007	201	Asymmetric
+P28007	77	Glycyl
+Q03655	498	GPI-anchor
+Q03655	201	N-linked
+Q03655	269	N-linked
+Q03655	350	N-linked
+Q03655	385	N-linked
+Q03655	404	N-linked
+Q03655	422	N-linked
+P39726	102	N6-lipoyllysine
+Q08271	447	GPI-anchor
+Q08271	151	N-linked
+Q08271	398	N-linked
+Q08193	462	GPI-anchor
+Q08193	24	N-linked
+Q08193	60	N-linked
+Q08193	166	N-linked
+Q08193	299	N-linked
+Q08193	344	N-linked
+Q08193	359	N-linked
+P38011	2	N-acetylalanine
+P38011	96	Phosphothreonine
+P38011	168	Phosphothreonine
+P38011	46	Glycyl
+P38011	53	Glycyl
+P38011	107	Glycyl
+P38011	137	Glycyl
+P38011	161	Glycyl
+P07261	447	Phosphothreonine
+P07261	449	Phosphoserine
+P07261	482	Phosphoserine
+P07261	489	Phosphoserine
+P07261	538	Phosphoserine
+P14065	306	Phosphoserine
+P32775	190	Phosphoserine
+P17695	37	Phosphoserine
+P17695	61	S-glutathionyl
+P17695	91	Phosphoserine
+P37303	213	N6-(pyridoxal
+P37303	367	Phosphoserine
+P37303	369	Phosphoserine
+P37303	370	Phosphothreonine
+P37303	228	Glycyl
+P38875	184	N-linked
+P40106	90	Phosphoserine
+P40106	64	Glycyl
+P40106	144	Glycyl
+P35197	151	Phosphothreonine
+P35197	157	Phosphoserine
+P35197	161	Phosphothreonine
+P35197	168	Phosphoserine
+P35197	170	Phosphothreonine
+P35197	260	Phosphoserine
+Q03016	68	Phosphoserine
+Q03016	99	Phosphothreonine
+Q03016	103	Phosphoserine
+Q03016	143	Phosphoserine
+Q03016	260	Phosphoserine
+Q03016	264	Phosphothreonine
+Q03016	269	Phosphoserine
+P03069	17	Phosphoserine
+P03069	165	Phosphothreonine%3B
+P03069	218	Phosphoserine
+Q01722	151	Phosphoserine
+Q01722	406	Phosphoserine
+Q01722	409	Phosphoserine
+P32621	41	N-linked
+P32621	280	N-linked
+P32621	335	N-linked
+Q02979	653	Phosphoserine
+Q02979	983	Phosphoserine
+P37291	20	Phosphothreonine
+P37291	26	Phosphoserine
+P37291	248	N6-(pyridoxal
+P37291	429	Phosphoserine
+P37291	456	Glycyl
+P40107	119	N-linked
+P40107	242	N-linked
+P40107	246	N-linked
+P40107	249	N-linked
+P0CE11	149	N-linked
+P0CE11	153	N-linked
+P43577	2	N-acetylserine
+P10823	2	N-myristoyl
+P10823	4	S-palmitoyl
+Q08886	91	Phosphoserine
+Q08886	161	Phosphothreonine
+Q05584	257	Phosphoserine
+P38682	170	Phosphoserine
+P38682	306	Phosphoserine
+P38682	389	Phosphoserine
+P38682	398	Phosphoserine
+P48813	29	Phosphoserine
+P48813	113	Phosphoserine
+P48813	124	Phosphoserine
+P48813	127	Phosphothreonine
+P48813	34	Glycyl
+P48813	39	Glycyl
+P48813	41	Glycyl
+P48813	61	Glycyl
+P48813	132	Glycyl
+P53839	31	Phosphothreonine
+Q00055	2	N-acetylserine
+Q00055	24	Phosphoserine
+Q00055	27	Phosphoserine
+Q06636	16	Phosphoserine
+P49095	773	N6-(pyridoxal
+Q06336	348	Phosphothreonine
+Q06336	353	Phosphoserine
+Q06336	357	Phosphoserine
+Q06336	378	Phosphoserine
+Q06336	394	Phosphoserine
+P38817	180	Glycyl
+P38817	287	Glycyl
+P38138	114	N-linked
+P38138	126	N-linked
+P38138	142	N-linked
+P38138	173	N-linked
+P38138	345	N-linked
+P38138	783	N-linked
+P38138	791	N-linked
+P38138	867	N-linked
+P38138	880	N-linked
+P38138	907	N-linked
+P38138	941	N-linked
+Q04924	145	N-linked
+Q04924	240	N-linked
+Q04924	358	N-linked
+Q04924	520	N-linked
+Q04924	525	N-linked
+Q04924	688	N-linked
+Q04924	699	N-linked
+Q12434	2	N-acetylalanine
+Q12434	27	Phosphothreonine
+Q12434	40	Phosphoserine
+P41818	12	Phosphoserine
+P41818	118	Phosphothreonine%3B
+P41818	158	Phosphoserine
+P41818	184	Phosphoserine
+P47011	230	O-linked
+P47011	232	O-linked
+P47011	367	O-linked
+P38263	27	Phosphoserine
+P38263	20	Glycyl
+Q12263	406	Phosphoserine
+Q12263	465	Phosphoserine
+Q12263	471	Phosphoserine
+Q12263	617	Phosphoserine
+Q12263	689	Phosphoserine
+Q12263	719	Phosphoserine
+Q12263	805	Phosphoserine
+Q12263	807	Phosphoserine
+Q12263	883	Phosphoserine
+Q12263	884	Phosphothreonine
+Q12263	930	Phosphoserine
+P32288	2	N-acetylalanine
+P32288	5	Phosphoserine
+P32288	283	Glycyl
+P32288	324	Glycyl
+P32288	363	Glycyl
+P25373	27	S-glutathionyl
+P25373	11	Glycyl
+Q12680	2070	Phosphothreonine
+P37292	265	N6-(pyridoxal
+Q07830	66	N-linked
+Q07830	71	N-linked
+Q07830	100	N-linked
+Q07830	182	N-linked
+Q07830	203	N-linked
+Q07830	411	N-linked
+Q07830	681	N-linked
+Q07830	682	N-linked
+Q07830	707	N-linked
+Q07830	742	N-linked
+P41277	90	Phosphoserine
+P41277	64	Glycyl
+P41277	64	Glycyl
+P41277	144	Glycyl
+P18494	251	Phosphoserine
+P18494	267	Phosphoserine
+P18494	285	Phosphoserine
+P18494	469	Phosphoserine
+P18494	552	Phosphoserine
+P18494	562	Phosphoserine
+P36148	632	Phosphoserine
+P36148	637	Phosphoserine
+P36148	647	Phosphoserine
+P36148	651	Phosphoserine
+P36148	654	Phosphoserine
+P36148	657	Phosphoserine
+P36148	664	Phosphoserine
+P36148	668	Phosphoserine
+P36148	671	Phosphoserine
+P36148	673	Phosphothreonine
+P36148	688	Phosphoserine
+P36148	692	Phosphothreonine
+P36148	693	Phosphoserine
+Q04410	1	N-acetylmethionine
+Q04410	155	Phosphoserine
+Q04322	1	N-acetylmethionine
+Q04322	17	Phosphothreonine
+Q04322	37	Phosphoserine
+Q04322	73	Phosphoserine
+Q04322	139	Phosphoserine
+Q04322	498	Glycyl
+P48365	265	Phosphoserine
+P48365	339	Phosphoserine
+P23337	159	Phosphoserine
+P23337	363	Phosphoserine
+P23337	560	Phosphoserine
+P23337	651	Phosphoserine
+P23337	655	Phosphoserine
+P23337	660	Phosphoserine%3B
+P23337	662	Phosphoserine%3B
+P23337	667	Phosphothreonine
+P04911	2	N-acetylserine
+P04911	5	N6-acetyllysine
+P04911	8	N6-acetyllysine
+P04911	106	N5-methylglutamine
+P04911	129	Phosphoserine
+P04911	127	Glycyl
+P02294	7	N6-acetyllysine%3B
+P02294	8	N6-acetyllysine%3B
+P02294	11	Phosphoserine
+P02294	12	N6-acetyllysine
+P02294	17	N6-acetyllysine%3B
+P02294	7	Glycyl
+P02294	8	Glycyl
+P02294	17	Glycyl
+P02294	18	Glycyl
+P02294	124	Glycyl
+P38736	2	N-acetylserine
+P38736	164	Phosphoserine
+P39717	24	Phosphoserine
+P40531	2	N-acetylserine
+P40531	2	Phosphoserine
+P40531	319	Phosphoserine
+P40531	13	Glycyl
+P40531	305	Glycyl
+P40531	313	Glycyl
+Q08484	69	Phosphoserine
+Q08484	250	Phosphoserine
+P48566	147	Phosphoserine
+P48566	484	Phosphoserine
+Q12753	125	Phosphoserine
+Q12753	231	Phosphoserine
+Q12753	241	Phosphoserine
+Q12753	291	Phosphoserine
+P32835	2	N-acetylserine
+P32835	2	Phosphoserine
+P53551	174	Phosphoserine
+Q12341	354	Phosphoserine
+P41921	1	N-acetylmethionine
+P32836	2	N-acetylserine
+P32836	2	Phosphoserine
+P39996	66	Phosphoserine
+P39996	72	Phosphoserine
+P39996	99	Phosphoserine
+P39996	116	Phosphoserine
+P38970	17	Phosphoserine
+P38970	19	Phosphoserine
+P38970	68	Phosphoserine
+P38970	72	Phosphoserine
+P38970	160	Phosphoserine
+P38970	273	Phosphoserine
+P38970	277	Phosphoserine
+P38970	324	Phosphoserine
+P38970	333	Phosphoserine
+P38970	336	Phosphoserine
+P38970	358	Phosphoserine
+P38970	391	Phosphoserine
+P38970	395	Phosphoserine
+P38199	358	Phosphoserine
+P38199	360	Phosphoserine
+P38199	362	Phosphoserine
+Q12361	373	Phosphoserine
+Q12361	903	Phosphoserine
+P24814	199	Phosphoserine
+P24814	300	Phosphoserine
+Q04697	89	N-linked
+Q04697	173	N-linked
+P32806	436	Phosphoserine
+Q96VH4	2	N-acetylserine
+Q12096	136	N-linked
+Q12096	177	N-linked
+Q12096	187	N-linked
+Q12096	425	N-linked
+Q04080	100	N-linked
+Q04080	170	N-linked
+Q04080	228	N-linked
+Q04080	247	N-linked
+Q04080	299	N-linked
+P38211	69	N-linked
+P38211	101	N-linked
+P40367	145	N-linked
+P40367	185	N-linked
+P40367	298	N-linked
+P40367	506	N-linked
+P47122	304	Phosphoserine
+P47122	308	Phosphoserine
+P47122	313	Phosphoserine
+P47122	352	Phosphoserine
+P47122	369	Glycyl
+Q12068	333	Phosphoserine
+P40956	153	Phosphoserine
+P40956	181	Phosphotyrosine
+P40956	184	Phosphoserine
+P40956	187	Phosphoserine
+P40956	240	Phosphoserine
+P40956	249	Phosphothreonine
+P38625	241	Glycyl
+P38625	426	Glycyl
+Q12180	221	Phosphoserine
+Q12180	937	Phosphoserine
+Q05580	2	N-acetylserine
+Q05580	57	Phosphothreonine
+Q05580	354	Phosphoserine
+P53258	2	N-acetylserine
+P53258	764	Phosphoserine
+P53258	871	Phosphoserine
+Q12344	25	Phosphoserine
+Q12344	30	Phosphoserine
+Q12344	89	Phosphothreonine
+Q12344	389	Phosphoserine
+P27472	159	Phosphoserine
+P27472	363	Phosphoserine
+P27472	467	Phosphoserine
+P27472	651	Phosphoserine
+P27472	655	Phosphoserine%3B
+P27472	661	Phosphoserine%3B
+P27472	663	Phosphoserine%3B
+P27472	668	Phosphothreonine%3B
+P36125	2	N-acetylserine
+P41911	70	Phosphoserine
+P41911	72	Phosphoserine
+P41911	75	Phosphoserine
+P49018	256	N-linked
+P49018	346	N-linked
+Q12214	110	Phosphoserine
+Q01448	47	Phosphoserine
+Q01448	49	Phosphoserine
+Q01448	435	Phosphoserine
+Q05905	143	Phosphoserine
+P09950	337	N6-(pyridoxal
+P28789	251	S-(dipyrrolylmethanemethyl)cysteine
+Q12276	102	Phosphoserine
+Q12276	128	Phosphothreonine
+Q12276	277	Phosphoserine
+Q12276	1013	Phosphoserine
+Q12276	1130	Phosphothreonine
+Q12276	1200	Phosphoserine
+Q12276	1204	Phosphoserine
+Q12276	1207	Phosphoserine
+P41809	24	N-linked
+P41809	1252	N-linked
+P41809	1293	N-linked
+P41809	1342	N-linked
+P41809	1400	N-linked
+P54839	276	Phosphoserine
+P40480	14	Phosphoserine
+P40480	16	Phosphoserine
+P40480	37	Phosphothreonine
+P40480	67	Phosphoserine
+P40480	290	Phosphoserine
+P40480	507	Phosphoserine
+P40480	698	Phosphoserine
+P40480	700	Phosphothreonine
+P40480	778	Phosphoserine
+P48570	385	Phosphoserine
+P48570	396	Phosphothreonine
+P48570	401	Phosphoserine
+P48570	410	Phosphoserine
+Q99332	167	Phosphoserine
+Q99332	342	Phosphoserine
+P17629	234	Phosphoserine
+P47171	302	Phosphothreonine
+P47171	304	Phosphoserine
+P48353	109	Phosphoserine
+P12683	552	Phosphothreonine
+P12683	115	N-linked
+P12683	181	N-linked
+P12683	452	N-linked
+P12683	490	N-linked
+P02293	7	N6-acetyllysine%3B
+P02293	8	N6-acetyllysine%3B
+P02293	11	Phosphoserine
+P02293	12	N6-acetyllysine
+P02293	17	N6-acetyllysine%3B
+P02293	7	Glycyl
+P02293	8	Glycyl
+P02293	17	Glycyl
+P02293	18	Glycyl
+P02293	124	Glycyl
+P32769	124	Phosphoserine
+Q07653	41	Phosphoserine
+Q07653	303	Phosphoserine
+Q07653	363	Phosphoserine
+Q07653	491	Phosphoserine
+Q07653	561	Phosphoserine
+Q07653	671	Phosphoserine
+Q07653	855	Phosphotyrosine
+Q07653	857	Phosphoserine
+Q07653	1005	Phosphoserine
+Q07653	1034	Phosphoserine
+P25364	342	Phosphothreonine
+P25364	496	Phosphoserine
+Q12373	174	Phosphoserine
+Q03281	123	Phosphoserine
+P05373	254	Phosphoserine
+P04912	2	N-acetylserine
+P04912	5	N6-acetyllysine
+P04912	8	N6-acetyllysine
+P04912	106	N5-methylglutamine
+P04912	129	Phosphoserine
+P04912	127	Glycyl
+Q12692	2	N-acetylserine
+Q12692	4	N6-acetyllysine
+Q12692	9	N6-acetyllysine
+Q12692	11	N6-acetyllysine
+Q12692	15	N6-acetyllysine
+P61830	5	N6%2CN6%2CN6-trimethyllysine%3B
+P61830	5	N6%2CN6-dimethyllysine%3B
+P61830	5	N6-methyllysine%3B
+P61830	10	N6-acetyllysine%3B
+P61830	10	N6-methyllysine%3B
+P61830	11	Phosphoserine
+P61830	15	N6%2CN6-dimethyllysine%3B
+P61830	15	N6-acetyllysine%3B
+P61830	19	N6-acetyllysine%3B
+P61830	19	N6-methyllysine%3B
+P61830	24	N6-acetyllysine%3B
+P61830	24	N6-methyllysine%3B
+P61830	28	N6%2CN6%2CN6-trimethyllysine%3B
+P61830	28	N6%2CN6-dimethyllysine%3B
+P61830	28	N6-acetyllysine%3B
+P61830	28	N6-methyllysine%3B
+P61830	37	N6%2CN6%2CN6-trimethyllysine%3B
+P61830	37	N6%2CN6-dimethyllysine%3B
+P61830	37	N6-acetyllysine%3B
+P61830	37	N6-methyllysine%3B
+P61830	57	N6-acetyllysine
+P61830	65	N6-acetyllysine
+P61830	80	N6%2CN6%2CN6-trimethyllysine%3B
+P61830	80	N6%2CN6-dimethyllysine%3B
+P61830	80	N6-methyllysine%3B
+P02309	6	N6-acetyllysine
+P02309	13	N6-acetyllysine
+P02309	17	N6-acetyllysine
+P02309	61	Phosphoserine
+P02309	65	Phosphoserine
+P02309	80	N6-acetyllysine
+Q01766	266	Phosphoserine
+P06774	2	N-acetylserine
+P06774	52	Phosphoserine
+P06774	265	Phosphothreonine
+Q02516	7	Phosphoserine
+Q03532	12	Phosphoserine
+Q04458	111	Phosphoserine
+P32480	713	Phosphoserine
+P00498	1	N-acetylmethionine
+Q05787	101	N-linked
+Q05787	123	N-linked
+Q05787	142	N-linked
+Q05787	429	N-linked
+Q05787	611	N-linked
+Q99383	2	Phosphoserine
+Q99383	3	Phosphoserine
+Q99383	206	Phosphoserine
+Q99383	458	Phosphothreonine
+Q99383	462	Phosphoserine
+P29295	143	Phosphoserine
+P32479	610	Phosphoserine
+P07172	230	N6-(pyridoxal
+P40037	52	Glycyl
+P19807	22	Phosphoserine
+P19807	42	Phosphoserine
+P19807	7	N-linked
+P19807	20	N-linked
+P19807	248	N-linked
+P19807	341	N-linked
+P47124	37	N-linked
+Q9URQ5	2	N-acetylserine
+P32874	804	N6-biotinyllysine
+Q02959	582	Phosphoserine
+Q02959	583	Phosphoserine
+Q02959	613	Phosphoserine
+Q02959	629	Phosphoserine
+P34244	511	Phosphoserine
+P34244	629	Phosphoserine
+P34244	685	Phosphoserine
+P34244	837	Phosphoserine
+P34244	866	Phosphoserine
+P34244	1220	Phosphoserine
+P34244	1250	Phosphoserine
+P34244	1284	Phosphoserine
+P34244	1287	Phosphoserine
+P34244	1325	Phosphoserine
+P48362	2	N-acetylthreonine
+P06775	76	Phosphothreonine
+P12684	565	Phosphothreonine
+P12684	115	N-linked
+P12684	150	N-linked
+P12684	158	N-linked
+P12684	179	N-linked
+P12684	428	N-linked
+P12684	455	N-linked
+Q05164	946	GPI-anchor
+Q05164	28	N-linked
+Q05164	35	N-linked
+Q05164	493	N-linked
+Q05164	601	N-linked
+Q05164	638	N-linked
+P38753	2	N-acetylserine
+P38753	162	Phosphoserine
+P10961	1	N-acetylmethionine
+P10961	97	Phosphothreonine
+P10961	450	Phosphoserine
+P10961	458	Phosphoserine
+P10961	471	Phosphoserine
+P10961	478	Phosphoserine
+P10961	528	Phosphoserine
+P22943	21	Phosphoserine%3B
+P22943	24	Phosphoserine
+P22943	59	Phosphoserine
+P22943	73	Phosphoserine
+P22943	97	Phosphoserine
+P32485	2	N-acetylthreonine
+P32485	174	Phosphothreonine
+P32485	176	Phosphotyrosine
+Q12122	399	Phosphoserine
+Q12122	410	Phosphothreonine
+Q03213	146	Phosphoserine
+Q03213	153	Phosphoserine
+P15992	2	N-acetylserine
+P15992	42	Phosphothreonine
+P15992	90	Phosphoserine
+P15992	163	Phosphothreonine
+P15992	208	Phosphoserine
+P15992	211	Phosphoserine
+P25619	308	Phosphoserine
+P25619	331	Phosphothreonine
+P40325	2	N-acetylserine
+P40325	3	Glycyl
+P40325	18	Glycyl
+Q12345	157	Phosphoserine
+Q12345	211	Phosphoserine
+P39730	405	Phosphoserine
+Q04432	138	Cysteine
+Q12329	182	Phosphoserine
+Q12329	213	Phosphoserine
+Q12329	214	Phosphoserine
+Q12329	215	Phosphoserine
+Q12329	223	Phosphoserine
+P53119	1	N-acetylmethionine
+P32465	23	Phosphoserine
+P32465	38	Phosphoserine
+P32465	44	Phosphoserine
+P32465	228	N-linked
+P32466	23	Phosphoserine
+P32466	225	N-linked
+P32466	416	N-linked
+P38695	126	N-linked
+P38695	249	N-linked
+P38695	61	Glycyl
+P39004	556	Phosphothreonine
+P39004	91	N-linked
+P39004	228	N-linked
+P39004	560	Glycyl
+P46958	1	N-acetylmethionine
+P46958	13	Phosphothreonine
+P46958	23	Phosphoserine
+P46958	27	Phosphoserine
+P46958	39	Phosphoserine
+P46958	122	Phosphoserine
+P46958	130	Phosphoserine
+P46958	136	Phosphoserine
+P46958	147	Phosphoserine
+P46958	148	Phosphoserine
+P40060	124	Phosphothreonine
+P20459	52	Phosphoserine%3B
+P20459	292	Phosphoserine
+P20459	294	Phosphoserine
+P28817	326	Phosphothreonine
+P0CY09	1	N-acetylmethionine
+Q04178	2	N-acetylserine
+P38922	343	Phosphoserine
+P38922	355	Phosphoserine
+Q08732	37	Phosphoserine
+Q08732	382	Phosphoserine
+Q08732	472	Phosphoserine
+Q08732	495	Phosphothreonine
+Q08732	498	Phosphoserine
+P50079	61	N-linked
+P50079	155	N-linked
+P50079	256	N-linked
+P50079	280	N-linked
+P50079	315	N-linked
+P50079	421	N-linked
+P04806	245	Phosphoserine
+P04806	272	Phosphoserine
+P04807	15	Phosphoserine
+P04807	38	Phosphothreonine
+P04807	158	Phosphoserine
+P04807	245	Phosphoserine
+P04807	272	Phosphoserine
+Q12520	165	N-linked
+P15496	7	Phosphoserine
+P09064	40	Phosphoserine
+P09064	69	Phosphothreonine
+P09064	80	Phosphoserine
+P09064	92	Phosphoserine
+P09064	112	Phosphoserine
+P09064	116	Phosphothreonine
+P09064	118	Phosphoserine
+P10081	2	N-acetylserine
+P10081	73	Phosphothreonine
+P10081	77	Phosphoserine
+P10081	129	Phosphoserine
+P10081	146	Phosphothreonine
+P39936	74	Phosphoserine
+P39936	196	Phosphothreonine
+P39936	301	Phosphothreonine
+P39936	503	Phosphoserine
+P39936	913	Phosphoserine
+P39979	2	N-acetylserine
+P19882	102	Phosphothreonine
+P19882	485	Phosphoserine
+P22202	552	Phosphoserine
+P53686	2	N-acetylserine
+P53686	340	Phosphoserine
+P54862	87	N-linked
+P54862	227	N-linked
+P40886	92	N-linked
+P40886	102	N-linked
+P40886	429	N-linked
+P53892	100	Phosphoserine
+P53892	106	Phosphoserine
+P53892	211	Phosphothreonine
+P38284	217	Phosphoserine
+P38274	317	Phosphoserine
+P38274	614	Phosphothreonine
+P0CS90	330	Phosphothreonine
+P19211	2	Phosphoserine
+P19211	7	Phosphothreonine
+P19211	51	Hypusine
+Q12522	174	Phosphoserine%3B
+Q12522	175	Phosphoserine%3B
+Q12522	231	Phosphoserine
+P06168	355	Phosphoserine
+Q03824	275	N-linked
+Q03824	343	N-linked
+Q03824	344	N-linked
+Q03824	379	N-linked
+Q03824	517	N-linked
+Q03824	569	N-linked
+Q03824	574	N-linked
+Q12271	497	Phosphoserine
+Q12271	986	Phosphoserine
+Q12271	1035	Phosphoserine
+Q12271	1105	Phosphothreonine
+P00724	23	N-linked
+P00724	64	N-linked
+P00724	97	N-linked
+P00724	111	N-linked
+P00724	118	N-linked
+P00724	165	N-linked
+P00724	266	N-linked
+P00724	275	N-linked
+P00724	356	N-linked
+P00724	369	N-linked
+P00724	384	N-linked
+P00724	398	N-linked
+P00724	512	N-linked
+P32589	2	N-acetylserine
+P32589	242	Phosphothreonine
+P32589	660	Phosphoserine
+P32589	195	Glycyl
+P17709	2	N-acetylserine
+P17709	2	Phosphoserine
+P17709	470	Phosphoserine
+P43581	75	N-linked
+P40441	194	N-linked
+P23585	2	N-acetylserine
+P23585	11	Phosphoserine
+P23585	13	Phosphoserine
+P23585	17	Phosphoserine
+P23585	20	Phosphoserine
+P23585	29	Phosphothreonine
+P23585	32	Phosphoserine
+P23585	266	Phosphoserine%3B
+P23585	539	Phosphoserine%3B
+P23585	82	N-linked
+P32467	425	N-linked
+P32467	45	Glycyl
+P39003	91	N-linked
+P39003	228	N-linked
+P39003	560	Glycyl
+P40885	87	N-linked
+P40885	227	N-linked
+P43598	64	Phosphoserine
+P43598	65	Phosphothreonine
+P43598	95	Phosphoserine
+P43598	96	Phosphoserine
+P43598	132	Phosphothreonine
+P43598	164	Phosphoserine
+Q02821	1	N-acetylmethionine
+P40069	646	Phosphoserine
+Q03694	273	Phosphoserine
+P47046	690	Phosphoserine
+P28241	105	Phosphothreonine
+P28241	153	Phosphothreonine
+P28241	327	Phosphothreonine
+P28241	349	Phosphothreonine
+P40154	67	Phosphoserine
+P40154	129	Phosphoserine
+P47170	680	Phosphoserine
+P47170	737	Phosphoserine
+P53901	392	Phosphoserine
+P50942	152	Phosphoserine
+P50942	522	Phosphoserine
+P50942	1005	Phosphoserine
+P50942	1016	Phosphoserine
+P50942	1032	Phosphothreonine
+P50942	1095	Phosphoserine
+Q04213	2	Phosphoserine
+Q04213	9	Phosphothreonine
+Q04213	65	Phosphoserine
+Q04213	73	Phosphoserine
+Q04213	242	Phosphoserine
+P07250	1	N-acetylmethionine
+P07250	97	Phosphoserine
+P07260	2	Phosphoserine%3B
+P07260	15	Phosphoserine%3B
+P07260	22	Phosphothreonine
+P07260	28	Phosphoserine
+P07260	30	Phosphoserine
+P07260	114	Glycyl
+P39520	208	Phosphoserine
+P39520	1041	Phosphoserine
+P43579	27	Phosphoserine
+P43579	487	Phosphoserine
+P43579	493	Phosphoserine
+P43579	504	Phosphoserine
+P43579	507	Phosphothreonine
+P32481	60	Phosphothreonine
+P32481	258	Phosphoserine
+P39935	181	Phosphothreonine
+P39935	883	Phosphoserine
+P39935	888	Phosphothreonine
+P39935	908	Phosphoserine
+P39935	948	Phosphoserine
+P23301	2	N-acetylserine
+P23301	2	Phosphoserine
+P23301	10	Phosphothreonine
+P23301	51	Hypusine
+P23301	74	Phosphoserine
+P23301	86	Glycyl
+Q9P305	2	N-acetylserine
+Q9P305	6	Phosphoserine
+Q9P305	63	Phosphoserine
+Q9P305	108	Phosphoserine
+Q9P305	119	Phosphoserine
+P47042	96	Phosphoserine
+P47169	903	Phosphoserine
+P05694	89	Phosphoserine
+P05694	242	Phosphoserine
+P05694	566	Phosphothreonine
+P05694	629	Phosphoserine
+P05694	706	Phosphoserine
+P38920	441	Phosphoserine%3B
+P40457	1512	Phosphoserine
+P40457	1670	Phosphoserine
+P53152	71	Phosphoserine
+P38888	86	N-linked
+P38888	517	N-linked
+P38888	672	N-linked
+P38888	762	N-linked
+P41821	32	N-linked
+P41821	70	N-linked
+P41821	112	N-linked
+P41821	125	N-linked
+P41821	159	N-linked
+P41821	175	N-linked
+P41821	228	N-linked
+P41821	238	N-linked
+P41821	265	N-linked
+P41821	282	N-linked
+P41821	285	N-linked
+P41821	291	N-linked
+P41821	324	N-linked
+P34072	25	Phosphothreonine
+P34072	247	Phosphoserine
+P34072	276	Phosphoserine
+P34072	442	Phosphoserine
+P34072	518	Phosphoserine%3B
+P32047	8	Phosphoserine
+P32047	11	Phosphoserine
+P32047	14	Phosphoserine
+P32047	56	Phosphoserine
+P32047	74	Phosphoserine
+P32047	79	Phosphoserine
+P32047	121	Phosphothreonine
+P32047	145	Phosphoserine
+P32047	156	Phosphoserine
+P32047	160	Phosphoserine
+P32047	169	Phosphothreonine
+P32047	171	Phosphoserine
+P32047	173	Phosphothreonine
+P32047	183	Phosphoserine
+P32047	189	Phosphoserine
+P32047	227	Phosphotyrosine
+P32047	228	Phosphoserine
+P32047	257	Phosphoserine
+P32047	265	Phosphoserine
+P32047	295	Phosphotyrosine
+P32047	297	Phosphoserine
+P32047	320	Phosphoserine
+P32047	353	Phosphoserine
+P32047	439	Phosphoserine
+Q12372	6	Phosphoserine
+Q12372	21	Phosphothreonine
+Q12372	23	Phosphoserine
+Q06324	12	Phosphothreonine
+Q06324	16	Phosphoserine
+Q06324	37	Phosphoserine
+P46982	113	N-linked
+P46982	136	N-linked
+P46982	259	N-linked
+P46982	264	N-linked
+P40549	34	N-linked
+P40549	168	N-linked
+P53745	132	N-linked
+P53745	167	N-linked
+P53745	223	N-linked
+P53745	349	N-linked
+P43563	33	Phosphotyrosine
+P43563	59	Phosphoserine
+P43563	76	Phosphothreonine
+P23641	2	N-acetylserine%3B
+P23641	4	Phosphoserine
+P23641	145	Phosphoserine
+P47083	2	N-acetylserine
+P47083	176	Phosphoserine
+P47083	177	Phosphoserine
+P47083	181	Phosphotyrosine
+Q06211	1294	Phosphothreonine
+Q12205	45	N-linked
+P38069	34	N-linked
+P38069	363	N-linked
+P38069	473	N-linked
+P53129	22	Phosphoserine
+P53129	71	Phosphoserine
+P53379	575	GPI-anchor
+P53379	180	N-linked
+P53379	190	N-linked
+P53379	219	N-linked
+P53379	229	N-linked
+P53379	232	N-linked
+P53379	286	N-linked
+P53379	346	N-linked
+P53379	471	N-linked
+P53379	517	N-linked
+P40577	293	Phosphoserine
+P39106	50	N-linked
+P39106	225	N-linked
+P39106	254	N-linked
+P39106	383	N-linked
+P35724	114	Phosphoserine
+P35724	175	Phosphoserine
+P35724	177	Phosphothreonine
+P35724	182	Phosphoserine
+P35724	383	Phosphoserine
+P35724	571	Phosphothreonine
+P35724	576	Phosphoserine
+P35724	582	Phosphoserine
+P53059	187	N-linked
+P38257	2	N-acetylserine
+P38257	48	Phosphoserine
+P38257	49	Phosphoserine
+P38257	61	Phosphoserine
+P40484	34	Phosphoserine
+P40484	36	Phosphoserine
+P40484	80	Phosphoserine
+P40484	229	Phosphoserine
+P54785	1	N-acetylmethionine
+P41940	153	Phosphothreonine
+P41940	244	Glycyl
+P53725	2	N-acetylserine
+P53725	42	Phosphoserine
+P53725	150	Phosphoserine
+Q08471	268	Phosphoserine
+P32333	93	Phosphoserine
+P32333	677	Phosphoserine
+P53163	34	N-linked
+P32906	96	N-linked
+P32906	155	N-linked
+P32906	224	N-linked
+Q12404	47	N-linked
+Q12404	307	N-linked
+P35728	221	Phosphoserine
+P39016	662	Phosphoserine
+P39016	834	Phosphoserine
+P39016	838	Phosphoserine
+P53045	96	Glycyl
+P33748	288	Phosphoserine
+P33748	304	Phosphoserine
+P33748	451	Phosphoserine
+P33748	582	Phosphoserine
+P33748	633	Phosphoserine
+P40029	58	Phosphoserine
+P40850	358	Phosphoserine
+P40850	362	Phosphoserine
+P40850	371	Phosphoserine
+P40850	4	Glycyl
+P53604	1	N-acetylmethionine
+P53604	102	Phosphoserine
+P20676	2	N-acetylserine
+P20676	54	Phosphoserine
+P20676	161	Phosphoserine
+P20676	381	Phosphothreonine
+P20676	383	Phosphoserine
+P20676	637	Phosphoserine
+Q12454	2	Phosphothreonine
+P31755	203	N-linked
+P31755	281	N-linked
+P31755	341	N-linked
+P31755	393	N-linked
+P38325	12	Phosphoserine
+P38325	15	Phosphoserine
+Q06593	374	N-linked
+Q06593	860	N-linked
+Q06144	9	Phosphoserine
+Q06144	15	Phosphoserine
+Q06144	18	Phosphothreonine
+Q06144	22	Phosphoserine
+Q06144	29	Phosphoserine
+Q06144	51	Phosphoserine
+P43558	160	Glycyl
+P32336	388	Phosphothreonine
+P32336	392	Phosphothreonine
+P32336	417	Phosphoserine
+P32336	419	Phosphoserine
+P32336	357	Glycyl
+P16387	313	Phosphoserine%3B
+Q06810	285	Phosphoserine
+Q06810	348	Phosphoserine
+Q06810	172	N-linked
+Q06810	185	N-linked
+P54784	237	Phosphoserine
+P07991	272	N6-(pyridoxal
+P07991	390	Glycyl
+P16451	73	N6-lipoyllysine
+Q02630	886	Phosphoserine
+P19262	114	N6-lipoyllysine
+P19262	340	Phosphothreonine
+P12695	75	N6-lipoyllysine
+P54790	2	N-acetylserine
+P05150	2	N-acetylserine
+P52593	340	Phosphoserine
+P52593	406	Glycyl
+P21957	10	Phosphoserine
+P54791	9	Phosphoserine
+P38351	147	Phosphoserine
+P38351	422	Phosphothreonine
+Q12033	2	N-acetylserine
+P37304	659	Phosphoserine
+P37304	732	Phosphoserine
+P37304	767	Phosphoserine
+P36102	57	Phosphothreonine
+P36102	252	Phosphoserine
+P53298	70	Phosphoserine
+P28273	930	Phosphoserine
+P28273	1077	Phosphoserine
+P40897	48	Phosphothreonine
+P40897	50	Phosphothreonine
+P40897	51	Phosphothreonine
+P40897	46	N-linked
+P40897	640	N-linked
+P32833	60	Phosphothreonine
+P32833	187	Phosphothreonine
+P32833	188	Phosphoserine
+P32567	110	Phosphoserine
+P32567	114	Phosphoserine
+P32567	168	Phosphoserine
+P32567	511	Phosphoserine
+P32567	602	Phosphoserine%3B
+P32567	723	Phosphothreonine%3B
+P32567	744	Phosphoserine%3B
+P32567	748	Phosphoserine
+P32567	773	Phosphoserine
+P32567	774	Phosphoserine
+P32567	810	Phosphoserine
+P32567	814	Phosphoserine
+P32567	816	Phosphothreonine
+P32567	844	Phosphoserine
+P32567	847	Phosphoserine
+P38826	146	Phosphothreonine
+Q05518	14	Phosphoserine
+Q05518	45	Phosphoserine
+Q05518	47	Phosphothreonine
+Q05518	49	Phosphoserine
+Q05518	64	Phosphoserine
+Q05518	114	Phosphoserine
+Q05518	121	Phosphoserine
+Q05518	153	Phosphothreonine
+Q05518	304	Phosphothreonine
+Q05518	307	Phosphoserine
+Q05518	135	Glycyl
+Q05518	138	Glycyl
+Q05518	292	Glycyl
+Q05518	328	Glycyl
+Q05518	445	Glycyl
+P53179	521	Glycyl
+P48565	409	Phosphoserine
+P32521	241	Phosphothreonine
+P32521	570	Phosphothreonine
+P32521	747	Phosphoserine
+P32521	757	Phosphoserine
+P32521	993	Phosphothreonine
+P32521	995	Phosphothreonine
+P32521	1003	Phosphoserine
+P32521	1180	Phosphoserine
+P32521	1250	Phosphoserine
+P32521	1253	Phosphoserine
+P32521	1281	Phosphoserine
+P32521	1321	Phosphothreonine
+Q12451	2	N-acetylserine
+Q12451	7	Phosphoserine
+Q12451	422	Phosphoserine
+Q12451	445	Phosphoserine
+Q12451	451	Phosphoserine
+Q12451	455	Phosphoserine
+Q12451	458	Phosphoserine
+Q12451	459	Phosphoserine
+Q12451	486	Phosphoserine
+Q12451	488	Phosphothreonine
+Q12451	512	Phosphoserine
+Q12451	515	Phosphoserine
+Q12451	717	Phosphoserine
+Q12451	783	Phosphothreonine
+Q12451	787	Phosphoserine
+Q12451	825	Phosphoserine
+Q12451	1151	Phosphoserine
+Q02201	16	Phosphoserine
+P50946	2	N-acetylthreonine
+P50946	24	Phosphoserine
+P33767	60	N-linked
+P33767	332	N-linked
+P43611	354	Phosphotyrosine
+P32263	246	Phosphothreonine
+P32263	279	Phosphoserine
+P32263	171	Glycyl
+P41543	18	N-linked
+P41543	99	N-linked
+P41543	217	N-linked
+P41543	336	N-linked
+P41543	400	N-linked
+Q08952	1	N-acetylmethionine
+Q08952	178	Phosphoserine
+P40091	230	Phosphoserine
+P40219	102	Phosphoserine
+Q03558	353	Phosphoserine
+Q03558	379	Phosphoserine
+P25644	2	N-acetylserine
+P25644	456	Phosphoserine
+P25644	457	Phosphoserine
+P24867	39	Phosphothreonine%3B
+P24867	43	Phosphoserine%3B
+P24867	82	Glycyl
+P24867	121	Glycyl
+Q08966	32	Phosphoserine
+P15873	127	Glycyl
+P15873	164	Glycyl
+P15873	164	Glycyl
+P26263	2	N-acetylserine
+P26263	223	Phosphoserine
+P26263	266	Phosphothreonine
+P26263	353	Phosphothreonine
+P26263	522	Phosphothreonine
+P26263	212	Glycyl
+P26263	233	Glycyl
+P26263	269	Glycyl
+P26263	505	Glycyl
+P29468	452	Phosphoserine
+P29468	550	Phosphoserine
+Q12515	2	N-acetylalanine
+Q12515	36	Phosphoserine
+Q12515	39	Phosphoserine
+Q12515	47	Phosphoserine
+Q12515	123	Phosphoserine
+Q12515	138	Phosphoserine
+Q12515	141	Phosphoserine
+Q12515	147	Phosphoserine
+Q12515	246	Phosphoserine
+P40186	69	Phosphoserine
+P17967	82	N-linked
+P17967	117	N-linked
+P17967	155	N-linked
+P17967	174	N-linked
+P17967	425	N-linked
+P40530	148	Phosphohistidine%3B
+P12383	21	Phosphoserine
+P12383	930	Phosphoserine
+P12383	942	Phosphoserine
+P12383	948	Phosphoserine
+P33302	22	Phosphoserine
+P33302	49	Phosphothreonine
+P33302	51	Phosphothreonine
+P33302	54	Phosphoserine
+P33302	58	Phosphoserine
+P33302	61	Phosphoserine
+P33302	837	Phosphoserine
+P33302	840	Phosphoserine
+P33302	841	Phosphoserine
+P33302	849	Phosphoserine
+P33302	850	Phosphoserine
+P33302	854	Phosphoserine
+P33302	734	N-linked
+P33302	1447	N-linked
+P33302	825	Glycyl
+P53224	29	Phosphoserine
+P53224	32	Phosphoserine
+P53224	56	Phosphoserine
+P35845	394	Phosphoserine
+P35845	490	Phosphoserine
+P35845	500	Phosphoserine
+P35845	678	Phosphoserine
+P35845	683	Phosphoserine
+P35845	691	Phosphoserine
+P35845	692	Phosphothreonine
+P35845	694	Phosphothreonine
+P35845	708	Phosphoserine
+P35845	712	Phosphoserine
+P38713	190	Phosphoserine
+P38713	193	Phosphoserine
+P38713	210	Phosphothreonine
+P38713	323	Phosphothreonine
+P38713	324	Phosphoserine
+P38713	325	Phosphothreonine
+P38713	352	Phosphothreonine
+P38713	605	Phosphoserine
+P38755	276	Glycyl
+P08018	68	Phosphoserine
+P08018	269	Phosphoserine
+P08018	514	Phosphoserine
+P08018	518	Phosphothreonine
+P13259	16	Phosphoserine
+P13259	59	Phosphothreonine
+P13259	346	Phosphoserine
+P13259	401	Phosphoserine%3B
+Q99220	52	N-linked
+Q99220	74	N-linked
+Q99220	380	N-linked
+P04147	2	N-acetylalanine
+P04147	107	Omega-N-methylarginine
+P04147	249	Phosphoserine
+P04147	332	Phosphoserine
+P04147	405	Phosphoserine
+P04147	7	Glycyl
+P04147	337	Glycyl
+P25580	24	N-linked
+P25580	85	N-linked
+P25580	120	N-linked
+P25580	212	N-linked
+P25580	365	N-linked
+P40038	61	Phosphoserine
+P40038	281	Phosphoserine
+P40038	312	Phosphoserine
+P40038	317	Phosphothreonine
+P40550	595	N-linked
+P40550	1289	N-linked
+P40550	1324	N-linked
+P40550	1346	N-linked
+Q04182	558	N-linked
+Q04182	744	N-linked
+P53756	48	N-linked
+P53756	144	N-linked
+P53756	205	N-linked
+P53756	350	N-linked
+P53756	697	N-linked
+P53756	733	N-linked
+P53756	958	N-linked
+P53756	1320	N-linked
+Q04264	1231	Phosphoserine
+Q04264	1233	Phosphoserine
+P36139	2	N-acetylserine
+P53112	2	N-acetylserine
+P53112	313	Phosphoserine
+P48363	1	N-acetylmethionine
+P38075	29	Glycyl
+P47116	56	Phosphothreonine
+P47116	59	Phosphoserine
+P47116	80	Phosphoserine
+P47116	623	Phosphoserine
+P47116	632	Phosphoserine
+P47116	694	Phosphoserine
+P47116	700	Phosphothreonine
+P47116	711	Phosphoserine
+P47116	737	Phosphothreonine
+P47116	752	Phosphoserine
+P47116	755	Phosphoserine
+P47116	778	Phosphoserine
+P47116	781	Phosphoserine
+P29461	258	Phosphoserine
+P29461	430	Phosphoserine
+P07244	455	Phosphoserine
+P07244	458	Phosphoserine
+P03962	2	N-acetylserine
+P03962	93	Glycyl
+P03962	209	Glycyl
+P03962	253	Glycyl
+P25339	205	Phosphothreonine
+P25339	212	Phosphothreonine
+P25339	252	Phosphothreonine
+P25339	256	Phosphoserine
+Q06991	100	N-linked
+Q06991	209	N-linked
+Q06991	260	Glycyl
+P38972	2	N-acetylthreonine
+P11154	734	N6-carboxylysine
+P11154	1135	N6-biotinyllysine
+P28272	46	Glycyl
+Q12355	419	GPI-anchor
+Q12355	57	N-linked
+Q12355	76	N-linked
+Q12355	83	N-linked
+Q12355	86	N-linked
+Q12355	196	N-linked
+Q12355	210	N-linked
+Q12355	228	N-linked
+Q12355	235	N-linked
+Q12355	242	N-linked
+Q12355	263	N-linked
+Q12355	268	N-linked
+Q12355	280	N-linked
+Q12355	292	N-linked
+Q12355	305	N-linked
+Q12355	329	N-linked
+P39927	272	Phosphoserine
+P27616	2	N-acetylserine
+Q05911	196	Glycyl
+P32641	652	Phosphoserine
+P32641	654	Phosphoserine
+Q00578	752	Phosphoserine
+Q04231	2	N-acetylserine
+Q04231	19	Glycyl
+P22216	24	Phosphoserine
+P22216	175	Phosphoserine
+P22216	547	Phosphoserine
+P22216	560	Phosphoserine
+P22216	774	Phosphoserine
+P22216	793	Phosphoserine
+P06779	64	Phosphoserine
+P06779	85	Phosphoserine
+P32864	470	Phosphoserine
+P25635	225	Phosphoserine
+P25635	232	Phosphoserine
+P25635	651	Phosphoserine
+P25635	664	Phosphoserine
+P25635	912	Phosphoserine
+P25635	913	Phosphoserine
+P34230	33	N-linked
+P34230	39	N-linked
+P34230	162	N-linked
+P34230	230	N-linked
+P34230	241	N-linked
+P34230	267	N-linked
+P34230	295	N-linked
+P34230	560	N-linked
+P34230	608	N-linked
+P34230	620	N-linked
+P34230	647	N-linked
+P34230	836	N-linked
+P32327	2	N-acetylserine
+P32327	735	N6-carboxylysine
+P32327	1136	N6-biotinyllysine
+P13298	213	Phosphoserine
+P13298	225	Phosphoserine
+P06777	613	Phosphoserine
+P06777	1071	Phosphoserine
+P06777	1072	Phosphothreonine
+P32628	94	Phosphothreonine
+P32628	121	Phosphoserine
+P32628	139	Phosphothreonine
+P32628	49	Glycyl
+P53037	1043	Pyruvic
+P31374	10	Phosphoserine
+P31374	192	Phosphoserine
+P31374	202	Phosphoserine
+P31374	255	Phosphoserine
+P31374	286	Phosphoserine
+P31374	327	Phosphoserine
+P31374	926	Phosphoserine
+P31374	1018	Phosphoserine
+P31374	1023	Phosphoserine
+P31374	1035	Phosphoserine
+P31374	1055	Phosphoserine
+P31374	1079	Phosphothreonine
+Q01329	500	Phosphoserine
+Q04373	31	Phosphoserine%3B
+Q04373	34	Phosphoserine
+Q04373	34	Phosphoserine%3B
+Q04373	35	Phosphoserine
+Q04373	35	Phosphoserine%3B
+Q02256	196	Phosphoserine
+P21304	52	Phosphoserine
+P21304	131	Phosphoserine
+P50896	31	Phosphoserine
+P50896	34	Phosphoserine
+P50896	36	Phosphoserine
+P50896	237	Phosphoserine
+P50896	334	Phosphothreonine
+P50896	520	Phosphoserine
+P34222	152	Glycyl
+Q08647	2	N-acetylserine
+P39006	463	Pyruvic
+P25044	83	Phosphoserine%3B
+P40048	75	Phosphothreonine
+P40048	248	Phosphoserine
+P40048	297	Phosphoserine
+P40048	368	Phosphoserine
+P40454	341	Phosphoserine
+P32588	2	N-acetylserine
+Q12221	72	Phosphoserine
+Q12221	198	Phosphoserine
+Q12221	872	Phosphoserine
+Q12221	876	Phosphoserine
+Q07807	83	Phosphothreonine
+Q07807	207	Phosphoserine
+Q07807	210	Phosphoserine
+P21264	37	Phosphoserine
+P41909	142	N-linked
+P41909	281	N-linked
+P41909	403	N-linked
+P36166	43	Phosphoserine
+P36166	63	Phosphoserine
+P53335	230	Phosphoserine
+P10622	2	N-acetylserine
+P10622	96	Phosphoserine
+P36159	824	Phosphoserine
+P51862	2	N-acetylserine
+P51862	76	Phosphoserine
+P51862	193	Phosphoserine
+P51862	223	Phosphoserine
+P51862	566	Phosphoserine
+P51862	628	Phosphoserine
+Q01080	34	Phosphoserine
+Q01080	151	Phosphoserine
+P27999	40	Phosphoserine
+Q02933	37	N-linked
+Q02933	70	N-linked
+Q02933	103	N-linked
+Q02933	123	N-linked
+P10964	889	Phosphoserine
+P10964	1636	Phosphoserine
+P07703	2	N-acetylserine
+P07703	17	Phosphoserine
+P16370	2	N-acetylserine
+Q12250	2	N-acetylserine
+Q06103	8	Phosphoserine
+Q06103	77	Phosphoserine
+P38061	40	Phosphoserine
+P05319	16	Phosphothreonine
+P05319	40	Phosphoserine
+P05319	43	Phosphoserine
+P05319	49	Phosphoserine
+P05319	96	Phosphoserine
+P05319	2	Glycyl
+P05319	48	Glycyl
+P02400	29	Phosphoserine
+P02400	100	Phosphoserine
+P02400	49	Glycyl
+Q12495	78	Phosphothreonine
+Q12495	94	Phosphoserine
+Q12495	509	Phosphothreonine
+Q03195	349	Phosphoserine
+Q12224	120	Phosphoserine
+Q12224	164	Phosphoserine
+Q12224	374	Phosphoserine
+Q12224	377	Phosphoserine
+P36534	2	N-acetylserine
+P43620	2	N-acetylserine
+P0CX26	40	Phosphoserine
+P0CX28	40	N6-methyllysine%3B
+P0CX28	55	N6-methyllysine%3B
+Q02326	2	N-acetylserine
+Q02326	12	Phosphoserine
+Q02326	128	Glycyl
+P05317	68	Phosphoserine
+P05317	302	Phosphoserine%3B
+P05317	14	Glycyl
+P05317	97	Glycyl
+P05317	144	Glycyl
+Q07915	172	Phosphoserine
+P38330	132	Phosphoserine
+P11745	360	Phosphoserine
+P05747	52	Glycyl
+P0CX27	40	N6-methyllysine%3B
+P0CX27	55	N6-methyllysine%3B
+P02406	96	Glycyl
+P0CX85	13	Phosphoserine
+P0CX85	50	Phosphoserine
+P14126	24	Phosphoserine
+P14126	103	Phosphothreonine
+P14126	156	Phosphoserine
+P14126	243	Pros-methylhistidine
+P14126	297	Phosphoserine
+P14126	39	Glycyl
+P14126	136	Glycyl
+P0CH09	76	Glycyl
+P0CH09	93	Glycyl
+P10664	2	N-acetylserine
+Q12487	2	N-acetylserine
+P0CX42	2	N-acetylserine
+P0CX42	106	N6%2CN6-dimethyllysine%3B
+P0CX42	110	N6%2CN6-dimethyllysine%3B
+P04456	61	Glycyl
+P05318	2	N-acetylserine
+P05318	96	Phosphoserine
+P0CH08	76	Glycyl
+P0CH08	93	Glycyl
+P0CX25	40	Phosphoserine
+P26321	167	Phosphoserine
+P26321	176	Phosphoserine
+P26321	235	Phosphoserine
+P26321	164	Glycyl
+P05739	12	Phosphoserine
+P05739	128	Glycyl
+P38144	694	Phosphothreonine
+P38144	846	Phosphoserine
+Q08773	17	Phosphoserine
+Q08773	19	Phosphoserine
+Q08773	831	Phosphoserine
+Q08773	1079	Phosphothreonine
+Q08773	1082	Phosphoserine
+Q03419	79	N-linked
+Q03419	207	N-linked
+P36224	91	Phosphoserine
+P07170	2	N-acetylserine
+P07170	3	N-acetylserine
+Q12055	183	Phosphotyrosine
+Q12055	188	Phosphoserine
+Q12055	196	Phosphoserine
+P06245	1	N-acetylmethionine
+P06245	224	Phosphothreonine
+Q04746	159	N-linked
+Q04746	206	N-linked
+Q04746	313	N-linked
+Q04746	404	N-linked
+P39962	517	S-palmitoyl
+P39962	518	S-palmitoyl
+P39962	519	S-palmitoyl
+P39962	520	S-palmitoyl
+P39962	522	S-palmitoyl
+P39962	523	S-palmitoyl
+P39962	524	S-palmitoyl
+P27466	343	Phosphotyrosine
+P27466	357	Phosphoserine
+P27466	417	Phosphoserine
+P27466	418	Phosphoserine
+P27466	420	Phosphoserine
+P27466	429	Phosphoserine
+P34167	65	Phosphoserine
+P34167	71	Phosphoserine
+P38431	170	Phosphoserine
+P38431	172	Phosphoserine
+P38431	191	Phosphothreonine
+P38431	228	Phosphoserine
+P38431	317	Phosphothreonine
+P38431	397	Phosphoserine
+P53897	32	Phosphoserine
+P53897	64	Phosphoserine
+P50094	125	Phosphoserine
+Q06704	308	Phosphoserine
+Q06704	660	Phosphoserine
+Q06704	827	Phosphoserine
+Q06704	830	Phosphothreonine
+P47031	265	Phosphoserine
+P47031	268	Phosphoserine
+P47031	378	Phosphoserine
+P47031	380	Phosphothreonine
+P47031	383	Phosphoserine
+P47031	392	Phosphoserine
+P32351	24	Phosphothreonine
+P11986	368	Phosphoserine
+P53115	65	Phosphoserine
+P53115	115	Phosphoserine
+P53115	133	Phosphoserine
+P53115	610	Phosphoserine
+P07278	3	Phosphoserine
+P07278	4	Phosphoserine
+P07278	9	Phosphoserine
+P07278	68	Phosphoserine
+P07278	70	Phosphoserine
+P07278	74	Phosphoserine
+P07278	77	Phosphoserine
+P07278	79	Phosphoserine
+P07278	81	Phosphoserine
+P07278	83	Phosphoserine
+P07278	84	Phosphoserine
+P07278	129	Phosphothreonine
+P07278	130	Phosphoserine
+P07278	131	Phosphothreonine
+P07278	144	Phosphothreonine
+P07278	145	Phosphoserine%3B
+P07278	147	Phosphoserine
+P07278	150	Phosphothreonine
+P07278	160	Phosphothreonine
+P23292	2	N-acetylserine
+P23292	455	Phosphoserine
+P23292	545	S-palmitoyl
+P23292	546	S-palmitoyl
+P23292	465	Glycyl
+P19158	635	Phosphothreonine
+P30605	12	Phosphothreonine
+P30605	26	Phosphoserine
+P30605	31	Phosphoserine
+P30605	35	Phosphoserine
+P30605	37	Phosphoserine
+P30605	46	Phosphoserine
+P30605	371	N-linked
+P30605	573	Glycyl
+Q07959	45	N-linked
+Q07959	123	N-linked
+Q07959	153	N-linked
+Q07959	256	N-linked
+Q07959	319	N-linked
+P53863	393	Phosphoserine
+P53863	504	Phosphothreonine
+P22517	316	Phosphothreonine%3B
+P22517	353	Phosphotyrosine
+P22517	354	Phosphoserine
+P22517	367	Phosphoserine
+P22517	371	Phosphoserine
+P22517	387	Phosphoserine%3B
+P22517	443	Phosphoserine
+Q12494	150	Phosphoserine
+Q12494	396	Phosphoserine
+Q12494	469	Phosphoserine
+Q12494	537	Phosphoserine
+Q12494	539	Phosphoserine
+Q12494	566	Phosphoserine
+Q12494	583	Phosphoserine
+Q12494	589	Phosphoserine
+Q12494	646	Phosphoserine
+Q12494	664	Phosphoserine
+Q12494	670	Phosphoserine
+Q06142	2	N-acetylserine
+Q06142	836	Phosphoserine
+P32337	2	N-acetylserine
+P32337	830	Phosphothreonine
+P53067	1	N-acetylmethionine
+P47135	129	Phosphoserine
+P47135	131	Phosphothreonine
+P47135	160	Phosphoserine
+P47135	168	Phosphoserine
+P47135	913	Phosphoserine
+Q02932	2	N-acetylalanine
+P01094	1	N-acetylmethionine
+P53877	388	Phosphoserine
+P18963	497	Phosphoserine
+P18963	915	Phosphoserine
+P18963	1342	Phosphoserine
+P18963	1753	Phosphoserine%3B
+P18963	3004	Phosphoserine%3B
+P47056	74	N-linked
+P47056	104	N-linked
+P00817	65	Phosphothreonine
+P00817	251	Phosphothreonine
+P00817	266	Phosphoserine
+P00817	286	Phosphoserine
+P00817	239	Glycyl
+P00817	279	Glycyl
+Q12280	264	Phosphothreonine
+Q12280	268	Phosphoserine
+Q12280	299	Phosphothreonine
+P32488	119	Phosphoserine
+Q07532	2	N-acetylserine
+P33417	532	Phosphoserine
+P0CT04	74	Phosphothreonine
+P36115	180	Phosphoserine
+Q12358	52	Phosphoserine
+P05986	15	Phosphoserine
+P05986	55	Phosphoserine
+P11927	233	Phosphothreonine
+P32526	496	Phosphoserine
+P23291	522	Phosphoserine
+P23291	523	Phosphoserine
+P23291	527	Phosphoserine
+P23291	537	S-palmitoyl
+P23291	538	S-palmitoyl
+P35844	370	Phosphothreonine
+P35844	389	Phosphoserine
+P13134	42	N-linked
+P13134	163	N-linked
+P13134	404	N-linked
+P13134	480	N-linked
+P38692	735	Phosphoserine
+P38991	5	Phosphoserine%3B
+P38991	76	Phosphoserine
+P38991	260	Phosphothreonine%3B
+P38250	638	Phosphoserine
+P38250	701	Phosphothreonine
+P38250	704	Phosphoserine
+P38250	720	Phosphoserine
+P38250	726	Phosphothreonine
+P38250	729	Phosphoserine
+P38250	730	Phosphotyrosine
+P38250	757	Phosphoserine
+P38250	793	Phosphoserine
+P38250	844	Phosphoserine
+P38250	847	Phosphoserine
+P38250	850	Phosphothreonine
+P25389	396	Phosphoserine
+P25389	675	Phosphoserine
+P25389	707	Phosphoserine
+P25389	777	Phosphoserine
+P25389	822	Phosphoserine
+P25389	825	Phosphoserine
+P25389	871	Phosphoserine
+P17423	133	Glycyl
+P13185	534	Phosphoserine
+P13185	593	Phosphoserine
+P13185	646	Phosphoserine
+P13185	764	Phosphoserine
+P13185	986	Phosphoserine
+P06242	162	Phosphothreonine%3B
+P24583	226	Phosphoserine
+P24583	761	Phosphoserine
+Q06505	15	Phosphothreonine
+Q06505	23	Phosphoserine%3B
+Q06505	40	Phosphoserine
+Q06505	85	Phosphoserine
+Q06505	86	Phosphothreonine
+Q06505	89	Phosphoserine
+Q03361	48	Phosphoserine
+Q03361	51	Phosphoserine
+Q03361	360	Phosphoserine
+Q03361	510	Phosphoserine
+Q03361	552	Phosphoserine
+Q03361	577	Phosphoserine
+Q03361	775	Phosphoserine
+P00549	2	N-acetylserine
+P00549	9	Phosphoserine
+P00549	16	Phosphoserine
+P00549	31	Phosphothreonine
+P00549	70	Phosphoserine
+P00549	184	Phosphothreonine
+P00549	213	Phosphoserine
+P00549	316	Phosphoserine
+P00549	450	Phosphoserine
+P00549	478	Phosphothreonine
+P00549	204	Glycyl
+P00549	255	Glycyl
+P00549	446	Glycyl
+P14681	183	Phosphothreonine
+P14681	185	Phosphotyrosine
+P50090	455	Phosphothreonine
+P50090	509	Phosphoserine
+P13186	22	Phosphoserine
+P13186	146	Phosphoserine
+P13186	549	Phosphoserine
+P13186	609	Phosphoserine
+P13186	888	Phosphoserine
+Q01919	365	Phosphoserine
+Q01919	388	Phosphoserine
+Q01919	521	Phosphoserine
+Q01919	748	Phosphoserine
+P52489	24	Phosphoserine
+P42846	177	Phosphoserine
+P42846	184	Phosphoserine
+P42846	185	Phosphoserine
+P42846	486	Phosphoserine
+P54070	82	N-linked
+P54070	98	N-linked
+Q06554	2	N-acetylserine
+Q06554	810	Phosphoserine
+P32361	840	Phosphoserine%3B
+P32361	841	Phosphoserine%3B
+P32361	111	N-linked
+P32361	213	N-linked
+P32361	298	N-linked
+P32361	397	N-linked
+P30606	394	N-linked
+Q04934	59	Phosphoserine
+Q04934	84	Phosphoserine
+Q04934	85	Phosphoserine
+Q04934	335	Phosphoserine
+P36035	2	N-acetylserine
+P36035	4	Phosphoserine
+P36035	11	Phosphoserine
+P36035	61	Phosphoserine
+P36035	66	Phosphoserine
+P36035	70	Phosphothreonine
+P36035	584	Phosphoserine
+P36035	603	Phosphoserine
+P36035	606	Phosphoserine
+P36035	9	Glycyl
+P36035	338	Glycyl
+P46997	229	Phosphoserine
+P06244	2	N-acetylserine
+Q07551	123	Phosphoserine
+Q08979	47	Phosphoserine
+Q04066	9	Phosphoserine
+P38853	20	Phosphoserine
+P38853	23	Phosphoserine
+P38853	25	Phosphoserine
+P38853	94	Phosphoserine
+P38853	467	Phosphothreonine
+P38853	477	Phosphothreonine
+P38853	503	Phosphoserine
+P38853	604	Phosphothreonine
+P38853	613	Phosphoserine
+P38853	626	Phosphothreonine
+P38853	689	Phosphoserine
+P38853	691	Phosphoserine
+P38853	717	Phosphoserine
+P38853	748	Phosphoserine
+P38853	837	Phosphoserine
+P38853	848	Phosphoserine
+P38853	958	Phosphoserine
+P38853	997	Phosphoserine
+P38853	1003	Phosphoserine
+P38853	1022	Phosphoserine
+P40309	557	Phosphoserine
+P40309	562	Glycyl
+P25341	203	Phosphoserine
+P40504	89	N-linked
+P40504	144	N-linked
+P09620	660	Phosphoserine
+P09620	81	N-linked
+P09620	459	N-linked
+P09620	467	N-linked
+P15454	2	N-acetylserine
+P15454	149	Phosphoserine
+P15454	157	Phosphotyrosine
+P17260	288	GPI-anchor
+P38691	416	Phosphoserine
+P38691	419	Phosphoserine
+P38691	501	Phosphothreonine
+P38691	504	Phosphothreonine
+P38691	526	Phosphothreonine
+P38691	529	Phosphoserine
+P38691	646	Phosphoserine
+P38691	845	Phosphoserine
+P38691	884	Phosphoserine
+P38691	1005	Phosphothreonine
+P38691	1014	Phosphoserine
+P38800	66	Phosphothreonine
+P38800	747	Phosphoserine
+P20485	30	Phosphoserine%3B
+P20485	48	Phosphoserine
+P20485	51	Phosphoserine
+P20485	54	Phosphothreonine
+P20485	85	Phosphoserine%3B
+P22023	115	N-linked
+P22023	228	N-linked
+P22023	293	N-linked
+P22023	457	N-linked
+P22023	519	N-linked
+P22023	523	N-linked
+P22023	644	N-linked
+P22023	870	N-linked
+P22023	1091	N-linked
+P22023	1150	N-linked
+P22023	1195	N-linked
+P33550	65	N-linked
+P33550	81	N-linked
+P33550	92	N-linked
+P33550	167	N-linked
+P43560	110	Phosphothreonine
+P43560	113	Phosphoserine
+P43560	140	Phosphoserine
+P43560	143	Phosphothreonine
+P43560	149	Phosphoserine
+P36004	19	Phosphoserine
+P36004	232	Phosphoserine
+P36004	238	Phosphoserine
+P36004	241	Phosphoserine
+P32350	562	Phosphothreonine
+P32895	199	Phosphoserine
+P32895	218	Phosphoserine
+P32895	271	Phosphoserine
+P32895	295	Phosphoserine
+P40970	366	N6-(pyridoxal
+P39002	2	N-acetylserine
+P40079	2	N-acetylserine
+P25587	180	Phosphothreonine
+P25587	184	Phosphothreonine
+P25587	241	Phosphoserine
+Q02799	21	Phosphoserine
+Q02799	30	Phosphoserine
+Q02799	282	Phosphoserine
+P53281	2	N-acetylserine
+P53281	48	Phosphoserine
+P53281	114	Phosphoserine
+P53281	116	Phosphoserine
+P53281	41	Glycyl
+P53281	79	Glycyl
+P53281	118	Glycyl
+P53281	219	Glycyl
+P42838	36	Phosphoserine
+P42838	113	N-linked
+P42838	240	N-linked
+P42838	256	N-linked
+P42838	279	N-linked
+P42838	298	N-linked
+P42838	332	N-linked
+Q12265	119	Phosphotyrosine
+Q12265	120	Phosphothreonine
+Q12265	123	Phosphoserine
+Q12265	127	Phosphothreonine
+Q12265	183	Phosphoserine
+Q12265	332	Phosphoserine
+P27810	120	N-linked
+Q92325	16	Glycyl
+Q12446	334	Phosphothreonine
+Q12446	337	Phosphoserine
+Q12446	588	Phosphoserine
+P07264	488	Phosphoserine
+P07264	494	Phosphothreonine
+P07264	495	Phosphoserine
+P53966	86	N-linked
+P32807	370	Phosphoserine
+P32807	371	Phosphoserine
+P32807	372	Phosphoserine
+P25045	121	Phosphothreonine
+Q06147	91	S-palmitoyl
+Q06147	94	S-palmitoyl
+P36016	128	N-linked
+P36016	458	N-linked
+P36016	474	N-linked
+P36016	481	N-linked
+P36016	489	N-linked
+P36016	527	N-linked
+P36016	844	N-linked
+P40026	81	Phosphoserine
+P40026	101	Phosphoserine
+P27809	197	N-linked
+P30624	189	Glycyl
+P32486	81	Phosphoserine
+P32486	116	Phosphoserine
+P32486	133	Phosphoserine
+P32486	134	Phosphoserine
+P32486	136	Phosphoserine
+P32486	139	Phosphoserine
+P32486	374	N-linked
+P32486	461	N-linked
+P32486	538	N-linked
+P32486	563	N-linked
+P32486	691	N-linked
+P33399	2	N-acetylserine
+P33399	15	Phosphoserine
+P33399	19	Phosphoserine
+P33399	104	Omega-N-methylarginine
+P33399	230	Phosphoserine
+P33399	233	Phosphoserine
+P33399	235	Phosphoserine
+Q05979	252	N6-(pyridoxal
+P28496	2	N-acetylserine
+P28496	23	Phosphoserine
+P28496	24	Phosphoserine
+P28496	103	N-linked
+P38703	23	Phosphoserine
+P38703	24	Phosphoserine
+P38703	103	N-linked
+P38851	1205	N-linked
+Q08001	343	Phosphothreonine
+Q08001	591	Phosphoserine
+Q08001	593	Phosphothreonine
+Q08001	594	Phosphoserine
+Q08001	597	Phosphoserine
+Q04377	10	Phosphoserine
+Q04377	11	Phosphoserine
+Q04377	76	Phosphoserine
+Q02786	81	GPI-anchor
+P38439	105	Phosphoserine
+P38439	132	Phosphoserine
+P38439	188	Phosphoserine
+P38439	358	Phosphoserine
+P38439	372	Phosphoserine
+Q12342	7	Phosphoserine
+Q12342	463	Phosphoserine
+Q12342	466	Phosphoserine
+P47055	42	N-linked
+P47055	62	N-linked
+P47055	136	N-linked
+P25579	393	Phosphoserine
+P25579	398	Phosphoserine
+P25579	516	Phosphoserine
+P25579	552	Phosphoserine
+P43586	24	Phosphoserine
+P35688	1	N-acetylmethionine
+P35688	562	Phosphoserine
+P40495	98	Phosphoserine
+Q04087	168	Phosphoserine
+Q04087	230	Phosphoserine
+P43603	227	Phosphoserine
+P43603	298	Phosphothreonine
+P43603	300	Phosphoserine
+P43603	303	Phosphoserine
+P43603	393	Phosphothreonine
+P43603	397	Phosphoserine
+P43603	402	Phosphoserine
+P43603	416	Phosphoserine
+Q12230	233	Phosphothreonine
+P22134	110	Phosphoserine
+Q12176	2	N-acetylserine
+Q12176	62	Phosphoserine
+Q12176	73	Phosphoserine
+Q12176	80	Phosphoserine
+Q12176	275	Phosphoserine
+Q12176	708	Phosphotyrosine
+Q12176	710	Phosphoserine
+Q12176	874	Phosphoserine
+Q12176	878	Phosphoserine
+Q12176	977	Phosphoserine
+Q12176	978	Phosphoserine
+Q12176	1024	Phosphoserine
+Q12246	111	Phosphoserine
+Q12246	120	Phosphoserine
+Q12246	154	Phosphoserine
+Q12246	160	Phosphoserine
+Q12246	451	Phosphoserine%3B
+Q12246	454	Phosphoserine
+Q12246	455	Phosphoserine%3B
+Q12246	460	Phosphoserine
+Q12246	43	S-palmitoyl
+Q12246	46	S-palmitoyl
+Q12246	148	Glycyl
+Q12502	93	Phosphothreonine
+Q12502	384	Phosphoserine
+Q12502	619	Phosphothreonine
+Q12502	808	Phosphoserine
+Q12502	486	Glycyl
+Q02783	202	N-linked
+P32487	64	Phosphoserine
+P32487	75	Phosphoserine
+P32487	77	Phosphothreonine
+P32487	79	Phosphoserine
+P32487	87	Phosphoserine
+P32487	90	Phosphothreonine
+P32487	54	Glycyl
+P38828	2	N-acetylserine
+P53048	523	N-linked
+Q01662	2	N-acetylserine
+P38174	35	Phosphoserine
+P34239	401	Phosphoserine
+P07866	271	Phosphoserine
+P07866	559	Phosphoserine
+P07866	689	Phosphoserine
+P07866	691	Phosphothreonine
+P07866	808	Phosphoserine
+P07866	810	Phosphoserine
+P07866	1028	Phosphoserine
+P07866	1109	Phosphoserine
+Q07508	2	N-acetylserine
+P35192	143	Phosphoserine
+P47074	268	Phosphoserine
+P41910	90	Phosphoserine
+P41910	209	Phosphoserine
+P41910	210	Phosphoserine
+P41910	347	Phosphothreonine
+Q07376	255	Phosphoserine
+Q07376	60	N-linked
+Q07376	131	N-linked
+Q07376	194	N-linked
+P36032	72	N-linked
+Q08777	125	N-linked
+Q08777	194	N-linked
+Q08777	419	N-linked
+Q06675	88	Phosphothreonine
+P11746	2	N-acetylserine
+P11746	2	Phosphoserine
+P11746	144	Phosphoserine
+P17505	177	Phosphoserine
+P17505	199	Phosphothreonine
+P53145	103	Phosphoserine
+P34078	2	N-acetylserine
+P34078	288	Phosphoserine
+P34078	293	Phosphoserine
+P34078	299	Phosphoserine
+P34078	303	Phosphoserine
+P40957	502	Phosphothreonine
+P20484	2	N-acetylserine
+P20484	376	Phosphoserine
+P20484	380	Phosphoserine
+P20484	382	Phosphothreonine
+P38112	135	Phosphothreonine
+P38112	138	Phosphoserine
+P38112	678	Phosphoserine
+P36007	53	N6-(pyridoxal
+P22855	2	N-acetylserine
+Q92328	49	Glycyl
+P38295	114	Glycyl
+P29469	14	Phosphoserine
+P29469	16	Phosphoserine
+P29469	23	Phosphoserine
+P29469	164	Phosphoserine
+P29469	170	Phosphoserine
+P30665	52	Phosphoserine
+P30665	56	Phosphoserine
+P30665	69	Phosphoserine
+P53091	78	Phosphoserine
+P53091	249	Phosphoserine
+P53091	372	Phosphoserine
+P53091	766	Phosphothreonine
+P38132	811	Phosphothreonine
+P38132	819	Phosphoserine
+P38132	838	Phosphoserine
+Q12198	376	N6-(pyridoxal
+Q99257	2	N-acetylserine
+P34166	35	Cysteine
+P34166	35	S-farnesyl
+P40578	255	Phosphoserine
+P40578	467	Phosphoserine
+P43638	1	N-acetylmethionine
+P43638	81	Phosphoserine
+P43638	222	Phosphothreonine
+P43638	309	Phosphoserine
+P43638	311	Phosphoserine
+P43638	354	Phosphoserine
+P43638	357	Phosphoserine
+P43638	577	Phosphothreonine
+P43638	221	Glycyl
+Q12019	1026	Phosphothreonine
+Q12019	2971	Phosphoserine
+Q12019	4353	Phosphoserine
+Q12019	4388	Phosphothreonine
+Q12019	4555	Phosphoserine
+P34165	33	Cysteine
+P34165	33	S-farnesyl
+P40002	152	Phosphoserine
+P32490	192	Phosphoserine
+P53141	116	Glycyl
+P38998	2	N-acetylalanine%3B
+P07702	880	O-(pantetheine
+P07702	541	Glycyl
+P07702	1276	Glycyl
+O14467	143	Phosphoserine
+P19659	2	N-acetylserine
+P19659	335	Phosphoserine
+P19659	736	Phosphoserine
+P19659	752	Phosphoserine
+P19659	783	Phosphoserine
+P19659	785	Phosphoserine
+P19659	789	Phosphoserine
+P19659	793	Phosphothreonine
+P19659	831	Phosphoserine
+P19659	1003	Phosphoserine
+P19659	1008	Phosphoserine
+P19659	1018	Phosphoserine
+P19659	1034	Phosphoserine
+Q02205	146	Phosphoserine
+Q02205	149	Phosphoserine
+Q02205	2	N-myristoyl
+Q02205	7	S-palmitoyl
+Q02205	8	S-palmitoyl
+P33441	266	Phosphoserine
+P35201	325	Phosphoserine
+P27705	278	Phosphoserine
+P27705	302	Phosphoserine
+P27705	310	Phosphoserine
+P27705	311	Phosphoserine
+P27705	314	Phosphoserine
+P27705	377	Phosphoserine
+Q06820	42	Phosphoserine
+Q02574	452	Phosphoserine
+Q12321	155	Phosphoserine
+Q12321	423	Phosphoserine
+P32570	2	N-acetylserine
+P43623	208	N6-(pyridoxal
+Q04533	287	Phosphoserine
+Q04533	451	N6-(pyridoxal
+P36027	260	Phosphoserine
+P36027	327	Phosphoserine
+P36027	329	Phosphoserine
+P36027	355	Phosphoserine
+P36027	35	N-linked
+P36027	211	N-linked
+Q02455	2	N-acetylserine
+Q02455	337	Phosphothreonine
+Q02455	379	Phosphoserine
+Q02455	1670	Phosphoserine
+Q02455	1710	Phosphoserine
+Q02455	1733	Phosphoserine
+Q02455	1803	Phosphoserine
+P32354	17	Phosphothreonine
+P32354	18	Phosphoserine
+P32354	453	Phosphoserine
+P32354	454	Phosphoserine
+P22133	6	Phosphothreonine
+P53094	472	Phosphoserine
+P53094	475	Phosphoserine
+P53094	621	Phosphoserine
+P53094	639	Phosphoserine
+P53094	693	Phosphoserine
+P53094	698	Phosphoserine
+P53094	744	Phosphoserine
+P53094	747	Phosphoserine
+P53094	756	Phosphoserine
+P53094	757	Phosphoserine
+P53094	781	Phosphoserine
+P53094	785	Phosphothreonine
+P53094	787	Phosphoserine
+P53094	900	Phosphoserine
+P53094	904	Phosphoserine
+P53094	930	Phosphothreonine
+P53094	1187	Phosphoserine
+P47025	376	Phosphoserine
+P19263	2	N-acetylthreonine
+P19263	7	Phosphoserine
+P19263	1036	Phosphothreonine
+P39014	67	Phosphoserine
+P47164	443	N6-(pyridoxal
+P19358	2	N-acetylserine
+P36051	90	N-linked
+P36051	138	N-linked
+P36051	198	N-linked
+P36051	202	N-linked
+P36051	286	N-linked
+P36051	312	N-linked
+P21965	2	N-acetylserine
+P21965	198	Phosphoserine
+P21965	199	Phosphotyrosine
+P21965	202	Phosphoserine
+P24279	761	Phosphoserine
+P24279	777	Phosphoserine
+P24279	781	Phosphoserine
+P24279	868	Phosphothreonine
+Q12343	2	N-acetylserine
+Q12343	237	Phosphothreonine%3B
+Q12343	242	Phosphoserine
+P40513	91	Phosphothreonine
+Q12296	439	Phosphoserine
+Q12296	447	Phosphoserine
+Q12296	527	Phosphoserine
+Q12296	603	Phosphoserine
+Q12296	604	Phosphotyrosine
+Q12296	607	Phosphothreonine
+Q12296	614	Phosphoserine
+P39678	110	Phosphoserine
+P39678	325	Phosphothreonine
+P39678	326	Phosphoserine
+P39678	330	Phosphoserine
+P39678	827	Phosphoserine
+P23493	159	Phosphothreonine
+P23493	177	Phosphoserine
+P23493	224	Phosphoserine
+P23493	227	Phosphoserine
+P36060	278	Phosphoserine
+P53885	160	Phosphoserine
+P53885	216	Phosphothreonine
+P53885	288	Phosphoserine
+P53885	314	Glycyl
+Q12124	6	Phosphoserine
+Q12124	208	Phosphoserine%3B
+P40260	442	Phosphoserine
+P40260	445	Phosphoserine
+P32389	416	Phosphoserine
+P32389	564	Phosphoserine
+Q08268	131	N-linked
+Q08268	54	Glycyl
+Q01846	670	Phosphoserine
+Q01846	673	Phosphoserine
+Q01846	692	Phosphoserine
+P40356	1	N-acetylmethionine
+P38782	225	Phosphoserine
+P41948	4	N-linked
+P38849	32	N-linked
+P38849	60	N-linked
+P38849	80	N-linked
+P38849	89	N-linked
+P38849	156	N-linked
+P38849	171	N-linked
+P38849	175	N-linked
+P38849	202	N-linked
+P38849	240	N-linked
+P38849	259	N-linked
+P38849	311	N-linked
+P38849	362	N-linked
+P38849	433	N-linked
+P0CX81	30	Glycyl
+P36006	357	Phosphoserine
+P47018	273	Phosphoserine
+P47018	436	Phosphoserine
+P53176	3	Phosphothreonine
+P36084	49	Phosphoserine
+P39552	3	Phosphothreonine
+P0CY08	1	N-acetylmethionine
+P38335	85	Phosphoserine
+P38335	263	Phosphothreonine
+P38335	481	Phosphoserine
+P38335	491	Phosphoserine
+P38335	493	Phosphotyrosine
+P46151	120	Phosphoserine
+P46151	301	Phosphoserine
+P46151	358	Phosphoserine
+Q06489	2	N-acetylserine
+Q06489	351	Phosphoserine
+Q06106	220	Phosphoserine
+Q06106	264	Phosphoserine
+Q12117	289	Phosphoserine
+Q12117	295	Phosphothreonine
+Q12117	299	Phosphoserine
+P50873	13	Phosphoserine
+P35719	23	Phosphoserine
+P35719	137	Glycyl
+P50276	552	Phosphothreonine
+P50276	573	Phosphoserine
+P50276	28	Glycyl
+P38994	207	Phosphoserine
+P38994	222	Phosphothreonine
+P38994	225	Phosphoserine
+P38994	659	Phosphothreonine
+P38994	661	Phosphoserine
+Q02642	151	Phosphothreonine
+P25588	144	Phosphoserine
+P25588	409	Phosphoserine
+P25588	411	Phosphoserine
+P25588	434	Phosphoserine
+P25588	605	Phosphoserine
+P25588	607	Phosphoserine
+P25588	609	Phosphothreonine
+P25588	801	Phosphoserine
+P25588	807	Phosphoserine
+P25588	911	Phosphoserine
+Q06815	335	Phosphoserine
+Q06815	339	Phosphoserine
+Q06815	342	Phosphoserine
+Q06815	371	Phosphoserine
+Q06815	380	Phosphoserine
+Q06815	116	N-linked
+Q06815	136	N-linked
+Q06815	178	N-linked
+Q06815	215	N-linked
+P36157	157	Phosphoserine
+P36157	292	Phosphoserine
+P32334	1300	Phosphoserine
+P32334	30	N-linked
+P32334	859	N-linked
+P32334	885	N-linked
+P32334	945	N-linked
+P32334	1049	N-linked
+P32334	1088	N-linked
+P32334	1175	N-linked
+P38694	15	N-linked
+P38694	565	N-linked
+P38694	627	N-linked
+P34232	125	Phosphothreonine
+P48563	2	N-acetylalanine
+P48563	564	Phosphoserine
+P48563	567	Phosphoserine
+P48563	571	Phosphoserine
+Q05812	57	Phosphoserine
+Q05812	64	Phosphoserine
+Q05812	127	Phosphoserine
+Q05812	151	Phosphoserine
+Q05812	155	Phosphoserine
+Q05812	363	Phosphoserine
+Q05812	646	Phosphothreonine
+Q05812	660	Phosphoserine
+P53214	481	Phosphoserine
+P53214	482	Phosphoserine
+P29952	2	N-acetylserine
+P29952	107	Phosphoserine
+P10507	243	Phosphoserine
+P21339	538	Phosphoserine
+P21339	776	Phosphoserine
+P21339	816	Phosphoserine
+Q03104	237	Phosphothreonine
+Q03104	243	Phosphoserine
+P38590	22	Phosphoserine
+P38590	98	Phosphoserine
+P38590	151	Phosphoserine
+P38590	178	Phosphothreonine
+Q03834	102	Phosphoserine
+Q03834	145	Phosphoserine
+Q03834	150	Phosphoserine
+Q03834	201	Phosphoserine
+Q03834	451	Phosphothreonine
+P33749	1	N-acetylmethionine
+P33749	178	Phosphoserine
+P33749	263	Phosphoserine
+P33749	316	Phosphoserine
+P33749	319	Phosphoserine
+P33749	479	Phosphothreonine
+P33749	558	Phosphoserine
+P47047	34	Phosphothreonine
+P47047	84	Phosphoserine
+P47047	843	Phosphoserine
+Q08750	285	N-linked
+P19524	2	N-acetylserine
+P19524	1097	Phosphothreonine
+P19524	1121	Phosphoserine
+P16603	666	Glycyl
+Q06389	2	N-myristoyl
+P0CX80	30	Glycyl
+Q04439	357	Phosphoserine
+Q04439	359	Phosphotyrosine
+Q04439	777	Phosphoserine
+Q04439	992	Phosphoserine
+Q04439	1205	Phosphoserine
+Q12387	2	N-acetylserine
+P12945	2	N-acetylserine
+P12945	674	Phosphoserine
+P52919	251	Phosphoserine
+P52919	260	Phosphoserine
+Q12163	102	Phosphoserine
+Q12163	196	Phosphoserine
+Q12163	235	Phosphoserine
+Q12374	29	Phosphoserine
+Q02866	67	Phosphoserine
+Q02866	163	Phosphoserine
+Q02866	185	Phosphoserine
+Q02866	245	Phosphoserine
+P25293	20	Phosphothreonine
+P25293	24	Phosphothreonine
+P25293	27	Phosphoserine
+P25293	53	Phosphothreonine
+P25293	69	Phosphoserine
+P25293	76	Phosphoserine
+P25293	82	Phosphoserine
+P25293	98	Phosphoserine
+P25293	104	Phosphoserine
+P25293	140	Phosphoserine
+P25293	159	Phosphoserine%3B
+P25293	177	Phosphoserine%3B
+P25293	397	Phosphoserine%3B
+P25293	50	Glycyl
+P42939	1	N-acetylmethionine
+P42939	94	Phosphoserine
+Q03735	2	N-acetylserine
+Q03735	464	Phosphoserine
+Q03735	467	Phosphoserine
+P53919	255	Phosphoserine
+P30771	56	Phosphoserine
+P30771	869	Phosphoserine
+Q08229	138	Phosphoserine
+Q08229	208	Phosphoserine
+Q08229	403	Phosphothreonine
+P38205	426	Phosphothreonine
+P38205	431	Phosphoserine
+P38205	667	Phosphoserine
+P38996	86	Phosphothreonine
+P38996	451	Phosphothreonine
+P38879	2	N-acetylserine
+P38879	93	Phosphoserine
+Q08887	319	Phosphothreonine%3B
+P36010	95	Phosphothreonine
+P25374	299	N6-(pyridoxal
+Q99271	568	Phosphoserine
+Q99271	765	Phosphothreonine
+Q99271	768	Phosphoserine
+Q99271	774	Phosphoserine
+P53914	1001	Phosphoserine
+P53914	1007	Phosphoserine
+P53914	1010	Phosphoserine
+P40096	27	Phosphoserine
+P40096	141	Phosphoserine
+P32500	401	Phosphoserine
+P32500	412	Phosphoserine
+P40460	38	Phosphothreonine
+P40460	248	Phosphothreonine
+P32831	1	N-acetylmethionine
+P32831	524	Phosphoserine
+P39744	70	Phosphoserine
+P39744	149	Phosphoserine
+P39744	160	Phosphoserine
+P39744	166	Phosphoserine
+P39744	698	Phosphoserine
+P39744	708	Phosphoserine
+P25353	161	N-linked
+P25353	204	N-linked
+P25353	264	N-linked
+P25353	296	N-linked
+P25353	403	N-linked
+P53718	145	Phosphoserine
+Q08485	560	Phosphoserine
+Q08485	572	Phosphoserine
+P53898	90	Phosphoserine
+Q12457	64	Phosphothreonine
+P36059	6	Phosphoserine
+P48234	529	Phosphoserine
+P48234	550	Phosphoserine
+P48234	555	Phosphoserine
+Q07623	45	Phosphoserine
+Q07623	160	Phosphoserine
+P27476	353	Asymmetric
+P27476	362	Asymmetric
+P27476	366	Asymmetric
+P27476	375	Asymmetric
+P27476	379	Asymmetric
+P27476	382	Asymmetric
+Q08214	194	Glycyl
+Q03210	62	Phosphoserine
+Q04121	490	Phosphothreonine
+Q04121	494	Phosphoserine
+Q04121	498	Phosphothreonine
+Q04121	499	Phosphoserine
+Q04121	569	Phosphoserine
+Q04121	420	N-linked
+Q04121	515	N-linked
+Q04121	550	N-linked
+Q04121	563	N-linked
+P32770	345	Phosphoserine
+P32770	455	Phosphoserine
+P32770	630	Phosphoserine
+P37838	247	Phosphoserine
+P37838	379	Phosphothreonine
+Q12080	31	Phosphoserine
+P22211	47	Phosphoserine%3B
+P22211	85	Phosphoserine
+P22211	90	Phosphoserine
+P22211	100	Phosphoserine
+P22211	111	Phosphoserine
+P22211	116	Phosphoserine
+P22211	125	Phosphoserine
+P22211	137	Phosphoserine
+P22211	141	Phosphoserine
+P22211	257	Phosphoserine%3B
+P22211	259	Phosphoserine
+P22211	260	Phosphoserine
+P22211	288	Phosphoserine
+P22211	292	Phosphoserine
+P22211	317	Phosphoserine
+P22211	320	Phosphoserine
+P22211	328	Phosphoserine
+P22211	334	Phosphotyrosine
+P22211	336	Phosphoserine
+P22211	353	Phosphoserine
+P22211	356	Phosphoserine
+P22211	357	Phosphoserine%3B
+P22211	385	Phosphoserine
+P53935	266	Phosphoserine
+Q12311	728	Phosphoserine
+Q02629	763	Phosphoserine
+Q02629	783	Phosphoserine
+Q92317	135	Phosphoserine
+Q92317	137	Phosphoserine
+Q92317	142	Phosphoserine
+P49954	34	Phosphothreonine
+Q06178	91	Phosphoserine
+Q06178	95	Phosphoserine
+Q06178	96	Phosphoserine
+Q06178	111	Phosphoserine
+P46970	977	Phosphoserine
+P53939	260	Phosphoserine
+P53939	264	Phosphoserine
+P53939	300	Phosphoserine
+P53939	302	Phosphoserine
+P34909	310	Phosphothreonine
+P34909	312	Phosphoserine
+P34909	326	Phosphothreonine
+P34909	360	Phosphoserine
+P34909	270	Glycyl
+P32494	134	Phosphoserine
+P32494	407	Phosphoserine
+P32494	464	Phosphothreonine
+Q6Q547	36	Phosphoserine
+Q6Q547	28	Glycyl
+Q01560	182	Phosphoserine
+Q01560	224	Phosphoserine
+Q12499	281	Glycyl
+P39923	362	Phosphoserine
+Q08972	443	Phosphoserine
+Q08972	1191	Phosphothreonine
+P0CE68	4	N-linked
+Q03435	2	N-acetylserine
+P53253	10	Glycyl
+Q08208	70	Phosphoserine
+Q08208	181	Phosphothreonine
+Q08208	184	Phosphoserine
+Q12460	321	Phosphoserine
+P47035	60	Phosphoserine
+P47035	166	Phosphoserine
+P47035	231	Phosphoserine
+P47035	252	Phosphoserine
+P47035	437	Phosphoserine
+P47035	439	Phosphoserine
+P47035	447	Phosphoserine
+P47035	452	Phosphoserine
+P47035	497	Phosphoserine
+P47035	676	Phosphothreonine
+P47035	830	Phosphoserine
+P47035	1042	Phosphothreonine
+P47035	1056	Phosphoserine
+P47035	1059	Phosphoserine
+Q07896	395	Phosphoserine
+Q03790	2	N-acetylalanine
+Q03790	101	Phosphoserine
+Q03790	297	Phosphoserine
+Q03790	438	Phosphoserine
+Q12493	222	Phosphoserine
+P36003	178	Phosphoserine
+P36003	179	Phosphoserine
+P36003	405	Phosphoserine
+P36003	426	Phosphoserine
+P36003	737	Phosphoserine
+P36003	739	Phosphotyrosine
+Q02892	563	Phosphoserine
+Q12514	306	Phosphothreonine
+Q12514	377	Phosphoserine
+Q12514	338	Glycyl
+P38742	76	Phosphoserine
+P38742	486	Phosphoserine
+P38742	987	Phosphoserine
+P32499	17	Phosphoserine
+P32499	20	Phosphoserine
+P32499	137	Phosphoserine
+P32499	165	Phosphoserine
+P32499	203	Phosphoserine
+P32499	205	Phosphoserine
+P32499	348	Phosphoserine
+P32499	351	Phosphoserine
+P32499	361	Phosphothreonine
+P32499	581	Phosphoserine
+P32499	590	Phosphothreonine
+P49686	137	Phosphoserine
+P49686	298	Phosphoserine
+Q05166	458	Phosphoserine
+Q05166	464	Phosphoserine
+Q12066	3	Phosphoserine
+Q12066	417	Phosphoserine
+Q12066	474	Phosphoserine
+P39720	155	Phosphoserine
+P53949	181	Phosphoserine
+P38837	39	Phosphoserine
+P38837	76	Phosphoserine
+Q12143	2	N-acetylserine
+P14907	238	Phosphoserine
+P14907	361	Phosphoserine
+P14907	456	Phosphoserine
+P14907	631	Phosphoserine
+P35729	417	Phosphothreonine
+P40064	1	N-acetylmethionine
+P40064	1034	Phosphoserine
+P40477	404	Phosphoserine
+P40477	657	Phosphoserine
+P40477	724	Phosphoserine
+P40477	735	Phosphoserine
+P40477	745	Phosphoserine
+P40477	803	Phosphothreonine
+P40477	805	Phosphoserine
+P40477	819	Phosphoserine
+P40477	889	Phosphoserine
+P40477	940	Phosphoserine
+P40010	337	Phosphoserine
+Q00402	611	Phosphoserine
+Q00402	675	Phosphoserine
+Q00402	746	Phosphoserine
+Q00402	881	Phosphoserine
+Q00402	945	Phosphoserine
+Q00402	1009	Phosphoserine
+Q00402	1201	Phosphoserine
+Q00402	1265	Phosphoserine
+Q00402	1329	Phosphoserine
+Q00402	2162	Phosphoserine
+Q00402	2164	Phosphoserine
+Q00402	2197	Phosphoserine
+Q00402	2217	Phosphoserine
+Q00402	2220	Phosphoserine
+Q00402	2221	Phosphoserine
+Q00402	2360	Phosphoserine
+Q00402	2424	Phosphoserine
+Q00402	2494	Phosphoserine
+Q00402	2545	Phosphoserine
+P39705	10	Phosphoserine
+P39705	49	Phosphoserine
+P39705	81	Phosphoserine
+P39705	89	Phosphoserine
+P39705	162	Phosphoserine
+P39705	171	Phosphoserine
+P39705	214	Phosphoserine
+P39705	222	Phosphoserine
+P39705	352	Phosphoserine
+P39705	360	Phosphoserine
+P39705	374	Phosphoserine
+P39705	382	Phosphoserine
+P39705	460	Phosphothreonine
+P39705	480	Phosphoserine
+P39705	483	Phosphoserine
+P38881	156	Phosphoserine
+P38881	199	Phosphoserine
+P38881	285	Phosphoserine
+P38881	298	Phosphoserine
+P38302	139	Phosphoserine
+P31378	194	Glycyl
+P49687	273	Phosphoserine
+P49687	403	Phosphoserine
+P49687	404	Phosphoserine
+P49687	414	Phosphoserine
+P49687	667	Phosphoserine
+P49687	679	Phosphoserine
+P49687	689	Phosphoserine
+P49687	751	Phosphothreonine
+P38219	89	Phosphothreonine
+P38219	116	Phosphoserine
+P38219	119	Phosphoserine
+P38219	98	Glycyl
+P53204	85	Phosphoserine
+P53204	89	Phosphoserine
+P53204	90	Phosphoserine
+P53883	2	N-acetylserine
+P53883	2	Phosphoserine
+P53883	105	Phosphothreonine
+P53883	335	Phosphoserine
+P25655	2102	Phosphothreonine
+P06102	303	Phosphoserine
+P06102	307	Phosphoserine
+P06102	322	Phosphoserine
+P06102	446	Phosphoserine
+P06102	450	Phosphoserine
+P06102	565	Phosphoserine
+P06102	569	Phosphoserine
+P06102	571	Phosphothreonine
+P06102	657	Phosphoserine
+P06102	535	Glycyl
+P39997	62	N-linked
+P39997	69	N-linked
+P39997	112	N-linked
+P39997	153	N-linked
+P39997	441	N-linked
+P53617	263	Phosphoserine
+P53617	265	Phosphoserine
+P53617	271	Phosphoserine
+P40007	176	Phosphoserine
+P40007	178	Phosphoserine
+P40991	580	Phosphoserine
+Q08287	234	Phosphoserine
+Q08287	239	Phosphoserine
+Q08287	268	Phosphoserine
+Q08287	370	Phosphoserine
+Q04958	300	Phosphoserine
+Q04958	312	Phosphoserine
+Q04958	632	Phosphoserine
+Q04958	634	Phosphoserine
+Q04958	653	Phosphoserine
+Q04958	661	Phosphoserine
+Q04958	670	Phosphoserine
+Q04958	680	Phosphoserine
+Q04958	739	Phosphoserine
+Q04958	803	Phosphothreonine
+P33331	2	N-acetylserine
+P33331	53	Glycyl
+P36118	40	Phosphoserine
+P36118	153	Phosphoserine
+P36118	197	Phosphoserine
+P36161	2	N-acetylserine
+P38181	1247	Phosphoserine
+P53742	60	Phosphoserine
+P53742	85	Phosphoserine
+P53742	155	Phosphoserine
+Q12200	123	N-linked
+Q12200	145	N-linked
+Q12200	178	N-linked
+Q12200	314	N-linked
+Q12200	401	N-linked
+Q12200	513	N-linked
+Q12200	900	N-linked
+Q12200	940	N-linked
+Q03125	163	Phosphoserine
+P51533	754	N-linked
+Q02785	2	N-acetylserine
+Q02785	32	Phosphoserine
+Q02785	52	Phosphoserine
+Q02785	56	Phosphoserine
+Q02785	1405	N-linked
+Q02785	426	Glycyl
+Q07418	62	Phosphoserine
+Q07418	304	Phosphoserine
+Q07418	339	Cysteine
+Q07418	339	S-farnesyl
+Q06169	2	N-acetylserine
+Q06169	52	Phosphoserine
+Q06169	420	Phosphoserine
+Q06169	424	Phosphoserine
+P07269	542	Phosphothreonine
+P17442	956	Phosphoserine
+P25360	162	N-linked
+P25360	202	N-linked
+P25360	274	N-linked
+P25360	102	Glycyl
+Q12057	141	Phosphothreonine
+Q12057	91	N-linked
+Q12057	132	N-linked
+Q12057	276	N-linked
+Q03407	294	Phosphoserine
+Q03407	296	Phosphoserine
+P39105	634	GPI-anchor
+P39105	26	N-linked
+P39105	33	N-linked
+P39105	52	N-linked
+P39105	78	N-linked
+P39105	92	N-linked
+P39105	123	N-linked
+P39105	160	N-linked
+P39105	170	N-linked
+P39105	215	N-linked
+P39105	277	N-linked
+P39105	307	N-linked
+P39105	345	N-linked
+P39105	388	N-linked
+P39105	459	N-linked
+P39105	489	N-linked
+P39105	513	N-linked
+P39105	541	N-linked
+P39105	565	N-linked
+P39105	582	N-linked
+Q03674	680	GPI-anchor
+Q03674	47	N-linked
+Q03674	80	N-linked
+Q03674	94	N-linked
+Q03674	125	N-linked
+Q03674	162	N-linked
+Q03674	181	N-linked
+Q03674	193	N-linked
+Q03674	217	N-linked
+Q03674	279	N-linked
+Q03674	309	N-linked
+Q03674	365	N-linked
+Q03674	390	N-linked
+Q03674	491	N-linked
+Q03674	515	N-linked
+Q03674	524	N-linked
+Q03674	543	N-linked
+Q03674	567	N-linked
+Q03674	584	N-linked
+Q03674	598	N-linked
+Q03674	630	N-linked
+Q03674	634	N-linked
+Q03674	642	N-linked
+Q03674	648	N-linked
+Q03674	652	N-linked
+Q03674	658	N-linked
+P27801	907	Phosphoserine
+P40335	216	Phosphoserine
+P53203	432	Phosphoserine
+P53203	435	Phosphothreonine
+P46988	2	N-acetylserine
+P52553	2	N-acetylserine
+P07270	100	Phosphoserine%3B
+P07270	114	Phosphoserine%3B
+P07270	128	Phosphoserine%3B
+P07270	152	Phosphoserine%3B
+P07270	204	Phosphoserine
+P07270	223	Phosphoserine%3B
+P07270	242	Phosphoserine
+P07270	243	Phosphoserine
+P20052	234	Phosphoserine%3B
+P20052	267	Phosphoserine%3B
+P06738	31	Phosphothreonine
+P06738	333	Phosphoserine
+P06738	751	N6-(pyridoxal
+P40187	162	Phosphoserine
+P40187	196	Phosphoserine
+P40187	296	Phosphoserine
+P40187	304	Phosphoserine
+Q12252	115	N-linked
+Q12252	132	N-linked
+P53297	106	Phosphoserine
+P53297	193	Phosphothreonine
+P53297	215	Phosphoserine
+P53297	436	Phosphoserine
+P53297	344	Glycyl
+P06169	2	N-acetylserine
+P06169	223	Phosphoserine
+P06169	266	Phosphothreonine
+P06169	336	Phosphothreonine
+P06169	353	Phosphothreonine
+P06169	522	Phosphothreonine
+P06169	526	Phosphoserine
+P06169	212	Glycyl
+P06169	233	Glycyl
+P06169	269	Glycyl
+P06169	332	Glycyl
+P06169	484	Glycyl
+P06169	505	Glycyl
+P06169	520	Glycyl
+P38848	361	N-linked
+P35056	1	N-acetylmethionine
+P35056	61	Phosphoserine
+P35056	6	Glycyl
+P35056	18	Glycyl
+P35056	24	Glycyl
+P53900	1	N-acetylmethionine
+P53872	174	GPI-anchor
+P53872	55	N-linked
+P53872	64	N-linked
+P53872	75	N-linked
+P53872	84	N-linked
+P53872	95	N-linked
+P53872	104	N-linked
+P53872	115	N-linked
+P53872	124	N-linked
+P53872	135	N-linked
+P53872	144	N-linked
+P53872	155	N-linked
+P53896	72	N-linked
+P53896	80	N-linked
+P32854	2	Phosphoserine
+P32854	23	Phosphoserine
+Q02969	58	Phosphoserine
+Q02969	63	Phosphoserine
+Q02969	289	Phosphoserine
+P53903	2	N-acetylserine
+P53903	119	Phosphoserine
+P07271	70	Phosphoserine
+P07271	72	Phosphoserine
+P07271	169	Phosphoserine
+P07271	584	Phosphoserine
+P14242	393	Phosphoserine
+P14242	566	Phosphoserine
+P47190	124	N-linked
+P47190	324	N-linked
+P47190	398	N-linked
+P52867	33	N-linked
+P52867	213	N-linked
+P52867	380	N-linked
+P52867	386	N-linked
+P42934	2	N-acetylserine
+P42934	156	N-linked
+P42934	404	N-linked
+P42934	481	N-linked
+Q05788	2	N-acetylserine
+Q05788	275	Phosphoserine
+P47180	318	N-linked
+P47180	330	N-linked
+P37012	2	N-acetylserine
+P37012	111	Phosphothreonine
+P37012	117	Phosphothreonine
+P37012	119	Phosphoserine
+Q03262	158	Phosphoserine
+P25297	302	Phosphothreonine
+P25297	303	Phosphoserine
+P25297	316	Phosphoserine
+P25297	317	Phosphothreonine
+P25297	321	Phosphoserine
+P25297	577	Phosphoserine
+P25297	579	Phosphoserine
+P25297	581	Phosphoserine
+P25297	6	Glycyl
+P25297	298	Glycyl
+P38264	157	Phosphoserine
+P27514	295	Phosphoserine
+P27514	311	Phosphoserine
+P27514	312	Phosphoserine
+Q03306	696	Phosphoserine
+Q03306	753	Phosphoserine
+Q03306	871	Phosphoserine
+P05030	61	Phosphoserine
+P05030	175	Phosphothreonine
+P05030	911	Phosphoserine
+P05030	912	Phosphothreonine
+P05030	918	Phosphothreonine
+P05030	252	Glycyl
+P05030	555	Glycyl
+P53261	288	Phosphoserine
+P53261	308	Phosphothreonine
+P16861	3	Phosphoserine
+P16861	166	Phosphoserine
+P16861	179	Phosphoserine
+P16861	185	Phosphoserine
+P16861	189	Phosphoserine
+P16861	192	Phosphoserine
+P16861	217	Phosphoserine
+P16861	450	Phosphothreonine
+P16861	89	Glycyl
+P16861	625	Glycyl
+P16862	152	Phosphothreonine
+P16862	163	Phosphoserine
+P16862	171	Phosphoserine
+P16862	803	Phosphoserine
+P00560	2	N-acetylserine
+P00560	93	Phosphothreonine
+P00560	110	Phosphoserine
+P00560	130	Phosphoserine
+P00560	154	Phosphoserine
+P00560	172	Phosphoserine
+P00560	203	Phosphothreonine
+P00560	241	Phosphothreonine
+P00560	298	Phosphothreonine
+P00560	318	Phosphoserine
+P00560	331	Phosphothreonine
+P00560	392	Phosphothreonine
+P00560	82	Glycyl
+P00560	197	Glycyl
+P00560	258	Glycyl
+P00560	274	Glycyl
+P00560	302	Glycyl
+P33401	2	N-acetylserine
+P33401	120	Phosphoserine
+P38244	96	N-linked
+P38244	121	N-linked
+P38244	189	N-linked
+P38244	217	N-linked
+P38244	656	N-linked
+P38244	768	N-linked
+P38244	796	N-linked
+P38244	811	N-linked
+P38244	866	N-linked
+P38244	937	N-linked
+P39104	10	Phosphoserine
+P39104	236	Phosphoserine
+P39104	384	Phosphoserine
+P39104	394	Phosphothreonine
+P39104	396	Phosphoserine
+P39104	592	Phosphoserine
+P53252	14	Phosphothreonine
+P53252	16	Phosphoserine
+P53252	45	Phosphoserine
+P53252	98	Phosphoserine
+P53252	163	Phosphoserine
+P53252	230	Phosphoserine
+P53252	233	Phosphothreonine
+P53252	299	Phosphoserine
+P53252	29	Glycyl
+Q12236	138	Phosphoserine
+Q12236	619	Phosphoserine
+Q12236	1009	Phosphoserine
+Q04383	281	Phosphoserine
+Q04383	295	Phosphoserine
+Q04383	302	Phosphoserine
+Q04383	384	Phosphoserine
+P38197	2	N-acetylserine
+P38197	49	N6-(pyridoxal
+Q12412	259	N-linked
+Q12445	270	Phosphoserine
+Q12445	273	Phosphothreonine
+Q12445	292	Phosphoserine
+Q12445	294	Phosphoserine
+P23287	2	N-acetylserine
+P39966	376	Phosphothreonine
+P39966	380	Phosphothreonine
+P11491	123	Phosphoserine
+P11491	268	N-linked
+P11491	401	N-linked
+Q04004	1	N-acetylmethionine
+P32634	298	Phosphothreonine
+P32634	838	Phosphoserine
+P32634	1289	Phosphoserine
+P32634	1307	Phosphoserine
+P32634	1356	Phosphoserine
+P32634	1664	Phosphoserine
+Q06644	347	N-linked
+Q99216	47	Phosphoserine
+Q99216	51	Phosphothreonine
+P38693	97	N-linked
+P38693	162	N-linked
+P38693	192	N-linked
+P38693	250	N-linked
+P38693	315	N-linked
+P38693	356	N-linked
+P38693	390	N-linked
+P38693	439	N-linked
+P38693	445	N-linked
+P38693	461	N-linked
+Q08108	659	GPI-anchor
+Q08108	56	N-linked
+Q08108	82	N-linked
+Q08108	129	N-linked
+Q08108	166	N-linked
+Q08108	221	N-linked
+Q08108	283	N-linked
+Q08108	313	N-linked
+Q08108	351	N-linked
+Q08108	495	N-linked
+Q08108	519	N-linked
+Q08108	547	N-linked
+Q08108	571	N-linked
+Q08108	588	N-linked
+Q08108	614	N-linked
+P41812	524	Phosphothreonine
+P00950	12	Phosphoserine
+P00950	49	Phosphotyrosine
+P00950	116	Phosphoserine
+P00950	127	Phosphoserine
+P00950	128	Phosphoserine
+P00950	185	Phosphoserine
+P00950	197	Phosphoserine
+P00950	31	Glycyl
+P00950	57	Glycyl
+P00950	71	Glycyl
+P00950	139	Glycyl
+P00950	175	Glycyl
+P00950	191	Glycyl
+P33775	2	N-acetylserine
+P33775	390	N-linked
+P33775	513	N-linked
+P33775	743	N-linked
+P31382	2	N-acetylserine
+P31382	32	Phosphoserine
+P31382	38	Phosphoserine
+P31382	39	Phosphoserine
+P31382	131	N-linked
+P31382	155	N-linked
+P31382	403	N-linked
+P46971	759	N-linked
+P39685	45	Phosphoserine
+P39685	60	Phosphoserine
+P39685	280	N-linked
+P23594	369	Leucine
+P00635	97	N-linked
+P00635	103	N-linked
+P00635	162	N-linked
+P00635	192	N-linked
+P00635	250	N-linked
+P00635	315	N-linked
+P00635	356	N-linked
+P00635	390	N-linked
+P00635	439	N-linked
+P00635	445	N-linked
+P00635	456	N-linked
+P00635	461	N-linked
+P40035	1	N-acetylmethionine
+P40473	152	Phosphoserine
+P40473	168	Phosphoserine
+P40473	314	Phosphoserine
+P39008	1	N-acetylmethionine
+P39008	97	Phosphothreonine%3B
+P17157	18	Phosphotyrosine
+P17157	289	Glycyl
+P53191	46	Phosphoserine
+P53191	53	Phosphoserine
+P53191	56	Phosphothreonine
+P53191	73	Phosphoserine
+P53191	113	Phosphoserine
+P53191	124	Phosphoserine
+P53191	148	Phosphoserine
+P53191	165	Phosphoserine
+P53191	174	Phosphoserine
+P53191	300	Phosphoserine
+P53191	309	Phosphoserine
+P53191	381	Phosphoserine
+P07283	240	Phosphoserine
+P38336	64	Phosphoserine
+P38291	115	Phosphoserine
+P23595	38	Phosphoserine
+P23595	43	Phosphothreonine
+P23595	377	Leucine
+P34221	324	Phosphoserine
+P34221	332	Phosphoserine
+P35842	97	N-linked
+P35842	162	N-linked
+P35842	192	N-linked
+P35842	250	N-linked
+P35842	315	N-linked
+P35842	356	N-linked
+P35842	390	N-linked
+P35842	439	N-linked
+P35842	445	N-linked
+P35842	461	N-linked
+P53549	2	N-acetylserine
+Q01939	2	N-acetylthreonine
+P25375	73	Phosphoserine
+Q04119	58	N-linked
+Q04119	505	N-linked
+Q04119	511	N-linked
+Q04119	6	Glycyl
+Q06449	2	N-acetylserine
+Q06449	52	Phosphoserine
+Q06449	55	Phosphoserine
+Q06449	80	Glycyl
+P34217	56	Phosphoserine
+P34217	189	Phosphoserine
+P34217	191	Phosphoserine
+P34217	194	Phosphoserine
+P34217	197	Phosphoserine
+P34217	305	Phosphothreonine
+P34217	393	Phosphoserine
+P34217	466	Phosphoserine
+P34217	541	Phosphoserine
+P34217	636	Phosphoserine
+P34217	638	Phosphoserine
+P34217	640	Phosphoserine
+P34217	653	Phosphoserine
+P34217	655	Phosphoserine
+Q12017	35	Phosphoserine
+Q12017	62	Phosphoserine
+Q12161	143	Phosphoserine
+Q12161	191	Phosphoserine
+Q12161	310	Phosphothreonine
+Q12161	403	Phosphoserine
+P08456	4	Phosphoserine
+P08456	34	Phosphoserine
+P08456	42	Phosphoserine
+P08456	46	Phosphoserine
+P08456	47	Phosphoserine
+P08456	50	Phosphoserine
+P28708	1	N-acetylmethionine
+P28708	132	Phosphoserine
+P23639	108	Glycyl
+P50109	238	Phosphoserine
+P50109	340	Phosphoserine
+Q07949	9	S-palmitoyl
+Q07949	10	S-palmitoyl
+P32901	37	Phosphotyrosine
+P32901	39	Phosphoserine
+P32901	45	Phosphoserine
+P32901	594	Phosphoserine
+P38193	347	Phosphothreonine
+P32857	480	Phosphoserine
+P32857	483	Phosphothreonine
+P32857	498	Phosphothreonine
+P32857	132	N-linked
+P23394	69	Phosphoserine
+P22141	1	N-acetylmethionine
+P22141	76	Phosphoserine
+P33329	55	Phosphoserine
+P33329	71	Phosphoserine
+P33329	161	Phosphothreonine
+P33329	203	Phosphoserine
+P33329	224	Phosphoserine
+P33329	271	Phosphothreonine
+P33329	275	Phosphoserine
+P33329	310	Phosphoserine
+P33329	2	N-myristoyl
+P40494	402	Phosphoserine
+P40494	428	Phosphoserine
+P40494	484	Phosphoserine
+P40494	553	Phosphothreonine
+P40494	556	Phosphoserine
+P53835	135	N-linked
+P53835	145	N-linked
+P53835	188	N-linked
+P53835	197	N-linked
+P53835	231	N-linked
+P53835	252	N-linked
+P53835	272	N-linked
+P53835	280	N-linked
+P53835	490	N-linked
+P53835	505	N-linked
+P53835	512	N-linked
+P53835	531	N-linked
+P53835	573	N-linked
+P53835	587	N-linked
+P21243	2	N-acetylserine
+P21243	237	Phosphoserine
+P21243	232	Glycyl
+P21242	2	N-acetylthreonine
+P26570	49	Phosphoserine
+P26570	171	Phosphothreonine
+P26570	209	Phosphoserine
+P26570	222	Phosphoserine
+P26570	261	Phosphothreonine
+P26570	265	Phosphoserine
+P26570	690	Phosphoserine
+P26570	2	N-myristoyl
+P49960	19	Phosphoserine
+P33203	576	Phosphothreonine
+P40303	60	Phosphothreonine
+P38624	1	N-acetylmethionine
+P25451	31	Phosphoserine
+P25451	70	Glycyl
+Q08217	118	Phosphothreonine
+P14747	31	Phosphothreonine
+P14747	489	Phosphoserine
+P14747	520	Phosphoserine
+P24031	97	N-linked
+P24031	103	N-linked
+P24031	162	N-linked
+P24031	192	N-linked
+P24031	250	N-linked
+P24031	315	N-linked
+P24031	356	N-linked
+P24031	390	N-linked
+P24031	439	N-linked
+P24031	445	N-linked
+P24031	456	N-linked
+P24031	461	N-linked
+P52290	98	N-linked
+P52290	163	N-linked
+P52290	193	N-linked
+P52290	202	N-linked
+P52290	238	N-linked
+P52290	251	N-linked
+P52290	316	N-linked
+P52290	357	N-linked
+P52290	391	N-linked
+P52290	457	N-linked
+P52290	462	N-linked
+P40347	57	Phosphoserine
+P40476	129	Phosphoserine
+P40476	279	Phosphoserine
+P40476	282	Phosphoserine
+P40476	288	Phosphoserine
+P40476	314	Glycyl
+P53131	8	Phosphoserine
+P53131	9	Phosphoserine
+P40327	2	N-myristoyl
+P40327	234	Glycyl
+P40327	255	Glycyl
+P40327	290	Glycyl
+P33297	2	N-acetylalanine
+P33297	180	Phosphotyrosine
+P33298	1	N-acetylmethionine
+P33298	280	Glycyl
+P09232	594	N-linked
+P23638	100	Glycyl
+P23638	199	Glycyl
+P23638	231	Glycyl
+P53633	1	N-acetylmethionine
+P53633	18	Phosphoserine
+P54885	2	N-acetylserine
+P20095	2	N-acetylserine
+P33299	164	Phosphoserine
+P33299	231	Phosphoserine
+P34227	53	Phosphoserine
+P47033	853	GPI-anchor
+P47033	101	N-linked
+P47033	360	N-linked
+P47033	488	N-linked
+P47033	535	N-linked
+P47033	547	N-linked
+P47033	569	N-linked
+P47033	625	N-linked
+P32379	55	Phosphothreonine
+P32379	56	Phosphoserine
+P32379	251	Phosphoserine
+P40302	14	Phosphoserine
+P40302	191	Glycyl
+Q07800	110	Phosphoserine
+Q07800	9	S-palmitoyl
+Q07800	10	S-palmitoyl
+Q07800	154	Glycyl
+P15380	72	N-linked
+P15380	78	N-linked
+P07259	2	N-acetylalanine
+P07259	1857	Phosphoserine%3B
+P07259	1853	Glycyl
+P32849	2	N-acetylserine
+P32849	20	Phosphoserine
+P32849	23	Phosphoserine
+P32849	129	Phosphoserine
+P32849	130	Phosphoserine
+P14737	26	Phosphoserine
+P14737	56	Phosphoserine
+P14737	205	Phosphoserine
+P14737	218	Phosphothreonine
+P14737	248	Phosphoserine
+P14737	312	Phosphoserine
+P14737	315	Phosphoserine
+P14737	462	Phosphoserine
+P14737	471	Phosphothreonine
+P14737	474	Phosphothreonine
+P14737	568	Phosphoserine
+P14737	729	Phosphoserine
+P20051	98	N6-carboxylysine
+P07257	141	Phosphoserine
+P07257	168	Phosphoserine
+P40474	21	Phosphoserine
+P40474	38	Phosphothreonine
+P40474	40	Phosphoserine
+P38227	436	Phosphoserine
+P48581	383	Phosphoserine
+P40352	30	Phosphoserine
+P21827	135	Phosphoserine
+P21827	136	Phosphoserine
+P07276	118	Phosphoserine
+P07276	367	Phosphoserine
+P07276	583	Phosphoserine
+Q12465	41	N-linked
+Q12465	45	N-linked
+Q12465	69	N-linked
+Q12465	88	N-linked
+Q12465	124	N-linked
+Q12465	134	N-linked
+Q12465	145	N-linked
+Q12465	158	N-linked
+Q12465	166	N-linked
+Q12465	171	N-linked
+Q12465	187	N-linked
+Q12465	200	N-linked
+Q12465	235	N-linked
+Q12465	238	N-linked
+Q12465	244	N-linked
+Q12465	333	N-linked
+Q12465	365	N-linked
+Q12465	379	N-linked
+Q12465	432	N-linked
+Q12465	445	N-linked
+Q12465	516	N-linked
+Q12465	524	N-linked
+Q12465	613	N-linked
+Q12465	620	N-linked
+Q12465	626	N-linked
+Q12465	640	N-linked
+Q12465	677	N-linked
+Q12465	705	N-linked
+Q12465	713	N-linked
+Q12465	721	N-linked
+Q12465	731	N-linked
+Q12465	749	N-linked
+Q12465	758	N-linked
+Q12465	792	N-linked
+Q12465	821	N-linked
+Q12465	848	N-linked
+Q12465	861	N-linked
+Q12465	884	N-linked
+Q12465	890	N-linked
+Q12465	908	N-linked
+Q12465	923	N-linked
+Q12465	942	N-linked
+Q12465	956	N-linked
+Q12465	980	N-linked
+Q12465	983	N-linked
+Q12465	1011	N-linked
+Q12465	1024	N-linked
+Q12465	1031	N-linked
+Q12465	1060	N-linked
+Q12465	1071	N-linked
+Q12465	1098	N-linked
+Q12465	1126	N-linked
+P31244	25	Phosphoserine
+P31244	109	Phosphoserine
+P11938	486	Phosphothreonine
+P11938	731	Phosphoserine
+P53295	364	Phosphoserine
+Q08096	2	N-acetylserine
+Q03446	161	Phosphoserine
+Q03446	191	Phosphothreonine
+P39531	409	Phosphoserine
+P03872	1	N-acetylmethionine
+P06780	2	N-acetylserine
+P06780	206	Cysteine
+P06780	206	S-geranylgeranyl
+Q05672	198	Phosphoserine
+Q05672	435	Phosphoserine
+Q05672	439	Phosphoserine
+Q05672	447	Phosphoserine
+Q08273	15	Phosphoserine
+P21538	355	Phosphoserine
+P21538	807	Glycyl
+P10862	155	Phosphothreonine
+P10862	174	Phosphoserine
+P10862	204	Glycyl
+P12753	469	Phosphoserine
+P12753	568	Phosphothreonine
+Q08760	167	Phosphoserine
+Q12044	104	Phosphoserine
+Q12044	110	Phosphoserine
+Q12044	132	Phosphothreonine
+Q12044	152	Phosphoserine
+Q12044	157	Phosphoserine
+Q12044	160	Phosphoserine
+Q12044	183	Phosphoserine
+Q12044	187	Phosphoserine
+Q12044	193	Phosphoserine
+Q12044	201	Phosphoserine
+Q12044	255	Phosphoserine
+Q04779	1	N-acetylmethionine
+Q04779	68	Phosphoserine
+Q04779	683	Phosphoserine
+P19541	102	Phosphoserine
+P19541	231	Phosphothreonine
+Q00816	2	N-acetylserine
+Q00816	73	Phosphothreonine
+Q00816	75	Phosphoserine
+Q00816	242	Phosphoserine
+Q00816	254	Phosphoserine
+Q00816	311	Phosphoserine
+Q00816	421	Phosphoserine
+Q00816	480	Phosphotyrosine
+Q00816	490	Phosphoserine
+Q00816	570	Phosphoserine
+Q00816	572	Phosphoserine
+Q00816	576	Phosphoserine
+Q00816	610	Phosphoserine
+Q00816	614	Phosphoserine
+Q00816	680	Phosphoserine
+Q00816	896	Phosphothreonine
+Q00816	898	Phosphoserine
+Q00816	980	Phosphoserine
+P38344	140	Phosphothreonine
+P39729	2	N-acetylserine
+P38623	46	Phosphoserine
+P38623	50	Phosphoserine
+P38623	187	Phosphoserine
+P38623	350	Phosphothreonine
+P38623	520	Phosphoserine
+P36054	113	Phosphoserine
+P36054	117	Phosphoserine
+P36054	182	Phosphothreonine
+P38086	649	Glycyl
+P01119	306	Cysteine
+P01119	305	S-palmitoyl
+P01119	306	S-farnesyl
+P01120	198	Phosphoserine
+P01120	202	Phosphoserine
+P01120	207	Phosphoserine
+P01120	214	Phosphoserine
+P01120	235	Phosphoserine
+P01120	238	Phosphoserine
+P01120	319	Cysteine
+P01120	318	S-palmitoyl
+P01120	319	S-farnesyl
+P01120	131	Glycyl
+P47104	1244	Phosphoserine
+P47104	1248	Phosphoserine
+Q12192	215	Phosphoserine
+P40043	68	Glycyl
+P32862	202	Phosphoserine
+P32862	205	Phosphoserine
+P32862	208	Phosphoserine
+P32862	229	Phosphoserine
+P32862	283	Phosphoserine
+P32862	284	Phosphoserine
+P32862	410	Phosphoserine
+P32862	414	Phosphoserine
+P32862	1130	Phosphoserine
+P25378	1	N-acetylmethionine
+P25378	206	Cysteine
+P25378	206	S-farnesyl
+Q12305	26	Phosphoserine
+P53331	24	Phosphoserine
+P38630	38	Phosphothreonine
+P38630	40	Phosphoserine
+P38630	63	Phosphothreonine
+P38629	2	N-acetylserine
+Q06624	9	Phosphoserine
+Q06624	35	Glycyl
+P43565	380	Phosphoserine
+P43565	476	Phosphoserine
+P43565	704	Phosphothreonine
+P43565	709	Phosphoserine
+P43565	733	Phosphoserine
+P43565	736	Phosphoserine
+P43565	737	Phosphoserine
+P43565	747	Phosphothreonine
+P43565	1044	Phosphoserine
+P43565	1048	Phosphoserine
+P43565	1064	Phosphoserine
+P43565	1075	Phosphothreonine%3B
+P43565	1421	Phosphoserine
+P43565	1531	Phosphoserine
+P43565	1538	Phosphoserine
+P43565	1542	Phosphoserine
+P43565	1565	Phosphoserine
+P43565	1764	Phosphoserine
+P39083	278	Phosphothreonine
+P39083	291	Phosphoserine
+P39083	532	Phosphothreonine
+Q06108	136	Phosphoserine
+Q06108	249	Phosphoserine
+Q06108	252	Phosphoserine
+Q06108	481	Phosphoserine
+Q06108	537	Phosphoserine
+Q06108	652	Phosphoserine
+Q06108	765	Phosphoserine
+Q06108	813	Phosphoserine
+Q06108	817	Phosphothreonine
+Q06108	857	Phosphothreonine
+Q06108	866	Phosphoserine
+Q06108	879	Phosphoserine
+Q06108	918	Phosphoserine
+Q06108	966	Phosphoserine
+Q06108	969	Phosphoserine
+Q06108	975	Phosphoserine
+Q06108	1059	Phosphoserine
+Q06108	1081	Phosphoserine
+Q06108	1082	Phosphoserine
+P16664	351	Phosphoserine
+P16664	354	Phosphoserine
+P16664	357	Phosphoserine
+P16664	363	Phosphoserine
+P16664	364	Phosphoserine
+P16664	370	Phosphoserine
+Q12300	136	N-linked
+Q12300	385	N-linked
+P21524	227	Phosphoserine
+P21524	816	Phosphoserine
+P21524	837	Phosphoserine
+P21524	887	Phosphoserine
+P21524	387	Glycyl
+P21524	853	Glycyl
+Q07844	42	Phosphoserine
+P26785	2	N-acetylserine%3B
+P26785	43	Phosphoserine
+P26785	181	Phosphoserine
+P26785	185	Phosphoserine
+P26785	187	Phosphoserine
+P26785	176	Glycyl
+P46990	70	Phosphothreonine
+P46990	46	Glycyl
+P36105	2	N-acetylserine
+P0CX49	50	N6%2CN6%2CN6-trimethyllysine
+P0CX49	116	Glycyl
+P0CX24	32	Phosphoserine
+P0CX24	125	Glycyl
+P0CX24	131	Glycyl
+P0CX24	149	Glycyl
+Q12672	32	Glycyl
+P0CX41	2	N-acetylserine
+P0CX41	106	N6%2CN6-dimethyllysine%3B
+P0CX41	110	N6%2CN6-dimethyllysine%3B
+P30775	287	N5-methylglutamine
+P53893	431	Phosphoserine
+P22336	2	N-acetylserine
+P22336	178	Phosphoserine%3B
+P26754	27	Phosphoserine
+P26754	122	Phosphoserine
+P40348	1	N-acetylmethionine
+P06781	189	Cysteine
+P06781	188	S-palmitoyl
+P06781	189	S-geranylgeranyl
+Q3E757	2	N-acetylserine
+Q3E757	75	N6%2CN6%2CN6-trimethyllysine
+P48743	173	Phosphoserine
+Q06407	763	Phosphoserine
+P38339	386	Phosphothreonine
+P40160	346	Phosphoserine
+P49723	1	N-acetylmethionine
+P49723	169	Phosphoserine
+P49723	332	Phosphoserine
+P49723	334	Phosphothreonine
+P49723	336	Phosphoserine
+P49723	337	Glycyl
+P38145	95	Phosphoserine
+Q00245	228	Cysteine
+Q00245	228	S-farnesyl
+P53879	223	Phosphoserine
+P53879	228	Phosphoserine
+P53879	232	Phosphothreonine
+P53879	244	Phosphothreonine
+P53879	328	Cysteine
+P53879	328	S-geranylgeranyl
+P53879	276	Glycyl
+P09938	15	Phosphoserine
+P09938	24	Phosphoserine
+P09938	41	Phosphoserine
+P21672	227	Phosphoserine
+P21672	806	Phosphoserine
+P21672	827	Phosphoserine
+P21672	868	Phosphoserine
+P21672	387	Glycyl
+P26784	2	N-acetylserine
+P26784	44	Phosphoserine
+P26784	188	Phosphoserine
+P26784	177	Glycyl
+Q99258	3	Phosphothreonine
+P29539	97	Phosphoserine
+P29539	1637	Phosphoserine
+P29539	1795	Phosphoserine
+P29539	1852	Phosphoserine
+P38883	2	N-acetylserine
+P0CX53	2	N%2CN-dimethylproline%3B
+P0CX53	4	N6%2CN6%2CN6-trimethyllysine%3B
+P0CX53	11	N6%2CN6%2CN6-trimethyllysine%3B
+P0CX53	25	Phosphoserine
+P0CX53	38	Phosphoserine
+P0CX53	67	N5-methylarginine%3B
+P0CX53	130	Glycyl
+P0CX53	146	Glycyl
+Q12690	144	Phosphothreonine
+Q12690	152	Phosphothreonine
+Q00246	264	Phosphoserine
+Q00246	268	Phosphoserine
+Q00246	276	Phosphoserine
+Q00246	288	Cysteine
+Q00246	288	S-farnesyl
+P38615	199	Phosphotyrosine
+Q12196	402	Phosphoserine%3B
+Q12196	403	Phosphoserine%3B
+Q12196	409	Phosphoserine%3B
+Q12196	416	Phosphoserine%3B
+Q12196	417	Phosphoserine%3B
+Q12196	419	Phosphoserine%3B
+P41805	143	Phosphoserine
+P41805	205	Phosphoserine
+P41805	40	Glycyl
+P41805	101	Glycyl
+P38741	525	Phosphoserine
+P0C0W9	2	N-acetylserine
+P0C0W9	75	N6%2CN6%2CN6-trimethyllysine
+P0CX54	2	N%2CN-dimethylproline%3B
+P0CX54	4	N6%2CN6%2CN6-trimethyllysine%3B
+P0CX54	11	N6%2CN6%2CN6-trimethyllysine%3B
+P0CX54	25	Phosphoserine
+P0CX54	38	Phosphoserine
+P0CX54	67	N5-methylarginine%3B
+P0CX54	130	Glycyl
+P0CX54	146	Glycyl
+P0CX44	2	N-acetylserine
+P0CX44	47	N6-methyllysine%3B
+P0CX44	79	Phosphoserine
+P0CX44	86	Phosphoserine
+P0CX23	32	Phosphoserine
+P0CX23	125	Glycyl
+P0CX23	131	Glycyl
+P0CX23	149	Glycyl
+P24000	7	Phosphoserine
+P0CX46	52	Phosphoserine
+P0CX46	95	Phosphoserine
+P0CX46	159	Phosphoserine
+P0CX46	160	Phosphoserine
+P0CX46	249	Phosphoserine
+P0CX46	46	Glycyl
+P0CX46	93	Glycyl
+P0CX46	119	Glycyl
+P0CX46	145	Glycyl
+P0CX45	52	Phosphoserine
+P0CX45	95	Phosphoserine
+P0CX45	159	Phosphoserine
+P0CX45	160	Phosphoserine
+P0CX45	249	Phosphoserine
+P0CX45	46	Glycyl
+P0CX45	93	Glycyl
+P0CX45	119	Glycyl
+P0CX45	145	Glycyl
+P14120	22	Glycyl
+P14120	53	Glycyl
+P14120	83	Glycyl
+P05744	2	N-acetylalanine%3B
+P05744	47	Glycyl
+P0CX84	13	Phosphoserine
+P0CX84	50	Phosphoserine
+P05745	2	N-acetylthreonine
+P49626	2	N-acetylserine
+Q02753	32	Glycyl
+P0CX82	30	Phosphoserine
+P0CX82	37	Phosphoserine
+P0CX82	91	Phosphoserine
+P0CX82	21	Glycyl
+P0CX82	53	Glycyl
+P0CX82	60	Glycyl
+P0CX82	146	Glycyl
+P0CX82	186	Glycyl
+P0CX83	30	Phosphoserine
+P0CX83	37	Phosphoserine
+P0CX83	91	Phosphoserine
+P0CX83	21	Glycyl
+P0CX83	53	Glycyl
+P0CX83	60	Glycyl
+P0CX83	146	Glycyl
+P0CX83	186	Glycyl
+P40212	144	Phosphothreonine
+P40212	152	Phosphothreonine
+P38754	2	N-acetylserine
+P05740	70	Phosphothreonine
+P05740	46	Glycyl
+P0CX50	50	N6%2CN6%2CN6-trimethyllysine
+P0CX50	116	Glycyl
+P0CX43	2	N-acetylserine
+P0CX43	47	N6-methyllysine%3B
+P0CX43	79	Phosphoserine
+P0CX43	86	Phosphoserine
+P04449	7	Phosphoserine
+P41056	2	N-acetylalanine%3B
+P41056	47	Glycyl
+P25367	143	Phosphoserine
+P25367	5	Glycyl
+P25367	84	Glycyl
+P39956	399	Phosphothreonine
+P39956	430	Phosphoserine
+P39956	459	Phosphoserine
+P39956	557	Phosphoserine
+P39956	561	Phosphoserine
+P39956	575	Phosphoserine
+P39956	584	Phosphoserine
+P39956	652	Phosphoserine
+P39956	689	Phosphoserine
+P40011	2	N-acetylserine
+P35178	1	N-acetylmethionine
+P35178	267	Phosphoserine
+Q05022	47	Phosphothreonine
+Q05022	187	Phosphoserine
+Q05022	188	Phosphoserine
+Q05022	1724	Phosphoserine
+P25381	38	N-linked
+P25381	64	N-linked
+P25381	106	N-linked
+P25381	121	N-linked
+P25381	268	N-linked
+P25381	356	N-linked
+P25381	449	N-linked
+P36121	61	Phosphothreonine
+P32565	2	N-acetylserine
+P32565	801	Phosphothreonine
+P32565	932	Phosphothreonine
+Q03305	181	Phosphoserine
+Q03305	184	Phosphoserine
+P22138	2	N-acetylserine
+P22138	81	Phosphoserine
+P22138	1156	Phosphoserine
+P20435	24	Phosphoserine
+P28000	15	Phosphothreonine
+P28000	33	Phosphothreonine
+P28000	134	Glycyl
+P04050	1471	Phosphothreonine
+P04050	695	Glycyl
+P04050	1246	Glycyl
+P04050	1350	Glycyl
+P20433	1	N-acetylmethionine
+P20433	91	Phosphothreonine
+P20433	92	Phosphothreonine
+P50106	121	Phosphoserine
+P32349	27	Phosphothreonine
+P32349	392	Phosphoserine
+P32349	394	Phosphoserine
+P17890	189	Phosphoserine
+P35718	162	Phosphoserine
+Q12377	2	N-acetylserine
+Q06506	2	N-acetylserine
+Q06506	50	Phosphoserine
+P0CX48	2	N-acetylserine
+P0CX48	15	Glycyl
+P0CX48	46	Glycyl
+P0CX48	56	Glycyl
+P0CX48	57	Glycyl
+P0CX48	79	Glycyl
+P0CX48	96	Glycyl
+P0CX48	105	Glycyl
+P0CX48	133	Glycyl
+P0CX48	141	Glycyl
+P0CX48	148	Glycyl
+P40693	2	N-acetylserine
+P40693	14	Phosphoserine
+P40693	120	Phosphothreonine
+P40693	278	Phosphoserine
+Q02805	138	Phosphoserine
+Q02805	141	Phosphoserine
+Q02805	436	Phosphoserine
+Q02805	536	Phosphoserine
+Q02805	720	Phosphoserine
+Q02805	725	Phosphoserine
+Q02805	401	Glycyl
+P53046	1	N-acetylmethionine
+P53046	154	Phosphoserine
+P53046	155	Phosphoserine
+P53046	180	Phosphothreonine
+P53046	433	Phosphoserine
+Q03691	103	N-linked
+Q03691	107	N-linked
+Q03691	139	N-linked
+P47006	10	Phosphoserine
+P47006	12	Phosphoserine
+P47006	14	Phosphoserine
+P47006	60	Phosphoserine
+P46669	244	Phosphoserine
+P46669	251	Phosphoserine
+P46669	265	Phosphoserine
+P46669	269	Phosphoserine
+P46669	285	Phosphoserine
+P20436	2	N-acetylserine
+P20436	68	Phosphothreonine
+P22139	59	Glycyl
+P25441	137	Phosphoserine
+P25441	138	Phosphoserine
+P25441	178	Phosphoserine
+P25441	182	Phosphoserine
+P25441	224	Phosphoserine
+P25441	228	Phosphothreonine
+P25441	232	Phosphothreonine
+Q12754	1059	Phosphoserine
+Q12754	1067	Phosphoserine
+Q06511	69	Phosphoserine
+P25359	2	N-acetylalanine
+P25359	26	Phosphoserine
+Q01855	2	N-acetylserine
+Q01855	24	Glycyl
+Q01855	35	Glycyl
+Q01855	64	Glycyl
+P38701	2	N-acetylserine
+P38701	6	Glycyl
+P38701	8	Glycyl
+P38701	21	Glycyl
+P38701	32	Glycyl
+P38701	101	Glycyl
+P0C0V8	1	N-acetylmethionine
+P08518	919	Phosphoserine
+P32561	394	Phosphothreonine
+P32561	408	Phosphoserine
+P43588	1	N-acetylmethionine
+P38764	16	Phosphoserine
+P38764	19	Phosphoserine
+P38764	24	Phosphothreonine
+P38764	178	Phosphoserine
+P38764	187	Phosphoserine
+P38764	695	Phosphoserine
+P40016	2	N-acetylalanine
+P40016	454	Phosphoserine
+P0CX47	2	N-acetylserine
+P0CX47	15	Glycyl
+P0CX47	46	Glycyl
+P0CX47	56	Glycyl
+P0CX47	57	Glycyl
+P0CX47	79	Glycyl
+P0CX47	96	Glycyl
+P0CX47	105	Glycyl
+P0CX47	133	Glycyl
+P0CX47	141	Glycyl
+P0CX47	148	Glycyl
+P36160	73	Phosphoserine
+O13563	2	N-acetylserine
+O13563	133	Phosphoserine
+O13563	135	Phosphoserine
+O13563	140	Phosphoserine
+Q08723	2	N-acetylserine
+Q08723	314	Phosphoserine
+Q08723	317	Phosphoserine
+Q08723	319	Phosphoserine
+Q08723	327	Phosphothreonine
+Q12532	797	Phosphoserine
+Q04031	113	Phosphoserine
+Q04031	116	Phosphoserine
+Q04031	122	Phosphoserine
+P38961	62	Phosphoserine
+P36080	2	N-acetylserine
+P40470	197	Phosphoserine
+P40470	202	Phosphoserine
+P40470	203	Phosphoserine
+Q3E792	2	N%2CN-dimethylproline%3B
+P41058	25	Phosphoserine
+P26783	2	N-acetylserine
+P26783	27	Phosphothreonine
+P26783	45	Glycyl
+P26783	203	Glycyl
+P48164	2	N-acetylserine
+P48164	10	Phosphoserine
+P48164	31	Phosphoserine
+Q06488	612	Phosphotyrosine
+Q06488	682	Phosphoserine
+P43609	485	Phosphoserine
+Q02950	327	Phosphoserine
+Q03919	76	Glycyl
+Q3E754	1	N-acetylmethionine
+P0CX31	2	N-acetylserine
+P0CX31	14	Phosphoserine
+P0CX31	56	Phosphoserine
+P0CX31	21	Glycyl
+Q08932	1	N-acetylmethionine
+Q08932	172	Phosphoserine
+P38781	150	Phosphoserine
+Q03201	193	Phosphoserine
+Q05468	119	Phosphoserine
+Q05468	158	Phosphothreonine
+Q05468	160	Phosphoserine
+Q04225	5	Phosphoserine
+P38766	64	Phosphoserine
+P38712	43	Phosphoserine
+P38712	45	Phosphoserine
+P38712	47	Phosphoserine
+P48589	85	Glycyl
+P48589	95	Glycyl
+P48589	114	Glycyl
+P23248	2	N-acetylalanine%3B
+P23248	245	Phosphoserine
+P23248	254	Phosphothreonine
+P23248	248	Glycyl
+P0CX52	2	N-acetylserine
+P0CX52	34	Phosphoserine
+P0CX52	61	Phosphoserine
+P0CX52	70	Phosphothreonine
+P0CX52	76	Phosphoserine
+P0CX52	30	Glycyl
+P0CX52	47	Glycyl
+P0CX52	59	Glycyl
+P0CX56	2	N-acetylserine
+P0CX56	48	N6-methyllysine%3B
+P0CX56	36	Glycyl
+P0CX56	49	Glycyl
+P0CX56	80	Glycyl
+P0CX56	96	Glycyl
+P0CX29	64	3%2C4-dihydroxyproline
+P0CX29	56	Glycyl
+P0CX32	2	N-acetylserine
+P0CX32	14	Phosphoserine
+P0CX32	56	Phosphoserine
+P0CX32	21	Glycyl
+P0C0T4	2	N%2CN-dimethylproline%3B
+P0CX35	32	Phosphoserine
+P0CX35	115	Phosphothreonine
+P0CX35	247	Phosphoserine
+P0CX35	62	Glycyl
+P0CX35	134	Glycyl
+P0CX35	161	Glycyl
+P0CX35	168	Glycyl
+P0CX35	174	Glycyl
+P0CX35	179	Glycyl
+P0CX35	211	Glycyl
+P0CX35	233	Glycyl
+P32832	86	Phosphoserine
+Q03124	44	Phosphoserine
+P38792	2	N-acetylserine
+P38792	28	Phosphoserine
+P38792	268	Phosphoserine
+Q12149	138	Phosphoserine
+Q12149	520	Phosphothreonine
+Q12149	640	Phosphoserine
+Q12149	645	Phosphoserine
+P35997	40	S-methylcysteine
+P0C0X0	1	N-acetylmethionine
+P25443	2	N-acetylserine
+P25443	11	Asymmetric
+P25443	11	Omega-N-methylarginine%3B
+P25443	33	Glycyl
+P0CX34	16	Phosphoserine
+P0CX34	48	Phosphothreonine
+Q05942	83	Phosphoserine
+Q05942	88	Phosphothreonine
+Q05942	99	Phosphoserine
+P53236	670	Phosphoserine
+Q02206	199	Phosphoserine
+Q02206	545	Phosphoserine
+P33442	2	N-acetylalanine%3B
+P33442	245	Phosphothreonine
+P33442	254	Phosphothreonine
+P33442	248	Glycyl
+P0CX37	163	Phosphothreonine
+P0CX37	116	Glycyl
+P0CX37	131	Glycyl
+P0CX37	149	Glycyl
+P0CX37	214	Glycyl
+P0CX40	62	Phosphothreonine
+P0CX40	66	Phosphoserine
+P0CX40	69	Phosphoserine
+P0CX40	73	Phosphoserine
+P0CX40	86	Phosphoserine
+P0CX40	107	Phosphothreonine
+P0CX40	154	Phosphoserine
+P0CX40	155	Phosphoserine
+P0CX40	158	Phosphoserine
+P0CX40	161	Phosphoserine
+Q08417	3	N-linked
+Q08417	6	N-linked
+P46974	231	Phosphoserine
+P46974	322	Phosphoserine
+P46974	544	Phosphoserine
+P46974	632	Phosphoserine
+Q03516	949	Phosphoserine
+P32905	2	N-acetylserine
+P40161	2	N-acetylserine
+P40161	408	Phosphoserine
+P40161	411	Phosphoserine
+P40161	450	Phosphoserine
+P53064	17	Phosphoserine
+P53064	69	Phosphotyrosine
+P53064	71	Phosphoserine
+P53064	477	Phosphoserine
+P0CX30	64	3%2C4-dihydroxyproline
+P0CX30	56	Glycyl
+P41057	25	Phosphoserine
+P05750	44	Phosphothreonine
+P05750	70	Phosphothreonine
+P05750	97	Phosphoserine
+P05750	129	Phosphoserine
+P05750	146	Omega-N-methylarginine%3B
+P05750	221	Phosphoserine
+P05750	231	Phosphothreonine
+P05750	106	Glycyl
+P05750	132	Glycyl
+P05750	141	Glycyl
+P05750	151	Glycyl
+P05750	200	Glycyl
+P05750	212	Glycyl
+O13516	184	Phosphoserine
+O13516	180	Glycyl
+Q12481	14	Phosphoserine
+Q12481	41	Phosphoserine
+Q12481	42	Phosphoserine
+P05756	32	Phosphoserine
+P05756	39	Glycyl
+P05756	43	Glycyl
+P06367	2	N-acetylserine
+P05759	122	Phosphoserine
+P05759	76	Glycyl
+P0CX51	2	N-acetylserine
+P0CX51	34	Phosphoserine
+P0CX51	61	Phosphoserine
+P0CX51	70	Phosphothreonine
+P0CX51	76	Phosphoserine
+P0CX51	30	Glycyl
+P0CX51	47	Glycyl
+P0CX51	59	Glycyl
+P0CX55	2	N-acetylserine
+P0CX55	48	N6-methyllysine%3B
+P0CX55	36	Glycyl
+P0CX55	49	Glycyl
+P0CX55	80	Glycyl
+P0CX55	96	Glycyl
+Q3E7X9	1	N-acetylmethionine
+P0CX33	16	Phosphoserine
+P0CX33	48	Phosphothreonine
+P0CX36	32	Phosphoserine
+P0CX36	115	Phosphothreonine
+P0CX36	247	Phosphoserine
+P0CX36	62	Glycyl
+P0CX36	134	Glycyl
+P0CX36	161	Glycyl
+P0CX36	168	Glycyl
+P0CX36	174	Glycyl
+P0CX36	179	Glycyl
+P0CX36	211	Glycyl
+P0CX36	233	Glycyl
+P0CX38	163	Phosphothreonine
+P0CX38	116	Glycyl
+P0CX38	131	Glycyl
+P0CX38	149	Glycyl
+P0CX38	214	Glycyl
+P0CX39	62	Phosphothreonine
+P0CX39	66	Phosphoserine
+P0CX39	69	Phosphoserine
+P0CX39	73	Phosphoserine
+P0CX39	86	Phosphoserine
+P0CX39	107	Phosphothreonine
+P0CX39	154	Phosphoserine
+P0CX39	155	Phosphoserine
+P0CX39	158	Phosphoserine
+P0CX39	161	Phosphoserine
+P05755	184	Phosphoserine
+P05755	180	Glycyl
+Q06639	95	Phosphoserine
+Q06639	236	Phosphoserine
+P38165	81	Phosphoserine
+P38165	123	Phosphoserine
+P38165	142	Phosphoserine
+P38165	150	Phosphothreonine
+P38165	227	Phosphoserine
+P38165	236	Phosphoserine
+P38165	241	Phosphoserine
+P38165	269	Phosphoserine
+Q12443	278	Phosphoserine
+Q12443	137	N-linked
+P26786	2	N-acetylserine
+P26786	124	Glycyl
+P38850	304	Phosphoserine
+P38850	532	Phosphothreonine
+P38850	591	Phosphoserine
+P38850	593	Phosphoserine
+P38850	720	Phosphoserine
+P38850	800	Phosphoserine
+P38850	806	Phosphoserine
+Q08281	1036	Phosphoserine
+Q08281	1080	Phosphoserine
+Q08281	1087	Phosphoserine
+Q08281	1089	Phosphoserine
+Q08281	1123	Phosphoserine
+Q08281	1133	Phosphoserine
+P53330	77	Phosphoserine
+P53330	122	Phosphoserine
+P53850	23	Phosphoserine
+Q04947	186	Phosphothreonine
+Q04947	219	Phosphothreonine
+Q04947	232	Phosphoserine
+P20606	155	Phosphothreonine
+P20606	157	Phosphoserine
+P20606	133	Glycyl
+P28707	2	N-acetylserine
+P06105	50	Phosphothreonine
+P06105	54	Phosphoserine
+P06105	63	Phosphoserine
+P06105	85	Phosphoserine
+P06105	87	Phosphoserine
+P06105	89	Phosphoserine
+P06105	630	Phosphoserine
+P06105	1112	Phosphoserine
+P40541	28	Phosphoserine
+P40541	628	Phosphoserine
+P11792	570	Phosphothreonine%3B
+P11792	711	Phosphoserine%3B
+P11792	723	Phosphothreonine%3B
+P11792	726	Phosphoserine%3B
+P11792	737	Phosphothreonine%3B
+P11792	758	Phosphoserine%3B
+P11792	765	Phosphoserine%3B
+P32607	50	Phosphoserine
+P32607	52	Phosphoserine
+P32607	60	Phosphothreonine
+Q03940	2	N-acetylvaline
+Q12158	161	Phosphoserine
+Q12158	175	Phosphoserine%3B
+Q12158	210	N6-acetyllysine%3B
+Q12158	263	Phosphoserine%3B
+Q12158	307	Phosphoserine
+Q12158	354	Phosphothreonine
+P34758	564	Phosphoserine
+P43612	58	Phosphoserine
+P43612	255	Phosphoserine
+P43612	613	Phosphothreonine
+P43612	618	Phosphothreonine
+P17121	37	Phosphoserine
+P17121	46	Phosphoserine
+P17121	435	Phosphoserine
+P17121	491	Phosphoserine
+P17121	632	Phosphoserine
+Q12136	12	Phosphoserine
+Q12136	314	Phosphoserine
+Q12136	316	Phosphoserine
+Q12136	336	Phosphoserine
+Q12136	339	Phosphoserine
+Q12136	477	Phosphoserine
+Q04002	43	Phosphoserine%3B
+Q04002	67	Phosphothreonine
+Q04002	74	Phosphoserine%3B
+Q04002	127	Phosphoserine
+Q04002	157	Phosphoserine
+Q04002	162	Phosphoserine%3B
+Q04002	163	Phosphoserine
+Q04002	231	Phosphothreonine
+Q04002	236	Phosphothreonine
+Q04002	305	Phosphoserine
+Q04002	320	Phosphoserine
+Q04002	360	Phosphothreonine%3B
+Q04002	753	Phosphoserine
+Q04002	1179	Phosphoserine%3B
+Q04002	1182	Phosphoserine
+Q04002	1183	Phosphoserine%3B
+Q04002	1185	Phosphoserine
+P45978	2	N-acetylserine
+Q04951	279	N-linked
+P13856	269	Cysteine
+P13856	269	S-geranylgeranyl
+P46654	2	N-acetylserine
+Q12100	58	Phosphothreonine
+Q12100	60	Phosphoserine
+Q12100	216	Phosphoserine
+Q12100	334	Glycyl
+P53289	172	Phosphoserine
+P53289	192	Phosphoserine
+P53289	214	Phosphoserine
+P53289	238	Phosphoserine
+Q12242	56	Phosphoserine
+P39743	2	N-acetylserine
+P39743	299	Phosphoserine%3B
+P39743	321	Phosphoserine%3B
+P39743	379	Phosphoserine%3B
+P39743	242	Glycyl
+P39743	481	Glycyl
+P40856	20	Glycyl
+P38352	16	Phosphoserine
+P38352	266	Phosphoserine
+P20840	627	GPI-anchor
+P20840	79	N-linked
+P20840	109	N-linked
+P20840	135	N-linked
+P20840	248	N-linked
+P20840	282	O-linked
+P20840	289	O-linked
+P20840	299	O-linked
+P20840	303	O-linked
+P20840	306	N-linked
+P20840	307	O-linked
+P20840	308	O-linked
+P20840	311	O-linked
+P20840	314	O-linked
+P20840	315	O-linked
+P20840	316	O-linked
+P20840	329	O-linked
+P20840	331	O-linked
+P20840	334	O-linked
+P20840	335	O-linked
+P20840	338	O-linked
+P20840	339	O-linked
+P20840	340	O-linked
+P20840	341	O-linked
+P20840	342	O-linked
+P20840	345	O-linked
+P20840	346	O-linked
+P20840	349	O-linked
+P20840	350	O-linked
+P20840	364	N-linked
+P20840	402	N-linked
+P20840	460	N-linked
+P20840	485	N-linked
+P20840	501	N-linked
+P20840	614	N-linked
+P39954	2	N-acetylserine
+P39954	393	Phosphothreonine
+P39954	21	Glycyl
+P39954	413	Glycyl
+Q08985	138	Phosphothreonine
+Q08873	2	N-acetylserine
+Q08873	11	Phosphoserine
+P40075	2	N-acetylserine
+P40075	106	Phosphoserine
+P40357	79	Phosphoserine
+P40357	92	Phosphoserine
+P40357	186	Phosphoserine
+P40357	190	Phosphoserine
+P40357	213	Phosphoserine
+P40357	271	Phosphoserine
+P40357	273	Phosphoserine
+P40357	315	Phosphoserine
+P40357	355	Phosphothreonine
+P40357	359	Phosphoserine
+Q01589	318	GPI-anchor
+Q01589	22	N-linked
+Q01589	56	N-linked
+Q01589	78	N-linked
+Q01589	92	N-linked
+Q01589	114	N-linked
+Q01589	136	N-linked
+Q01589	152	N-linked
+P34228	8	Phosphoserine
+P34228	263	Phosphoserine
+P34228	806	Phosphoserine
+P36123	774	Phosphoserine
+P36123	857	Phosphoserine
+P36123	862	Phosphoserine
+P36123	892	Phosphoserine
+P36123	990	Phosphothreonine
+P36123	991	Phosphoserine
+P32368	246	Glycyl
+P32368	358	Glycyl
+P46674	568	Phosphoserine
+P46674	748	N6-acetyllysine
+P46674	866	Phosphoserine
+P43589	1	N-acetylmethionine
+Q08986	10	Phosphoserine
+Q08986	27	Phosphoserine
+Q08986	44	Phosphoserine
+Q08986	184	N-linked
+Q08986	243	N-linked
+P53324	2	N-acetylalanine
+P53324	85	N-linked
+P53324	283	N-linked
+P53324	401	N-linked
+P38814	72	Phosphoserine
+P38814	201	Phosphoserine
+P38814	459	Phosphoserine
+P38814	517	Phosphoserine
+P38814	520	Phosphoserine
+P42223	82	Phosphoserine
+P42223	83	Phosphoserine
+P42223	450	Phosphoserine
+P42223	532	Phosphoserine
+P47052	84	Tele-8alpha-FAD
+P36047	56	Phosphoserine
+Q06245	142	Phosphoserine
+Q06245	485	Phosphoserine
+Q06245	507	Phosphoserine
+P48415	28	Phosphoserine
+P48415	73	Phosphoserine
+P48415	144	Phosphoserine
+P48415	313	Phosphoserine
+P48415	472	Phosphoserine
+P48415	483	Phosphoserine
+P48415	595	Phosphothreonine
+P48415	607	Phosphoserine
+P48415	660	Phosphoserine
+P48415	663	Phosphoserine
+P48415	665	Phosphoserine
+P48415	674	Phosphoserine
+P48415	678	Phosphoserine
+P48415	681	Phosphoserine
+P48415	701	Phosphoserine
+P48415	704	Phosphoserine
+P48415	706	Phosphoserine
+P48415	759	Phosphoserine
+P48415	762	Phosphoserine
+P48415	765	Phosphoserine
+P48415	768	Phosphoserine
+P48415	843	Phosphoserine
+P48415	1511	Phosphoserine
+P48415	1515	Phosphoserine
+P48415	1578	Phosphoserine
+P48415	1602	Phosphoserine
+P48415	1603	Phosphoserine
+P48415	1611	Phosphoserine
+P48415	1617	Phosphoserine
+P48415	1778	Phosphoserine
+P48415	1875	Phosphoserine
+P48415	1973	Phosphoserine
+P48415	1986	Phosphoserine
+P48415	1992	Phosphoserine
+P48415	2049	Phosphothreonine
+P48415	2130	Phosphoserine
+P18759	226	Phosphoserine
+P15303	1	N-acetylmethionine
+P17065	1	N-acetylmethionine
+P17065	168	Phosphothreonine
+P17065	171	Phosphoserine
+P17065	515	Phosphoserine
+P38968	349	Phosphoserine
+P38968	836	Phosphoserine
+P38968	974	Phosphoserine
+P38968	977	Phosphoserine
+P38968	980	Phosphoserine
+P38968	988	Phosphoserine
+P38968	992	Phosphoserine
+P38968	999	Phosphoserine
+P38968	1050	Phosphothreonine
+P38968	1053	Phosphoserine
+P21825	2	N-acetylserine
+P33754	5	N-linked
+P33754	12	N-linked
+Q05567	380	N6-(pyridoxal
+Q07657	2	N-acetylserine
+Q07657	400	Phosphotyrosine
+Q07657	408	Phosphoserine
+Q07657	416	Phosphoserine
+Q07657	447	Phosphoserine
+Q07657	460	Phosphoserine
+Q07657	519	Phosphoserine
+Q07657	520	Phosphoserine
+Q07657	522	Phosphoserine
+Q07657	525	Phosphoserine
+Q07657	539	Phosphothreonine
+Q07657	545	Phosphoserine
+Q07657	548	Phosphoserine
+Q07657	426	Glycyl
+Q07657	437	Glycyl
+P38717	1206	N-linked
+P32900	137	Phosphoserine
+P32900	169	Phosphothreonine
+P32900	191	Phosphoserine
+P32900	193	Phosphoserine
+P32900	219	Phosphoserine
+P32900	221	Phosphothreonine
+P32900	222	Phosphoserine
+P32900	251	Phosphoserine
+P32900	369	Phosphoserine
+P32900	672	Phosphoserine
+P32900	717	Phosphoserine
+P35207	209	Phosphoserine
+Q08491	88	Phosphoserine
+Q08491	90	Phosphoserine
+P42843	594	Phosphothreonine
+Q00772	190	Phosphothreonine
+Q00772	192	Phosphotyrosine
+P32566	202	Phosphoserine
+P32566	203	Phosphoserine
+P32566	376	Phosphothreonine
+P32566	381	Phosphoserine
+P32566	394	Phosphoserine
+P32566	400	Phosphoserine
+P32566	453	Glycyl
+Q04174	403	N-linked
+Q04174	452	N-linked
+P38990	43	Phosphothreonine
+P38990	964	Phosphoserine
+P38990	1126	Phosphoserine
+P39955	536	Phosphoserine
+Q99314	144	Phosphoserine
+Q00711	90	Tele-8alpha-FAD
+P24280	302	Phosphoserine
+P24280	42	Glycyl
+P24280	84	Glycyl
+P40510	2	N-acetylserine
+P40510	22	Phosphoserine
+P40510	29	Phosphoserine
+P40510	33	Phosphoserine
+P46995	10	Phosphoserine
+P46995	522	Phosphoserine
+Q08446	168	Phosphoserine
+Q08446	171	Phosphoserine
+Q08446	32	Glycyl
+P38634	5	Phosphothreonine%3B
+P38634	33	Phosphothreonine
+P38634	76	Phosphoserine
+P38634	173	Phosphothreonine
+P38634	198	Phosphoserine
+P38634	201	Phosphoserine
+P38634	268	Lysine
+P38634	272	Lysine
+P38634	274	Lysine
+P38262	137	Phosphoserine
+Q06315	10	Phosphoserine
+Q06315	31	Phosphoserine
+Q06315	578	Phosphothreonine
+Q06315	580	Phosphoserine
+Q06315	592	Phosphoserine
+Q06315	701	Phosphoserine
+Q06315	954	Phosphoserine
+P38314	94	Phosphoserine
+P38314	458	Phosphoserine
+P38314	524	Phosphoserine
+P38164	123	Phosphoserine
+P38164	136	Phosphoserine
+P33332	290	Phosphothreonine
+P33332	606	Phosphoserine
+P89102	184	Phosphoserine
+P38890	517	Phosphoserine
+P47166	2	N-acetylserine
+P47166	151	Phosphoserine
+P47166	538	Phosphoserine
+P47166	549	Phosphoserine
+P47166	568	Phosphoserine
+P47166	571	Phosphoserine
+P47166	576	Phosphoserine
+P47166	589	Phosphoserine
+P32578	33	Phosphoserine
+P32578	181	Phosphoserine
+P32578	198	Phosphoserine
+P32578	200	Phosphoserine
+P32578	206	Phosphoserine
+P32578	209	Phosphoserine
+P32578	220	Phosphoserine
+P32578	331	Phosphoserine
+P32578	494	Phosphoserine
+P32578	497	Phosphoserine
+P32578	643	Phosphoserine
+P32578	2	N-myristoyl
+P33336	56	Phosphoserine
+P33336	65	Phosphoserine
+P33336	67	Phosphoserine
+P33336	92	Phosphoserine
+P33336	103	Phosphoserine
+P33336	142	Phosphoserine
+P33336	162	Phosphoserine
+P33336	165	Phosphoserine
+P33336	170	Phosphoserine
+P33336	176	Phosphoserine
+P33336	337	N-linked
+P33336	426	N-linked
+P33336	513	N-linked
+P33336	590	N-linked
+P33336	615	N-linked
+P33336	743	N-linked
+Q03656	383	Phosphothreonine
+Q03656	386	Phosphothreonine
+Q03656	388	Phosphoserine
+Q03656	393	Phosphoserine
+Q03656	410	Phosphoserine
+Q03656	427	Phosphoserine
+Q03656	432	Phosphoserine
+Q03656	445	Phosphoserine
+Q03656	449	Phosphoserine
+Q03656	453	Phosphoserine
+P38283	268	Phosphoserine
+P38283	489	Phosphoserine
+P14906	512	Phosphoserine
+Q04279	48	Phosphoserine
+Q04279	220	Phosphoserine
+Q04279	235	Phosphoserine
+Q04279	238	Phosphoserine
+Q04279	319	Phosphoserine
+Q04279	339	Phosphoserine
+Q04279	352	Phosphoserine
+Q04279	434	Phosphoserine
+Q04279	461	Phosphoserine
+Q04279	467	Phosphothreonine
+Q04279	630	Phosphoserine
+Q04279	675	Phosphothreonine
+Q04279	758	Phosphoserine
+Q04279	816	Phosphoserine
+Q04279	818	Phosphoserine
+Q04279	855	Phosphoserine
+P53011	257	Phosphoserine
+O94742	2	N-acetylserine
+O94742	12	Phosphoserine
+P53953	51	Phosphoserine
+P38166	2	N-acetylserine
+P38166	60	Phosphoserine
+P53965	94	Phosphoserine
+Q04195	132	Phosphoserine
+Q04195	794	Phosphoserine
+Q3E784	2	N-acetylserine
+Q3E784	10	Phosphoserine
+Q02775	120	Phosphoserine
+Q02775	212	Phosphothreonine
+P40072	50	Phosphoserine
+P40072	66	Phosphothreonine
+P40072	67	Phosphoserine
+P11655	439	N-linked
+P11655	462	N-linked
+P22224	286	Phosphoserine
+P22214	160	Phosphoserine
+P07560	201	Phosphoserine
+P07560	204	Phosphoserine
+P07560	214	S-geranylgeranyl
+P07560	215	S-geranylgeranyl
+P11075	212	Phosphoserine
+P11075	215	Phosphoserine
+P11075	334	Phosphothreonine
+P11075	447	Phosphoserine
+P11075	452	Phosphoserine
+P11075	455	Phosphoserine
+P11075	807	Phosphoserine
+P11075	1226	Phosphoserine
+P11075	1240	Phosphothreonine
+P11075	1741	Phosphoserine
+P11075	1752	Phosphoserine
+P11075	797	Glycyl
+P32855	16	Phosphoserine
+P32855	19	Phosphoserine
+P40316	185	Phosphoserine
+P40316	186	Phosphoserine
+P40316	212	Phosphoserine
+P40316	213	Phosphoserine
+P40316	277	Phosphoserine
+P40316	292	Phosphoserine%3B
+P25365	65	Phosphoserine
+P25365	388	N-linked
+P25365	620	N-linked
+P25365	1039	N-linked
+P40054	22	Phosphoserine
+P40054	29	Phosphoserine
+P40054	33	Phosphoserine
+P36124	236	Phosphoserine
+P36124	684	Phosphoserine
+P36124	718	Phosphoserine
+P36124	719	Phosphothreonine
+P36124	741	Phosphoserine
+Q12314	204	Phosphoserine
+Q12314	207	Phosphoserine
+P53313	278	Phosphoserine
+P32602	2	N-acetylserine
+P32602	261	Glycyl
+P40482	178	Phosphoserine
+P32844	2	N-acetylserine
+P34250	137	Phosphoserine
+P34250	280	Phosphoserine
+P34250	504	Phosphoserine
+P34250	507	Phosphoserine
+P34250	556	Phosphoserine
+P34250	980	Phosphoserine
+P34250	1022	Phosphoserine
+P34250	526	Glycyl
+P34250	743	Glycyl
+P38272	343	Phosphoserine
+P38272	394	Phosphoserine
+P53334	89	N-linked
+P33330	20	Phosphothreonine
+P33330	112	Phosphoserine
+P33330	218	N6-(pyridoxal
+P38827	625	Phosphoserine
+P38827	875	Phosphothreonine
+Q12369	10	Phosphoserine
+Q12369	855	Phosphoserine
+P35735	208	Phosphoserine
+P20134	220	Phosphoserine
+P20134	556	Phosphoserine
+P20134	733	Phosphoserine
+Q12234	55	Phosphoserine
+Q12234	64	Phosphoserine
+Q12234	468	Phosphoserine
+Q07458	2	N-acetylserine
+P34218	367	N6-acetyllysine%3B
+P40963	168	N6-acetyllysine%3B
+P36048	85	Phosphoserine
+P36048	88	Phosphothreonine
+P10870	383	N-linked
+P18888	165	Phosphothreonine
+P39929	72	Phosphothreonine
+P39929	119	Phosphoserine
+P39929	193	Phosphoserine
+P39929	229	Glycyl
+P00445	26	Phosphoserine
+P00445	39	Phosphoserine
+P00445	99	Phosphoserine
+P00445	117	Phosphoserine
+P00445	132	Phosphothreonine
+P00445	138	Phosphothreonine
+P00445	19	Glycyl
+P00445	70	Glycyl
+Q03954	107	Phosphoserine
+Q03954	116	Phosphoserine
+Q12455	5	Phosphoserine
+P06843	2	N-acetylserine
+P06843	126	Phosphoserine
+P35177	78	Phosphothreonine%3B
+P35177	88	Phosphoserine
+P35177	1293	Phosphoserine
+P38985	8	Phosphoserine
+P32342	2	N-acetylserine
+P40505	166	Phosphoserine
+P40505	211	Phosphoserine
+P15367	121	N-linked
+P38810	15	Phosphoserine
+P38810	72	Phosphothreonine
+P38810	83	Phosphoserine
+P38810	85	Phosphoserine
+P38810	94	Phosphoserine
+P38810	101	Phosphoserine
+P38810	110	Phosphoserine
+P38810	216	Phosphothreonine
+P51534	18	Phosphoserine
+P40073	166	Phosphoserine
+P40073	59	N-linked
+P25294	275	Phosphoserine
+P52286	177	Phosphothreonine
+P33338	294	Phosphothreonine
+P33338	298	Phosphothreonine
+P33338	308	Phosphoserine
+P33338	555	Phosphoserine
+Q12078	87	N-linked
+P25357	187	Phosphoserine
+P25357	395	Phosphoserine
+P25357	796	Phosphothreonine
+P25357	1037	Phosphoserine
+P50278	65	Phosphoserine
+P50278	68	Phosphoserine
+P50278	320	Phosphothreonine
+Q08199	105	N-linked
+Q08199	181	N-linked
+Q08199	215	N-linked
+Q08199	233	N-linked
+Q08199	315	N-linked
+Q08199	333	N-linked
+P40472	423	N-linked
+P11978	692	Phosphoserine
+P11978	1128	Glycyl
+P36169	142	Phosphoserine
+P36169	273	Phosphothreonine
+P32790	447	Phosphoserine
+P32790	449	Phosphoserine
+P32790	454	Phosphoserine
+P32790	799	Phosphoserine
+P32790	831	Phosphothreonine
+P32790	858	Phosphothreonine
+P32790	887	Phosphothreonine
+P32790	904	Phosphothreonine
+P32790	984	Phosphothreonine
+P32790	993	Phosphothreonine
+P32790	996	Phosphoserine
+P32790	1075	Phosphothreonine
+P32790	471	Glycyl
+P32790	548	Glycyl
+P47037	112	N6-acetyllysine
+P47037	113	N6-acetyllysine
+P38925	24	Phosphoserine
+P38925	33	Glycyl
+P38925	34	Glycyl
+Q04007	309	Phosphoserine
+Q04007	310	Phosphoserine
+Q04007	311	Phosphoserine
+Q04007	332	Phosphoserine
+Q04007	334	Phosphoserine
+Q04007	692	Phosphoserine
+Q04007	694	Phosphoserine
+Q04007	706	Phosphoserine
+Q04007	841	Phosphoserine
+Q04007	668	Glycyl
+Q04007	670	Glycyl
+P38956	2	N-acetylserine
+P22082	358	Phosphoserine
+P22082	383	Phosphothreonine
+P22082	716	Phosphoserine
+P22082	1340	Phosphoserine
+P22082	543	Glycyl
+P46950	91	Phosphothreonine
+P53438	771	Phosphoserine
+P37262	42	Phosphoserine
+P37262	64	Phosphoserine
+P31109	95	S-palmitoyl
+P31109	63	Glycyl
+P33328	58	Phosphoserine
+P33328	94	S-palmitoyl
+P33328	62	Glycyl
+Q12420	268	Phosphoserine
+P40317	40	Phosphoserine
+P40317	53	Phosphoserine
+P40317	191	Phosphoserine
+P40317	193	Phosphoserine
+P40317	245	Phosphoserine
+P25808	254	Phosphoserine
+P46965	2	N-acetylserine
+P38915	85	Phosphothreonine
+P38915	108	Phosphoserine
+P38915	123	Phosphoserine
+P38915	131	Phosphoserine
+P38915	451	Phosphoserine
+Q03707	78	Phosphoserine
+Q03707	80	Phosphoserine
+Q03707	85	Phosphoserine
+Q03707	181	Phosphoserine
+Q03707	203	Phosphoserine
+Q03707	204	Phosphoserine
+Q03707	206	Phosphoserine
+Q03707	301	Phosphoserine
+Q03707	394	Phosphothreonine
+Q03707	427	Phosphoserine
+P39931	212	Phosphothreonine
+P53172	9	Phosphoserine
+P53172	42	Phosphoserine
+P53172	46	Phosphoserine
+P53172	430	Phosphoserine
+Q12118	308	Phosphothreonine
+P38200	165	Phosphoserine
+P36024	47	Phosphoserine
+P36024	50	Phosphoserine
+P36024	54	Phosphoserine
+P36024	56	Phosphoserine
+P36024	155	Phosphoserine
+P38889	427	4-aspartylphosphate
+Q02100	94	Phosphoserine
+Q02100	113	Phosphothreonine
+Q02100	399	Phosphoserine
+Q02100	558	Phosphoserine
+P34252	84	Phosphothreonine%3B
+Q04964	1	N-acetylmethionine
+Q04964	56	Phosphoserine%3B
+Q04964	58	Phosphoserine%3B
+Q04964	60	Phosphoserine%3B
+Q12306	2	N-acetylserine
+Q12306	2	Phosphoserine
+Q12306	4	Phosphoserine
+Q12306	98	Glycyl
+P32364	583	Phosphothreonine
+P32909	12	Phosphoserine
+P32909	96	Phosphoserine
+P32909	129	Phosphothreonine
+P32909	311	Phosphothreonine
+P32909	545	Phosphoserine
+P32909	602	Phosphoserine
+P56508	71	Phosphoserine
+P56508	77	Phosphoserine
+P00447	147	Phosphothreonine
+P00447	149	Phosphothreonine
+P23201	182	Phosphoserine
+P23201	183	Phosphoserine
+P23201	220	Phosphothreonine
+P23201	254	Phosphoserine
+P23201	274	Phosphoserine
+P23201	301	Phosphoserine
+P23201	585	Phosphoserine
+P23201	599	Phosphoserine
+P23201	646	Phosphoserine
+P23201	817	Phosphoserine
+P23201	820	Phosphoserine
+P23201	865	Phosphoserine
+P23201	883	Phosphoserine
+P23201	910	Phosphoserine
+P23201	937	Phosphoserine
+P23201	961	Phosphoserine
+P23201	979	Phosphoserine
+P23201	1053	Phosphoserine
+P23201	1056	Phosphoserine
+P23201	1080	Phosphoserine
+P23201	1173	Phosphoserine
+P23201	1179	Phosphothreonine
+P23201	1180	Phosphoserine
+P23201	1251	Phosphothreonine
+P23201	1263	Phosphoserine
+P36131	199	Phosphothreonine%3B
+P53540	124	Phosphoserine
+P53540	136	Phosphoserine
+P40092	127	GPI-anchor
+P40092	41	N-linked
+P40092	59	N-linked
+P53541	233	N-linked
+P53541	293	N-linked
+P53541	303	N-linked
+P53541	500	N-linked
+P53541	536	N-linked
+P53541	560	N-linked
+P53541	563	N-linked
+P53541	572	N-linked
+P35209	454	Phosphoserine
+Q06168	78	Phosphoserine
+P25554	139	Phosphoserine
+P22579	137	Phosphoserine
+P22579	303	Phosphothreonine
+P22579	304	Phosphothreonine
+P22579	316	Phosphoserine
+P22579	1046	Phosphoserine
+P34164	66	Phosphoserine
+P34164	298	Phosphoserine
+P34164	2	N-myristoyl
+P40210	13	Phosphoserine
+P40210	183	Phosphothreonine
+P40210	433	Phosphothreonine
+P40210	436	Phosphoserine
+P40210	438	Phosphothreonine
+P53955	626	Phosphoserine
+P53955	649	Phosphoserine
+P53955	653	Phosphoserine
+Q12098	72	Phosphothreonine%3B
+Q12098	113	Phosphothreonine%3B
+Q12098	289	Phosphoserine%3B
+Q12098	319	Phosphothreonine%3B
+Q12098	329	Phosphoserine%3B
+Q12098	355	Phosphoserine%3B
+P54867	331	Phosphoserine
+P54867	353	Phosphoserine
+P54867	65	N-linked
+P40485	145	Phosphoserine
+P40485	150	Phosphoserine
+P40485	153	Phosphoserine
+P39928	502	Phosphoserine
+P39928	576	Phosphohistidine%3B
+P39928	758	Phosphoserine
+P39928	833	Phosphoserine
+P39928	1041	Phosphoserine
+P39928	1044	Phosphoserine
+P39928	1144	4-aspartylphosphate
+P39928	100	N-linked
+P39928	138	N-linked
+P39928	142	N-linked
+P39928	181	N-linked
+P39928	224	N-linked
+P39928	272	N-linked
+Q12267	2	N-acetylserine
+Q12267	43	Phosphothreonine
+Q12267	113	Phosphoserine
+P18480	818	Phosphoserine
+P32568	2	N-acetylserine
+P32568	26	Phosphoserine
+P32568	29	Phosphoserine
+P32568	64	Phosphoserine
+P32568	80	Phosphoserine
+P32568	86	Phosphoserine
+P32568	1153	Phosphothreonine
+P32568	273	N-linked
+P32568	334	N-linked
+P32568	518	N-linked
+P32568	730	N-linked
+P32568	874	N-linked
+P32568	1401	N-linked
+P53207	512	Phosphoserine
+P53207	514	Phosphoserine
+Q12133	102	N-linked
+Q12133	173	N-linked
+P36094	213	Phosphoserine
+P36094	217	Phosphoserine
+P36094	284	Phosphoserine
+P36094	329	Phosphoserine
+P17123	2	N-acetylserine
+P17123	118	Phosphoserine
+P17123	125	Phosphoserine
+P50875	446	Phosphoserine
+P50875	516	Phosphothreonine
+Q06132	736	Phosphoserine
+P06701	2	N-acetylalanine
+P34226	148	Phosphoserine
+P34226	561	Phosphoserine
+P34226	563	Phosphoserine
+P34226	564	Phosphothreonine
+P34226	693	Cysteine
+P34226	693	S-farnesyl
+Q08581	7	Phosphothreonine%3B
+Q08581	188	Phosphoserine
+Q08581	189	Phosphoserine
+Q08581	201	Phosphoserine%3B
+Q08581	216	Phosphoserine
+Q08581	273	Phosphothreonine
+Q08581	283	Phosphoserine
+Q12232	25	N-linked
+Q12232	378	N-linked
+Q12232	381	N-linked
+Q12232	408	N-linked
+Q12232	448	N-linked
+Q12232	486	N-linked
+P32380	18	Phosphothreonine
+P32380	60	Phosphoserine%3B
+P32380	64	Phosphothreonine%3B
+P32380	68	Phosphothreonine%3B
+P32380	80	Phosphoserine
+P32380	529	Phosphoserine
+P25582	455	Phosphoserine
+P25582	464	Phosphoserine
+P25582	529	Phosphoserine
+Q04398	86	N-linked
+P33419	18	Phosphothreonine
+P33419	65	Phosphoserine
+P33419	240	Phosphothreonine%3B
+Q03029	198	GPI-anchor
+P38904	1014	Phosphoserine
+P38904	1067	Phosphoserine
+P38904	981	Glycyl
+P38904	1154	Glycyl
+P32603	201	N-linked
+P32573	188	Glycyl
+P32558	526	Phosphoserine
+P32558	765	Phosphoserine
+P35210	468	Phosphoserine
+P53866	105	Phosphoserine
+P53866	217	Phosphoserine
+P53866	255	Phosphoserine
+P53866	334	Phosphoserine
+P53866	343	Phosphoserine
+P53866	345	Phosphoserine
+P24276	2	N-acetylserine
+P24276	40	Phosphoserine
+P24276	164	Phosphoserine
+P24276	183	Phosphoserine
+P24276	227	Phosphothreonine
+P24276	286	Phosphoserine
+P24276	322	Phosphoserine
+P24276	491	Phosphoserine
+P24276	492	Phosphoserine
+P24276	688	Phosphotyrosine
+P32343	358	Phosphoserine
+P32343	212	N-linked
+P32343	356	N-linked
+P32343	430	N-linked
+P32343	507	N-linked
+P32343	557	N-linked
+P32343	575	N-linked
+P32343	367	Glycyl
+P15705	227	Phosphoserine
+P15705	99	Glycyl
+P15705	168	Glycyl
+P15705	384	Glycyl
+P14359	125	Glycyl
+P38839	59	Phosphoserine
+P38839	86	Phosphoserine
+Q12516	45	Phosphoserine
+Q12516	167	Phosphoserine
+Q12516	297	N-linked
+Q12516	385	N-linked
+Q12020	11	Phosphoserine
+Q12020	139	Phosphoserine
+P36167	212	Phosphoserine
+P25567	55	Phosphoserine
+P25567	148	Phosphoserine
+P25567	422	Phosphoserine
+P25567	156	Glycyl
+P25567	301	Glycyl
+P25567	342	Glycyl
+P25567	352	Glycyl
+P42845	2	N-acetylserine
+P42845	7	Phosphoserine
+P42845	72	Phosphoserine
+P42845	99	Phosphothreonine
+P42845	102	Phosphoserine
+P42845	419	Phosphothreonine
+Q03497	2	N-acetylserine
+Q03497	87	Phosphoserine
+Q03497	165	Phosphoserine
+Q03497	167	Phosphothreonine
+Q03497	169	Phosphoserine
+Q03497	203	Phosphothreonine
+Q03497	418	Phosphoserine
+Q03497	502	Phosphoserine
+Q03497	547	Phosphoserine
+Q03497	562	Phosphoserine
+Q03497	573	Phosphothreonine
+Q03497	585	Phosphoserine
+Q03497	773	Phosphothreonine
+Q03497	924	Phosphoserine
+Q03497	927	Phosphothreonine
+P32917	329	Phosphoserine
+P12866	61	N-linked
+P12866	1022	Glycyl
+P06784	359	Phosphoserine
+P06784	363	Phosphothreonine
+P39932	197	N-linked
+P39932	319	N-linked
+P09959	149	Phosphoserine
+P09959	160	Phosphoserine%3B
+P09959	176	Phosphoserine
+P09959	179	Phosphothreonine
+P09959	182	Phosphothreonine
+P09959	547	Phosphoserine
+P46655	300	Phosphothreonine
+P53277	45	Phosphoserine
+P53277	124	Phosphoserine
+P53277	125	Phosphoserine
+P11972	252	Phosphoserine
+P11972	408	Phosphoserine
+P11972	539	Phosphoserine%3B
+P11972	587	Phosphoserine
+P41930	444	Phosphoserine
+P41930	448	Phosphoserine
+P41930	450	Phosphoserine
+P08153	225	Phosphoserine
+P08153	278	Phosphoserine
+P08153	300	Phosphoserine
+P08153	339	Phosphothreonine
+P08153	376	Phosphoserine
+P08153	488	Phosphoserine
+P08153	492	Phosphoserine
+P08153	505	Phosphoserine
+P08153	522	Phosphoserine%3B
+P08153	646	Phosphoserine%3B
+P08153	664	Phosphoserine%3B
+P53852	326	Phosphoserine
+P23615	94	Phosphoserine
+P23615	134	Phosphoserine
+P23615	136	Phosphoserine
+P23615	148	Phosphoserine
+P23615	155	Phosphoserine
+P23615	206	Phosphoserine
+P23615	295	Phosphoserine
+Q08673	23	N-linked
+Q08673	174	N-linked
+Q08673	200	N-linked
+Q08673	206	N-linked
+P10080	2	N-acetylserine
+P10080	91	Phosphothreonine
+P10080	119	Phosphothreonine
+P10080	242	Phosphothreonine
+P10080	244	Phosphoserine
+P53599	57	Phosphoserine
+P53599	62	Phosphoserine
+P53599	78	Phosphoserine
+P53599	118	Phosphoserine
+P53599	290	Phosphoserine
+P53599	1424	Phosphoserine
+Q07084	110	Phosphoserine
+Q07084	195	Phosphoserine
+Q07084	327	Phosphoserine
+Q07084	351	Phosphoserine
+Q07084	368	Phosphoserine
+Q07084	380	Phosphoserine
+Q07084	554	4-aspartylphosphate
+Q07084	673	Phosphoserine
+Q07084	693	Phosphothreonine
+Q07084	703	Phosphoserine
+Q07084	706	Phosphoserine
+Q12427	254	Phosphoserine
+P36085	514	Phosphoserine
+D6VTK4	310	Phosphoserine
+D6VTK4	315	Phosphoserine
+D6VTK4	329	Phosphothreonine
+D6VTK4	331	Phosphoserine
+D6VTK4	360	Phosphoserine
+D6VTK4	363	Phosphothreonine
+D6VTK4	366	Phosphoserine
+D6VTK4	382	Phosphothreonine
+D6VTK4	385	Phosphoserine
+D6VTK4	386	Phosphoserine
+D6VTK4	411	Phosphothreonine
+D6VTK4	414	Phosphothreonine
+D6VTK4	25	N-linked
+D6VTK4	32	N-linked
+D6VTK4	374	Glycyl
+D6VTK4	400	Glycyl
+D6VTK4	422	Glycyl
+P25344	202	Phosphoserine
+P25344	244	Phosphothreonine
+P25344	248	Phosphoserine
+P16965	28	Phosphoserine
+P16965	69	Phosphoserine
+P53312	102	Phosphoserine
+P53312	263	Phosphoserine
+P53312	276	Phosphoserine
+P38359	51	N-linked
+P38359	93	N-linked
+P38359	358	N-linked
+P38359	391	N-linked
+P38359	630	N-linked
+P38359	653	N-linked
+P38359	718	N-linked
+Q03088	471	Phosphoserine
+Q03088	496	Phosphothreonine
+Q03088	551	Phosphoserine
+Q03088	662	Phosphoserine
+Q03088	739	Phosphothreonine
+Q03088	756	Phosphothreonine
+Q03088	757	Phosphoserine
+Q06677	52	Phosphoserine
+Q06677	64	Phosphoserine
+Q06677	264	Phosphoserine
+Q06677	308	Phosphoserine
+Q06677	312	Phosphoserine
+P32828	14	Phosphoserine
+P32828	29	Phosphoserine
+Q08817	214	Phosphothreonine
+P39543	35	N-linked
+P39543	53	N-linked
+P39543	85	N-linked
+P39543	115	N-linked
+P39543	170	N-linked
+P53148	77	Phosphoserine
+P53148	356	Phosphothreonine
+P53148	380	Phosphoserine
+P06844	270	Phosphoserine
+P32916	239	Phosphoserine
+P32916	523	Phosphoserine
+P12954	833	Phosphoserine
+P13130	26	N-linked
+P13130	50	N-linked
+P13130	58	N-linked
+P13130	64	N-linked
+P13130	76	N-linked
+P13130	108	N-linked
+P13130	181	N-linked
+P13130	190	N-linked
+P13130	199	N-linked
+P13130	205	N-linked
+P13130	248	N-linked
+P13130	281	N-linked
+Q07549	134	Phosphoserine
+Q07549	2	S-palmitoyl
+Q07549	3	S-palmitoyl
+Q07549	5	S-palmitoyl
+Q07549	7	S-palmitoyl
+Q07549	8	S-palmitoyl
+Q07549	128	Glycyl
+Q04477	2	N-acetylserine
+P40014	2	N-acetylalanine
+Q03012	87	Phosphoserine
+P25380	440	GPI-anchor
+P25380	256	N-linked
+P25380	314	N-linked
+P25380	327	N-linked
+P27692	35	Phosphothreonine
+P27692	133	Phosphothreonine
+P27692	136	Phosphoserine
+P27692	188	Phosphoserine
+P27692	219	Phosphoserine
+P39015	2	N-acetylserine
+P39015	55	Phosphoserine
+P39015	118	Phosphoserine
+P39015	229	Phosphoserine
+P39015	46	Glycyl
+P39015	121	Glycyl
+P39015	171	Glycyl
+P39015	184	Glycyl
+Q05937	71	Phosphoserine
+Q05937	111	Phosphoserine
+Q07351	153	Phosphoserine
+Q07351	155	Phosphoserine
+Q12038	591	Phosphoserine
+Q12038	602	Phosphoserine
+P32583	133	Phosphoserine
+P32583	289	Phosphothreonine
+P32583	293	Phosphoserine
+P32583	394	Phosphoserine
+P38931	370	Phosphoserine
+P38931	375	Phosphoserine
+P38931	425	Phosphoserine
+P38931	601	Phosphothreonine
+P38931	608	Phosphoserine%3B
+P38931	636	Phosphoserine
+P38931	748	Phosphoserine
+P37296	1	N-acetylmethionine
+P37296	223	Phosphoserine
+P37296	228	Phosphoserine
+P31377	238	S-palmitoyl
+P36126	2	N-acetylserine
+P36126	8	Phosphoserine
+P36126	30	Phosphoserine
+P36126	145	Phosphoserine
+P36126	1461	Phosphoserine
+P36126	1462	Phosphothreonine
+Q07798	2	N-linked
+Q07798	184	N-linked
+Q07798	503	N-linked
+P08459	475	GPI-anchor
+P08459	77	N-linked
+P08459	135	N-linked
+P08459	285	N-linked
+P08459	303	N-linked
+P08459	340	N-linked
+P08459	343	N-linked
+P08459	355	N-linked
+P38789	301	Phosphothreonine
+P39926	31	Phosphoserine
+P39926	34	Phosphoserine
+P38788	477	Phosphoserine
+P38788	480	Phosphoserine
+P25379	2	N-acetylserine
+P25379	37	N6-(pyridoxal
+P33894	377	N-linked
+P33894	814	N-linked
+P53101	213	N6-(pyridoxal
+P46676	2	N-acetylserine
+P46676	378	Phosphoserine
+P46676	379	Phosphoserine
+P46676	628	Phosphoserine
+P46676	681	Phosphoserine
+P46676	697	Phosphothreonine
+P46676	712	Phosphoserine%3B
+P46676	738	Phosphoserine
+P46676	817	Phosphothreonine
+P53616	395	N-linked
+P33300	349	Phosphoserine
+P54003	293	Phosphoserine
+P54003	301	Phosphoserine
+P54003	47	N-linked
+P04802	2	N-acetylserine
+P04802	14	Phosphoserine
+P04802	301	Phosphoserine
+P04802	502	Phosphoserine
+P04802	546	Phosphoserine
+Q02875	350	Phosphothreonine
+P54000	119	Phosphoserine
+P54000	268	Phosphoserine
+P54000	269	Phosphoserine
+P54000	289	Phosphoserine
+Q07478	2	N-acetylserine
+Q07478	13	Phosphoserine
+Q07478	37	Phosphoserine
+Q07478	169	Phosphothreonine
+P53201	2	N-acetylserine
+P38326	209	Phosphoserine
+P38088	25	N-acetylserine
+P38088	226	Phosphoserine
+P38088	476	Phosphoserine
+P38088	528	Phosphoserine
+P38088	689	Phosphothreonine
+Q6WNK7	68	Glycyl
+P38869	115	N-linked
+P32591	88	Phosphoserine
+P32591	185	Phosphoserine
+P32591	235	Phosphothreonine
+P32591	657	Phosphoserine
+P40825	504	Phosphoserine
+P40825	975	Phosphoserine
+P40528	172	Phosphoserine
+P40528	179	Phosphoserine
+P40528	859	Phosphoserine
+P40528	860	Phosphoserine
+P46679	594	Phosphoserine
+P46679	625	Phosphoserine
+P23561	323	Phosphoserine
+P23561	465	Phosphoserine
+P01098	24	Phosphoserine
+P39007	60	N-linked
+P39007	535	N-linked
+P39007	539	N-linked
+P38198	997	Phosphoserine
+P38198	1018	Phosphoserine
+P38198	1047	Phosphothreonine
+P38198	1063	Phosphoserine
+P38198	1167	Phosphoserine
+P46675	2	Phosphoserine
+P46675	277	Phosphoserine
+P46675	813	Phosphoserine
+P32911	2	N-acetylserine
+Q12254	23	N-linked
+Q12254	249	N-linked
+Q12254	256	N-linked
+P15180	2	N-acetylserine
+P15180	30	Phosphoserine
+P15180	62	Phosphothreonine
+P15180	308	Glycyl
+P15180	577	Glycyl
+Q05506	2	N-acetylalanine
+Q05506	15	Phosphoserine
+P40150	2	N-acetylalanine
+P40150	47	Phosphothreonine
+P40150	431	Phosphothreonine
+P13574	29	Phosphothreonine
+P13574	214	Phosphoserine
+P13574	226	Phosphoserine
+P13574	289	Phosphothreonine
+P13574	400	Phosphoserine
+P32597	38	Phosphoserine
+P37297	459	Phosphoserine
+P32944	36	Phosphoserine%3B
+P32944	45	Phosphothreonine%3B
+P32944	56	Phosphoserine%3B
+P32944	63	Phosphoserine%3B
+P32944	70	Phosphoserine
+P32944	74	Phosphothreonine%3B
+P32944	102	Phosphoserine%3B
+P32944	105	Phosphoserine%3B
+P32944	111	Phosphoserine%3B
+P32944	118	Phosphoserine%3B
+P32944	121	Phosphothreonine%3B
+P32944	124	Phosphothreonine%3B
+P32944	127	Phosphoserine%3B
+P32944	131	Phosphothreonine%3B
+P32944	133	Phosphoserine%3B
+P32944	136	Phosphoserine%3B
+P32944	156	Phosphoserine%3B
+P32944	169	Phosphoserine%3B
+P32944	196	Phosphothreonine%3B
+P32944	201	Phosphoserine%3B
+P32944	225	Phosphoserine%3B
+P32944	254	Phosphoserine%3B
+P32944	262	Phosphoserine
+P32944	263	Phosphoserine%3B
+P32944	266	Phosphoserine%3B
+P32944	280	Phosphothreonine%3B
+P32944	284	Phosphoserine
+P32944	294	Phosphoserine
+P32944	312	Phosphoserine%3B
+P32944	345	Phosphoserine
+P32944	367	Phosphothreonine%3B
+P32944	373	Phosphothreonine%3B
+P32944	379	Phosphoserine%3B
+P32944	384	Phosphothreonine%3B
+P32944	395	Phosphoserine%3B
+P32944	438	Phosphoserine%3B
+P32944	610	Phosphoserine%3B
+P32944	629	Phosphothreonine%3B
+P32944	688	Phosphothreonine%3B
+P32944	692	Phosphothreonine
+P32944	741	Glycyl
+P25302	255	Phosphoserine
+P25302	806	Phosphoserine
+P15625	2	N-acetylserine
+P07806	73	Phosphoserine
+P07806	294	Phosphoserine
+P07806	332	Phosphoserine
+P07806	707	Phosphoserine
+P07806	1003	Phosphothreonine
+P41895	198	Phosphoserine
+P41895	200	Phosphothreonine
+P41895	515	Phosphoserine
+P41895	560	Phosphoserine
+P41895	562	Phosphoserine
+P41895	571	Phosphoserine
+P41895	655	Phosphoserine
+Q12030	58	Phosphoserine
+Q12030	146	Phosphoserine
+P35189	181	Glycyl
+P23255	158	Phosphothreonine
+P23255	161	Phosphothreonine
+P23255	163	Phosphoserine
+P23255	318	Phosphoserine
+Q12297	237	Phosphothreonine
+Q12297	310	Phosphoserine
+Q12297	346	Phosphoserine
+P09436	829	Phosphoserine
+P09436	1059	Phosphoserine
+P09436	486	Glycyl
+Q06836	277	Phosphothreonine
+Q06836	369	Phosphoserine
+P25638	2	N-acetylserine
+P15019	2	N-acetylserine
+P13188	378	Phosphoserine
+P32774	95	Phosphoserine
+P32774	102	Phosphoserine
+P36421	2	N-acetylserine
+P36421	235	Phosphoserine
+P36421	359	Phosphothreonine
+Q04226	236	Phosphoserine
+Q04226	238	Phosphoserine
+P38129	299	Phosphoserine
+P38129	411	Phosphoserine
+P38129	415	Phosphoserine
+P38129	787	Phosphoserine
+Q03750	269	Phosphoserine
+Q04545	527	Phosphoserine
+Q04545	603	Phosphoserine
+P34163	462	Phosphoserine
+P34163	466	Phosphoserine
+P34163	521	Phosphoserine
+P34163	538	Phosphoserine
+P34163	539	Phosphothreonine
+P34163	246	Glycyl
+Q12043	645	Phosphoserine
+Q12043	270	N-linked
+Q12043	289	N-linked
+Q12043	297	N-linked
+Q12043	304	N-linked
+Q12043	321	N-linked
+Q12043	474	N-linked
+Q12043	589	N-linked
+Q12043	680	N-linked
+Q12043	714	N-linked
+Q12043	742	N-linked
+P04801	195	Phosphoserine
+P04801	289	Phosphoserine
+P04801	297	Phosphothreonine
+P04801	381	Phosphothreonine
+P04801	453	Phosphoserine
+P04801	457	Phosphoserine
+P04801	460	Phosphothreonine
+P04801	605	Phosphoserine
+P38854	236	Phosphothreonine
+P38854	244	Phosphoserine
+P38854	286	Phosphoserine
+Q03533	504	Phosphothreonine
+Q03533	509	Phosphoserine
+Q03533	518	Phosphoserine
+Q03533	538	Phosphothreonine
+Q03533	578	Phosphoserine
+P40045	2	N-acetylserine
+P02557	278	Phosphoserine
+P02557	280	Phosphoserine
+Q12466	1000	Phosphoserine
+Q03640	67	Phosphoserine
+Q03640	112	Phosphoserine
+Q03640	1340	Phosphoserine
+Q03640	1342	Phosphoserine
+Q03640	1346	Phosphoserine
+Q03640	1350	Phosphothreonine
+Q03640	1354	Phosphoserine
+Q03640	1400	Phosphoserine
+P40533	38	N-linked
+P40533	147	N-linked
+P40533	229	N-linked
+P40533	266	N-linked
+P40533	307	N-linked
+Q03761	2	N-acetylserine
+Q03761	129	Phosphoserine
+Q03761	286	Phosphoserine
+P50105	36	Phosphoserine
+P50105	49	Phosphoserine
+P50105	80	Phosphoserine
+P53072	72	Phosphoserine
+P39076	2	N-acetylserine
+P39079	2	N-acetylserine
+P39079	249	Phosphoserine
+P38758	189	Phosphoserine
+P38758	204	Phosphoserine
+P38758	306	Phosphoserine
+P53882	628	Phosphoserine
+P53882	4	N-linked
+P53882	257	N-linked
+P53882	492	N-linked
+P53882	557	N-linked
+P53882	562	N-linked
+P53882	626	N-linked
+P53882	512	Glycyl
+Q12004	1	N-acetylmethionine
+P34111	546	Phosphoserine
+P40085	22	Phosphoserine
+P40085	318	N-linked
+P38756	259	Phosphoserine
+Q06466	61	N-linked
+Q06466	124	N-linked
+Q06466	141	N-linked
+P47988	22	Phosphothreonine
+P47988	755	Phosphothreonine
+P18412	2	N-acetylserine
+P18412	325	Phosphoserine
+P53038	417	Phosphoserine
+P53038	419	Phosphoserine
+P32367	617	Phosphoserine
+P53215	2	N-acetylalanine
+Q07748	62	N6-(pyridoxal
+Q08579	560	Phosphoserine
+Q08579	572	Phosphoserine
+P41544	192	Phosphoserine
+P41544	15	Glycyl
+P41896	28	Phosphoserine
+P41896	34	Phosphoserine
+P41896	56	Phosphoserine
+Q05021	99	Phosphotyrosine
+Q05021	101	Phosphoserine
+Q05021	104	Phosphoserine
+P40468	141	Phosphoserine
+P40468	1144	Phosphoserine
+P40468	2264	Phosphothreonine
+P40468	2267	Phosphoserine
+P40468	2355	Phosphoserine
+P26637	2	N-acetylserine
+P26637	142	Phosphothreonine
+P00958	2	N-acetylserine
+P36145	52	Phosphoserine
+P36145	97	Phosphoserine
+P36145	106	Phosphoserine
+P11747	131	Phosphothreonine
+P38085	13	Phosphoserine
+P38085	80	Phosphoserine
+P38085	84	Phosphoserine
+P38085	39	Glycyl
+P48606	94	Phosphoserine
+P48231	991	Phosphoserine
+P12612	2	N-acetylserine
+P47079	505	Phosphoserine
+P47079	15	Glycyl
+P38321	105	Phosphoserine
+P38177	433	Phosphoserine
+P38177	439	Phosphoserine
+Q07793	416	Phosphoserine
+Q05497	113	Phosphoserine
+P43600	25	N-linked
+P43600	26	N-linked
+P43600	53	N-linked
+P43600	77	N-linked
+P43600	163	N-linked
+P53185	856	Phosphoserine
+P53185	898	Phosphoserine
+P0CX18	184	GPI-anchor
+P0CX18	28	N-linked
+P0CX18	138	N-linked
+Q03856	416	Phosphoserine
+O74302	416	Phosphoserine
+P0CX70	416	Phosphoserine
+Q12424	28	N-linked
+Q12424	148	N-linked
+Q12424	280	N-linked
+Q12424	329	N-linked
+Q12424	645	N-linked
+Q07629	43	N-linked
+Q07629	129	N-linked
+P14680	38	Phosphoserine
+P14680	115	Phosphoserine
+P14680	118	Phosphoserine
+P14680	127	Phosphoserine
+P14680	206	Phosphoserine
+P14680	240	Phosphoserine
+P14680	245	Phosphoserine
+P14680	247	Phosphoserine
+P14680	288	Phosphothreonine
+P14680	295	Phosphoserine
+P14680	530	Phosphotyrosine
+P46683	78	Phosphoserine
+P39548	217	Glycyl
+P40917	85	Phosphoserine
+P40917	89	Phosphoserine
+P40917	196	Phosphoserine
+Q3E821	33	N-linked
+Q3E6R4	42	GPI-anchor
+Q3E6R4	20	N-linked
+Q3E6R4	24	N-linked
+Q3E6R4	27	N-linked
+Q3E6R4	30	N-linked
+Q3E6R4	33	N-linked
+Q03612	416	Phosphoserine
+P40052	18	Phosphoserine
+P40052	39	Phosphoserine
+P40052	41	Phosphoserine
+P40052	57	Phosphoserine
+P40052	60	Phosphoserine
+P40052	178	Phosphoserine
+P40052	189	Phosphoserine
+P40052	192	Phosphoserine
diff --git a/test_files/uniprot_mod_raw.txt b/test_files/uniprot_mod_raw.txt
new file mode 100644
index 0000000..3ee2a2a
--- /dev/null
+++ b/test_files/uniprot_mod_raw.txt
@@ -0,0 +1,92278 @@
+##gff-version 3
+##sequence-region P12688 1 680
+P12688	UniProtKB	Chain	1	680	.	.	.	ID=PRO_0000086835;Note=Serine/threonine-protein kinase YPK1	
+P12688	UniProtKB	Domain	347	602	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P12688	UniProtKB	Domain	603	673	.	.	.	Note=AGC-kinase C-terminal	
+P12688	UniProtKB	Nucleotide binding	353	361	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P12688	UniProtKB	Active site	470	470	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P12688	UniProtKB	Binding site	376	376	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P12688	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P12688	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12688	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12688	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12688	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P12688	UniProtKB	Modified residue	502	502	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12688	UniProtKB	Modified residue	504	504	.	.	.	Note=Phosphothreonine%3B by PKH1;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10074427,ECO:0000269|PubMed:15840588;Dbxref=PMID:19779198,PMID:10074427,PMID:15840588	
+P12688	UniProtKB	Modified residue	644	644	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P12688	UniProtKB	Modified residue	653	653	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P12688	UniProtKB	Modified residue	662	662	.	.	.	Note=Phosphothreonine%3B by PKH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15840588;Dbxref=PMID:15840588	
+P12688	UniProtKB	Modified residue	671	671	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12688	UniProtKB	Mutagenesis	376	376	.	.	.	Note=No kinase activity. ATP-binding defect. Internalization defects. K->A%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10825204,ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:12221112,ECO:0000269|PubMed:15470109,ECO:0000269|PubMed:15820214,ECO:0000269|PubMed:15840588;Dbxref=PMID:10825204,PMID:11807089,PMID:12221112,PMID:15470109,PMID:15820214,PMID:15840588	
+P12688	UniProtKB	Mutagenesis	488	488	.	.	.	Note=Catalytically inactive. Internalization defects. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15470109;Dbxref=PMID:11807089,PMID:15470109	
+P12688	UniProtKB	Mutagenesis	490	490	.	.	.	Note=Reduced sphingolipid biosynthesis inhibitor drug myriocin (ISP-1) resistance. Defective in growth and endocytosis. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15820214;Dbxref=PMID:11807089,PMID:15820214	
+P12688	UniProtKB	Mutagenesis	504	504	.	.	.	Note=Reduced sphingolipid biosynthesis inhibitor drug myriocin (ISP-1) resistance. Defective in growth and endocytosis. T->A%2CD%2CE;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15470109,ECO:0000269|PubMed:15820214,ECO:0000269|PubMed:15840588;Dbxref=PMID:11807089,PMID:15470109,PMID:15820214,PMID:15840588	
+P12688	UniProtKB	Mutagenesis	504	504	.	.	.	Note=No phosphorylation%3B when associated with A-662 or D-662. T->A%2CD;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15470109,ECO:0000269|PubMed:15820214,ECO:0000269|PubMed:15840588;Dbxref=PMID:11807089,PMID:15470109,PMID:15820214,PMID:15840588	
+P12688	UniProtKB	Mutagenesis	662	662	.	.	.	Note=No phosphorylation%3B when associated with A-504 or D-504. T->A%2CD;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15470109,ECO:0000269|PubMed:15820214,ECO:0000269|PubMed:15840588;Dbxref=PMID:11807089,PMID:15470109,PMID:15820214,PMID:15840588	
+P12688	UniProtKB	Mutagenesis	662	662	.	.	.	Note=No phosphorylation. Reduced sphingolipid biosynthesis inhibitor drug myriocin (ISP-1) resistance. No defect in growth or endocytosis. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15470109,ECO:0000269|PubMed:15820214,ECO:0000269|PubMed:15840588;Dbxref=PMID:11807089,PMID:15470109,PMID:15820214,PMID:15840588	
+P12688	UniProtKB	Sequence conflict	201	201	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12688	UniProtKB	Sequence conflict	553	553	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25491 1 409
+P25491	UniProtKB	Chain	1	406	.	.	.	ID=PRO_0000071093;Note=Mitochondrial protein import protein MAS5	
+P25491	UniProtKB	Propeptide	407	409	.	.	.	ID=PRO_0000396684;Note=Removed in mature form;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25491	UniProtKB	Domain	4	72	.	.	.	Note=J	
+P25491	UniProtKB	Repeat	143	150	.	.	.	Note=CXXCXGXG motif	
+P25491	UniProtKB	Repeat	159	166	.	.	.	Note=CXXCXGXG motif	
+P25491	UniProtKB	Repeat	185	192	.	.	.	Note=CXXCXGXG motif	
+P25491	UniProtKB	Repeat	201	208	.	.	.	Note=CXXCXGXG motif	
+P25491	UniProtKB	Zinc finger	130	213	.	.	.	Note=CR-type	
+P25491	UniProtKB	Region	1	172	.	.	.	Note=Necessary for HAP1 repression in the absence of heme	
+P25491	UniProtKB	Region	135	137	.	.	.	Note=Substrate binding	
+P25491	UniProtKB	Region	215	216	.	.	.	Note=Substrate binding	
+P25491	UniProtKB	Region	247	249	.	.	.	Note=Substrate binding	
+P25491	UniProtKB	Compositional bias	73	103	.	.	.	Note=Gly-rich	
+P25491	UniProtKB	Metal binding	143	143	.	.	.	Note=Zinc 1	
+P25491	UniProtKB	Metal binding	146	146	.	.	.	Note=Zinc 1	
+P25491	UniProtKB	Metal binding	159	159	.	.	.	Note=Zinc 2	
+P25491	UniProtKB	Metal binding	162	162	.	.	.	Note=Zinc 2	
+P25491	UniProtKB	Metal binding	185	185	.	.	.	Note=Zinc 2	
+P25491	UniProtKB	Metal binding	188	188	.	.	.	Note=Zinc 2	
+P25491	UniProtKB	Metal binding	201	201	.	.	.	Note=Zinc 1	
+P25491	UniProtKB	Metal binding	204	204	.	.	.	Note=Zinc 1	
+P25491	UniProtKB	Binding site	116	116	.	.	.	Note=Substrate%3B via amide nitrogen	
+P25491	UniProtKB	Site	335	335	.	.	.	Note=Involved in dimerization	
+P25491	UniProtKB	Modified residue	406	406	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25491	UniProtKB	Lipidation	406	406	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1527016;Dbxref=PMID:1527016	
+P25491	UniProtKB	Cross-link	198	198	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25491	UniProtKB	Mutagenesis	335	335	.	.	.	Note=Prevents dimerization. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14656432;Dbxref=PMID:14656432	
+P25491	UniProtKB	Beta strand	116	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Helix	126	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	131	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Turn	144	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Turn	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	162	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	168	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	189	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	209	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	229	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	247	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO	
+P25491	UniProtKB	Beta strand	265	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO	
+P25491	UniProtKB	Helix	274	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO	
+P25491	UniProtKB	Beta strand	281	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO	
+P25491	UniProtKB	Beta strand	288	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	292	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO	
+P25491	UniProtKB	Turn	299	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	308	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO	
+P25491	UniProtKB	Beta strand	319	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT	
+P25491	UniProtKB	Beta strand	327	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO	
+P25491	UniProtKB	Helix	343	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO	
+P25491	UniProtKB	Beta strand	367	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO	
+##sequence-region P16521 1 1044
+P16521	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649	
+P16521	UniProtKB	Chain	2	1044	.	.	.	ID=PRO_0000093458;Note=Elongation factor 3A	
+P16521	UniProtKB	Repeat	5	42	.	.	.	Note=HEAT 1	
+P16521	UniProtKB	Repeat	86	123	.	.	.	Note=HEAT 2	
+P16521	UniProtKB	Repeat	125	162	.	.	.	Note=HEAT 3	
+P16521	UniProtKB	Repeat	166	203	.	.	.	Note=HEAT 4	
+P16521	UniProtKB	Repeat	205	241	.	.	.	Note=HEAT 5	
+P16521	UniProtKB	Repeat	242	279	.	.	.	Note=HEAT 6	
+P16521	UniProtKB	Repeat	285	323	.	.	.	Note=HEAT 7	
+P16521	UniProtKB	Domain	426	641	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P16521	UniProtKB	Domain	667	993	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P16521	UniProtKB	Nucleotide binding	463	470	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P16521	UniProtKB	Nucleotide binding	701	708	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P16521	UniProtKB	Compositional bias	1009	1031	.	.	.	Note=Lys-rich (basic)	
+P16521	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649	
+P16521	UniProtKB	Modified residue	187	187	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802	
+P16521	UniProtKB	Modified residue	196	196	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802	
+P16521	UniProtKB	Modified residue	642	642	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P16521	UniProtKB	Modified residue	789	789	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802	
+P16521	UniProtKB	Modified residue	972	972	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P16521	UniProtKB	Modified residue	974	974	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P16521	UniProtKB	Modified residue	1039	1039	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P16521	UniProtKB	Modified residue	1040	1040	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P16521	UniProtKB	Cross-link	350	350	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P16521	UniProtKB	Cross-link	636	636	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P16521	UniProtKB	Mutagenesis	650	650	.	.	.	Note=Reduces ATPase activity and interaction with eEF1A. Required for growth at 37 degrees Celsius and causes a 50%25 reduction of total protein synthesis at permissive temperatures. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12493761;Dbxref=PMID:12493761	
+P16521	UniProtKB	Sequence conflict	153	153	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16521	UniProtKB	Sequence conflict	153	153	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16521	UniProtKB	Sequence conflict	153	153	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16521	UniProtKB	Sequence conflict	332	332	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16521	UniProtKB	Sequence conflict	332	332	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16521	UniProtKB	Sequence conflict	332	332	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16521	UniProtKB	Helix	3	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	23	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	26	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	48	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	61	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	85	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	92	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	104	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	126	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	143	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	161	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	184	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	210	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	222	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	241	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	257	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	260	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	280	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	284	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	291	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	304	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	338	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	349	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	356	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	359	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	380	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	388	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	392	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	397	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	426	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	430	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	443	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	458	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	469	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	487	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	492	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	508	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	514	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IX3	
+P16521	UniProtKB	Helix	520	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	534	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	541	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	546	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	563	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	570	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	576	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	591	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	600	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	608	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	617	623	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	625	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	633	637	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	638	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	641	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	664	674	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	679	681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IX3	
+P16521	UniProtKB	Beta strand	683	692	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	696	699	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	705	714	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	721	727	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	733	736	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	738	743	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	744	746	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	752	759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	760	762	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	766	772	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	783	785	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	788	790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	793	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	809	821	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	828	831	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	834	836	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	838	841	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	842	844	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	846	863	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	872	881	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	886	891	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	894	896	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	899	911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	916	921	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	923	925	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	929	940	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	943	949	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Helix	953	956	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Turn	957	959	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+P16521	UniProtKB	Beta strand	962	964	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3	
+##sequence-region P11484 1 613
+P11484	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P11484	UniProtKB	Chain	2	613	.	.	.	ID=PRO_0000078389;Note=Ribosome-associated molecular chaperone SSB1	
+P11484	UniProtKB	Nucleotide binding	16	18	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P11484	UniProtKB	Nucleotide binding	205	207	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P11484	UniProtKB	Nucleotide binding	271	278	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P11484	UniProtKB	Region	2	391	.	.	.	Note=Nucleotide binding domain (NBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P11484	UniProtKB	Region	392	402	.	.	.	Note=Inter-domain linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P11484	UniProtKB	Region	403	613	.	.	.	Note=Substrate binding domain (SBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P11484	UniProtKB	Region	516	612	.	.	.	Note=Lid domain (SBDalpha);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P11484	UniProtKB	Region	601	613	.	.	.	Note=Required for interaction with ribosomes;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27917864;Dbxref=PMID:27917864	
+P11484	UniProtKB	Motif	428	430	.	.	.	Note=Contributes to ribosome binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27917864;Dbxref=PMID:27917864	
+P11484	UniProtKB	Motif	574	582	.	.	.	Note=Nuclear export signal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10347213;Dbxref=PMID:10347213	
+P11484	UniProtKB	Binding site	73	73	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P11484	UniProtKB	Binding site	342	342	.	.	.	Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P11484	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P11484	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P11484	UniProtKB	Modified residue	431	431	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P11484	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Unable to hydrolyze ATP and moderately reduces ribosome binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27882919;Dbxref=PMID:27882919	
+P11484	UniProtKB	Mutagenesis	567	568	.	.	.	Note=In SSB1-L(BC): Reduces ribosome-binding to less than 50%25. KR->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27882919;Dbxref=PMID:27882919	
+P11484	UniProtKB	Mutagenesis	596	597	.	.	.	Note=In SSB1-D1: Reduces ribosome-binding to less than 50%25. RK->DD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27882919;Dbxref=PMID:27882919	
+P11484	UniProtKB	Mutagenesis	603	604	.	.	.	Note=In SSB1-D2: Reduces ribosome-binding to less than 50%25. KR->DD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27882919;Dbxref=PMID:27882919	
+P11484	UniProtKB	Sequence conflict	180	184	.	.	.	Note=AAAIA->VVVIV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11484	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11484	UniProtKB	Sequence conflict	192	192	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11484	UniProtKB	Beta strand	10	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	16	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	55	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Turn	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	83	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	93	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	102	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	112	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	118	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	143	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	154	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	170	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	177	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Turn	185	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	196	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	208	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	219	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	233	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	260	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Turn	277	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	280	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	294	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	302	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	310	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	317	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	331	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Beta strand	336	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	342	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	347	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Turn	357	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Turn	368	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+P11484	UniProtKB	Helix	371	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1	
+##sequence-region P39940 1 809
+P39940	UniProtKB	Chain	1	809	.	.	.	ID=PRO_0000120335;Note=E3 ubiquitin-protein ligase RSP5	
+P39940	UniProtKB	Domain	1	88	.	.	.	Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+P39940	UniProtKB	Domain	229	262	.	.	.	Note=WW 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224	
+P39940	UniProtKB	Domain	331	364	.	.	.	Note=WW 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224	
+P39940	UniProtKB	Domain	387	420	.	.	.	Note=WW 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224	
+P39940	UniProtKB	Domain	705	809	.	.	.	Note=HECT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104	
+P39940	UniProtKB	Compositional bias	315	322	.	.	.	Note=Poly-Ala	
+P39940	UniProtKB	Active site	777	777	.	.	.	Note=Glycyl thioester intermediate	
+P39940	UniProtKB	Cross-link	258	258	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P39940	UniProtKB	Mutagenesis	516	516	.	.	.	Note=Has subtle defects on both initial ubiquitination and chain elongation of substrate proteins. Y->A	
+P39940	UniProtKB	Mutagenesis	521	521	.	.	.	Note=Has defects on both initial ubiquitination and chain elongation of substrate proteins. Y->A	
+P39940	UniProtKB	Mutagenesis	537	537	.	.	.	Note=Has defects on both initial ubiquitination and chain elongation of substrate proteins. I->D	
+P39940	UniProtKB	Mutagenesis	618	618	.	.	.	Note=Has defects on both initial ubiquitination and chain elongation of substrate proteins. F->D	
+P39940	UniProtKB	Mutagenesis	733	733	.	.	.	Note=In RSP5-1%3B impairs ubiquitin-thioester formation and catalysis of substrate ubiquitination. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9858558;Dbxref=PMID:9858558	
+P39940	UniProtKB	Mutagenesis	777	777	.	.	.	Note=Loss of ubiquitination. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9858558;Dbxref=PMID:9858558	
+P39940	UniProtKB	Beta strand	393	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LCD	
+P39940	UniProtKB	Beta strand	405	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OLM	
+P39940	UniProtKB	Turn	408	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OLM	
+P39940	UniProtKB	Beta strand	412	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OLM	
+P39940	UniProtKB	Helix	435	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	446	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Beta strand	451	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	461	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	464	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Beta strand	482	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	496	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	514	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Beta strand	517	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Beta strand	526	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	535	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	541	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	568	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	581	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	589	600	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Turn	604	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Beta strand	610	617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Beta strand	620	627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	630	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Beta strand	633	635	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LCD	
+P39940	UniProtKB	Turn	637	639	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	640	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Turn	653	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	657	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	673	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	681	689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	696	701	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Beta strand	703	708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	713	724	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	727	738	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	748	750	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Beta strand	754	757	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LCD	
+P39940	UniProtKB	Beta strand	760	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Beta strand	773	775	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Turn	776	779	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Beta strand	780	782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+P39940	UniProtKB	Helix	789	801	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL	
+##sequence-region Q04437 1 629
+Q04437	UniProtKB	Chain	1	629	.	.	.	ID=PRO_0000084339;Note=ATP-dependent DNA helicase II subunit 2	
+Q04437	UniProtKB	Domain	254	476	.	.	.	Note=Ku	
+Q04437	UniProtKB	Natural variant	149	149	.	.	.	Note=In strain: DBVPG6044%2C SK1 and YPS128. L->V	
+Q04437	UniProtKB	Natural variant	301	301	.	.	.	Note=In strain: DBVPG1853. S->L	
+Q04437	UniProtKB	Natural variant	349	349	.	.	.	Note=In strain: DBVPG6044%2C SK1 and YPS128. N->D	
+Q04437	UniProtKB	Natural variant	499	499	.	.	.	Note=In strain: DBVPG1853. G->D	
+Q04437	UniProtKB	Natural variant	518	518	.	.	.	Note=In strain: DBVPG6044%2C SK1 and YPS128. E->A	
+Q04437	UniProtKB	Natural variant	528	528	.	.	.	Note=In strain: DBVPG1853. T->A	
+Q04437	UniProtKB	Natural variant	585	585	.	.	.	Note=In strain: DBVPG6763. I->S	
+##sequence-region Q06224 1 779
+Q06224	UniProtKB	Chain	1	779	.	.	.	ID=PRO_0000076368;Note=Endoribonuclease YSH1	
+Q06224	UniProtKB	Active site	408	408	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06224	UniProtKB	Metal binding	68	68	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06224	UniProtKB	Metal binding	70	70	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06224	UniProtKB	Metal binding	72	72	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06224	UniProtKB	Metal binding	73	73	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06224	UniProtKB	Metal binding	163	163	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06224	UniProtKB	Metal binding	184	184	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06224	UniProtKB	Metal binding	184	184	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06224	UniProtKB	Metal binding	430	430	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06224	UniProtKB	Modified residue	517	517	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06224	UniProtKB	Mutagenesis	37	37	.	.	.	Note=Loss of endonuclease activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037765;Dbxref=PMID:15037765	
+Q06224	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Loss of endonuclease activity. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037765;Dbxref=PMID:15037765	
+Q06224	UniProtKB	Mutagenesis	184	184	.	.	.	Note=Loss of endonuclease activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037765;Dbxref=PMID:15037765	
+Q06224	UniProtKB	Mutagenesis	209	209	.	.	.	Note=Loss of endonuclease activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037765;Dbxref=PMID:15037765	
+Q06224	UniProtKB	Mutagenesis	408	408	.	.	.	Note=Loss of endonuclease activity. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037765;Dbxref=PMID:15037765	
+##sequence-region P32795 1 747
+P32795	UniProtKB	Chain	1	747	.	.	.	ID=PRO_0000084664;Note=Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1	
+P32795	UniProtKB	Nucleotide binding	321	328	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32795	UniProtKB	Active site	541	541	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32795	UniProtKB	Metal binding	540	540	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32795	UniProtKB	Metal binding	544	544	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32795	UniProtKB	Metal binding	618	618	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32795	UniProtKB	Mutagenesis	327	327	.	.	.	Note=Does not complement a YME1 deletion mutant%2C for K327R no longer binds or degrades COX2. Probably has no ATPase activity. K->I%2CR%2CT;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16527490,ECO:0000269|PubMed:8688560;Dbxref=PMID:16527490,PMID:8688560	
+P32795	UniProtKB	Mutagenesis	354	354	.	.	.	Note=Partially complements a YME1 deletion mutant. Y->A%2CC%2CI%2CL%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16527490;Dbxref=PMID:16527490	
+P32795	UniProtKB	Mutagenesis	354	354	.	.	.	Note=Complements a YME1 deletion mutant. Y->F%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16527490;Dbxref=PMID:16527490	
+P32795	UniProtKB	Mutagenesis	354	354	.	.	.	Note=Does not complement a YME1 deletion mutant. Y->K%2CN%2CR%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16527490;Dbxref=PMID:16527490	
+P32795	UniProtKB	Mutagenesis	354	354	.	.	.	Note=Does not complement a YME1 deletion mutant%2C retains 20%25 protease activity in vitro%2C binds an unfolded hybrid substrate protein. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16527490;Dbxref=PMID:16527490	
+P32795	UniProtKB	Mutagenesis	381	381	.	.	.	Note=Does not complement a YME1 deletion mutant%2C no longer binds or degrades COX2. Probably has no ATPase activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16527490;Dbxref=PMID:16527490	
+P32795	UniProtKB	Mutagenesis	541	541	.	.	.	Note=Does not complement a YME1 deletion mutant%2C for E541A stabilizes otherwise unstable COX2. E->A%2CG%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8688560;Dbxref=PMID:8688560	
+P32795	UniProtKB	Sequence conflict	52	52	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32795	UniProtKB	Sequence conflict	88	88	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32795	UniProtKB	Sequence conflict	584	584	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32795	UniProtKB	Helix	102	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MV3	
+P32795	UniProtKB	Helix	118	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MV3	
+P32795	UniProtKB	Helix	134	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MV3	
+P32795	UniProtKB	Helix	150	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MV3	
+P32795	UniProtKB	Helix	166	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MV3	
+##sequence-region Q06102 1 208
+Q06102	UniProtKB	Chain	1	208	.	.	.	ID=PRO_0000213910;Note=mRNA 3'-end-processing protein YTH1	
+Q06102	UniProtKB	Zinc finger	28	59	.	.	.	Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q06102	UniProtKB	Zinc finger	61	88	.	.	.	Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q06102	UniProtKB	Zinc finger	89	117	.	.	.	Note=C3H1-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q06102	UniProtKB	Zinc finger	118	145	.	.	.	Note=C3H1-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q06102	UniProtKB	Zinc finger	147	170	.	.	.	Note=C3H1-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q06102	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Lethal. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131	
+Q06102	UniProtKB	Mutagenesis	70	70	.	.	.	Note=Temperature- and formamide-sensitive%3B abolishes cleavage and polyadenylation activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131	
+Q06102	UniProtKB	Mutagenesis	75	75	.	.	.	Note=Lethal. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131	
+Q06102	UniProtKB	Mutagenesis	79	79	.	.	.	Note=Temperature- and formamide-sensitive%3B impaired polyadenylation activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131	
+Q06102	UniProtKB	Mutagenesis	81	81	.	.	.	Note=Lethal. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131	
+Q06102	UniProtKB	Mutagenesis	142	142	.	.	.	Note=Temperature- and formamide-sensitive%3B impaired polyadenylation activity. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131	
+##sequence-region P02829 1 709
+P02829	UniProtKB	Chain	1	709	.	.	.	ID=PRO_0000062957;Note=ATP-dependent molecular chaperone HSP82	
+P02829	UniProtKB	Repeat	221	225	.	.	.	Note=1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10786835;Dbxref=PMID:10786835	
+P02829	UniProtKB	Repeat	226	230	.	.	.	Note=2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10786835;Dbxref=PMID:10786835	
+P02829	UniProtKB	Repeat	231	235	.	.	.	Note=3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10786835;Dbxref=PMID:10786835	
+P02829	UniProtKB	Repeat	237	241	.	.	.	Note=4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10786835;Dbxref=PMID:10786835	
+P02829	UniProtKB	Repeat	250	254	.	.	.	Note=5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10786835;Dbxref=PMID:10786835	
+P02829	UniProtKB	Nucleotide binding	99	100	.	.	.	Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188	
+P02829	UniProtKB	Nucleotide binding	119	124	.	.	.	Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188	
+P02829	UniProtKB	Region	221	263	.	.	.	Note=5 X 5 AA repeats of [DE]-[DE]-[DE]-K-K%3B highly charged region	
+P02829	UniProtKB	Motif	705	709	.	.	.	Note=TPR repeat-binding	
+P02829	UniProtKB	Binding site	33	33	.	.	.	Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188	
+P02829	UniProtKB	Binding site	37	37	.	.	.	Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188	
+P02829	UniProtKB	Binding site	79	79	.	.	.	Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188	
+P02829	UniProtKB	Binding site	84	84	.	.	.	Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188	
+P02829	UniProtKB	Binding site	92	92	.	.	.	Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188	
+P02829	UniProtKB	Binding site	98	98	.	.	.	Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188	
+P02829	UniProtKB	Binding site	171	171	.	.	.	Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188	
+P02829	UniProtKB	Binding site	380	380	.	.	.	Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188	
+P02829	UniProtKB	Modified residue	657	657	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15108	
+P02829	UniProtKB	Mutagenesis	22	22	.	.	.	Note=Induces a 6-fold increase in ATPase activity and a reduced client protein activation activity%2C leading to growth defect at high temperatures. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797	
+P02829	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Causes a 98%25 reduction in ATPase activity and a reduced client protein activation activity%2C leading to growth defect at high temperatures. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797	
+P02829	UniProtKB	Mutagenesis	81	81	.	.	.	Note=Reduces client protein activation activity%2C leading to growth defect at high temperatures. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797	
+P02829	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Abolishes ATPase activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18256191;Dbxref=PMID:18256191	
+P02829	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Abolishes interaction with SBA1. A->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632755;Dbxref=PMID:9632755	
+P02829	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Causes a 90%25 reduction in ATPase activity and a reduced client protein activation activity%2C leading to growth defect at high temperatures. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797	
+P02829	UniProtKB	Mutagenesis	107	107	.	.	.	Note=Induces a 6-fold increase in ATPase activity. A->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10944121;Dbxref=PMID:10944121	
+P02829	UniProtKB	Mutagenesis	170	170	.	.	.	Note=Induces a total loss of function at 34 degrees Celsius. Abolishes interaction with SBA1. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797	
+P02829	UniProtKB	Mutagenesis	313	313	.	.	.	Note=Reduces client protein activation activity%2C leading to growth defect at high temperatures. G->N%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7791797,ECO:0000269|PubMed:8248264;Dbxref=PMID:7791797,PMID:8248264	
+P02829	UniProtKB	Mutagenesis	349	349	.	.	.	Note=Induces a loss of ATPase activity. Can be reactivated by AHA1. F->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12667448;Dbxref=PMID:12667448	
+P02829	UniProtKB	Mutagenesis	380	380	.	.	.	Note=Induces a loss of ATPase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12667448;Dbxref=PMID:12667448	
+P02829	UniProtKB	Mutagenesis	381	381	.	.	.	Note=Reduces client protein activation activity. Resistant to ATPase activation by AHA1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797	
+P02829	UniProtKB	Mutagenesis	384	384	.	.	.	Note=Induces a loss of ATPase activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12667448;Dbxref=PMID:12667448	
+P02829	UniProtKB	Mutagenesis	387	387	.	.	.	Note=Decreases AHA1 binding affinity%2C but has no effect on client protein activation activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935	
+P02829	UniProtKB	Mutagenesis	387	387	.	.	.	Note=Decreases AHA1 binding affinity and substantially reduces client protein activation activity. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935	
+P02829	UniProtKB	Mutagenesis	431	431	.	.	.	Note=Specifically reduces the activation of the exogenous ligand glucocorticoid receptor. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8248264;Dbxref=PMID:8248264	
+P02829	UniProtKB	Mutagenesis	485	485	.	.	.	Note=Abolishes interaction with SBA1. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632755;Dbxref=PMID:9632755	
+P02829	UniProtKB	Mutagenesis	525	525	.	.	.	Note=Abolishes interaction with SBA1. Reduces client protein activation activity%2C leading to growth defect at high temperatures. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8248264;Dbxref=PMID:8248264	
+P02829	UniProtKB	Mutagenesis	576	576	.	.	.	Note=Reduces client protein activation activity%3B when associated with K-579. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8248264;Dbxref=PMID:8248264	
+P02829	UniProtKB	Mutagenesis	577	577	.	.	.	Note=Enhances ATPase activity and client protein activation. A->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19696785;Dbxref=PMID:19696785	
+P02829	UniProtKB	Mutagenesis	577	577	.	.	.	Note=Reduces ATPase activity and client protein activation. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19696785;Dbxref=PMID:19696785	
+P02829	UniProtKB	Mutagenesis	577	577	.	.	.	Note=Enhances homodimerization%2C ATPase activity and client protein activation. A->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19696785;Dbxref=PMID:19696785	
+P02829	UniProtKB	Mutagenesis	577	577	.	.	.	Note=Reduces homodimerization%2C ATPase activity and client protein activation. A->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19696785;Dbxref=PMID:19696785	
+P02829	UniProtKB	Mutagenesis	579	579	.	.	.	Note=Reduces client protein activation activity%3B when associated with T-576. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8248264;Dbxref=PMID:8248264	
+P02829	UniProtKB	Mutagenesis	587	587	.	.	.	Note=No effect on ATPase activity. Reduces client protein activation activity%2C leading to growth defect at high temperatures. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797	
+P02829	UniProtKB	Sequence conflict	481	481	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02829	UniProtKB	Beta strand	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Helix	10	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ASB	
+P02829	UniProtKB	Helix	29	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Turn	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Helix	53	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Beta strand	64	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Helix	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Beta strand	74	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Helix	86	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Turn	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BRC	
+P02829	UniProtKB	Helix	101	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Helix	114	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Helix	123	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Beta strand	131	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Beta strand	146	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Beta strand	152	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Beta strand	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Beta strand	168	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Helix	182	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Helix	187	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Beta strand	200	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AKP	
+P02829	UniProtKB	Beta strand	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX	
+P02829	UniProtKB	Helix	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Helix	281	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Helix	286	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	304	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	313	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	317	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Turn	329	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	335	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P02829	UniProtKB	Beta strand	341	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	348	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	355	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HK7	
+P02829	UniProtKB	Helix	360	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	366	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Helix	380	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HK7	
+P02829	UniProtKB	Helix	387	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Helix	411	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Turn	433	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Helix	436	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	444	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	450	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Helix	457	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	470	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Helix	479	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Helix	488	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	498	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Helix	504	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Beta strand	519	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+P02829	UniProtKB	Turn	524	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HK7	
+P02829	UniProtKB	Beta strand	530	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Helix	535	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Beta strand	563	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Beta strand	573	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Beta strand	582	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Helix	587	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Beta strand	600	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Beta strand	611	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Helix	620	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Turn	630	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Helix	633	635	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Helix	637	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+P02829	UniProtKB	Helix	661	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE	
+##sequence-region P38801 1 184
+P38801	UniProtKB	Chain	1	184	.	.	.	ID=PRO_0000202902;Note=Exosome complex protein LRP1	
+P38801	UniProtKB	Helix	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC	
+P38801	UniProtKB	Helix	8	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC	
+P38801	UniProtKB	Helix	33	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC	
+P38801	UniProtKB	Helix	43	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC	
+P38801	UniProtKB	Helix	74	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC	
+##sequence-region P40009 1 630
+P40009	UniProtKB	Chain	1	630	.	.	.	ID=PRO_0000209920;Note=Golgi apyrase	
+P40009	UniProtKB	Topological domain	1	500	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40009	UniProtKB	Transmembrane	501	517	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40009	UniProtKB	Topological domain	518	630	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40009	UniProtKB	Active site	152	152	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40009	UniProtKB	Mutagenesis	152	152	.	.	.	Note=Expressed at lower levels. GTPase activity reduced. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227198;Dbxref=PMID:16227198	
+P40009	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Expressed at the same level as wild-type. GTPase and GDPase activities decreased more than 20-fold toward GTP and 3-fold for GDP. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227198;Dbxref=PMID:16227198	
+P40009	UniProtKB	Sequence conflict	498	498	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P10591 1 642
+P10591	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P10591	UniProtKB	Chain	2	642	.	.	.	ID=PRO_0000078385;Note=Heat shock protein SSA1	
+P10591	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P10591	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P10591	UniProtKB	Modified residue	551	551	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P10591	UniProtKB	Modified residue	603	603	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P10591	UniProtKB	Cross-link	556	556	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P10591	UniProtKB	Sequence conflict	208	208	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10591	UniProtKB	Sequence conflict	418	418	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10591	UniProtKB	Sequence conflict	422	422	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38340 1 232
+P38340	UniProtKB	Chain	1	232	.	.	.	ID=PRO_0000119292;Note=Alpha N-terminal protein methyltransferase 1	
+P38340	UniProtKB	Region	123	124	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38340	UniProtKB	Binding site	71	71	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38340	UniProtKB	Binding site	76	76	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38340	UniProtKB	Binding site	139	139	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P41800 1 426
+P41800	UniProtKB	Chain	1	426	.	.	.	ID=PRO_0000096506;Note=Maintenance of mitochondrial morphology protein 1	
+P41800	UniProtKB	Topological domain	1	100	.	.	.	Note=Lumenal	
+P41800	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03103	
+P41800	UniProtKB	Topological domain	122	426	.	.	.	Note=Cytoplasmic	
+P41800	UniProtKB	Glycosylation	6	6	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03103	
+P41800	UniProtKB	Glycosylation	50	50	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03103	
+P41800	UniProtKB	Glycosylation	55	55	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03103	
+P41800	UniProtKB	Glycosylation	59	59	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03103	
+P41800	UniProtKB	Mutagenesis	215	215	.	.	.	Note=In MMM1-6%3B impairs both mtDNA maintenance and mitochondrial morpholgy. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12454062;Dbxref=PMID:12454062	
+P41800	UniProtKB	Sequence conflict	200	200	.	.	.	Note=W->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41800	UniProtKB	Sequence conflict	225	225	.	.	.	Note=S->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41800	UniProtKB	Sequence conflict	357	357	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41800	UniProtKB	Sequence conflict	365	365	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41800	UniProtKB	Sequence conflict	368	368	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00546 1 298
+P00546	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P00546	UniProtKB	Chain	2	298	.	.	.	ID=PRO_0000085722;Note=Cyclin-dependent kinase 1	
+P00546	UniProtKB	Domain	8	295	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P00546	UniProtKB	Nucleotide binding	14	22	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P00546	UniProtKB	Active site	136	136	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P00546	UniProtKB	Binding site	40	40	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P00546	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P00546	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00546	UniProtKB	Modified residue	169	169	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P15108 1 705
+P15108	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7483834;Dbxref=PMID:7483834	
+P15108	UniProtKB	Chain	2	705	.	.	.	ID=PRO_0000062958;Note=ATP-dependent molecular chaperone HSC82	
+P15108	UniProtKB	Repeat	221	225	.	.	.	Note=1	
+P15108	UniProtKB	Repeat	226	230	.	.	.	Note=2	
+P15108	UniProtKB	Repeat	232	236	.	.	.	Note=3	
+P15108	UniProtKB	Repeat	246	250	.	.	.	Note=4	
+P15108	UniProtKB	Region	221	259	.	.	.	Note=4 X 5 AA repeats of [DE]-[DE]-[DE]-K-K%3B highly charged region	
+P15108	UniProtKB	Motif	701	705	.	.	.	Note=TPR repeat-binding	
+P15108	UniProtKB	Binding site	37	37	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15108	UniProtKB	Binding site	79	79	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15108	UniProtKB	Binding site	98	98	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15108	UniProtKB	Binding site	124	124	.	.	.	Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15108	UniProtKB	Binding site	376	376	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15108	UniProtKB	Modified residue	653	653	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P15108	UniProtKB	Mutagenesis	453	453	.	.	.	Note=Leads to growth defect at 37 degrees Celsius%2C probably by disrupting the intramolecular interaction of the N-termini with the middle domains%3B when associated with A-493. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121981;Dbxref=PMID:12121981	
+P15108	UniProtKB	Mutagenesis	493	493	.	.	.	Note=Leads to growth defect at 37 degrees Celsius%2C probably by disrupting the intramolecular interaction of the N-termini with the middle domains%3B when associated with A-453. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121981;Dbxref=PMID:12121981	
+P15108	UniProtKB	Sequence conflict	619	619	.	.	.	Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15108	UniProtKB	Sequence conflict	621	621	.	.	.	Note=L->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P31539 1 908
+P31539	UniProtKB	Chain	1	908	.	.	.	ID=PRO_0000191212;Note=Heat shock protein 104	
+P31539	UniProtKB	Nucleotide binding	212	219	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31539	UniProtKB	Nucleotide binding	614	621	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31539	UniProtKB	Region	167	411	.	.	.	Note=NBD1	
+P31539	UniProtKB	Region	541	731	.	.	.	Note=NBD2	
+P31539	UniProtKB	Region	905	908	.	.	.	Note=Interaction surface for TPR repeats	
+P31539	UniProtKB	Coiled coil	412	536	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31539	UniProtKB	Motif	773	789	.	.	.	Note=Nuclear localization signal	
+P31539	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P31539	UniProtKB	Modified residue	206	206	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P31539	UniProtKB	Modified residue	306	306	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P31539	UniProtKB	Modified residue	499	499	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P31539	UniProtKB	Modified residue	535	535	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P31539	UniProtKB	Cross-link	442	442	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P31539	UniProtKB	Cross-link	620	620	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538	
+P31539	UniProtKB	Mutagenesis	184	184	.	.	.	Note=Confers resistance to prion-curing by guanidine. D->A%2CD%2CF%2CN%2CL%2CQ%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105276;Dbxref=PMID:12105276	
+P31539	UniProtKB	Mutagenesis	184	184	.	.	.	Note=Impairs prion propagation. D->K%2CW%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105276;Dbxref=PMID:12105276	
+P31539	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Largely reduces ATP hydrolysis. Alters bud morphology and causes septin mislocalization%3B when associated with I-499. G->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11158570,ECO:0000269|PubMed:14978213,ECO:0000269|PubMed:9624144;Dbxref=PMID:11158570,PMID:14978213,PMID:9624144	
+P31539	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Completely abolishes ATP hydrolysis. G->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11158570,ECO:0000269|PubMed:14978213,ECO:0000269|PubMed:9624144;Dbxref=PMID:11158570,PMID:14978213,PMID:9624144	
+P31539	UniProtKB	Mutagenesis	218	218	.	.	.	Note=Abolishes substrate binding. Unable to confer thermotolerance. Reduces ATP hydrolysis by 98%25%3B when associated with T-315. Comletely abolishes ATPase activity%3B when associated with T-620. K->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11158570,ECO:0000269|PubMed:11442834,ECO:0000269|PubMed:11983167,ECO:0000269|PubMed:12101251,ECO:0000269|PubMed:16135516,ECO:0000269|PubMed:17259993,ECO:0000269|PubMed:17543332,ECO:0000269|PubMed:1896074,ECO:0000269|PubMed:8308017,ECO:0000269|PubMed:9624144;Dbxref=PMID:11158570,PMID:11442834,PMID:11983167,PMID:12101251,PMID:16135516,PMID:17259993,PMID:17543332,PMID:1896074,PMID:8308017,PMID:9624144	
+P31539	UniProtKB	Mutagenesis	257	257	.	.	.	Note=Reduces thermotolerance 10-fold. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15128736;Dbxref=PMID:15128736	
+P31539	UniProtKB	Mutagenesis	285	285	.	.	.	Note=In HSP104(TRAP)%3B completely abolishes ATP hydrolysis%2C but does not affect nucleotide binding%2C thus keeping HSP104 in an ATP-bound state%3B when associated with Q-687. E->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135516,ECO:0000269|PubMed:17543332;Dbxref=PMID:16135516,PMID:17543332	
+P31539	UniProtKB	Mutagenesis	315	315	.	.	.	Note=Reduces ATP hydrolysis by 98%25%3B when associated with T-218. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983167;Dbxref=PMID:11983167	
+P31539	UniProtKB	Mutagenesis	317	317	.	.	.	Note=Reduces rate of ATP hydrolysis at NBD1 nearly 10-fold. No effect on oligomerization. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11782421,ECO:0000269|PubMed:17259993;Dbxref=PMID:11782421,PMID:17259993	
+P31539	UniProtKB	Mutagenesis	334	334	.	.	.	Note=Reduces ATPase activity by 80%25. Impairs oligomerization. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18160044;Dbxref=PMID:18160044	
+P31539	UniProtKB	Mutagenesis	419	419	.	.	.	Note=Reduces ATPase activity by 80%25. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18160044;Dbxref=PMID:18160044	
+P31539	UniProtKB	Mutagenesis	444	444	.	.	.	Note=Reduces ATPase activity by 80%25. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18160044;Dbxref=PMID:18160044	
+P31539	UniProtKB	Mutagenesis	462	462	.	.	.	Note=Impairs prion propagation%2C but does not affect thermotolerance. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17367387;Dbxref=PMID:17367387	
+P31539	UniProtKB	Mutagenesis	495	495	.	.	.	Note=Increases ATPase activity 3-fold. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18160044;Dbxref=PMID:18160044	
+P31539	UniProtKB	Mutagenesis	499	499	.	.	.	Note=Reduces ATP hydrolysis by 50%25. Alters bud morphology and causes septin mislocalization%3B when associated with S-217. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978213;Dbxref=PMID:14978213	
+P31539	UniProtKB	Mutagenesis	503	503	.	.	.	Note=Increases basal level of ATPase activity and abolishes stimulation of ATP hydrolysis upon substrate binding. Inhibits growth at 37 degrees Celsius. A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11983167,ECO:0000269|PubMed:14978213;Dbxref=PMID:11983167,PMID:14978213	
+P31539	UniProtKB	Mutagenesis	509	509	.	.	.	Note=Reduces thermotolerance. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978213;Dbxref=PMID:14978213	
+P31539	UniProtKB	Mutagenesis	557	557	.	.	.	Note=Impairs prion propagation%2C but does not affect thermotolerance. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17367387;Dbxref=PMID:17367387	
+P31539	UniProtKB	Mutagenesis	619	619	.	.	.	Note=Impairs oligomerization at low protein concentrations. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11158570,ECO:0000269|PubMed:9624144;Dbxref=PMID:11158570,PMID:9624144	
+P31539	UniProtKB	Mutagenesis	620	620	.	.	.	Note=Impairs oligomerization at low protein concentrations. Reduces ATP hydrolysis rate. Unable to confer thermotolerance. Comletely abolishes ATPase activity%3B when associated with T-218. K->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11158570,ECO:0000269|PubMed:11442834,ECO:0000269|PubMed:12101251,ECO:0000269|PubMed:16135516,ECO:0000269|PubMed:17259993,ECO:0000269|PubMed:17543332,ECO:0000269|PubMed:1896074,ECO:0000269|PubMed:8308017,ECO:0000269|PubMed:9624144;Dbxref=PMID:11158570,PMID:11442834,PMID:12101251,PMID:16135516,PMID:17259993,PMID:17543332,PMID:1896074,PMID:8308017,PMID:9624144	
+P31539	UniProtKB	Mutagenesis	621	621	.	.	.	Note=Reduces ATP hydrolysis%2C but does not affect oligomerization. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11158570;Dbxref=PMID:11158570	
+P31539	UniProtKB	Mutagenesis	645	645	.	.	.	Note=Abolishes the ability to refold aggregated protein in vitro and to provide thermotolerance in vivo. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15128736;Dbxref=PMID:15128736	
+P31539	UniProtKB	Mutagenesis	662	662	.	.	.	Note=Abolishes the ability to refold aggregated protein in vitro and to provide thermotolerance in vivo. Y->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15128736;Dbxref=PMID:15128736	
+P31539	UniProtKB	Mutagenesis	662	662	.	.	.	Note=No effect. Y->F%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15128736;Dbxref=PMID:15128736	
+P31539	UniProtKB	Mutagenesis	687	687	.	.	.	Note=In HSP104(TRAP)%3B completely abolishes ATP hydrolysis%2C but does not affect nucleotide binding%2C thus keeping HSP104 in an ATP-bound state%3B when associated with Q-285. E->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135516,ECO:0000269|PubMed:17543332;Dbxref=PMID:16135516,PMID:17543332	
+P31539	UniProtKB	Mutagenesis	704	704	.	.	.	Note=Impairs prion propagation%2C but does not affect thermotolerance. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17367387;Dbxref=PMID:17367387	
+P31539	UniProtKB	Mutagenesis	728	728	.	.	.	Note=Almost completely abolishes ATP hydrolysis at NBD2%2C but does not affect nucleotide binding%2C thus keeping NBD2 in an ATP-bound state. Reduces stimulation of ATP hydrolysis upon substrate binding. N->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11782421,ECO:0000269|PubMed:11983167,ECO:0000269|PubMed:17259993,ECO:0000269|PubMed:18160044;Dbxref=PMID:11782421,PMID:11983167,PMID:17259993,PMID:18160044	
+P31539	UniProtKB	Mutagenesis	765	765	.	.	.	Note=Can oligomerize in the absence of nucleotides. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18160044;Dbxref=PMID:18160044	
+P31539	UniProtKB	Mutagenesis	778	778	.	.	.	Note=In NLS17KA%3B fails to concentrate in the nucleus%3B when associated with A-782 and A-789. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17973656;Dbxref=PMID:17973656	
+P31539	UniProtKB	Mutagenesis	782	782	.	.	.	Note=In NLS17KA%3B fails to concentrate in the nucleus%3B when associated with A-778 and A-789. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17973656;Dbxref=PMID:17973656	
+P31539	UniProtKB	Mutagenesis	789	789	.	.	.	Note=In NLS17KA%3B fails to concentrate in the nucleus%3B when associated with A-778 and A-782. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17973656;Dbxref=PMID:17973656	
+P31539	UniProtKB	Mutagenesis	819	819	.	.	.	Note=Site-specific fluorescent probe in an otherwise Trp-less HSP104. Fluorescence of this Trp changes in response to ATP and ADP binding at NBD2. Has no effect on ATP hydrolysis or protein stability. Y->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11867765;Dbxref=PMID:11867765	
+P31539	UniProtKB	Mutagenesis	826	826	.	.	.	Note=Reduces ATP and ADP binding at NBD2 6-fold%2C but does not affect ATP hydrolysis at NBD2. Reduces catalytic rate at NBD1. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11867765;Dbxref=PMID:11867765	
+P31539	UniProtKB	Helix	9	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U	
+P31539	UniProtKB	Beta strand	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U	
+P31539	UniProtKB	Helix	32	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U	
+P31539	UniProtKB	Helix	50	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U	
+P31539	UniProtKB	Helix	62	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U	
+P31539	UniProtKB	Helix	90	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U	
+P31539	UniProtKB	Beta strand	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U	
+P31539	UniProtKB	Helix	113	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U	
+P31539	UniProtKB	Helix	124	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U	
+P31539	UniProtKB	Helix	137	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U	
+##sequence-region P25623 1 870
+P25623	UniProtKB	Chain	1	870	.	.	.	ID=PRO_0000072390;Note=Suppressor of yeast profilin deletion	
+P25623	UniProtKB	Domain	609	869	.	.	.	Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404	
+P25623	UniProtKB	Compositional bias	308	405	.	.	.	Note=Ser-rich	
+P25623	UniProtKB	Compositional bias	417	528	.	.	.	Note=Pro-rich	
+P25623	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25623	UniProtKB	Modified residue	331	331	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25623	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25623	UniProtKB	Modified residue	496	496	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25623	UniProtKB	Modified residue	500	500	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P25623	UniProtKB	Modified residue	577	577	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25623	UniProtKB	Cross-link	256	256	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25623	UniProtKB	Helix	7	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G	
+P25623	UniProtKB	Turn	12	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G	
+P25623	UniProtKB	Helix	18	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G	
+P25623	UniProtKB	Helix	67	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G	
+P25623	UniProtKB	Helix	83	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G	
+P25623	UniProtKB	Helix	97	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G	
+P25623	UniProtKB	Helix	127	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G	
+P25623	UniProtKB	Beta strand	133	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G	
+P25623	UniProtKB	Helix	138	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G	
+P25623	UniProtKB	Helix	168	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G	
+P25623	UniProtKB	Helix	233	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G	
+P25623	UniProtKB	Beta strand	611	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	628	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	646	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	654	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Helix	663	665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	666	671	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Turn	673	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	676	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	683	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Turn	688	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	695	705	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	709	718	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	720	731	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	741	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	758	766	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	771	773	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	775	779	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	784	787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	793	803	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	812	818	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Turn	827	830	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	836	845	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+P25623	UniProtKB	Beta strand	856	869	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H	
+##sequence-region P08539 1 472
+P08539	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+P08539	UniProtKB	Chain	2	472	.	.	.	ID=PRO_0000203616;Note=Guanine nucleotide-binding protein alpha-1 subunit	
+P08539	UniProtKB	Nucleotide binding	48	55	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08539	UniProtKB	Nucleotide binding	294	300	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08539	UniProtKB	Nucleotide binding	319	323	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08539	UniProtKB	Nucleotide binding	388	391	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08539	UniProtKB	Region	127	235	.	.	.	Note=Insert%3B not present in other G-proteins	
+P08539	UniProtKB	Metal binding	55	55	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08539	UniProtKB	Metal binding	300	300	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08539	UniProtKB	Binding site	444	444	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08539	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1936988,ECO:0000269|PubMed:8415763,ECO:0000269|PubMed:8702760;Dbxref=PMID:1936988,PMID:8415763,PMID:8702760	
+P08539	UniProtKB	Lipidation	3	3	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10712512,ECO:0000269|PubMed:8942643;Dbxref=PMID:10712512,PMID:8942643	
+P08539	UniProtKB	Cross-link	165	165	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11955054;Dbxref=PMID:11955054	
+P08539	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Abolishes both palmitoylation and N-myristoylation. G->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10712512,ECO:0000269|PubMed:8702760,ECO:0000269|PubMed:8942643;Dbxref=PMID:10712512,PMID:8702760,PMID:8942643	
+P08539	UniProtKB	Mutagenesis	3	3	.	.	.	Note=Abolishes palmitoylation but not N-myristoylation. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10712512,ECO:0000269|PubMed:8942643;Dbxref=PMID:10712512,PMID:8942643	
+P08539	UniProtKB	Mutagenesis	15	15	.	.	.	Note=Slightly reduces ligand-dependent pheromone signaling. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14767760;Dbxref=PMID:14767760	
+P08539	UniProtKB	Mutagenesis	17	17	.	.	.	Note=Leads to a hypersensitive signaling phenotype resulting in greatly enhanced signal at low alpha-factor concentrations. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14767760;Dbxref=PMID:14767760	
+P08539	UniProtKB	Mutagenesis	18	18	.	.	.	Note=Reduces ligand-dependent pheromone signaling. L->P%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14767760;Dbxref=PMID:14767760	
+P08539	UniProtKB	Mutagenesis	21	22	.	.	.	Note=Impairs interaction with FUS3. KR->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12029138;Dbxref=PMID:12029138	
+P08539	UniProtKB	Mutagenesis	50	50	.	.	.	Note=Confers insensitivity to pheromone. G->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10705368,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:2548076;Dbxref=PMID:10705368,PMID:1900495,PMID:2117698,PMID:2548076	
+P08539	UniProtKB	Mutagenesis	50	50	.	.	.	Note=Has increased GTP occupancy and moderately reduces hydrolysis of GTP%2C resulting in a constitutively active form that down-regulates the pheromone response and causes hyperadaptation to pheromone. G->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10705368,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:2548076;Dbxref=PMID:10705368,PMID:1900495,PMID:2117698,PMID:2548076	
+P08539	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Prevents GDP to GTP exchange%3B suppressor of L-323. K->E%2CI;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14767760,ECO:0000269|PubMed:9786851;Dbxref=PMID:14767760,PMID:9786851	
+P08539	UniProtKB	Mutagenesis	165	165	.	.	.	Note=Substantial decrease in ubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11955054;Dbxref=PMID:11955054	
+P08539	UniProtKB	Mutagenesis	297	297	.	.	.	Note=Slows hydrolysis of GTP. R->H	
+P08539	UniProtKB	Mutagenesis	302	302	.	.	.	Note=In GPA1(SST)%3B weakens interaction to SST2 and blocks its negative regulatory effect. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9488712;Dbxref=PMID:9488712	
+P08539	UniProtKB	Mutagenesis	321	321	.	.	.	Note=Causes a specific mating defect in alpha cells. G->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9604890;Dbxref=PMID:9604890	
+P08539	UniProtKB	Mutagenesis	322	322	.	.	.	Note=Confers insensitivity to pheromone. G->A%2CE%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:8887662;Dbxref=PMID:1900495,PMID:2117698,PMID:8887662	
+P08539	UniProtKB	Mutagenesis	323	323	.	.	.	Note=Prevents hydrolysis of GTP%3B eliminates the interaction with STE4 and constitutively activates the pheromone response pathway. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9604890;Dbxref=PMID:9604890	
+P08539	UniProtKB	Mutagenesis	327	327	.	.	.	Note=Suppressor of L-323%3B does not prevent GTP binding to GPA1. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9786851;Dbxref=PMID:9786851	
+P08539	UniProtKB	Mutagenesis	345	345	.	.	.	Note=Suppressor of a STE2-L236H mutant. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866688;Dbxref=PMID:10866688	
+P08539	UniProtKB	Mutagenesis	353	353	.	.	.	Note=Suppressor of L-323. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9786851;Dbxref=PMID:9786851	
+P08539	UniProtKB	Mutagenesis	355	355	.	.	.	Note=Confers insensitivity to pheromone. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2117698;Dbxref=PMID:2117698	
+P08539	UniProtKB	Mutagenesis	364	364	.	.	.	Note=Enhances the rate of GDP for GTP exchange and slows hydrolysis of GTP%2C resulting in a constitutively active form that down-regulates the pheromone response independently of the pheromone receptor. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11394869,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:8887662;Dbxref=PMID:11394869,PMID:2117698,PMID:8887662	
+P08539	UniProtKB	Mutagenesis	388	388	.	.	.	Note=Forms a nondissociable complex with the pheromone receptor in response to receptor activation%2C resulting in reduced pheromone responsiveness. N->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11394869,ECO:0000269|PubMed:15197187,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:8887662;Dbxref=PMID:11394869,PMID:15197187,PMID:1900495,PMID:8887662	
+P08539	UniProtKB	Mutagenesis	388	388	.	.	.	Note=Causes constitutive activation of the pheromone response pathway. N->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11394869,ECO:0000269|PubMed:15197187,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:8887662;Dbxref=PMID:11394869,PMID:15197187,PMID:1900495,PMID:8887662	
+P08539	UniProtKB	Mutagenesis	391	391	.	.	.	Note=Causes constitutive activation of the pheromone response pathway. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1900495;Dbxref=PMID:1900495	
+P08539	UniProtKB	Mutagenesis	467	467	.	.	.	Note=Impairs pheromone signaling in a and alpha cells. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1848203;Dbxref=PMID:1848203	
+P08539	UniProtKB	Mutagenesis	468	468	.	.	.	Note=Impairs pheromone signaling specifically in a cells. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1848203;Dbxref=PMID:1848203	
+P08539	UniProtKB	Mutagenesis	470	470	.	.	.	Note=Confers insensitivity to pheromone. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2117698;Dbxref=PMID:2117698	
+P08539	UniProtKB	Sequence conflict	82	82	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08539	UniProtKB	Sequence conflict	194	194	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08539	UniProtKB	Sequence conflict	226	226	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08539	UniProtKB	Sequence conflict	246	246	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08539	UniProtKB	Sequence conflict	469	469	.	.	.	Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32502 1 381
+P32502	UniProtKB	Chain	1	381	.	.	.	ID=PRO_0000156066;Note=Translation initiation factor eIF-2B subunit beta	
+##sequence-region P15442 1 1659
+P15442	UniProtKB	Chain	1	1659	.	.	.	ID=PRO_0000085963;Note=eIF-2-alpha kinase GCN2	
+P15442	UniProtKB	Domain	17	128	.	.	.	Note=RWD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00179	
+P15442	UniProtKB	Domain	256	527	.	.	.	Note=Protein kinase 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P15442	UniProtKB	Domain	599	981	.	.	.	Note=Protein kinase 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P15442	UniProtKB	Nucleotide binding	605	613	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P15442	UniProtKB	Region	999	1519	.	.	.	Note=Histidyl-tRNA synthetase-like	
+P15442	UniProtKB	Active site	835	835	.	.	.	Note=Proton acceptor	
+P15442	UniProtKB	Binding site	628	628	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P15442	UniProtKB	Modified residue	761	761	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P15442	UniProtKB	Modified residue	882	882	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799	
+P15442	UniProtKB	Modified residue	887	887	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799	
+P15442	UniProtKB	Mutagenesis	74	74	.	.	.	Note=Inhibits interaction with GCN1%2C eIF-2-alpha phosphorylation and fails to derepress GCN4 translation in amino acid-starved cells. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10801780,ECO:0000269|PubMed:11350982;Dbxref=PMID:10801780,PMID:11350982	
+P15442	UniProtKB	Mutagenesis	582	582	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107	
+P15442	UniProtKB	Mutagenesis	594	594	.	.	.	Note=Inhibits autophosphorylation%2C eIF-2-alpha kinase activity and derepression of GCN4 translation. Restores eIF-2-alpha kinase activity and derepression of GCN4%2C but not autophosphorylation%3B when associated with R-598. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17202131;Dbxref=PMID:17202131	
+P15442	UniProtKB	Mutagenesis	598	598	.	.	.	Note=Inhibits autophosphorylation%2C eIF-2-alpha kinase activity and derepression of GCN4 translation. Restores eIF-2-alpha kinase activity and derepression of GCN4%2C but not autophosphorylation%3B when associated with D-594. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17202131;Dbxref=PMID:17202131	
+P15442	UniProtKB	Mutagenesis	601	601	.	.	.	Note=Increases the constitutive kinase activity in absence of amino acid starvation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2188100;Dbxref=PMID:2188100	
+P15442	UniProtKB	Mutagenesis	628	628	.	.	.	Note=Inhibits autophosphorylation%2C eIF-2-alpha kinase activity and derepression of GCN4 translation in amino acid-starved cells. K->V%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:17202131,ECO:0000269|PubMed:1739968,ECO:0000269|PubMed:2188100,ECO:0000269|PubMed:2660141,ECO:0000269|PubMed:8798780;Dbxref=PMID:10983975,PMID:17202131,PMID:1739968,PMID:2188100,PMID:2660141,PMID:8798780	
+P15442	UniProtKB	Mutagenesis	629	629	.	.	.	Note=Does not abolish derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2660141;Dbxref=PMID:2660141	
+P15442	UniProtKB	Mutagenesis	716	716	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107	
+P15442	UniProtKB	Mutagenesis	788	788	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107	
+P15442	UniProtKB	Mutagenesis	794	794	.	.	.	Note=Constitutively active allele%2C bypass the tRNA binding-requirement for kinase activity. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15964839;Dbxref=PMID:15964839	
+P15442	UniProtKB	Mutagenesis	803	803	.	.	.	Note=Increases tRNA binding and the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. E->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:1448107;Dbxref=PMID:10983975,PMID:1448107	
+P15442	UniProtKB	Mutagenesis	821	821	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1448107,ECO:0000269|PubMed:2188100;Dbxref=PMID:1448107,PMID:2188100	
+P15442	UniProtKB	Mutagenesis	835	835	.	.	.	Note=Loss of function. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15964839;Dbxref=PMID:15964839	
+P15442	UniProtKB	Mutagenesis	861	861	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107	
+P15442	UniProtKB	Mutagenesis	882	882	.	.	.	Note=Partially impairs kinase activity. T->A%2CE%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799	
+P15442	UniProtKB	Mutagenesis	882	882	.	.	.	Note=No effect. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799	
+P15442	UniProtKB	Mutagenesis	887	887	.	.	.	Note=Completely abolishes kinase activity. T->A%2CE%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799	
+P15442	UniProtKB	Mutagenesis	887	887	.	.	.	Note=Partially impairs kinase activity. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799	
+P15442	UniProtKB	Mutagenesis	1080	1080	.	.	.	Note=Inhibits dimerization%3B when associated with A-1088 and A-1090. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11250908;Dbxref=PMID:11250908	
+P15442	UniProtKB	Mutagenesis	1088	1088	.	.	.	Note=Inhibits dimerization%3B when associated with A-1080 and A-1090. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11250908;Dbxref=PMID:11250908	
+P15442	UniProtKB	Mutagenesis	1090	1090	.	.	.	Note=Inhibits dimerization%3B when associated with A-1080 and A-1088. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11250908;Dbxref=PMID:11250908	
+P15442	UniProtKB	Mutagenesis	1119	1119	.	.	.	Note=Inhibits binding to uncharged tRNAs%2C decreases eIF-2-alpha kinase activity and derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells%3B when associated with L-1120. Y->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:7623840,ECO:0000269|PubMed:8798780;Dbxref=PMID:10983975,PMID:7623840,PMID:8798780	
+P15442	UniProtKB	Mutagenesis	1120	1120	.	.	.	Note=Inhibits binding to uncharged tRNAs%2C decreases eIF-2-alpha kinase activity and derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells%3B when associated with L-1119. R->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:7623840,ECO:0000269|PubMed:8798780;Dbxref=PMID:10983975,PMID:7623840,PMID:8798780	
+P15442	UniProtKB	Mutagenesis	1134	1134	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107	
+P15442	UniProtKB	Mutagenesis	1138	1138	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107	
+P15442	UniProtKB	Mutagenesis	1197	1197	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107	
+P15442	UniProtKB	Mutagenesis	1308	1308	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107	
+P15442	UniProtKB	Mutagenesis	1338	1338	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107	
+P15442	UniProtKB	Mutagenesis	1552	1556	.	.	.	Note=Fails to derepress of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells and does not inhibit autophosphorylation. KKANK->LLANI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9430731;Dbxref=PMID:9430731	
+P15442	UniProtKB	Mutagenesis	1552	1552	.	.	.	Note=Reduces interaction with TIF11%2C Inhibits binding to uncharged tRNAs%2C reduces autophosphorylation%2C eIF-2-alpha kinase activity and ribosome association%2C but not dimerization%3B when associated with I-1553 and I-1556. K->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:21849502;Dbxref=PMID:10983975,PMID:21849502	
+P15442	UniProtKB	Mutagenesis	1553	1553	.	.	.	Note=Reduces interaction with TIF11%2C Inhibits binding to uncharged tRNAs%2C reduces autophosphorylation%2C eIF-2-alpha kinase activity and ribosome association%2C but not dimerization%3B when associated with L-1552 and I-1556. K->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:21849502;Dbxref=PMID:10983975,PMID:21849502	
+P15442	UniProtKB	Mutagenesis	1556	1556	.	.	.	Note=Reduces interaction with TIF11%2C Inhibits binding to uncharged tRNAs%2C reduces autophosphorylation%2C eIF-2-alpha kinase activity and ribosome association%2C but not dimerization%3B when associated with L-1552 and I-1553. K->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:21849502;Dbxref=PMID:10983975,PMID:21849502	
+P15442	UniProtKB	Mutagenesis	1557	1557	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107	
+P15442	UniProtKB	Mutagenesis	1591	1591	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107	
+P15442	UniProtKB	Mutagenesis	1606	1606	.	.	.	Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1448107,ECO:0000269|PubMed:2188100;Dbxref=PMID:1448107,PMID:2188100	
+P15442	UniProtKB	Sequence conflict	70	70	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	220	226	.	.	.	Note=TIKAKLP->NYKGKIA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	271	279	.	.	.	Note=LMSSEMMEN->YVFSNHGKS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	374	374	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	392	392	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	395	395	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	407	407	.	.	.	Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	411	413	.	.	.	Note=IPK->MPE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	475	475	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	589	589	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	604	605	.	.	.	Note=VL->FS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	622	622	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	640	641	.	.	.	Note=IL->MI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	727	727	.	.	.	Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	839	839	.	.	.	Note=M->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	954	954	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	1144	1144	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	1328	1331	.	.	.	Note=TLIS->RFHT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	1348	1348	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	1356	1356	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Sequence conflict	1434	1434	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15442	UniProtKB	Beta strand	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0	
+P15442	UniProtKB	Helix	8	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0	
+P15442	UniProtKB	Beta strand	26	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0	
+P15442	UniProtKB	Beta strand	37	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0	
+P15442	UniProtKB	Beta strand	48	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0	
+P15442	UniProtKB	Beta strand	63	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0	
+P15442	UniProtKB	Beta strand	80	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0	
+P15442	UniProtKB	Helix	92	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0	
+P15442	UniProtKB	Helix	114	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0	
+P15442	UniProtKB	Helix	594	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Beta strand	599	607	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Beta strand	609	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Turn	619	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Beta strand	624	633	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	634	647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Beta strand	653	655	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYC	
+P15442	UniProtKB	Beta strand	658	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Beta strand	781	789	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	796	802	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	805	807	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	809	828	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	838	840	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Beta strand	841	843	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Beta strand	849	851	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	888	890	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZXE	
+P15442	UniProtKB	Helix	893	896	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	905	919	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	925	936	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Turn	948	950	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	952	961	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	966	968	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	972	977	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Helix	986	995	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4	
+P15442	UniProtKB	Beta strand	1541	1543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+P15442	UniProtKB	Beta strand	1551	1553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+P15442	UniProtKB	Helix	1560	1577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+P15442	UniProtKB	Beta strand	1582	1586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+P15442	UniProtKB	Helix	1590	1598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+P15442	UniProtKB	Beta strand	1601	1603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+P15442	UniProtKB	Helix	1604	1612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+P15442	UniProtKB	Helix	1615	1617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+P15442	UniProtKB	Helix	1621	1636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+P15442	UniProtKB	Beta strand	1641	1646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+P15442	UniProtKB	Turn	1647	1649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+P15442	UniProtKB	Beta strand	1652	1656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM	
+##sequence-region P10592 1 639
+P10592	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649	
+P10592	UniProtKB	Chain	2	639	.	.	.	ID=PRO_0000078386;Note=Heat shock protein SSA2	
+P10592	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649	
+P10592	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P10592	UniProtKB	Modified residue	551	551	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10591	
+P10592	UniProtKB	Modified residue	603	603	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10591	
+P10592	UniProtKB	Cross-link	556	556	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P06782 1 633
+P06782	UniProtKB	Chain	1	633	.	.	.	ID=PRO_0000086670;Note=Carbon catabolite-derepressing protein kinase	
+P06782	UniProtKB	Domain	55	306	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000269|PubMed:16236260,ECO:0000269|PubMed:16531232;Dbxref=PMID:16236260,PMID:16531232	
+P06782	UniProtKB	Domain	348	389	.	.	.	Note=UBA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25869125;Dbxref=PMID:25869125	
+P06782	UniProtKB	Nucleotide binding	61	69	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06782	UniProtKB	Region	313	392	.	.	.	Note=Auto-inhibitory domain (AID);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17851534,ECO:0000269|PubMed:19474788;Dbxref=PMID:17851534,PMID:19474788	
+P06782	UniProtKB	Compositional bias	18	32	.	.	.	Note=Poly-His	
+P06782	UniProtKB	Active site	177	177	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P06782	UniProtKB	Binding site	84	84	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06782	UniProtKB	Modified residue	210	210	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11486005,ECO:0000269|PubMed:12748292,ECO:0000269|PubMed:22019086,ECO:0000269|PubMed:26394309,ECO:0000269|PubMed:7905477;Dbxref=PMID:11486005,PMID:12748292,PMID:22019086,PMID:26394309,PMID:7905477	
+P06782	UniProtKB	Modified residue	413	413	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P06782	UniProtKB	Modified residue	487	487	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P06782	UniProtKB	Modified residue	632	632	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06782	UniProtKB	Cross-link	461	461	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P06782	UniProtKB	Cross-link	549	549	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24108357;Dbxref=PMID:24108357	
+P06782	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Exhibits greater activity than wild-type SNFl in an immune complex assay where other associated molecules are present%2C but exhibits the same activity in a protein blot assay. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1468623;Dbxref=PMID:1468623	
+P06782	UniProtKB	Mutagenesis	84	84	.	.	.	Note=Inactivates the kinase activity without affecting protein levels. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11486005,ECO:0000269|PubMed:2557546;Dbxref=PMID:11486005,PMID:2557546	
+P06782	UniProtKB	Mutagenesis	210	210	.	.	.	Note=Inactivates the kinase activity without affecting protein levels. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11486005,ECO:0000269|PubMed:1468623;Dbxref=PMID:11486005,PMID:1468623	
+P06782	UniProtKB	Mutagenesis	357	357	.	.	.	Note=Alters kinase activation and biological activity%2C including enhanced allosteric subunit associations and increased oxidative stress resistance and life span%3B when associated with I-367. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25869125;Dbxref=PMID:25869125	
+P06782	UniProtKB	Mutagenesis	367	367	.	.	.	Note=Alters kinase activation and biological activity%2C including enhanced allosteric subunit associations and increased oxidative stress resistance and life span%3B when associated with A-357. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25869125;Dbxref=PMID:25869125	
+P06782	UniProtKB	Mutagenesis	549	549	.	.	.	Note=Decreases sumoylation of SNF1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24108357;Dbxref=PMID:24108357	
+P06782	UniProtKB	Beta strand	56	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Helix	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MN3	
+P06782	UniProtKB	Beta strand	69	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Turn	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Beta strand	80	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Helix	88	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DAE	
+P06782	UniProtKB	Helix	97	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Beta strand	118	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Beta strand	125	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Helix	139	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Helix	151	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Turn	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Beta strand	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Beta strand	191	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Turn	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MN3	
+P06782	UniProtKB	Helix	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MN3	
+P06782	UniProtKB	Helix	220	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Beta strand	224	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Helix	232	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Helix	257	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Helix	277	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Helix	291	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Helix	297	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Helix	304	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Helix	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH	
+P06782	UniProtKB	Turn	317	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MN3	
+P06782	UniProtKB	Helix	471	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P06782	UniProtKB	Helix	475	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P06782	UniProtKB	Helix	489	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P06782	UniProtKB	Beta strand	506	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P06782	UniProtKB	Helix	515	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P06782	UniProtKB	Beta strand	532	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P06782	UniProtKB	Helix	538	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P06782	UniProtKB	Beta strand	543	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P06782	UniProtKB	Beta strand	565	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P06782	UniProtKB	Beta strand	579	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P06782	UniProtKB	Helix	607	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV	
+P06782	UniProtKB	Helix	613	628	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+##sequence-region P22147 1 1528
+P22147	UniProtKB	Chain	1	1528	.	.	.	ID=PRO_0000071395;Note=5'-3' exoribonuclease 1	
+P22147	UniProtKB	Modified residue	1506	1506	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22147	UniProtKB	Modified residue	1510	1510	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P22147	UniProtKB	Mutagenesis	37	37	.	.	.	Note=Reduces strongly exonuclease activity. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Reduces strongly exonuclease activity. H->R%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	86	86	.	.	.	Note=Reduces strongly exonuclease activity. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Reduces strongly exonuclease activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	93	93	.	.	.	Note=Reduces strongly exonuclease activity. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Reduces strongly exonuclease activity. Q->E%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Reduces strongly exonuclease activity. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Reduces strongly exonuclease activity. E->G	
+P22147	UniProtKB	Mutagenesis	178	178	.	.	.	Note=Reduces strongly exonuclease activity. E->D%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	201	201	.	.	.	Note=Reduces strongly exonuclease activity. C->Y%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	206	206	.	.	.	Note=Abolishes exonuclease activity in vitro. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10454540;Dbxref=PMID:10454540	
+P22147	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Abolishes exonuclease activity in vitro. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10454540;Dbxref=PMID:10454540	
+P22147	UniProtKB	Mutagenesis	592	592	.	.	.	Note=Reduces strongly exonuclease activity%3B when associated with Y-710. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	710	710	.	.	.	Note=Reduces strongly exonuclease activity%3B when associated with P-592. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	798	798	.	.	.	Note=Reduces strongly exonuclease activity%3B when associated with D-1024%3B F-1043 and P-1197. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	1024	1024	.	.	.	Note=Reduces strongly exonuclease activity%3B when associated with R-798%3B F-1043 and P-1197. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	1043	1043	.	.	.	Note=Reduces strongly exonuclease activity%3B when associated with R-798%3B D-1024 and P-1197. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+P22147	UniProtKB	Mutagenesis	1197	1197	.	.	.	Note=Reduces strongly exonuclease activity%3B when associated with R-798%3B D-1024 and F-1043. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486	
+##sequence-region P32598 1 312
+P32598	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000058820;Note=Serine/threonine-protein phosphatase PP1-2	
+P32598	UniProtKB	Active site	124	124	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32598	UniProtKB	Metal binding	63	63	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32598	UniProtKB	Metal binding	65	65	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32598	UniProtKB	Metal binding	91	91	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32598	UniProtKB	Metal binding	91	91	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32598	UniProtKB	Metal binding	123	123	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32598	UniProtKB	Metal binding	172	172	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32598	UniProtKB	Metal binding	247	247	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32598	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32598	UniProtKB	Cross-link	22	22	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32598	UniProtKB	Cross-link	47	47	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32598	UniProtKB	Mutagenesis	73	73	.	.	.	Note=In GLC7-1%3B decreased glycogen accumulation. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8150278;Dbxref=PMID:8150278	
+P32598	UniProtKB	Sequence conflict	137	137	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32598	UniProtKB	Sequence conflict	273	273	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53230 1 385
+P53230	UniProtKB	Transit peptide	1	34	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53230	UniProtKB	Chain	35	385	.	.	.	ID=PRO_0000202796;Note=Phosphatidate cytidylyltransferase%2C mitochondrial	
+P53230	UniProtKB	Natural variant	8	8	.	.	.	Note=In strain: SK1. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P53230	UniProtKB	Natural variant	127	127	.	.	.	Note=In strain: SK1. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P53230	UniProtKB	Mutagenesis	130	132	.	.	.	Note=Completely abolishes the enzymatic activity. YGS->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23623749;Dbxref=PMID:23623749	
+P53230	UniProtKB	Mutagenesis	220	220	.	.	.	Note=Completely abolishes the enzymatic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23623749;Dbxref=PMID:23623749	
+##sequence-region Q06510 1 381
+Q06510	UniProtKB	Chain	1	381	.	.	.	ID=PRO_0000220934;Note=Lysophosphatidylcholine acyltransferase	
+Q06510	UniProtKB	Topological domain	1	25	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06510	UniProtKB	Transmembrane	26	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06510	UniProtKB	Topological domain	48	381	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06510	UniProtKB	Motif	77	82	.	.	.	Note=HXXXXD motif	
+Q06510	UniProtKB	Sequence conflict	11	11	.	.	.	Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02457 1 562
+Q02457	UniProtKB	Chain	1	562	.	.	.	ID=PRO_0000197125;Note=Protein TBF1	
+Q02457	UniProtKB	Domain	404	460	.	.	.	Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+Q02457	UniProtKB	DNA binding	431	456	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+Q02457	UniProtKB	Sequence conflict	71	71	.	.	.	Note=E->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02457	UniProtKB	Sequence conflict	371	373	.	.	.	Note=DAA->ERR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39078 1 528
+P39078	UniProtKB	Chain	1	528	.	.	.	ID=PRO_0000128345;Note=T-complex protein 1 subunit delta	
+P39078	UniProtKB	Sequence conflict	254	254	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q3E7C1 1 72
+Q3E7C1	UniProtKB	Chain	1	72	.	.	.	ID=PRO_0000119287;Note=RNA polymerase II transcription factor B subunit 5	
+Q3E7C1	UniProtKB	Beta strand	3	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q3E7C1	UniProtKB	Helix	14	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q3E7C1	UniProtKB	Beta strand	29	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q3E7C1	UniProtKB	Beta strand	39	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q3E7C1	UniProtKB	Helix	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q3E7C1	UniProtKB	Helix	47	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+##sequence-region Q06339 1 672
+Q06339	UniProtKB	Chain	1	672	.	.	.	ID=PRO_0000252483;Note=Transcription factor tau 91 kDa subunit	
+Q06339	UniProtKB	DNA binding	6	18	.	.	.	Note=A.T hook	
+Q06339	UniProtKB	Region	1	158	.	.	.	Note=Required for DNA-binding	
+Q06339	UniProtKB	Region	159	672	.	.	.	Note=Sufficient for interaction with TFC8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16115780;Dbxref=PMID:16115780	
+Q06339	UniProtKB	Disulfide bond	375	383	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17052456;Dbxref=PMID:17052456	
+Q06339	UniProtKB	Helix	167	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Helix	178	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Helix	200	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	218	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Helix	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Turn	226	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Helix	241	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	253	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	261	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Helix	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	283	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	308	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	339	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Turn	348	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	353	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	365	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	378	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	383	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	393	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	402	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	415	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Turn	421	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	425	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	443	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	457	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	463	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	467	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	481	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	489	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Helix	496	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Helix	499	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	504	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	517	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Turn	521	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	525	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	531	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	547	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	556	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	569	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Turn	573	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	576	578	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Turn	586	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	601	604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	609	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	613	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	645	647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Turn	651	655	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	656	660	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q06339	UniProtKB	Beta strand	664	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+##sequence-region Q12308 1 588
+Q12308	UniProtKB	Chain	1	588	.	.	.	ID=PRO_0000252484;Note=Transcription factor tau 60 kDa subunit	
+Q12308	UniProtKB	Region	399	588	.	.	.	Note=Sufficient for SPT15-binding	
+Q12308	UniProtKB	Site	358	358	.	.	.	Note=Involved in the interaction with TFC6	
+Q12308	UniProtKB	Sequence conflict	36	36	.	.	.	Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12308	UniProtKB	Beta strand	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	29	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	34	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	56	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Turn	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	88	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	100	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	109	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	116	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Turn	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	132	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	139	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	144	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	151	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Turn	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	169	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	185	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	194	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	211	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	218	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	232	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	238	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	244	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Turn	252	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	256	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	270	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	280	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	289	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	307	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Turn	317	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	323	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	330	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	342	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	361	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	366	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	386	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Turn	395	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	412	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	423	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	434	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Turn	443	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	446	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	452	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	465	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	472	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	495	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	503	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	510	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	516	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	526	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	531	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	542	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Turn	546	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	551	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	555	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	559	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Helix	565	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Beta strand	575	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+Q12308	UniProtKB	Turn	579	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04	
+##sequence-region Q06490 1 572
+Q06490	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06490	UniProtKB	Chain	20	572	.	.	.	ID=PRO_0000034064;Note=Thiamine biosynthesis protein THI22	
+Q06490	UniProtKB	Sequence conflict	95	95	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04083 1 370
+Q04083	UniProtKB	Chain	1	370	.	.	.	ID=PRO_0000252277;Note=Thiamine-repressible mitochondrial transport protein THI74	
+Q04083	UniProtKB	Topological domain	1	10	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Topological domain	32	42	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Topological domain	64	119	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Topological domain	141	146	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Topological domain	168	169	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Transmembrane	170	190	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Topological domain	191	203	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Topological domain	225	239	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Transmembrane	240	260	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Topological domain	261	273	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Transmembrane	274	294	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Topological domain	295	303	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Transmembrane	304	324	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Topological domain	325	326	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Transmembrane	327	347	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Topological domain	348	370	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04083	UniProtKB	Domain	129	190	.	.	.	Note=EamA	
+##sequence-region P35202 1 319
+P35202	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P35202	UniProtKB	Chain	2	319	.	.	.	ID=PRO_0000072513;Note=Thiamine pyrophosphokinase	
+P35202	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P35202	UniProtKB	Beta strand	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	23	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	37	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	52	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	63	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	71	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	83	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	92	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	103	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	115	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	126	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	141	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Turn	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Turn	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	164	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	184	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	196	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	216	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	223	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	235	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	241	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	248	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	260	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Turn	279	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	285	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	292	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Beta strand	304	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	312	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+P35202	UniProtKB	Helix	316	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0	
+##sequence-region Q08231 1 455
+Q08231	UniProtKB	Chain	1	455	.	.	.	ID=PRO_0000270618;Note=Nuclear mRNA export protein THP1	
+Q08231	UniProtKB	Domain	297	428	.	.	.	Note=PCI	
+Q08231	UniProtKB	Helix	4	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Beta strand	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	27	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	42	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	59	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	84	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Beta strand	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	106	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	140	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	170	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TRQ	
+Q08231	UniProtKB	Helix	195	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	202	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	216	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	236	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	258	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	284	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	288	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	293	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	311	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	322	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	331	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Turn	355	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Beta strand	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	365	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Turn	390	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TRQ	
+Q08231	UniProtKB	Helix	400	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Beta strand	415	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Turn	419	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Beta strand	423	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	432	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+Q08231	UniProtKB	Helix	439	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+##sequence-region P16120 1 514
+P16120	UniProtKB	Chain	1	514	.	.	.	ID=PRO_0000185645;Note=Threonine synthase	
+P16120	UniProtKB	Modified residue	124	124	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16120	UniProtKB	Modified residue	467	467	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P16120	UniProtKB	Sequence conflict	176	176	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16120	UniProtKB	Beta strand	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	21	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	46	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Turn	52	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	58	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Turn	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	77	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Turn	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	110	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	125	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	154	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	164	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	178	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	191	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	205	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	214	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	244	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	263	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	270	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	277	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	280	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	298	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	307	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	315	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	329	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	339	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	356	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	374	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	380	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Turn	387	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	390	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	397	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	421	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Beta strand	442	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	452	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	456	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	471	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	478	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	483	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+P16120	UniProtKB	Helix	498	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7	
+##sequence-region P40328 1 754
+P40328	UniProtKB	Chain	1	754	.	.	.	ID=PRO_0000084759;Note=Probable 26S proteasome subunit YTA6	
+P40328	UniProtKB	Nucleotide binding	511	518	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40328	UniProtKB	Modified residue	255	255	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40328	UniProtKB	Sequence conflict	20	20	.	.	.	Note=L->LQL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40328	UniProtKB	Sequence conflict	85	85	.	.	.	Note=D->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39077 1 534
+P39077	UniProtKB	Chain	1	534	.	.	.	ID=PRO_0000128331;Note=T-complex protein 1 subunit gamma	
+P39077	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39077	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39077	UniProtKB	Disulfide bond	371	377	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39077	UniProtKB	Sequence conflict	25	26	.	.	.	Note=IT->HA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39077	UniProtKB	Sequence conflict	86	89	.	.	.	Note=DEEV->ERRG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39077	UniProtKB	Sequence conflict	111	111	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39077	UniProtKB	Sequence conflict	265	265	.	.	.	Note=K->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39077	UniProtKB	Sequence conflict	274	274	.	.	.	Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39077	UniProtKB	Sequence conflict	292	292	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39077	UniProtKB	Sequence conflict	478	478	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35691 1 167
+P35691	UniProtKB	Chain	1	167	.	.	.	ID=PRO_0000211311;Note=Translationally-controlled tumor protein homolog	
+P35691	UniProtKB	Domain	1	167	.	.	.	Note=TCTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01133	
+P35691	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35691	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35691	UniProtKB	Sequence conflict	19	20	.	.	.	Note=DA->AD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35691	UniProtKB	Sequence conflict	70	70	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38987 1 245
+P38987	UniProtKB	Chain	1	245	.	.	.	ID=PRO_0000122466;Note=Protein TEM1	
+P38987	UniProtKB	Nucleotide binding	27	34	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38987	UniProtKB	Nucleotide binding	75	79	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38987	UniProtKB	Nucleotide binding	132	135	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38987	UniProtKB	Region	16	244	.	.	.	Note=Small GTPase-like	
+##sequence-region P53916 1 434
+P53916	UniProtKB	Chain	1	434	.	.	.	ID=PRO_0000215906;Note=Probable phosphatidylinositol 3%2C4%2C5-trisphosphate 3-phosphatase TEP1	
+P53916	UniProtKB	Domain	33	255	.	.	.	Note=Phosphatase tensin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00590	
+P53916	UniProtKB	Active site	193	193	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00590	
+##sequence-region P29055 1 345
+P29055	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000119308;Note=Transcription initiation factor IIB	
+P29055	UniProtKB	Repeat	136	212	.	.	.	Note=1	
+P29055	UniProtKB	Repeat	242	318	.	.	.	Note=2	
+P29055	UniProtKB	Zinc finger	20	53	.	.	.	Note=TFIIB-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00469	
+P29055	UniProtKB	Metal binding	24	24	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29055	UniProtKB	Metal binding	27	27	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29055	UniProtKB	Metal binding	45	45	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29055	UniProtKB	Metal binding	48	48	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29055	UniProtKB	Sequence conflict	10	10	.	.	.	Note=R->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29055	UniProtKB	Beta strand	34	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Turn	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Beta strand	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Turn	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Beta strand	50	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Helix	59	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Turn	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Beta strand	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Beta strand	80	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Helix	85	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Beta strand	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Helix	104	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Beta strand	122	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Helix	128	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Helix	144	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Turn	161	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Helix	168	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Helix	189	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P29055	UniProtKB	Helix	202	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+##sequence-region P29056 1 596
+P29056	UniProtKB	Chain	1	596	.	.	.	ID=PRO_0000119346;Note=Transcription factor IIIB 70 kDa subunit	
+P29056	UniProtKB	Repeat	90	166	.	.	.	Note=1	
+P29056	UniProtKB	Repeat	185	264	.	.	.	Note=2	
+P29056	UniProtKB	Zinc finger	1	33	.	.	.	Note=TFIIB-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00469	
+P29056	UniProtKB	Metal binding	4	4	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29056	UniProtKB	Metal binding	7	7	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29056	UniProtKB	Metal binding	25	25	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29056	UniProtKB	Metal binding	28	28	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29056	UniProtKB	Modified residue	381	381	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P29056	UniProtKB	Modified residue	384	384	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P29056	UniProtKB	Helix	442	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM	
+P29056	UniProtKB	Helix	448	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM	
+P29056	UniProtKB	Helix	470	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM	
+P29056	UniProtKB	Helix	477	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM	
+P29056	UniProtKB	Turn	491	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM	
+P29056	UniProtKB	Helix	494	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM	
+P29056	UniProtKB	Turn	501	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM	
+##sequence-region P38141 1 450
+P38141	UniProtKB	Chain	1	450	.	.	.	ID=PRO_0000114984;Note=Thiamine biosynthesis regulatory protein	
+P38141	UniProtKB	DNA binding	30	57	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P32318 1 326
+P32318	UniProtKB	Chain	1	326	.	.	.	ID=PRO_0000034058;Note=Thiamine thiazole synthase	
+P32318	UniProtKB	Region	97	98	.	.	.	Note=Substrate binding	
+P32318	UniProtKB	Region	301	303	.	.	.	Note=Substrate binding	
+P32318	UniProtKB	Binding site	76	76	.	.	.	Note=Substrate%3B via amide nitrogen	
+P32318	UniProtKB	Binding site	105	105	.	.	.	Note=Substrate%3B via amide nitrogen	
+P32318	UniProtKB	Binding site	170	170	.	.	.	Note=Substrate%3B via amide nitrogen and carbonyl oxygen	
+P32318	UniProtKB	Binding site	207	207	.	.	.	Note=Substrate	
+P32318	UniProtKB	Binding site	237	237	.	.	.	Note=Substrate	
+P32318	UniProtKB	Binding site	291	291	.	.	.	Note=Substrate%3B via amide nitrogen	
+P32318	UniProtKB	Modified residue	205	205	.	.	.	Note=2%2C3-didehydroalanine (Cys)	
+P32318	UniProtKB	Mutagenesis	97	97	.	.	.	Note=No activity. E->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261	
+P32318	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Partially active%2C trapping the enzyme at an advanced intermediate%2C just before the sulfide transfer reaction. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261	
+P32318	UniProtKB	Mutagenesis	204	204	.	.	.	Note=Partially active%2C trapping the enzyme at an advanced intermediate%2C just before the sulfide transfer reaction. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261	
+P32318	UniProtKB	Mutagenesis	205	205	.	.	.	Note=Partially active%2C with very weak activity toward NAD. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261	
+P32318	UniProtKB	Mutagenesis	207	207	.	.	.	Note=No activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261	
+P32318	UniProtKB	Mutagenesis	237	237	.	.	.	Note=No activity. H->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261	
+P32318	UniProtKB	Mutagenesis	238	238	.	.	.	Note=Partially active%2C with very weak activity toward NAD. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261	
+P32318	UniProtKB	Mutagenesis	301	301	.	.	.	Note=No activity. R->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261	
+P32318	UniProtKB	Mutagenesis	304	304	.	.	.	Note=No activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261	
+P32318	UniProtKB	Helix	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Turn	25	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Helix	45	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	65	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Helix	75	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Turn	104	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	116	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Turn	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Helix	123	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	137	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Helix	145	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	168	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	180	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	185	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Helix	194	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Turn	198	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Y4L	
+P32318	UniProtKB	Beta strand	209	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	230	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Helix	244	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Helix	266	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Beta strand	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Helix	291	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+P32318	UniProtKB	Helix	307	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ	
+##sequence-region P32897 1 222
+P32897	UniProtKB	Chain	1	222	.	.	.	ID=PRO_0000210307;Note=Mitochondrial import inner membrane translocase subunit TIM23	
+P32897	UniProtKB	Transmembrane	97	118	.	.	.	Note=Helical%3B Note%3DInner membrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32897	UniProtKB	Topological domain	119	144	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32897	UniProtKB	Transmembrane	145	166	.	.	.	Note=Helical%3B Note%3DInner membrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32897	UniProtKB	Topological domain	167	174	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32897	UniProtKB	Transmembrane	175	189	.	.	.	Note=Helical%3B Note%3DInner membrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32897	UniProtKB	Topological domain	190	196	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32897	UniProtKB	Transmembrane	197	215	.	.	.	Note=Helical%3B Note%3DInner membrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32897	UniProtKB	Topological domain	216	222	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08144 1 397
+Q08144	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000210279;Note=T-SNARE affecting a late Golgi compartment protein 2	
+Q08144	UniProtKB	Topological domain	1	317	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08144	UniProtKB	Transmembrane	318	338	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08144	UniProtKB	Topological domain	339	397	.	.	.	Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08144	UniProtKB	Domain	244	306	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+Q08144	UniProtKB	Coiled coil	74	96	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08144	UniProtKB	Modified residue	109	109	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08144	UniProtKB	Sequence conflict	397	397	.	.	.	Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07273 1 309
+P07273	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000121443;Note=Transcription elongation factor S-II	
+P07273	UniProtKB	Domain	5	79	.	.	.	Note=TFIIS N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00649	
+P07273	UniProtKB	Domain	148	264	.	.	.	Note=TFIIS central;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00651	
+P07273	UniProtKB	Zinc finger	267	307	.	.	.	Note=TFIIS-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00472	
+P07273	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07273	UniProtKB	Sequence conflict	35	35	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07273	UniProtKB	Sequence conflict	35	35	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07273	UniProtKB	Sequence conflict	74	77	.	.	.	Note=DAIN->AQLI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07273	UniProtKB	Sequence conflict	74	77	.	.	.	Note=DAIN->AQLI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07273	UniProtKB	Sequence conflict	82	82	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07273	UniProtKB	Sequence conflict	82	82	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07273	UniProtKB	Sequence conflict	85	85	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07273	UniProtKB	Sequence conflict	85	85	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07273	UniProtKB	Helix	3	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0	
+P07273	UniProtKB	Beta strand	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0	
+P07273	UniProtKB	Helix	21	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0	
+P07273	UniProtKB	Turn	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0	
+P07273	UniProtKB	Helix	40	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0	
+P07273	UniProtKB	Beta strand	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0	
+P07273	UniProtKB	Helix	61	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0	
+P07273	UniProtKB	Turn	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ENW	
+P07273	UniProtKB	Helix	147	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Beta strand	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Helix	170	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Beta strand	189	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Helix	194	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Beta strand	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Helix	213	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Helix	226	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Turn	232	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Helix	240	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Beta strand	266	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Beta strand	272	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Beta strand	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P07273	UniProtKB	Turn	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+##sequence-region P54857 1 326
+P54857	UniProtKB	Chain	1	326	.	.	.	ID=PRO_0000090380;Note=Lipase 2	
+P54857	UniProtKB	Active site	144	144	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54857	UniProtKB	Sequence conflict	104	104	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54857	UniProtKB	Sequence conflict	300	300	.	.	.	Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12052 1 315
+Q12052	UniProtKB	Chain	1	315	.	.	.	ID=PRO_0000270619;Note=Trimethylguanosine synthase	
+Q12052	UniProtKB	Region	1	58	.	.	.	Note=Required for correct nucleolar localization	
+Q12052	UniProtKB	Binding site	126	126	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12052	UniProtKB	Mutagenesis	75	75	.	.	.	Note=No effect. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12907733;Dbxref=PMID:12907733	
+Q12052	UniProtKB	Mutagenesis	81	81	.	.	.	Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12907733;Dbxref=PMID:12907733	
+Q12052	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Loss of function. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12907733;Dbxref=PMID:12907733	
+Q12052	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Loss of catalytic activity%2C but not required for pre-rRNA processing. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11983179,ECO:0000269|PubMed:15340060;Dbxref=PMID:11983179,PMID:15340060	
+Q12052	UniProtKB	Mutagenesis	126	126	.	.	.	Note=Loss of function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983179;Dbxref=PMID:11983179	
+Q12052	UniProtKB	Mutagenesis	175	175	.	.	.	Note=No effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12907733;Dbxref=PMID:12907733	
+Q12052	UniProtKB	Mutagenesis	175	175	.	.	.	Note=Loss of function. S->E%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12907733;Dbxref=PMID:12907733	
+Q12052	UniProtKB	Mutagenesis	178	178	.	.	.	Note=Loss of catalytic activity%2C but not required for pre-rRNA processing. W->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12907733,ECO:0000269|PubMed:15340060,ECO:0000269|PubMed:18840651;Dbxref=PMID:12907733,PMID:15340060,PMID:18840651	
+##sequence-region P00927 1 576
+P00927	UniProtKB	Domain	393	473	.	.	.	Note=ACT-like 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01008	
+P00927	UniProtKB	Domain	495	566	.	.	.	Note=ACT-like 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01008	
+P00927	UniProtKB	Modified residue	109	109	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00927	UniProtKB	Sequence conflict	259	259	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P41338 1 398
+P41338	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378	
+P41338	UniProtKB	Chain	2	398	.	.	.	ID=PRO_0000206416;Note=Acetyl-CoA acetyltransferase	
+P41338	UniProtKB	Active site	91	91	.	.	.	Note=Acyl-thioester intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41338	UniProtKB	Active site	354	354	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10020	
+P41338	UniProtKB	Active site	384	384	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10020	
+P41338	UniProtKB	Metal binding	186	186	.	.	.	Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41338	UniProtKB	Metal binding	248	248	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41338	UniProtKB	Metal binding	249	249	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41338	UniProtKB	Metal binding	251	251	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41338	UniProtKB	Metal binding	350	350	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41338	UniProtKB	Binding site	186	186	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41338	UniProtKB	Binding site	231	231	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41338	UniProtKB	Binding site	252	252	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41338	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378	
+##sequence-region P57744 1 87
+P57744	UniProtKB	Chain	1	87	.	.	.	ID=PRO_0000193594;Note=Mitochondrial import inner membrane translocase subunit TIM8	
+P57744	UniProtKB	Motif	44	68	.	.	.	Note=Twin CX3C motif	
+P57744	UniProtKB	Disulfide bond	44	68	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P57744	UniProtKB	Disulfide bond	48	64	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P57744	UniProtKB	Helix	30	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CJH	
+P57744	UniProtKB	Beta strand	53	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CJH	
+P57744	UniProtKB	Helix	59	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CJH	
+##sequence-region O74700 1 87
+O74700	UniProtKB	Chain	1	87	.	.	.	ID=PRO_0000193610;Note=Mitochondrial import inner membrane translocase subunit TIM9	
+O74700	UniProtKB	Motif	35	59	.	.	.	Note=Twin CX3C motif;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11867522;Dbxref=PMID:11867522	
+O74700	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+O74700	UniProtKB	Disulfide bond	35	59	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11867522;Dbxref=PMID:11867522	
+O74700	UniProtKB	Disulfide bond	39	55	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11867522;Dbxref=PMID:11867522	
+O74700	UniProtKB	Mutagenesis	40	40	.	.	.	Note=In tim9-3%3B impairs the import of mitochondrial carrier proteins into mitochondria%3B when associated with P-60. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12656987;Dbxref=PMID:12656987	
+O74700	UniProtKB	Mutagenesis	52	52	.	.	.	Note=In tim9-19%3B impairs the import of mitochondrial carrier proteins into mitochondria. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12656987;Dbxref=PMID:12656987	
+O74700	UniProtKB	Mutagenesis	60	60	.	.	.	Note=In tim9-3%3B impairs the import of mitochondrial carrier proteins into mitochondria%3B when associated with A-40. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12656987;Dbxref=PMID:12656987	
+O74700	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Impairs the import of mitochondrial carrier proteins into mitochondria. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9822593;Dbxref=PMID:9822593	
+O74700	UniProtKB	Helix	14	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR	
+O74700	UniProtKB	Beta strand	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR	
+O74700	UniProtKB	Helix	50	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR	
+##sequence-region Q12218 1 487
+Q12218	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12218	UniProtKB	Chain	23	465	.	.	.	ID=PRO_0000267640;Note=Cell wall protein TIR4	
+Q12218	UniProtKB	Propeptide	466	487	.	.	.	ID=PRO_0000267641;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12218	UniProtKB	Repeat	137	148	.	.	.	Note=1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q12218	UniProtKB	Repeat	149	160	.	.	.	Note=2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q12218	UniProtKB	Repeat	161	172	.	.	.	Note=3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q12218	UniProtKB	Repeat	173	184	.	.	.	Note=4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q12218	UniProtKB	Repeat	185	196	.	.	.	Note=5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q12218	UniProtKB	Repeat	197	208	.	.	.	Note=6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q12218	UniProtKB	Repeat	209	220	.	.	.	Note=7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q12218	UniProtKB	Repeat	221	232	.	.	.	Note=8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q12218	UniProtKB	Repeat	233	244	.	.	.	Note=9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q12218	UniProtKB	Repeat	245	256	.	.	.	Note=10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q12218	UniProtKB	Repeat	257	268	.	.	.	Note=11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q12218	UniProtKB	Region	137	268	.	.	.	Note=11 X 12 AA approximate tandem repeats%2C Ser-rich	
+Q12218	UniProtKB	Compositional bias	113	365	.	.	.	Note=Ser-rich	
+Q12218	UniProtKB	Lipidation	465	465	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12218	UniProtKB	Glycosylation	327	327	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12218	UniProtKB	Glycosylation	348	348	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12218	UniProtKB	Glycosylation	368	368	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12218	UniProtKB	Glycosylation	403	403	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12218	UniProtKB	Glycosylation	404	404	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04562 1 672
+Q04562	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Chain	19	672	.	.	.	ID=PRO_0000244444;Note=Transmembrane 9 superfamily member 2	
+Q04562	UniProtKB	Topological domain	19	307	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Transmembrane	308	328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Topological domain	329	383	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Transmembrane	384	404	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Topological domain	405	410	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Transmembrane	411	431	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Topological domain	432	447	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Transmembrane	448	468	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Topological domain	469	479	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Transmembrane	480	500	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Topological domain	501	532	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Transmembrane	533	553	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Topological domain	554	565	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Transmembrane	566	586	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Topological domain	587	601	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Transmembrane	602	622	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Topological domain	623	628	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Transmembrane	629	649	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04562	UniProtKB	Topological domain	650	672	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53507 1 60
+P53507	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8641278;Dbxref=PMID:8641278	
+P53507	UniProtKB	Chain	2	60	.	.	.	ID=PRO_0000046767;Note=Mitochondrial import receptor subunit TOM7	
+P53507	UniProtKB	Topological domain	2	19	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53507	UniProtKB	Transmembrane	20	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53507	UniProtKB	Topological domain	42	60	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q07904 1 523
+Q07904	UniProtKB	Chain	1	523	.	.	.	ID=PRO_0000247182;Note=Thiamine pathway transporter THI73	
+Q07904	UniProtKB	Topological domain	1	79	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	101	118	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	140	141	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	163	176	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	198	207	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	229	239	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	240	260	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	261	312	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	313	333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	334	345	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	346	366	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	367	371	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	393	400	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	401	421	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	422	432	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	433	452	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	453	466	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Transmembrane	467	487	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07904	UniProtKB	Topological domain	488	523	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05998 1 598
+Q05998	UniProtKB	Chain	1	598	.	.	.	ID=PRO_0000197926;Note=Thiamine transporter	
+Q05998	UniProtKB	Topological domain	1	41	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	63	73	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	95	111	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	133	173	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	195	197	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	219	240	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	262	274	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	275	295	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	296	332	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	333	353	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	354	371	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	393	394	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	395	415	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	416	446	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	447	467	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	468	483	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Transmembrane	484	504	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Topological domain	505	598	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05998	UniProtKB	Modified residue	560	560	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P40040 1 218
+P40040	UniProtKB	Chain	1	218	.	.	.	ID=PRO_0000072519;Note=Protein THO1	
+P40040	UniProtKB	Domain	4	38	.	.	.	Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186	
+P40040	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40040	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40040	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40040	UniProtKB	Helix	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H1J	
+P40040	UniProtKB	Helix	9	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H1J	
+P40040	UniProtKB	Helix	27	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H1J	
+P40040	UniProtKB	Helix	122	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UZX	
+P40040	UniProtKB	Helix	147	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UZX	
+P40040	UniProtKB	Helix	170	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UZX	
+##sequence-region P53552 1 1597
+P53552	UniProtKB	Chain	1	1597	.	.	.	ID=PRO_0000097359;Note=THO complex subunit 2	
+##sequence-region O13539 1 261
+O13539	UniProtKB	Chain	1	261	.	.	.	ID=PRO_0000267642;Note=THO complex subunit THP2	
+##sequence-region Q07914 1 168
+Q07914	UniProtKB	Chain	1	168	.	.	.	ID=PRO_0000071118;Note=Mitochondrial import inner membrane translocase subunit TIM14	
+Q07914	UniProtKB	Topological domain	1	65	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07914	UniProtKB	Transmembrane	66	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07914	UniProtKB	Topological domain	84	168	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07914	UniProtKB	Domain	112	168	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+Q07914	UniProtKB	Mutagenesis	141	143	.	.	.	Note=Induces lethality. HPD->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14605210;Dbxref=PMID:14605210	
+Q07914	UniProtKB	Mutagenesis	141	141	.	.	.	Note=Induces lethality. H->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517234,ECO:0000269|PubMed:14605210;Dbxref=PMID:14517234,PMID:14605210	
+Q07914	UniProtKB	Mutagenesis	142	142	.	.	.	Note=Induces a strong reduction in ability to stimulate mtHSP70 activity but does not affect import of proteins into mitochondrial matrix. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16105940;Dbxref=PMID:16105940	
+Q07914	UniProtKB	Mutagenesis	143	143	.	.	.	Note=Induces lethality. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16105940;Dbxref=PMID:16105940	
+Q07914	UniProtKB	Mutagenesis	144	144	.	.	.	Note=Induces a strong reduction in ability to stimulate mtHSP70 activity but does not affect import of proteins into mitochondrial matrix. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16105940;Dbxref=PMID:16105940	
+Q07914	UniProtKB	Mutagenesis	150	150	.	.	.	Note=Temperature-sensitive mutant that impairs heterodimerization with PAM16 and import of proteins into mitochondrial matrix when incubated at 37 degrees Celsius. L->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16105940;Dbxref=PMID:16105940	
+Q07914	UniProtKB	Helix	110	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ	
+Q07914	UniProtKB	Turn	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ	
+Q07914	UniProtKB	Helix	126	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ	
+Q07914	UniProtKB	Helix	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ	
+Q07914	UniProtKB	Helix	148	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ	
+##sequence-region P39515 1 158
+P39515	UniProtKB	Chain	1	158	.	.	.	ID=PRO_0000210296;Note=Mitochondrial import inner membrane translocase subunit TIM17	
+P39515	UniProtKB	Topological domain	1	11	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39515	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39515	UniProtKB	Topological domain	33	58	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39515	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39515	UniProtKB	Topological domain	80	87	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39515	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39515	UniProtKB	Topological domain	109	112	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39515	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39515	UniProtKB	Topological domain	134	158	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39515	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Induces abolition of mitochondrial import of transit peptide-containing proteins%3B when associated with K-8. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15618217;Dbxref=PMID:15618217	
+P39515	UniProtKB	Mutagenesis	8	8	.	.	.	Note=Induces abolition of mitochondrial import of transit peptide-containing proteins%3B when associated with K-4. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15618217;Dbxref=PMID:15618217	
+P39515	UniProtKB	Sequence conflict	33	33	.	.	.	Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q01852 1 431
+Q01852	UniProtKB	Nucleotide binding	101	108	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01852	UniProtKB	Region	43	209	.	.	.	Note=Interaction with SSC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18426906;Dbxref=PMID:18426906	
+Q01852	UniProtKB	Mutagenesis	180	180	.	.	.	Note=Disrupts association with the translocase complex. R->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18426906;Dbxref=PMID:18426906	
+Q01852	UniProtKB	Helix	237	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Helix	249	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Turn	259	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FXT	
+Q01852	UniProtKB	Helix	271	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Helix	286	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Helix	297	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Helix	310	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Helix	319	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Turn	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Beta strand	337	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Beta strand	342	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Beta strand	358	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Beta strand	363	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Beta strand	377	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Beta strand	386	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Beta strand	394	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+Q01852	UniProtKB	Beta strand	406	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FXT	
+Q01852	UniProtKB	Beta strand	412	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FXT	
+Q01852	UniProtKB	Beta strand	417	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9	
+##sequence-region P27654 1 210
+P27654	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10216230,ECO:0000269|PubMed:7746155,ECO:0000269|PubMed:7768807,ECO:0000269|PubMed:9818717;Dbxref=PMID:10216230,PMID:7746155,PMID:7768807,PMID:9818717	
+P27654	UniProtKB	Chain	20	186	.	.	.	ID=PRO_0000033237;Note=Temperature shock-inducible protein 1	
+P27654	UniProtKB	Propeptide	187	210	.	.	.	ID=PRO_0000033238;Note=Removed in mature form	
+P27654	UniProtKB	Compositional bias	101	120	.	.	.	Note=Ala/Ser-rich	
+P27654	UniProtKB	Lipidation	186	186	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10216230;Dbxref=PMID:10216230	
+##sequence-region P10863 1 254
+P10863	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10863	UniProtKB	Chain	19	233	.	.	.	ID=PRO_0000033233;Note=Cold shock-induced protein TIR1	
+P10863	UniProtKB	Propeptide	234	254	.	.	.	ID=PRO_0000033234;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10863	UniProtKB	Repeat	114	119	.	.	.	Note=1-1	
+P10863	UniProtKB	Repeat	120	125	.	.	.	Note=1-2	
+P10863	UniProtKB	Repeat	126	131	.	.	.	Note=1-3	
+P10863	UniProtKB	Repeat	132	137	.	.	.	Note=1-4	
+P10863	UniProtKB	Repeat	138	143	.	.	.	Note=1-5	
+P10863	UniProtKB	Repeat	144	155	.	.	.	Note=2-1	
+P10863	UniProtKB	Repeat	156	167	.	.	.	Note=2-2	
+P10863	UniProtKB	Repeat	168	179	.	.	.	Note=2-3	
+P10863	UniProtKB	Repeat	180	191	.	.	.	Note=2-4	
+P10863	UniProtKB	Repeat	192	203	.	.	.	Note=2-5	
+P10863	UniProtKB	Repeat	210	224	.	.	.	Note=PIR1/2/3	
+P10863	UniProtKB	Region	114	143	.	.	.	Note=5 X 6 AA approximate tandem repeats%2C Ala/Ser-rich	
+P10863	UniProtKB	Region	144	203	.	.	.	Note=5 X 12 AA approximate tandem repeats%2C Ala/Ser-rich	
+P10863	UniProtKB	Site	220	220	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P10863	UniProtKB	Lipidation	233	233	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P54837 1 211
+P54837	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10713261,ECO:0000269|PubMed:8900179;Dbxref=PMID:10713261,PMID:8900179	
+P54837	UniProtKB	Chain	21	211	.	.	.	ID=PRO_0000010414;Note=Endoplasmic reticulum vesicle protein 25	
+P54837	UniProtKB	Topological domain	21	180	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54837	UniProtKB	Transmembrane	181	201	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54837	UniProtKB	Topological domain	202	211	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54837	UniProtKB	Domain	33	121	.	.	.	Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096	
+P54837	UniProtKB	Mutagenesis	206	208	.	.	.	Note=Decrease in COPI-binding. KTK->ATA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11560939;Dbxref=PMID:11560939	
+##sequence-region P32802 1 667
+P32802	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8314797;Dbxref=PMID:8314797	
+P32802	UniProtKB	Chain	23	667	.	.	.	ID=PRO_0000034371;Note=Transmembrane 9 superfamily member 1	
+P32802	UniProtKB	Chain	23	250	.	.	.	ID=PRO_0000034372;Note=Protein p24a	
+P32802	UniProtKB	Topological domain	23	302	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Transmembrane	303	323	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Topological domain	324	370	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Transmembrane	371	391	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Topological domain	392	405	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Transmembrane	406	426	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Topological domain	427	442	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Transmembrane	443	463	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Topological domain	464	474	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Transmembrane	475	495	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Topological domain	496	527	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Transmembrane	528	548	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Topological domain	549	560	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Transmembrane	561	581	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Topological domain	582	596	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Transmembrane	597	617	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Topological domain	618	635	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Transmembrane	636	656	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Topological domain	657	667	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Site	250	251	.	.	.	Note=Cleavage%3B by KEX2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Glycosylation	61	61	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Glycosylation	282	282	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32802	UniProtKB	Sequence conflict	207	207	.	.	.	Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32802	UniProtKB	Sequence conflict	268	268	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32802	UniProtKB	Sequence conflict	488	488	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06417 1 326
+Q06417	UniProtKB	Chain	1	326	.	.	.	ID=PRO_0000247778;Note=Uncharacterized oxidoreductase TDA5	
+Q06417	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06417	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06417	UniProtKB	Nucleotide binding	74	98	.	.	.	Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06417	UniProtKB	Active site	214	214	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001	
+Q06417	UniProtKB	Binding site	201	201	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03290 1 321
+Q03290	UniProtKB	Chain	1	321	.	.	.	ID=PRO_0000055942;Note=RNA polymerase II transcription factor B subunit 3	
+Q03290	UniProtKB	Zinc finger	13	60	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q03290	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03290	UniProtKB	Modified residue	258	258	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region P46678 1 594
+P46678	UniProtKB	Chain	1	594	.	.	.	ID=PRO_0000072498;Note=Transcription factor TFIIIB component B''	
+P46678	UniProtKB	Domain	415	466	.	.	.	Note=SANT	
+P46678	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P46678	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q12415 1 435
+Q12415	UniProtKB	Chain	1	435	.	.	.	ID=PRO_0000072499;Note=Transcription factor tau 55 kDa subunit	
+Q12415	UniProtKB	Modified residue	365	365	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12415	UniProtKB	Sequence conflict	9	9	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12415	UniProtKB	Beta strand	5	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Helix	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Beta strand	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Helix	38	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Beta strand	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Helix	67	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Helix	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Helix	108	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Turn	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Helix	136	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Beta strand	163	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Helix	170	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Beta strand	204	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Helix	231	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Beta strand	236	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+Q12415	UniProtKB	Helix	257	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0	
+##sequence-region P40308 1 642
+P40308	UniProtKB	Chain	1	642	.	.	.	ID=PRO_0000203356;Note=Lipase 3	
+P40308	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40308	UniProtKB	Transmembrane	228	248	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40308	UniProtKB	Domain	204	392	.	.	.	Note=PNPLA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+P40308	UniProtKB	Motif	235	239	.	.	.	Note=GXSXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+P40308	UniProtKB	Active site	237	237	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40308	UniProtKB	Sequence conflict	96	96	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40308	UniProtKB	Sequence conflict	100	100	.	.	.	Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P42883 1 340
+P42883	UniProtKB	Chain	1	340	.	.	.	ID=PRO_0000211620;Note=4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI12	
+P42883	UniProtKB	Region	115	118	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+P42883	UniProtKB	Motif	195	199	.	.	.	Note=CCCFC%3B essential for catalytic activity%2C may be the site of iron coordination;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+P42883	UniProtKB	Active site	66	66	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+P42883	UniProtKB	Modified residue	62	62	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+##sequence-region Q08224 1 551
+Q08224	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000192041;Note=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20	
+Q08224	UniProtKB	Binding site	64	64	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08224	UniProtKB	Sequence conflict	323	323	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08224	UniProtKB	Beta strand	3	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Beta strand	25	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Beta strand	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	39	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Beta strand	53	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Beta strand	69	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	77	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Beta strand	94	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	103	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Beta strand	122	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	142	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Beta strand	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	161	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	178	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Beta strand	196	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Beta strand	212	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Turn	220	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Beta strand	224	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	241	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	259	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Turn	293	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	300	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	333	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Turn	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	344	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	354	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	366	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	397	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Turn	430	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	440	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	458	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Turn	478	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	490	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	501	518	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	523	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+Q08224	UniProtKB	Helix	526	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5	
+##sequence-region P40340 1 1379
+P40340	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P40340	UniProtKB	Chain	2	1379	.	.	.	ID=PRO_0000084771;Note=Tat-binding homolog 7	
+P40340	UniProtKB	Domain	1044	1086	.	.	.	Note=Bromo%3B divergent;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+P40340	UniProtKB	Nucleotide binding	454	461	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40340	UniProtKB	Compositional bias	135	139	.	.	.	Note=Poly-Glu	
+P40340	UniProtKB	Compositional bias	157	160	.	.	.	Note=Poly-Arg	
+P40340	UniProtKB	Compositional bias	358	361	.	.	.	Note=Poly-Asn	
+P40340	UniProtKB	Compositional bias	390	395	.	.	.	Note=Poly-Lys	
+P40340	UniProtKB	Compositional bias	737	740	.	.	.	Note=Poly-Glu	
+P40340	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P40340	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P40340	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P40340	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40340	UniProtKB	Modified residue	212	212	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40340	UniProtKB	Modified residue	229	229	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40340	UniProtKB	Modified residue	241	241	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40340	UniProtKB	Modified residue	259	259	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40340	UniProtKB	Modified residue	285	285	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40340	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40340	UniProtKB	Modified residue	369	369	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40340	UniProtKB	Modified residue	370	370	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40340	UniProtKB	Modified residue	735	735	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40340	UniProtKB	Modified residue	1142	1142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40340	UniProtKB	Modified residue	1256	1256	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40340	UniProtKB	Sequence conflict	70	70	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40340	UniProtKB	Sequence conflict	241	241	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40340	UniProtKB	Sequence conflict	1016	1016	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40340	UniProtKB	Sequence conflict	1142	1142	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40340	UniProtKB	Sequence conflict	1153	1153	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40340	UniProtKB	Sequence conflict	1250	1250	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40340	UniProtKB	Sequence conflict	1276	1276	.	.	.	Note=I->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40340	UniProtKB	Sequence conflict	1283	1283	.	.	.	Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38228 1 572
+P38228	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38228	UniProtKB	Chain	17	572	.	.	.	ID=PRO_0000063639;Note=Mitochondrial chaperone TCM62	
+P38228	UniProtKB	Topological domain	17	471	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38228	UniProtKB	Transmembrane	472	488	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38228	UniProtKB	Topological domain	489	572	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08921 1 799
+Q08921	UniProtKB	Chain	1	799	.	.	.	ID=PRO_0000271786;Note=Target of rapamycin complex 1 subunit TCO89	
+Q08921	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08921	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08921	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08921	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q08921	UniProtKB	Modified residue	107	107	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q08921	UniProtKB	Modified residue	115	115	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08921	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08921	UniProtKB	Modified residue	203	203	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08921	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08921	UniProtKB	Modified residue	290	290	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08921	UniProtKB	Modified residue	397	397	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08921	UniProtKB	Modified residue	575	575	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08921	UniProtKB	Modified residue	707	707	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32776 1 642
+P32776	UniProtKB	Chain	1	642	.	.	.	ID=PRO_0000119261;Note=RNA polymerase II transcription factor B subunit 1	
+P32776	UniProtKB	Domain	165	221	.	.	.	Note=BSD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00036	
+P32776	UniProtKB	Domain	243	295	.	.	.	Note=BSD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00036	
+P32776	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32776	UniProtKB	Sequence conflict	209	209	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32776	UniProtKB	Beta strand	3	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O	
+P32776	UniProtKB	Beta strand	13	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O	
+P32776	UniProtKB	Beta strand	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O	
+P32776	UniProtKB	Beta strand	26	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O	
+P32776	UniProtKB	Beta strand	37	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O	
+P32776	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O	
+P32776	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LOX	
+P32776	UniProtKB	Beta strand	56	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O	
+P32776	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O	
+P32776	UniProtKB	Beta strand	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K2U	
+P32776	UniProtKB	Beta strand	85	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O	
+P32776	UniProtKB	Helix	94	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O	
+##sequence-region P33339 1 1025
+P33339	UniProtKB	Chain	1	1025	.	.	.	ID=PRO_0000106364;Note=Transcription factor tau 131 kDa subunit	
+P33339	UniProtKB	Repeat	128	161	.	.	.	Note=TPR 1	
+P33339	UniProtKB	Repeat	162	195	.	.	.	Note=TPR 2	
+P33339	UniProtKB	Repeat	196	229	.	.	.	Note=TPR 3	
+P33339	UniProtKB	Repeat	230	263	.	.	.	Note=TPR 4	
+P33339	UniProtKB	Repeat	264	297	.	.	.	Note=TPR 5	
+P33339	UniProtKB	Repeat	432	465	.	.	.	Note=TPR 6	
+P33339	UniProtKB	Repeat	467	501	.	.	.	Note=TPR 7	
+P33339	UniProtKB	Repeat	502	535	.	.	.	Note=TPR 8	
+P33339	UniProtKB	Repeat	536	569	.	.	.	Note=TPR 9	
+P33339	UniProtKB	Repeat	875	908	.	.	.	Note=TPR 10	
+P33339	UniProtKB	Repeat	959	992	.	.	.	Note=TPR 11	
+P33339	UniProtKB	Region	128	569	.	.	.	Note=Sufficient to bind BDP1	
+P33339	UniProtKB	Modified residue	311	311	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33339	UniProtKB	Natural variant	280	280	.	.	.	Note=In strain: SK1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P33339	UniProtKB	Natural variant	635	635	.	.	.	Note=In strain: SK1. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P33339	UniProtKB	Natural variant	1025	1025	.	.	.	Note=In strain: SK1. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P33339	UniProtKB	Mutagenesis	148	148	.	.	.	Note=In PCF1-17%3B increases RNA polymerase III gene transcription. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943	
+P33339	UniProtKB	Mutagenesis	162	162	.	.	.	Note=In PCF1-12%3B increases RNA polymerase III gene transcription. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943	
+P33339	UniProtKB	Mutagenesis	162	162	.	.	.	Note=In PCF1-139%3B increases RNA polymerase III gene transcription. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943	
+P33339	UniProtKB	Mutagenesis	164	164	.	.	.	Note=In PCF1-19%3B increases RNA polymerase III gene transcription. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943	
+P33339	UniProtKB	Mutagenesis	167	167	.	.	.	Note=In PCF1-2%3B increases RNA polymerase III gene transcription due to an increase in the recruitment of BRF1 to TFIIIC-DNA. No affect on affinity of TFIIIC for DNA. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943	
+P33339	UniProtKB	Mutagenesis	172	172	.	.	.	Note=In PCF1-11%3B increases RNA polymerase III gene transcription. Y->C	
+P33339	UniProtKB	Mutagenesis	188	188	.	.	.	Note=In PCF1-23%3B increases RNA polymerase III gene transcription. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943	
+P33339	UniProtKB	Mutagenesis	190	190	.	.	.	Note=In PCF1-1%3B affects the rate of recruitment of TFIIIB to the template. Increases the amount of transcriptionally active TFIIIB. Increases RNA polymerase III gene transcription. Increases the binding affinity for BRF1%2C but does not affect the binding affinity for BDP1 in the TFIIIC-dependent assembly of TFIIIB. Overcomes autoinhibition of BRF1 binding. H->Y;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12167707,ECO:0000269|PubMed:7488859,ECO:0000269|PubMed:8264649,ECO:0000269|PubMed:9372943;Dbxref=PMID:12167707,PMID:7488859,PMID:8264649,PMID:9372943	
+P33339	UniProtKB	Mutagenesis	192	192	.	.	.	Note=In PCF1-138%3B increases RNA polymerase III gene transcription. N->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943	
+P33339	UniProtKB	Mutagenesis	199	199	.	.	.	Note=In PCF1-15%3B increases RNA polymerase III gene transcription. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943	
+P33339	UniProtKB	Mutagenesis	469	469	.	.	.	Note=RNA polymerase III defective. Defect in the recruitment of BRF1 into TFIIIB-TFIIIC-DNA complexes and diminished direct interaction between TFC4 and BRF1. Decreased binding affinity for BDP1 incorporation into TFIIIB-TFIIIC-DNA complexes and inhibited binary interaction between BDP1 and TFC4. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12930823;Dbxref=PMID:12930823	
+P33339	UniProtKB	Mutagenesis	472	472	.	.	.	Note=RNA polymerase III defective. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12930823;Dbxref=PMID:12930823	
+P33339	UniProtKB	Mutagenesis	504	504	.	.	.	Note=RNA polymerase III defective. V->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12930823;Dbxref=PMID:12930823	
+P33339	UniProtKB	Mutagenesis	541	541	.	.	.	Note=RNA polymerase III defective. S->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12930823;Dbxref=PMID:12930823	
+P33339	UniProtKB	Mutagenesis	542	542	.	.	.	Note=RNA polymerase III defective. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12930823;Dbxref=PMID:12930823	
+P33339	UniProtKB	Mutagenesis	728	728	.	.	.	Note=In PCF1-8%3B increases RNA polymerase III transcription. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859	
+P33339	UniProtKB	Mutagenesis	728	728	.	.	.	Note=In PCF1-7%3B increases RNA polymerase III transcription. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859	
+P33339	UniProtKB	Mutagenesis	728	728	.	.	.	Note=In PCF1-4%3B increases RNA polymerase III transcription ninefold over wild-type. Increases the amount of transcriptionally active TFIIIB. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859	
+P33339	UniProtKB	Mutagenesis	728	728	.	.	.	Note=In PCF1-3%3B increases RNA polymerase III transcription two- to threefold over wild-type. Increases the amount of transcriptionally active TFIIIB. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859	
+P33339	UniProtKB	Mutagenesis	728	728	.	.	.	Note=In PCF1-5%3B increases RNA polymerase III transcription. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859	
+P33339	UniProtKB	Mutagenesis	728	728	.	.	.	Note=In PCF1-6%3B increases RNA polymerase III transcription. R->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859	
+P33339	UniProtKB	Helix	133	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	146	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	151	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	162	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	178	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	196	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	212	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	230	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	246	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	264	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	280	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	344	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	357	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	374	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	388	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	396	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	408	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	414	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Turn	421	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Beta strand	424	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	432	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Turn	444	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	448	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	456	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	463	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	467	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	483	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	491	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	497	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	502	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	518	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	536	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+P33339	UniProtKB	Helix	552	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO	
+##sequence-region Q08686 1 304
+Q08686	UniProtKB	Chain	1	304	.	.	.	ID=PRO_0000139402;Note=Thiosulfate sulfurtransferase TUM1	
+Q08686	UniProtKB	Domain	20	137	.	.	.	Note=Rhodanese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+Q08686	UniProtKB	Domain	177	299	.	.	.	Note=Rhodanese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+Q08686	UniProtKB	Active site	259	259	.	.	.	Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+Q08686	UniProtKB	Binding site	191	191	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08686	UniProtKB	Modified residue	201	201	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08686	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08686	UniProtKB	Beta strand	5	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	9	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	24	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	40	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Turn	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	75	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	92	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	98	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	104	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	117	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	125	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	158	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	165	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	177	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	182	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	189	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	199	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	216	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Turn	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	232	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	255	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	263	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Beta strand	279	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	286	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+Q08686	UniProtKB	Helix	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN	
+##sequence-region P42949 1 149
+P42949	UniProtKB	Chain	1	149	.	.	.	ID=PRO_0000214098;Note=Mitochondrial import inner membrane translocase subunit TIM16	
+P42949	UniProtKB	Region	57	113	.	.	.	Note=J-like	
+P42949	UniProtKB	Mutagenesis	88	90	.	.	.	Note=Does not confer ability to stimulate the ATPase activity of mtHSP70. DKE->HPD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15218029;Dbxref=PMID:15218029	
+P42949	UniProtKB	Sequence conflict	114	114	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P42949	UniProtKB	Helix	55	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ	
+P42949	UniProtKB	Helix	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ	
+P42949	UniProtKB	Helix	73	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ	
+P42949	UniProtKB	Helix	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ	
+P42949	UniProtKB	Helix	95	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ	
+##sequence-region Q12328 1 207
+Q12328	UniProtKB	Chain	1	207	.	.	.	ID=PRO_0000210301;Note=Mitochondrial import inner membrane translocase subunit TIM22	
+Q12328	UniProtKB	Transmembrane	47	67	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12328	UniProtKB	Transmembrane	152	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12328	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P33315 1 681
+P33315	UniProtKB	Chain	1	681	.	.	.	ID=PRO_0000191905;Note=Transketolase 2	
+P33315	UniProtKB	Nucleotide binding	116	118	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Active site	418	418	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Metal binding	157	157	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Metal binding	187	187	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Metal binding	189	189	.	.	.	Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	30	30	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	69	69	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	158	158	.	.	.	Note=Thiamine pyrophosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	187	187	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	263	263	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	263	263	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	359	359	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	386	386	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	418	418	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	445	445	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	469	469	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	477	477	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Binding site	528	528	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Site	30	30	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Site	263	263	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33315	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23254	
+P33315	UniProtKB	Cross-link	648	648	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23254	
+##sequence-region Q12239 1 342
+Q12239	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000235931;Note=Transmembrane protein 115 homolog	
+Q12239	UniProtKB	Topological domain	1	21	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12239	UniProtKB	Transmembrane	22	42	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12239	UniProtKB	Topological domain	43	121	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12239	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12239	UniProtKB	Topological domain	143	159	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12239	UniProtKB	Transmembrane	160	180	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12239	UniProtKB	Topological domain	181	207	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12239	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12239	UniProtKB	Topological domain	229	342	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12239	UniProtKB	Glycosylation	114	114	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03525 1 211
+Q03525	UniProtKB	Chain	1	211	.	.	.	ID=PRO_0000203349;Note=Protein TMA23	
+Q03525	UniProtKB	Compositional bias	130	133	.	.	.	Note=Poly-Arg	
+Q03525	UniProtKB	Compositional bias	158	167	.	.	.	Note=Poly-Lys	
+##sequence-region Q04600 1 565
+Q04600	UniProtKB	Chain	1	565	.	.	.	ID=PRO_0000244640;Note=Translation machinery-associated protein 64	
+Q04600	UniProtKB	Domain	89	170	.	.	.	Note=PUA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00161	
+Q04600	UniProtKB	Domain	363	446	.	.	.	Note=SWIB	
+Q04600	UniProtKB	Domain	475	547	.	.	.	Note=SUI1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00200	
+Q04600	UniProtKB	Compositional bias	558	565	.	.	.	Note=Poly-Lys	
+##sequence-region P36165 1 910
+P36165	UniProtKB	Chain	1	910	.	.	.	ID=PRO_0000203227;Note=Lipase 4	
+P36165	UniProtKB	Transmembrane	282	302	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36165	UniProtKB	Transmembrane	310	326	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36165	UniProtKB	Transmembrane	426	442	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36165	UniProtKB	Domain	282	483	.	.	.	Note=PNPLA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+P36165	UniProtKB	Motif	286	291	.	.	.	Note=GXGXXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+P36165	UniProtKB	Motif	313	317	.	.	.	Note=GXSXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+P36165	UniProtKB	Active site	315	315	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+P36165	UniProtKB	Active site	470	470	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+P36165	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36165	UniProtKB	Modified residue	737	737	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36165	UniProtKB	Modified residue	749	749	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36165	UniProtKB	Modified residue	751	751	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P36165	UniProtKB	Modified residue	836	836	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P47183 1 340
+P47183	UniProtKB	Chain	1	340	.	.	.	ID=PRO_0000211619;Note=4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI11	
+P47183	UniProtKB	Region	115	118	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+P47183	UniProtKB	Motif	195	199	.	.	.	Note=CCCFC%3B essential for catalytic activity%2C may be the site of iron coordination;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+P47183	UniProtKB	Active site	66	66	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+P47183	UniProtKB	Modified residue	62	62	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+##sequence-region Q07471 1 609
+Q07471	UniProtKB	Chain	1	609	.	.	.	ID=PRO_0000090836;Note=Thiamine metabolism regulatory protein THI3	
+##sequence-region P43534 1 340
+P43534	UniProtKB	Chain	1	340	.	.	.	ID=PRO_0000211618;Note=4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI5	
+P43534	UniProtKB	Region	115	118	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Motif	195	199	.	.	.	Note=CCCFC%3B essential for catalytic activity%2C may be the site of iron coordination;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Active site	66	66	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Modified residue	62	62	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Unable to sustain growth in thiamine-free medium. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Mutagenesis	12	12	.	.	.	Note=Unable to sustain growth in thiamine-free medium. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Mutagenesis	62	62	.	.	.	Note=Unable to sustain growth in thiamine-free medium. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Mutagenesis	66	66	.	.	.	Note=Unable to sustain growth in thiamine-free medium. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Mutagenesis	195	195	.	.	.	Note=Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Mutagenesis	196	196	.	.	.	Note=Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Mutagenesis	197	197	.	.	.	Note=Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Mutagenesis	199	199	.	.	.	Note=Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037	
+P43534	UniProtKB	Beta strand	6	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Beta strand	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	19	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	29	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Beta strand	37	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	48	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Beta strand	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Beta strand	59	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	64	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Turn	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Beta strand	77	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Beta strand	89	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Turn	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Beta strand	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	117	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H67	
+P43534	UniProtKB	Turn	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H67	
+P43534	UniProtKB	Beta strand	135	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	145	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Beta strand	153	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Turn	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	164	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Beta strand	182	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Beta strand	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H6D	
+P43534	UniProtKB	Helix	196	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H6D	
+P43534	UniProtKB	Beta strand	201	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	207	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	214	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	235	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	247	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	252	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Turn	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	273	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+P43534	UniProtKB	Helix	315	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65	
+##sequence-region P41835 1 540
+P41835	UniProtKB	Chain	1	540	.	.	.	ID=PRO_0000157090;Note=Thiamine biosynthetic bifunctional enzyme	
+P41835	UniProtKB	Region	1	238	.	.	.	Note=Thiamine-phosphate synthase	
+P41835	UniProtKB	Region	43	47	.	.	.	Note=HMP-PP binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Region	143	145	.	.	.	Note=THZ-P binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Region	209	210	.	.	.	Note=THZ-P binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Region	239	540	.	.	.	Note=Hydroxyethylthiazole kinase	
+P41835	UniProtKB	Active site	465	465	.	.	.	Note=Proton acceptor%3B for hydroxyethylthiazole kinase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Metal binding	76	76	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Metal binding	95	95	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Binding site	75	75	.	.	.	Note=HMP-PP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Binding site	114	114	.	.	.	Note=HMP-PP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Binding site	146	146	.	.	.	Note=HMP-PP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Binding site	181	181	.	.	.	Note=THZ-P%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Binding site	290	290	.	.	.	Note=4-methyl-5-(2-hydroxyethyl)thiazole%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Binding site	365	365	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Binding site	415	415	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Binding site	462	462	.	.	.	Note=4-methyl-5-(2-hydroxyethyl)thiazole%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41835	UniProtKB	Natural variant	370	370	.	.	.	Note=In THI6-3%3B possesses TMP-PPASE activity only. E->K	
+P41835	UniProtKB	Natural variant	476	476	.	.	.	Note=In THI6-2%3B both enzyme activities greatly decreased. G->D	
+P41835	UniProtKB	Natural variant	510	510	.	.	.	Note=In THI6-1%3B both enzyme activities greatly decreased. G->D	
+##sequence-region P27796 1 417
+P27796	UniProtKB	Active site	125	125	.	.	.	Note=Acyl-thioester intermediate	
+P27796	UniProtKB	Active site	375	375	.	.	.	Note=Proton acceptor	
+P27796	UniProtKB	Active site	403	403	.	.	.	Note=Proton acceptor	
+P27796	UniProtKB	Helix	1	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P27796	UniProtKB	Turn	26	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Beta strand	36	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Turn	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Turn	53	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	59	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Beta strand	88	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	100	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Beta strand	118	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	127	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Beta strand	145	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	155	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	171	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	179	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	186	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	201	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Turn	225	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	251	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Turn	263	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Turn	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Beta strand	276	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	288	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Beta strand	300	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	312	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	318	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Beta strand	338	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	347	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	361	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	370	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Turn	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Helix	380	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Beta strand	397	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Turn	405	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+P27796	UniProtKB	Beta strand	408	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW	
+##sequence-region P87108 1 93
+P87108	UniProtKB	Chain	1	93	.	.	.	ID=PRO_0000193622;Note=Mitochondrial import inner membrane translocase subunit TIM10	
+P87108	UniProtKB	Region	1	31	.	.	.	Note=Interaction with transmembrane regions of transmembrane proteins in transit	
+P87108	UniProtKB	Region	73	93	.	.	.	Note=Required for heterohexamerization	
+P87108	UniProtKB	Motif	40	65	.	.	.	Note=Twin CX3C motif	
+P87108	UniProtKB	Disulfide bond	40	65	.	.	.	.	
+P87108	UniProtKB	Disulfide bond	44	61	.	.	.	.	
+P87108	UniProtKB	Mutagenesis	40	40	.	.	.	Note=Induces impairment in folding and loss of zinc-binding. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12882976,ECO:0000269|PubMed:14973126;Dbxref=PMID:12882976,PMID:14973126	
+P87108	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Loss of function due to severely affected folding and the presence of non-native disulfide bonds%3B loss of zinc-binding. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12882976,ECO:0000269|PubMed:14973126;Dbxref=PMID:12882976,PMID:14973126	
+P87108	UniProtKB	Mutagenesis	61	61	.	.	.	Note=Loss of function due to severely affected folding and the presence of non-native disulfide bonds%3B loss of zinc-binding. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12882976,ECO:0000269|PubMed:14973126;Dbxref=PMID:12882976,PMID:14973126	
+P87108	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Induces impairment in folding and loss of zinc-binding. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12882976,ECO:0000269|PubMed:14973126;Dbxref=PMID:12882976,PMID:14973126	
+P87108	UniProtKB	Turn	16	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR	
+P87108	UniProtKB	Helix	20	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR	
+P87108	UniProtKB	Helix	56	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR	
+##sequence-region P33891 1 701
+P33891	UniProtKB	Chain	1	701	.	.	.	ID=PRO_0000072543;Note=Protein transport protein TIP20	
+P33891	UniProtKB	Domain	147	701	.	.	.	Note=RINT1/TIP20;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00717	
+P33891	UniProtKB	Helix	10	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P33891	UniProtKB	Helix	46	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	59	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	73	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	115	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	142	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	161	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Turn	179	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	192	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	239	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	262	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	296	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	309	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	324	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	352	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	358	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	383	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	389	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	406	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	413	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	417	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	427	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Beta strand	446	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	450	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	478	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	500	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	513	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	531	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	538	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	558	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	561	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	581	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Turn	602	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	611	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	637	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	650	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	655	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Turn	658	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	663	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	673	678	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Beta strand	681	683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+P33891	UniProtKB	Helix	685	696	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN	
+##sequence-region P89886 1 181
+P89886	UniProtKB	Chain	1	181	.	.	.	ID=PRO_0000245367;Note=Translation machinery-associated protein 20	
+P89886	UniProtKB	Domain	90	172	.	.	.	Note=PUA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00161	
+P89886	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q12049 1 470
+Q12049	UniProtKB	Chain	1	470	.	.	.	ID=PRO_0000257823;Note=Protein THP3	
+Q12049	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P40462 1 946
+P40462	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40462	UniProtKB	Chain	2	946	.	.	.	ID=PRO_0000095121;Note=Protein TMA108	
+P40462	UniProtKB	Region	293	297	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40462	UniProtKB	Active site	331	331	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P40462	UniProtKB	Metal binding	330	330	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P40462	UniProtKB	Metal binding	334	334	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P40462	UniProtKB	Metal binding	353	353	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P40462	UniProtKB	Site	423	423	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40462	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P36142 1 418
+P36142	UniProtKB	Chain	1	418	.	.	.	ID=PRO_0000211558;Note=Transmembrane protein 184 homolog YKR051W	
+P36142	UniProtKB	Topological domain	1	5	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Transmembrane	6	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Topological domain	27	43	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Transmembrane	44	64	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Topological domain	65	78	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Transmembrane	79	99	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Topological domain	100	141	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Topological domain	163	168	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Transmembrane	169	189	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Topological domain	190	205	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Transmembrane	206	226	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Topological domain	227	246	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Transmembrane	247	267	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36142	UniProtKB	Topological domain	268	418	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12513 1 150
+Q12513	UniProtKB	Chain	1	150	.	.	.	ID=PRO_0000240701;Note=Translation machinery-associated protein 17	
+Q12513	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12513	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P53840 1 1238
+P53840	UniProtKB	Chain	1	1238	.	.	.	ID=PRO_0000072620;Note=Topoisomerase 1-associated factor 1	
+P53840	UniProtKB	Modified residue	626	626	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53840	UniProtKB	Modified residue	654	654	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53840	UniProtKB	Modified residue	1056	1056	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53840	UniProtKB	Modified residue	1058	1058	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53840	UniProtKB	Modified residue	1213	1213	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P40310 1 691
+P40310	UniProtKB	Chain	1	691	.	.	.	ID=PRO_0000101774;Note=Outward-rectifier potassium channel TOK1	
+P40310	UniProtKB	Topological domain	1	71	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical%3B Name%3DS1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Topological domain	93	137	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Transmembrane	138	158	.	.	.	Note=Helical%3B Name%3DS2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Topological domain	159	170	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical%3B Name%3DS3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Topological domain	192	203	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical%3B Name%3DS4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Topological domain	225	246	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Transmembrane	247	266	.	.	.	Note=Helical%3B Name%3DS5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Topological domain	267	301	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Transmembrane	302	322	.	.	.	Note=Helical%3B Name%3DS6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Topological domain	323	379	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Transmembrane	380	400	.	.	.	Note=Helical%3B Name%3DS7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Topological domain	401	435	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Transmembrane	436	456	.	.	.	Note=Helical%3B Name%3DS8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Topological domain	457	691	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40310	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40310	UniProtKB	Sequence conflict	442	442	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40310	UniProtKB	Sequence conflict	512	512	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03280 1 3268
+Q03280	UniProtKB	Chain	1	3268	.	.	.	ID=PRO_0000120348;Note=E3 ubiquitin-protein ligase TOM1	
+Q03280	UniProtKB	Domain	2932	3268	.	.	.	Note=HECT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104	
+Q03280	UniProtKB	Compositional bias	1879	2054	.	.	.	Note=Asp-rich	
+Q03280	UniProtKB	Active site	3235	3235	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104	
+Q03280	UniProtKB	Modified residue	1890	1890	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03280	UniProtKB	Modified residue	2096	2096	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03280	UniProtKB	Modified residue	2119	2119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03280	UniProtKB	Modified residue	2376	2376	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03280	UniProtKB	Modified residue	2406	2406	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03280	UniProtKB	Modified residue	2418	2418	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03280	UniProtKB	Mutagenesis	3235	3235	.	.	.	Note=Loss of function. Induces a decrease in transcription activation. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10395901,ECO:0000269|PubMed:10873801,ECO:0000269|PubMed:9753545;Dbxref=PMID:10395901,PMID:10873801,PMID:9753545	
+##sequence-region P35180 1 183
+P35180	UniProtKB	Chain	1	183	.	.	.	ID=PRO_0000051550;Note=Mitochondrial import receptor subunit TOM20	
+P35180	UniProtKB	Topological domain	1	8	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35180	UniProtKB	Transmembrane	9	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35180	UniProtKB	Topological domain	29	183	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35180	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P23644 1 387
+P23644	UniProtKB	Chain	1	387	.	.	.	ID=PRO_0000051535;Note=Mitochondrial import receptor subunit TOM40	
+P23644	UniProtKB	Sequence conflict	387	387	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P80967 1 50
+P80967	UniProtKB	Chain	1	50	.	.	.	ID=PRO_0000218264;Note=Mitochondrial import receptor subunit TOM5	
+P80967	UniProtKB	Topological domain	1	26	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P80967	UniProtKB	Transmembrane	27	45	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38825 1 639
+P38825	UniProtKB	Chain	1	639	.	.	.	ID=PRO_0000106420;Note=Protein TOM71	
+P38825	UniProtKB	Topological domain	1	14	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38825	UniProtKB	Transmembrane	15	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38825	UniProtKB	Topological domain	33	639	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38825	UniProtKB	Repeat	127	160	.	.	.	Note=TPR 1	
+P38825	UniProtKB	Repeat	162	194	.	.	.	Note=TPR 2	
+P38825	UniProtKB	Repeat	345	378	.	.	.	Note=TPR 3	
+P38825	UniProtKB	Repeat	379	411	.	.	.	Note=TPR 4	
+P38825	UniProtKB	Repeat	412	445	.	.	.	Note=TPR 5	
+P38825	UniProtKB	Repeat	447	479	.	.	.	Note=TPR 6	
+P38825	UniProtKB	Repeat	480	513	.	.	.	Note=TPR 7	
+P38825	UniProtKB	Repeat	530	563	.	.	.	Note=TPR 8	
+P38825	UniProtKB	Repeat	565	597	.	.	.	Note=TPR 9	
+P38825	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P38825	UniProtKB	Helix	112	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	120	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	147	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	161	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	177	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	195	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	211	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	235	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	266	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	278	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	295	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	310	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	338	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	361	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	378	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	395	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	412	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	428	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	447	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	462	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	481	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	496	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	521	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	543	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	564	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	580	593	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	598	617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2	
+P38825	UniProtKB	Helix	620	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP3	
+##sequence-region P32830 1 109
+P32830	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32830	UniProtKB	Chain	2	109	.	.	.	ID=PRO_0000096581;Note=Mitochondrial import inner membrane translocase subunit TIM12	
+P32830	UniProtKB	Motif	40	66	.	.	.	Note=Twin CX3C motif	
+P32830	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32830	UniProtKB	Disulfide bond	40	66	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32830	UniProtKB	Disulfide bond	44	62	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53299 1 105
+P53299	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000193632;Note=Mitochondrial import inner membrane translocase subunit TIM13	
+P53299	UniProtKB	Motif	57	77	.	.	.	Note=Twin CX3C motif	
+P53299	UniProtKB	Disulfide bond	57	77	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53299	UniProtKB	Disulfide bond	61	73	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53299	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Abolishes import into mitochondrion%3B when associated with S-61. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941692;Dbxref=PMID:12941692	
+P53299	UniProtKB	Mutagenesis	61	61	.	.	.	Note=Abolishes import into mitochondrion%3B when associated with S-57. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941692;Dbxref=PMID:12941692	
+P53299	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Abolishes import into mitochondrion%3B when associated with S-77. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941692;Dbxref=PMID:12941692	
+P53299	UniProtKB	Mutagenesis	77	77	.	.	.	Note=Abolishes import into mitochondrion%3B when associated with S-73. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941692;Dbxref=PMID:12941692	
+P53299	UniProtKB	Helix	47	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CJH	
+P53299	UniProtKB	Helix	71	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CJH	
+##sequence-region Q08749 1 192
+Q08749	UniProtKB	Transit peptide	1	42	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08749	UniProtKB	Chain	43	192	.	.	.	ID=PRO_0000228080;Note=Mitochondrial import inner membrane translocase subunit TIM18	
+Q08749	UniProtKB	Topological domain	43	88	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08749	UniProtKB	Transmembrane	89	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08749	UniProtKB	Topological domain	110	113	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08749	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08749	UniProtKB	Topological domain	135	144	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08749	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08749	UniProtKB	Topological domain	166	192	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08749	UniProtKB	Sequence conflict	137	137	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08749	UniProtKB	Sequence conflict	137	137	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08749	UniProtKB	Sequence conflict	137	137	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53220 1 239
+P53220	UniProtKB	Transit peptide	1	70	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53220	UniProtKB	Chain	71	239	.	.	.	ID=PRO_0000043166;Note=Mitochondrial import inner membrane translocase subunit TIM21	
+P53220	UniProtKB	Topological domain	71	75	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53220	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53220	UniProtKB	Topological domain	97	239	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53220	UniProtKB	Sequence conflict	39	39	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53220	UniProtKB	Helix	104	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU	
+P53220	UniProtKB	Helix	120	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU	
+P53220	UniProtKB	Beta strand	139	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU	
+P53220	UniProtKB	Beta strand	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU	
+P53220	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU	
+P53220	UniProtKB	Beta strand	158	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU	
+P53220	UniProtKB	Beta strand	168	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU	
+P53220	UniProtKB	Beta strand	182	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU	
+P53220	UniProtKB	Beta strand	199	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU	
+P53220	UniProtKB	Beta strand	213	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU	
+##sequence-region P33890 1 251
+P33890	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33890	UniProtKB	Chain	19	231	.	.	.	ID=PRO_0000033235;Note=Cold shock-induced protein TIR2	
+P33890	UniProtKB	Propeptide	232	251	.	.	.	ID=PRO_0000372445;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33890	UniProtKB	Repeat	207	225	.	.	.	Note=PIR1/2/3	
+P33890	UniProtKB	Compositional bias	112	251	.	.	.	Note=Ala/Ser-rich	
+P33890	UniProtKB	Site	217	217	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33890	UniProtKB	Lipidation	231	231	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33890	UniProtKB	Sequence conflict	69	69	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33890	UniProtKB	Sequence conflict	179	179	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33890	UniProtKB	Sequence conflict	192	192	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08422 1 150
+Q08422	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08422	UniProtKB	Chain	2	150	.	.	.	ID=PRO_0000237648;Note=AN1-type zinc finger protein TMC1	
+Q08422	UniProtKB	Zinc finger	82	134	.	.	.	Note=AN1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00449	
+Q08422	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08422	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08422	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region P40071 1 706
+P40071	UniProtKB	Signal peptide	1	33	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Chain	34	706	.	.	.	ID=PRO_0000034373;Note=Transmembrane 9 superfamily member 3	
+P40071	UniProtKB	Topological domain	34	290	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Transmembrane	291	311	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Topological domain	312	371	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Topological domain	393	405	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Transmembrane	406	426	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Topological domain	427	456	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Transmembrane	457	477	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Topological domain	478	494	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Transmembrane	495	515	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Topological domain	516	553	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Transmembrane	554	574	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Topological domain	575	592	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Transmembrane	593	613	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Topological domain	614	637	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Transmembrane	638	658	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Topological domain	659	665	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Transmembrane	666	686	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40071	UniProtKB	Topological domain	687	706	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32773 1 286
+P32773	UniProtKB	Chain	1	286	.	.	.	ID=PRO_0000072617;Note=Transcription initiation factor IIA large subunit	
+P32773	UniProtKB	Sequence conflict	15	15	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32773	UniProtKB	Helix	4	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+P32773	UniProtKB	Helix	22	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+P32773	UniProtKB	Helix	32	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+P32773	UniProtKB	Helix	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RM1	
+P32773	UniProtKB	Beta strand	243	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+P32773	UniProtKB	Beta strand	257	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+P32773	UniProtKB	Beta strand	272	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+##sequence-region P04786 1 769
+P04786	UniProtKB	Chain	1	769	.	.	.	ID=PRO_0000145211;Note=DNA topoisomerase 1	
+P04786	UniProtKB	Region	357	358	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04786	UniProtKB	Region	420	425	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04786	UniProtKB	Region	512	514	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04786	UniProtKB	Compositional bias	16	20	.	.	.	Note=Poly-Asp	
+P04786	UniProtKB	Compositional bias	55	136	.	.	.	Note=Lys-rich	
+P04786	UniProtKB	Compositional bias	105	139	.	.	.	Note=Glu-rich	
+P04786	UniProtKB	Active site	727	727	.	.	.	Note=O-(3'-phospho-DNA)-tyrosine intermediate;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10130,ECO:0000269|PubMed:2542938,ECO:0000269|PubMed:2547758;Dbxref=PMID:2542938,PMID:2547758	
+P04786	UniProtKB	Site	296	296	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04786	UniProtKB	Site	344	344	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04786	UniProtKB	Site	375	375	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04786	UniProtKB	Site	432	432	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04786	UniProtKB	Site	458	458	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04786	UniProtKB	Site	501	501	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04786	UniProtKB	Site	558	558	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04786	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P04786	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P04786	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04786	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04786	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P04786	UniProtKB	Beta strand	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Beta strand	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Helix	179	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Turn	191	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Helix	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Helix	200	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Helix	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Helix	235	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Helix	256	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Beta strand	272	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Beta strand	278	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Turn	300	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Helix	311	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Beta strand	315	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Beta strand	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Beta strand	334	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Beta strand	345	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Turn	351	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+P04786	UniProtKB	Beta strand	356	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS	
+##sequence-region P06786 1 1428
+P06786	UniProtKB	Chain	1	1428	.	.	.	ID=PRO_0000145387;Note=DNA topoisomerase 2	
+P06786	UniProtKB	Domain	443	557	.	.	.	Note=Toprim;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995	
+P06786	UniProtKB	Nucleotide binding	127	129	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963818;Dbxref=PMID:12963818	
+P06786	UniProtKB	Nucleotide binding	140	147	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963818;Dbxref=PMID:12963818	
+P06786	UniProtKB	Nucleotide binding	365	367	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963818;Dbxref=PMID:12963818	
+P06786	UniProtKB	Region	333	336	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23022727;Dbxref=PMID:23022727	
+P06786	UniProtKB	Region	965	974	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485342;Dbxref=PMID:20485342	
+P06786	UniProtKB	Active site	782	782	.	.	.	Note=O-(5'-phospho-DNA)-tyrosine intermediate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20485342,ECO:0000269|PubMed:9685374;Dbxref=PMID:20485342,PMID:9685374	
+P06786	UniProtKB	Metal binding	449	449	.	.	.	Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00995,ECO:0000269|PubMed:18097402;Dbxref=PMID:18097402	
+P06786	UniProtKB	Metal binding	526	526	.	.	.	Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00995,ECO:0000269|PubMed:18097402;Dbxref=PMID:18097402	
+P06786	UniProtKB	Metal binding	526	526	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00995,ECO:0000269|PubMed:18097402;Dbxref=PMID:18097402	
+P06786	UniProtKB	Metal binding	528	528	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00995,ECO:0000269|PubMed:18097402;Dbxref=PMID:18097402	
+P06786	UniProtKB	Binding site	70	70	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963818;Dbxref=PMID:12963818	
+P06786	UniProtKB	Binding site	99	99	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963818;Dbxref=PMID:12963818	
+P06786	UniProtKB	Site	477	477	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995	
+P06786	UniProtKB	Site	480	480	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485342;Dbxref=PMID:20485342	
+P06786	UniProtKB	Site	650	650	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485342;Dbxref=PMID:20485342	
+P06786	UniProtKB	Site	651	651	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485342;Dbxref=PMID:20485342	
+P06786	UniProtKB	Site	700	700	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485342;Dbxref=PMID:20485342	
+P06786	UniProtKB	Site	734	734	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995	
+P06786	UniProtKB	Site	740	740	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995	
+P06786	UniProtKB	Site	781	781	.	.	.	Note=Transition state stabilizer	
+P06786	UniProtKB	Site	833	833	.	.	.	Note=Important for DNA bending%3B intercalates between base pairs of target DNA	
+P06786	UniProtKB	Site	908	908	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995	
+P06786	UniProtKB	Modified residue	1086	1086	.	.	.	Note=Phosphothreonine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274	
+P06786	UniProtKB	Modified residue	1087	1087	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274	
+P06786	UniProtKB	Modified residue	1252	1252	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06786	UniProtKB	Modified residue	1258	1258	.	.	.	Note=Phosphothreonine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274	
+P06786	UniProtKB	Modified residue	1266	1266	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274	
+P06786	UniProtKB	Modified residue	1269	1269	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274	
+P06786	UniProtKB	Modified residue	1272	1272	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274	
+P06786	UniProtKB	Modified residue	1353	1353	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274	
+P06786	UniProtKB	Modified residue	1356	1356	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274	
+P06786	UniProtKB	Modified residue	1408	1408	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274	
+P06786	UniProtKB	Modified residue	1423	1423	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274	
+P06786	UniProtKB	Mutagenesis	333	336	.	.	.	Note=Reduced enzyme activity%3B abolishes stimulation of ATPase activity upon DNA binding. KKKK->AAAA	
+P06786	UniProtKB	Mutagenesis	333	336	.	.	.	Note=Strongly reduced enzyme activity%3B abolishes stimulation of ATPase activity upon DNA binding. KKKK->AEEA	
+P06786	UniProtKB	Mutagenesis	690	690	.	.	.	Note=Loss of enzyme activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374	
+P06786	UniProtKB	Mutagenesis	697	697	.	.	.	Note=Strongly reduced enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374	
+P06786	UniProtKB	Mutagenesis	700	700	.	.	.	Note=Strongly reduced enzyme activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374	
+P06786	UniProtKB	Mutagenesis	704	704	.	.	.	Note=Strongly reduced enzyme activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374	
+P06786	UniProtKB	Mutagenesis	736	736	.	.	.	Note=No effect. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374	
+P06786	UniProtKB	Mutagenesis	781	781	.	.	.	Note=Strongly reduced enzyme activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374	
+P06786	UniProtKB	Mutagenesis	782	782	.	.	.	Note=Loss of enzyme activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374	
+P06786	UniProtKB	Mutagenesis	828	828	.	.	.	Note=Strongly reduced enzyme activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374	
+P06786	UniProtKB	Sequence conflict	74	74	.	.	.	Note=N->NN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06786	UniProtKB	Sequence conflict	547	547	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06786	UniProtKB	Sequence conflict	837	837	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06786	UniProtKB	Helix	8	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	12	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	17	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	26	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	35	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Turn	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	48	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	58	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	83	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Turn	90	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	94	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Turn	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	116	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	123	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	145	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	153	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Turn	163	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	167	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Turn	175	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	184	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	194	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	203	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	213	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	234	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	247	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Turn	253	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	280	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	288	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	300	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	315	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	342	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	349	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	374	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Beta strand	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	385	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Helix	395	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG	
+P06786	UniProtKB	Turn	433	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	438	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	444	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	451	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	466	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW	
+P06786	UniProtKB	Helix	486	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RGR	
+P06786	UniProtKB	Helix	492	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Turn	503	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW	
+P06786	UniProtKB	Beta strand	506	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	513	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	519	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	527	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW	
+P06786	UniProtKB	Helix	534	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	547	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW	
+P06786	UniProtKB	Beta strand	555	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	563	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	574	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	581	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Turn	591	594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	597	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	609	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	634	642	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RGR	
+P06786	UniProtKB	Helix	647	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RGR	
+P06786	UniProtKB	Beta strand	668	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RGR	
+P06786	UniProtKB	Helix	678	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Turn	695	697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	701	713	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	721	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	736	738	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	741	749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Turn	753	755	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RGR	
+P06786	UniProtKB	Beta strand	760	765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Turn	770	773	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Turn	780	782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	784	787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	791	794	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	797	802	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	805	808	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	811	816	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	824	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	830	833	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	838	841	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	846	857	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	874	880	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	883	887	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	889	894	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	897	902	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	909	920	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	924	926	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW	
+P06786	UniProtKB	Beta strand	932	935	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	938	940	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	943	946	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	949	958	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	960	963	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	967	971	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	975	978	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	984	989	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	990	1034	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Beta strand	1041	1043	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW	
+P06786	UniProtKB	Helix	1045	1054	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Turn	1108	1110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	1114	1117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	1121	1124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	1126	1147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+P06786	UniProtKB	Helix	1151	1176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT	
+##sequence-region P35169 1 2470
+P35169	UniProtKB	Chain	1	2470	.	.	.	ID=PRO_0000088813;Note=Serine/threonine-protein kinase TOR1	
+P35169	UniProtKB	Repeat	114	151	.	.	.	Note=HEAT 1	
+P35169	UniProtKB	Repeat	249	286	.	.	.	Note=HEAT 2	
+P35169	UniProtKB	Repeat	627	663	.	.	.	Note=HEAT 3	
+P35169	UniProtKB	Repeat	664	701	.	.	.	Note=HEAT 4	
+P35169	UniProtKB	Repeat	747	784	.	.	.	Note=HEAT 5	
+P35169	UniProtKB	Repeat	788	826	.	.	.	Note=HEAT 6	
+P35169	UniProtKB	Repeat	832	870	.	.	.	Note=HEAT 7	
+P35169	UniProtKB	Repeat	908	946	.	.	.	Note=HEAT 8	
+P35169	UniProtKB	Repeat	950	987	.	.	.	Note=HEAT 9	
+P35169	UniProtKB	Repeat	1069	1107	.	.	.	Note=HEAT 10	
+P35169	UniProtKB	Repeat	1109	1147	.	.	.	Note=HEAT 11	
+P35169	UniProtKB	Domain	1331	1919	.	.	.	Note=FAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534	
+P35169	UniProtKB	Domain	2125	2437	.	.	.	Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269	
+P35169	UniProtKB	Domain	2438	2470	.	.	.	Note=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535	
+P35169	UniProtKB	Region	1775	2157	.	.	.	Note=Interaction with FKBP-rapamycin	
+P35169	UniProtKB	Compositional bias	441	447	.	.	.	Note=Arg/Lys-rich (basic)	
+P35169	UniProtKB	Mutagenesis	1972	1972	.	.	.	Note=No effect. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7606777,ECO:0000269|PubMed:8413204;Dbxref=PMID:7606777,PMID:8413204	
+P35169	UniProtKB	Mutagenesis	1972	1972	.	.	.	Note=Confers resistance to rapamycin. Abolishes interaction with FKBP-rapamycin. S->E%2CI;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7606777,ECO:0000269|PubMed:8413204;Dbxref=PMID:7606777,PMID:8413204	
+P35169	UniProtKB	Mutagenesis	1972	1972	.	.	.	Note=In DRR1-27%3B confers resistance to rapamycin. S->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7606777,ECO:0000269|PubMed:8413204;Dbxref=PMID:7606777,PMID:8413204	
+P35169	UniProtKB	Mutagenesis	1972	1972	.	.	.	Note=In DRR1-1%3B confers resistance to rapamycin. Abolishes interaction with FKBP-rapamycin. S->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7606777,ECO:0000269|PubMed:8413204;Dbxref=PMID:7606777,PMID:8413204	
+P35169	UniProtKB	Mutagenesis	2275	2275	.	.	.	Note=Abolishes protein kinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10436010;Dbxref=PMID:10436010	
+P35169	UniProtKB	Mutagenesis	2276	2276	.	.	.	Note=Abolishes rapamycin-resistance of mutants E-1972%3B I-1972 and R-1972. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7606777;Dbxref=PMID:7606777	
+P35169	UniProtKB	Mutagenesis	2294	2294	.	.	.	Note=Abolishes rapamycin-resistance of mutants E-1972%3B I-1972 and R-1972. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7606777;Dbxref=PMID:7606777	
+P35169	UniProtKB	Sequence conflict	58	58	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	115	115	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	133	133	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	231	231	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	396	396	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	396	396	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	547	547	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	547	547	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	675	675	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	1292	1292	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	1436	1436	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	1468	1468	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	1468	1468	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	1469	1471	.	.	.	Note=WGL->GGS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	1478	1479	.	.	.	Note=EQ->DE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	1590	1590	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	1632	1642	.	.	.	Note=NDPSLPNTFKA->TILVYQIRSKP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	1640	1640	.	.	.	Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	1844	1844	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	2202	2202	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	2414	2414	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Sequence conflict	2414	2414	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35169	UniProtKB	Helix	2444	2460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1N	
+##sequence-region P53147 1 276
+P53147	UniProtKB	Chain	1	276	.	.	.	ID=PRO_0000049400;Note=Homeobox protein TOS8	
+P53147	UniProtKB	DNA binding	194	256	.	.	.	Note=Homeobox%3B TALE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108	
+##sequence-region Q12272 1 230
+Q12272	UniProtKB	Chain	1	230	.	.	.	ID=PRO_0000157497;Note=tRNA 2'-phosphotransferase	
+##sequence-region Q06177 1 86
+Q06177	UniProtKB	Chain	1	86	.	.	.	ID=PRO_0000072270;Note=Translation machinery-associated protein 10	
+Q06177	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06177	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q12116 1 473
+Q12116	UniProtKB	Chain	1	473	.	.	.	ID=PRO_0000218972;Note=Membrane protein TMS1	
+Q12116	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Transmembrane	7	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Topological domain	30	38	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Transmembrane	39	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Topological domain	62	81	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Transmembrane	82	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Topological domain	105	118	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Transmembrane	119	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Topological domain	139	144	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Transmembrane	145	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Topological domain	168	194	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Transmembrane	195	217	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Topological domain	218	228	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Transmembrane	229	246	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Topological domain	247	295	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Transmembrane	296	318	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Topological domain	319	398	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Transmembrane	399	421	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Topological domain	422	435	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Transmembrane	436	458	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12116	UniProtKB	Topological domain	459	473	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P13099 1 656
+P13099	UniProtKB	Chain	1	656	.	.	.	ID=PRO_0000145198;Note=DNA topoisomerase 3	
+P13099	UniProtKB	Domain	2	156	.	.	.	Note=Toprim;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995	
+P13099	UniProtKB	Active site	356	356	.	.	.	Note=O-(5'-phospho-DNA)-tyrosine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P49334 1 152
+P49334	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7760834;Dbxref=PMID:7760834	
+P49334	UniProtKB	Chain	2	152	.	.	.	ID=PRO_0000076113;Note=Mitochondrial import receptor subunit TOM22	
+P49334	UniProtKB	Topological domain	2	97	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49334	UniProtKB	Transmembrane	98	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49334	UniProtKB	Topological domain	120	152	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49334	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P49334	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P38288 1 455
+P38288	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38288	UniProtKB	Chain	24	455	.	.	.	ID=PRO_0000022563;Note=Protein TOS1	
+P38288	UniProtKB	Compositional bias	172	273	.	.	.	Note=Ser-rich	
+P38288	UniProtKB	Compositional bias	206	209	.	.	.	Note=Poly-Ala	
+P38288	UniProtKB	Compositional bias	210	217	.	.	.	Note=Poly-Ser	
+P38288	UniProtKB	Glycosylation	236	236	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38288	UniProtKB	Glycosylation	417	417	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43637 1 560
+P43637	UniProtKB	Chain	1	560	.	.	.	ID=PRO_0000086126;Note=Serine/threonine-protein kinase TOS3	
+P43637	UniProtKB	Domain	50	344	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P43637	UniProtKB	Nucleotide binding	56	64	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P43637	UniProtKB	Active site	189	189	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P43637	UniProtKB	Binding site	79	79	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region Q03796 1 238
+Q03796	UniProtKB	Chain	1	238	.	.	.	ID=PRO_0000065580;Note=Polynucleotide 3'-phosphatase	
+##sequence-region P53738 1 135
+P53738	UniProtKB	Chain	1	135	.	.	.	ID=PRO_0000215805;Note=Multifunctional methyltransferase subunit TRM112	
+P53738	UniProtKB	Domain	2	131	.	.	.	Note=TRM112	
+P53738	UniProtKB	Helix	3	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Helix	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Beta strand	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Turn	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Beta strand	33	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Helix	44	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Helix	56	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Helix	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Helix	87	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Beta strand	103	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Turn	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Beta strand	118	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+P53738	UniProtKB	Beta strand	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A	
+##sequence-region P12685 1 1235
+P12685	UniProtKB	Chain	1	1235	.	.	.	ID=PRO_0000070462;Note=High-affinity potassium transport protein	
+P12685	UniProtKB	Transmembrane	49	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Transmembrane	107	127	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Transmembrane	778	800	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Transmembrane	813	834	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Transmembrane	838	858	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Transmembrane	862	882	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Transmembrane	898	918	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Transmembrane	923	943	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Transmembrane	971	991	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Transmembrane	1078	1098	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Transmembrane	1111	1131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12685	UniProtKB	Modified residue	414	414	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P12685	UniProtKB	Modified residue	534	534	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12685	UniProtKB	Glycosylation	100	100	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	169	169	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	222	222	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	227	227	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	251	251	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	369	369	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	383	383	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	497	497	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	501	501	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	532	532	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	580	580	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	677	677	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	919	919	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	1030	1030	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12685	UniProtKB	Glycosylation	1135	1135	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12400 1 293
+Q12400	UniProtKB	Chain	1	293	.	.	.	ID=PRO_0000060520;Note=tRNA (guanine(9)-N1)-methyltransferase	
+Q12400	UniProtKB	Domain	83	279	.	.	.	Note=SAM-dependent MTase TRM10-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01012	
+Q12400	UniProtKB	Region	186	187	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q12400	UniProtKB	Region	210	214	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q12400	UniProtKB	Region	244	246	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q12400	UniProtKB	Coiled coil	32	61	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12400	UniProtKB	Active site	210	210	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582	
+Q12400	UniProtKB	Binding site	206	206	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen	
+Q12400	UniProtKB	Binding site	218	218	.	.	.	Note=S-adenosyl-L-methionine	
+Q12400	UniProtKB	Binding site	232	232	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen	
+Q12400	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12400	UniProtKB	Modified residue	283	283	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12400	UniProtKB	Mutagenesis	118	118	.	.	.	Note=Completely abolishes catalytic activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582	
+Q12400	UniProtKB	Mutagenesis	209	209	.	.	.	Note=Reduces catalytic activity. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582	
+Q12400	UniProtKB	Mutagenesis	210	210	.	.	.	Note=Completely abolishes catalytic activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582	
+Q12400	UniProtKB	Mutagenesis	211	211	.	.	.	Note=Reduces catalytic activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582	
+Q12400	UniProtKB	Mutagenesis	212	212	.	.	.	Note=Has weaker affinity for S-adenosyl-L-methionine and reduces catalytic activity by 90%25. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582	
+Q12400	UniProtKB	Mutagenesis	247	247	.	.	.	Note=Reduces catalytic activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582	
+Q12400	UniProtKB	Beta strand	91	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Helix	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Helix	109	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Beta strand	129	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Helix	142	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Helix	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Helix	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Beta strand	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Beta strand	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Helix	170	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Beta strand	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Helix	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Beta strand	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Beta strand	191	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Beta strand	202	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Helix	217	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Beta strand	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Helix	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Helix	248	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Turn	259	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+Q12400	UniProtKB	Helix	264	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ	
+##sequence-region Q12463 1 433
+Q12463	UniProtKB	Chain	1	433	.	.	.	ID=PRO_0000270922;Note=tRNA (guanine(10)-N2)-methyltransferase	
+Q12463	UniProtKB	Mutagenesis	215	215	.	.	.	Note=Abolishes activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15899842;Dbxref=PMID:15899842	
+Q12463	UniProtKB	Mutagenesis	291	291	.	.	.	Note=Abolishes activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15899842;Dbxref=PMID:15899842	
+##sequence-region P15565 1 570
+P15565	UniProtKB	Domain	43	489	.	.	.	Note=Trm1 methyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00958	
+P15565	UniProtKB	Region	133	155	.	.	.	Note=Required and sufficient for inner nuclear membrane localization	
+P15565	UniProtKB	Motif	95	101	.	.	.	Note=Nuclear localization signal	
+P15565	UniProtKB	Alternative sequence	1	16	.	.	.	ID=VSP_018902;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15565	UniProtKB	Natural variant	203	203	.	.	.	Note=In strain: D4 and YF+. T->S	
+P15565	UniProtKB	Natural variant	467	467	.	.	.	Note=In strain: D4%3B loss of activity. S->L	
+P15565	UniProtKB	Natural variant	517	517	.	.	.	Note=In strain: D4 and YF+. G->R	
+P15565	UniProtKB	Mutagenesis	290	290	.	.	.	Note=Loss of activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10048958;Dbxref=PMID:10048958	
+##sequence-region Q02648 1 567
+Q02648	UniProtKB	Chain	1	567	.	.	.	ID=PRO_0000249911;Note=tRNA (uracil-O(2)-)-methyltransferase	
+Q02648	UniProtKB	Modified residue	107	107	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P41814 1 478
+P41814	UniProtKB	Chain	1	478	.	.	.	ID=PRO_0000123558;Note=tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6	
+P41814	UniProtKB	Turn	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	12	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	22	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	43	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	53	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	82	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	189	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	198	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Turn	211	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	219	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	236	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	243	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	246	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	267	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	280	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	289	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	296	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	301	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	310	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	322	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5ERG	
+P41814	UniProtKB	Helix	330	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	361	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	369	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	373	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	385	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Helix	393	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	409	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P41814	UniProtKB	Beta strand	441	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+##sequence-region Q08687 1 178
+Q08687	UniProtKB	Chain	1	178	.	.	.	ID=PRO_0000237637;Note=Translation machinery-associated protein 16	
+Q08687	UniProtKB	Helix	55	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM	
+Q08687	UniProtKB	Turn	71	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM	
+Q08687	UniProtKB	Helix	81	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM	
+Q08687	UniProtKB	Helix	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM	
+Q08687	UniProtKB	Helix	115	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM	
+Q08687	UniProtKB	Beta strand	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM	
+Q08687	UniProtKB	Helix	142	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM	
+Q08687	UniProtKB	Helix	157	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM	
+Q08687	UniProtKB	Beta strand	163	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM	
+Q08687	UniProtKB	Turn	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM	
+##sequence-region Q3E764 1 64
+Q3E764	UniProtKB	Chain	1	64	.	.	.	ID=PRO_0000247142;Note=Translation machinery-associated protein 7	
+##sequence-region P32643 1 299
+P32643	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32643	UniProtKB	Chain	2	299	.	.	.	ID=PRO_0000202658;Note=Trans-aconitate 3-methyltransferase	
+P32643	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32643	UniProtKB	Helix	2	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	11	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	23	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Beta strand	38	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Turn	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	49	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Beta strand	62	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	71	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Turn	85	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Beta strand	91	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Turn	106	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Beta strand	114	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	128	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Beta strand	139	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	164	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Turn	172	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	183	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Turn	189	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Turn	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Beta strand	201	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	211	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	217	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Beta strand	231	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	236	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	247	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Helix	264	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+P32643	UniProtKB	Beta strand	285	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T	
+##sequence-region P32600 1 2474
+P32600	UniProtKB	Chain	1	2474	.	.	.	ID=PRO_0000088815;Note=Serine/threonine-protein kinase TOR2	
+P32600	UniProtKB	Repeat	588	626	.	.	.	Note=HEAT 1	
+P32600	UniProtKB	Repeat	636	674	.	.	.	Note=HEAT 2	
+P32600	UniProtKB	Repeat	676	710	.	.	.	Note=HEAT 3	
+P32600	UniProtKB	Repeat	756	793	.	.	.	Note=HEAT 4	
+P32600	UniProtKB	Repeat	797	835	.	.	.	Note=HEAT 5	
+P32600	UniProtKB	Repeat	841	879	.	.	.	Note=HEAT 6	
+P32600	UniProtKB	Repeat	917	955	.	.	.	Note=HEAT 7	
+P32600	UniProtKB	Repeat	1039	1076	.	.	.	Note=HEAT 8	
+P32600	UniProtKB	Repeat	1079	1116	.	.	.	Note=HEAT 9	
+P32600	UniProtKB	Repeat	1118	1155	.	.	.	Note=HEAT 10	
+P32600	UniProtKB	Repeat	1292	1331	.	.	.	Note=HEAT 11	
+P32600	UniProtKB	Domain	1338	1922	.	.	.	Note=FAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534	
+P32600	UniProtKB	Domain	2123	2441	.	.	.	Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269	
+P32600	UniProtKB	Domain	2442	2474	.	.	.	Note=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535	
+P32600	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32600	UniProtKB	Mutagenesis	1975	1975	.	.	.	Note=In TOR2-1%3B confers resistance to rapamycin. S->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8846782;Dbxref=PMID:8846782	
+P32600	UniProtKB	Mutagenesis	2129	2129	.	.	.	Note=Causes defect in receptor endocytosis. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14593073;Dbxref=PMID:14593073	
+P32600	UniProtKB	Mutagenesis	2279	2279	.	.	.	Note=Loss of function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8846782;Dbxref=PMID:8846782	
+P32600	UniProtKB	Mutagenesis	2298	2298	.	.	.	Note=Loss of kinase activity. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732	
+P32600	UniProtKB	Sequence conflict	1473	1473	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P17536 1 199
+P17536	UniProtKB	Chain	1	199	.	.	.	ID=PRO_0000205692;Note=Tropomyosin-1	
+P17536	UniProtKB	Coiled coil	1	199	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17536	UniProtKB	Modified residue	195	195	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P17536	UniProtKB	Cross-link	39	39	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P17536	UniProtKB	Cross-link	59	59	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P17536	UniProtKB	Cross-link	187	187	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P53099 1 579
+P53099	UniProtKB	Chain	1	579	.	.	.	ID=PRO_0000197929;Note=Vitamin B6 transporter TPN1	
+P53099	UniProtKB	Topological domain	1	98	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	120	122	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	144	157	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	158	178	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	179	198	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	220	221	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	222	242	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	243	274	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	275	295	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	296	302	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	303	323	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	324	362	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	363	383	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	384	394	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	395	415	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	416	421	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	422	442	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	443	519	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	520	540	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	541	545	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Transmembrane	546	566	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53099	UniProtKB	Topological domain	567	579	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53283 1 614
+P53283	UniProtKB	Chain	1	614	.	.	.	ID=PRO_0000173439;Note=Polyamine transporter 2	
+P53283	UniProtKB	Topological domain	1	173	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	195	206	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	207	227	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	228	236	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	237	257	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	258	266	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	288	297	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	298	318	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	319	326	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	327	347	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	348	407	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	408	428	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	429	437	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	438	458	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	459	478	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	479	499	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	500	503	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	504	524	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	525	541	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	542	562	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	563	574	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Transmembrane	575	595	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Topological domain	596	614	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53283	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q12256 1 659
+Q12256	UniProtKB	Chain	1	659	.	.	.	ID=PRO_0000262732;Note=Polyamine transporter 4	
+Q12256	UniProtKB	Topological domain	1	99	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	121	128	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	129	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	150	157	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	158	178	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	179	187	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	209	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	237	246	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	247	267	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	268	316	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	317	337	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	338	355	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	356	376	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	377	423	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	424	444	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	445	456	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	457	477	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	478	486	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	487	509	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	510	518	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Transmembrane	519	539	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Topological domain	540	659	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12256	UniProtKB	Modified residue	589	589	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12256	UniProtKB	Modified residue	606	606	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12256	UniProtKB	Modified residue	608	608	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12256	UniProtKB	Modified residue	633	633	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12256	UniProtKB	Modified residue	646	646	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q03496 1 1420
+Q03496	UniProtKB	Chain	1	1420	.	.	.	ID=PRO_0000203343;Note=tRNA (cytidine(32)-2'-O)-methyltransferase non-catalytic subunit TRM732	
+##sequence-region Q05024 1 226
+Q05024	UniProtKB	Chain	1	226	.	.	.	ID=PRO_0000203334;Note=Protein TRI1	
+Q05024	UniProtKB	Compositional bias	103	110	.	.	.	Note=Poly-Lys	
+Q05024	UniProtKB	Modified residue	113	113	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05024	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q05024	UniProtKB	Cross-link	201	201	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
+Q05024	UniProtKB	Cross-link	215	215	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
+Q05024	UniProtKB	Mutagenesis	201	201	.	.	.	Note=Impairs sumoylation%3B when associated with R-215. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17603101;Dbxref=PMID:17603101	
+Q05024	UniProtKB	Mutagenesis	215	215	.	.	.	Note=Impairs sumoylation%3B when associated with R-201. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17603101;Dbxref=PMID:17603101	
+##sequence-region P33753 1 639
+P33753	UniProtKB	Chain	1	639	.	.	.	ID=PRO_0000162059;Note=tRNA (uracil(54)-C(5))-methyltransferase	
+P33753	UniProtKB	Domain	163	228	.	.	.	Note=TRAM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00208	
+P33753	UniProtKB	Compositional bias	5	12	.	.	.	Note=Poly-Phe	
+P33753	UniProtKB	Active site	591	591	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01024	
+P33753	UniProtKB	Active site	631	631	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10015	
+P33753	UniProtKB	Binding site	461	461	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01024	
+P33753	UniProtKB	Binding site	496	496	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01024	
+P33753	UniProtKB	Binding site	517	517	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01024	
+P33753	UniProtKB	Binding site	564	564	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01024	
+P33753	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P33753	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P33753	UniProtKB	Mutagenesis	498	498	.	.	.	Note=Unable to methylate tRNA. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12003492;Dbxref=PMID:12003492	
+P33753	UniProtKB	Mutagenesis	591	591	.	.	.	Note=Unable to methylate tRNA. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12003492;Dbxref=PMID:12003492	
+P33753	UniProtKB	Sequence conflict	24	24	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38793 1 499
+P38793	UniProtKB	Transit peptide	1	44	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03152	
+P38793	UniProtKB	Chain	45	499	.	.	.	ID=PRO_0000202899;Note=tRNA (guanine(37)-N1)-methyltransferase	
+P38793	UniProtKB	Region	307	308	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03152	
+P38793	UniProtKB	Region	335	336	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03152	
+P38793	UniProtKB	Binding site	268	268	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03152	
+P38793	UniProtKB	Binding site	399	399	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03152	
+P38793	UniProtKB	Mutagenesis	1	33	.	.	.	Note=Abolishes mitochondrial localization and activity%2C but not cytoplasmic activity of the enzyme. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17652090;Dbxref=PMID:17652090	
+##sequence-region P09880 1 827
+P09880	UniProtKB	Chain	1	827	.	.	.	ID=PRO_0000065635;Note=tRNA ligase	
+P09880	UniProtKB	Active site	114	114	.	.	.	Note=N6-AMP-lysine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2207062;Dbxref=PMID:2207062	
+##sequence-region P46944 1 698
+P46944	UniProtKB	Chain	1	698	.	.	.	ID=PRO_0000065642;Note=Trafficking protein particle complex III-specific subunit 85	
+P46944	UniProtKB	Sequence conflict	277	277	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P22217 1 103
+P22217	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7961686;Dbxref=PMID:7961686	
+P22217	UniProtKB	Chain	2	103	.	.	.	ID=PRO_0000120044;Note=Thioredoxin-1	
+P22217	UniProtKB	Domain	2	103	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P22217	UniProtKB	Active site	30	30	.	.	.	Note=Nucleophile	
+P22217	UniProtKB	Active site	33	33	.	.	.	Note=Nucleophile	
+P22217	UniProtKB	Site	24	24	.	.	.	Note=Deprotonates C-terminal active site Cys	
+P22217	UniProtKB	Site	31	31	.	.	.	Note=Contributes to redox potential value	
+P22217	UniProtKB	Site	32	32	.	.	.	Note=Contributes to redox potential value	
+P22217	UniProtKB	Disulfide bond	30	33	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00691,ECO:0000269|PubMed:19362171;Dbxref=PMID:19362171	
+P22217	UniProtKB	Cross-link	54	54	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P22217	UniProtKB	Cross-link	66	66	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P22217	UniProtKB	Cross-link	96	96	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P22217	UniProtKB	Beta strand	2	4	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3R	
+P22217	UniProtKB	Helix	8	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q	
+P22217	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q	
+P22217	UniProtKB	Beta strand	21	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q	
+P22217	UniProtKB	Helix	31	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q	
+P22217	UniProtKB	Beta strand	50	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q	
+P22217	UniProtKB	Turn	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q	
+P22217	UniProtKB	Helix	61	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q	
+P22217	UniProtKB	Beta strand	71	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q	
+P22217	UniProtKB	Beta strand	82	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q	
+P22217	UniProtKB	Helix	92	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q	
+##sequence-region P34760 1 196
+P34760	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8344960;Dbxref=PMID:8344960	
+P34760	UniProtKB	Chain	2	196	.	.	.	ID=PRO_0000135095;Note=Peroxiredoxin TSA1	
+P34760	UniProtKB	Domain	3	161	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P34760	UniProtKB	Region	45	47	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SBC,ECO:0000269|PubMed:22985967;Dbxref=PMID:22985967	
+P34760	UniProtKB	Active site	48	48	.	.	.	Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8041739;Dbxref=PMID:8041739	
+P34760	UniProtKB	Binding site	124	124	.	.	.	Note=Substrate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SBC,ECO:0000269|PubMed:22985967;Dbxref=PMID:22985967	
+P34760	UniProtKB	Site	45	45	.	.	.	Note=Important for catalytic activity%2C helps activating the peroxidatic cysteine through H-bonding	
+P34760	UniProtKB	Modified residue	174	174	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P34760	UniProtKB	Disulfide bond	48	48	.	.	.	Note=Interchain (with C-171)%3B in linked form;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7961686;Dbxref=PMID:7961686	
+P34760	UniProtKB	Disulfide bond	48	48	.	.	.	Note=Interchain (with C-84 in SRX1)%3B transient;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14586471;Dbxref=PMID:14586471	
+P34760	UniProtKB	Disulfide bond	171	171	.	.	.	Note=Interchain (with C-48)%3B in linked form;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7961686;Dbxref=PMID:7961686	
+P34760	UniProtKB	Cross-link	14	14	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P34760	UniProtKB	Cross-link	89	89	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P34760	UniProtKB	Cross-link	132	132	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P34760	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Exists mainly as monomer. Has no peroxiredoxin activity. Fails to protect glutamine synthetase against damage by DTT oxidation. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7961686,ECO:0000269|PubMed:8041739;Dbxref=PMID:7961686,PMID:8041739	
+P34760	UniProtKB	Mutagenesis	171	171	.	.	.	Note=Exists mainly as monomer. Has no peroxiredoxin activity. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7961686,ECO:0000269|PubMed:8041739;Dbxref=PMID:7961686,PMID:8041739	
+P34760	UniProtKB	Beta strand	14	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Beta strand	21	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Helix	27	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Beta strand	33	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Helix	47	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Beta strand	67	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Helix	77	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Helix	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Helix	107	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Turn	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Beta strand	124	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Beta strand	133	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Helix	149	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Turn	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+P34760	UniProtKB	Helix	187	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC	
+##sequence-region P40061 1 1430
+P40061	UniProtKB	Chain	1	1430	.	.	.	ID=PRO_0000202640;Note=Target of rapamycin complex 2 subunit TSC11	
+P40061	UniProtKB	Domain	995	1100	.	.	.	Note=N-terminal Ras-GEF	
+P40061	UniProtKB	Coiled coil	91	180	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40061	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40061	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40061	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40061	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40061	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q02776 1 476
+Q02776	UniProtKB	Transit peptide	1	43	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12437924,ECO:0000305|PubMed:12437925;Dbxref=PMID:12437924,PMID:12437925	
+Q02776	UniProtKB	Chain	44	476	.	.	.	ID=PRO_0000043139;Note=Mitochondrial import inner membrane translocase subunit TIM50	
+Q02776	UniProtKB	Topological domain	44	114	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02776	UniProtKB	Transmembrane	115	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02776	UniProtKB	Topological domain	132	476	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02776	UniProtKB	Domain	187	330	.	.	.	Note=FCP1 homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00336	
+Q02776	UniProtKB	Turn	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Beta strand	191	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Turn	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Beta strand	203	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Beta strand	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Beta strand	213	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	221	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Turn	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Beta strand	232	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	242	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Turn	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Beta strand	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	265	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Beta strand	268	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Beta strand	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Beta strand	289	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	296	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Beta strand	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	324	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	339	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	348	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+Q02776	UniProtKB	Helix	351	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF	
+##sequence-region P40552 1 269
+P40552	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40552	UniProtKB	Chain	23	245	.	.	.	ID=PRO_0000033236;Note=Cell wall protein TIR3	
+P40552	UniProtKB	Propeptide	246	269	.	.	.	ID=PRO_0000372446;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40552	UniProtKB	Compositional bias	126	269	.	.	.	Note=Ala/Ser-rich	
+P40552	UniProtKB	Lipidation	245	245	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40552	UniProtKB	Glycosylation	234	234	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12000 1 345
+Q12000	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000237638;Note=Translation machinery-associated protein 46	
+Q12000	UniProtKB	Zinc finger	87	114	.	.	.	Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q12000	UniProtKB	Zinc finger	158	196	.	.	.	Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q12000	UniProtKB	Modified residue	301	301	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12000	UniProtKB	Helix	222	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+Q12000	UniProtKB	Helix	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+Q12000	UniProtKB	Helix	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+Q12000	UniProtKB	Helix	243	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+Q12000	UniProtKB	Helix	272	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+Q12000	UniProtKB	Helix	306	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+Q12000	UniProtKB	Helix	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+Q12000	UniProtKB	Beta strand	323	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+Q12000	UniProtKB	Beta strand	329	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+##sequence-region Q06266 1 489
+Q06266	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000262748;Note=Protein TOS4	
+Q06266	UniProtKB	Domain	118	170	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+Q06266	UniProtKB	Compositional bias	181	184	.	.	.	Note=Poly-Asn	
+Q06266	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06266	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q07824 1 586
+Q07824	UniProtKB	Chain	1	586	.	.	.	ID=PRO_0000262730;Note=Polyamine transporter 1	
+Q07824	UniProtKB	Topological domain	1	145	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	167	181	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	203	212	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	213	233	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	234	242	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	264	271	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	272	292	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	293	301	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	302	322	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	323	376	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	377	397	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	398	414	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	415	435	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	436	454	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	455	475	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	476	483	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	484	504	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	505	505	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	506	526	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	527	528	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	529	549	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Transmembrane	550	570	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Topological domain	571	586	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07824	UniProtKB	Compositional bias	17	25	.	.	.	Note=Poly-Ser	
+Q07824	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075	
+Q07824	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphothreonine%3B by CK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075	
+Q07824	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q07824	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q07824	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q07824	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q07824	UniProtKB	Modified residue	342	342	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075	
+Q07824	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Reduces transport activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075	
+Q07824	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Enhances transport activity. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075	
+Q07824	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Reduces transport activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075	
+Q07824	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Enhances transport activity. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075	
+Q07824	UniProtKB	Mutagenesis	207	207	.	.	.	Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171066;Dbxref=PMID:11171066	
+Q07824	UniProtKB	Mutagenesis	323	323	.	.	.	Note=Loss of function%3B when associated with Q-324. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171066;Dbxref=PMID:11171066	
+Q07824	UniProtKB	Mutagenesis	324	324	.	.	.	Note=Loss of function%3B when associated with Q-323. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171066;Dbxref=PMID:11171066	
+Q07824	UniProtKB	Mutagenesis	342	342	.	.	.	Note=Interferes with correct plasma membrane localization. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075	
+Q07824	UniProtKB	Mutagenesis	342	342	.	.	.	Note=Enhances transport activity. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075	
+Q07824	UniProtKB	Mutagenesis	574	574	.	.	.	Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171066;Dbxref=PMID:11171066	
+##sequence-region P47045 1 478
+P47045	UniProtKB	Chain	1	478	.	.	.	ID=PRO_0000203062;Note=Mitochondrial import inner membrane translocase subunit TIM54	
+P47045	UniProtKB	Topological domain	1	32	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47045	UniProtKB	Transmembrane	33	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47045	UniProtKB	Topological domain	50	478	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12199 1 356
+Q12199	UniProtKB	Chain	1	356	.	.	.	ID=PRO_0000247903;Note=Type 2A phosphatase activator TIP41	
+Q12199	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P23254 1 680
+P23254	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1812485;Dbxref=PMID:1812485	
+P23254	UniProtKB	Chain	2	680	.	.	.	ID=PRO_0000191904;Note=Transketolase 1	
+P23254	UniProtKB	Nucleotide binding	116	118	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292	
+P23254	UniProtKB	Active site	418	418	.	.	.	Note=Proton donor;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23254	UniProtKB	Metal binding	157	157	.	.	.	Note=Magnesium	
+P23254	UniProtKB	Metal binding	187	187	.	.	.	Note=Magnesium	
+P23254	UniProtKB	Metal binding	189	189	.	.	.	Note=Magnesium%3B via carbonyl oxygen	
+P23254	UniProtKB	Binding site	30	30	.	.	.	Note=Substrate	
+P23254	UniProtKB	Binding site	69	69	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292	
+P23254	UniProtKB	Binding site	158	158	.	.	.	Note=Thiamine pyrophosphate%3B via amide nitrogen;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292	
+P23254	UniProtKB	Binding site	187	187	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292	
+P23254	UniProtKB	Binding site	263	263	.	.	.	Note=Substrate	
+P23254	UniProtKB	Binding site	263	263	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292	
+P23254	UniProtKB	Binding site	359	359	.	.	.	Note=Substrate	
+P23254	UniProtKB	Binding site	386	386	.	.	.	Note=Substrate	
+P23254	UniProtKB	Binding site	418	418	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292	
+P23254	UniProtKB	Binding site	445	445	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292	
+P23254	UniProtKB	Binding site	469	469	.	.	.	Note=Substrate	
+P23254	UniProtKB	Binding site	477	477	.	.	.	Note=Substrate	
+P23254	UniProtKB	Binding site	528	528	.	.	.	Note=Substrate	
+P23254	UniProtKB	Site	30	30	.	.	.	Note=Important for catalytic activity	
+P23254	UniProtKB	Site	263	263	.	.	.	Note=Important for catalytic activity	
+P23254	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23254	UniProtKB	Modified residue	335	335	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23254	UniProtKB	Modified residue	402	402	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P23254	UniProtKB	Modified residue	492	492	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P23254	UniProtKB	Cross-link	647	647	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P23254	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Strongly reduced catalytic activity. Decreases affinity for xylulose 5-phosphate about 15 times. H->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9398292;Dbxref=PMID:9398292	
+P23254	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Loss of activity. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9398292;Dbxref=PMID:9398292	
+P23254	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Reduces catalytic activity by about 98%25. Decreased affinity for donor substrate. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9398292;Dbxref=PMID:9398292	
+P23254	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Reduces activity by over 96%25 and decreases affinity for thiamine pyrophosphate and xylulose 5-phosphate. H->A%2CN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8521838,ECO:0000269|PubMed:9398292;Dbxref=PMID:8521838,PMID:9398292	
+P23254	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Loss of activity. H->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8521838,ECO:0000269|PubMed:9398292;Dbxref=PMID:8521838,PMID:9398292	
+P23254	UniProtKB	Mutagenesis	162	162	.	.	.	Note=Most catalytic properties similar to wild-type. E->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9119035;Dbxref=PMID:9119035	
+P23254	UniProtKB	Mutagenesis	263	263	.	.	.	Note=Strongly reduced catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9398292;Dbxref=PMID:9398292	
+P23254	UniProtKB	Mutagenesis	359	359	.	.	.	Note=Slightly reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8999873;Dbxref=PMID:8999873	
+P23254	UniProtKB	Mutagenesis	382	382	.	.	.	Note=Severe loss of activity. D->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9119035;Dbxref=PMID:9119035	
+P23254	UniProtKB	Mutagenesis	469	469	.	.	.	Note=Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8999873;Dbxref=PMID:8999873	
+P23254	UniProtKB	Mutagenesis	477	477	.	.	.	Note=Strongly reduced catalytic activity. Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8999873;Dbxref=PMID:8999873	
+P23254	UniProtKB	Mutagenesis	481	481	.	.	.	Note=Reduces catalytic activity by about 95%25. H->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9398292;Dbxref=PMID:9398292	
+P23254	UniProtKB	Mutagenesis	528	528	.	.	.	Note=Reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8999873;Dbxref=PMID:8999873	
+P23254	UniProtKB	Sequence conflict	37	38	.	.	.	Note=MA->RS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23254	UniProtKB	Sequence conflict	45	77	.	.	.	Note=WSQMRMNPTNPDWINRDRFVLSNGHAVALLYSM->GESNAHEPNQPKTGSTEIDLSCLTVTRSLCCIY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23254	UniProtKB	Sequence conflict	136	143	.	.	.	Note=AATYNKPG->DMPLTTSRA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23254	UniProtKB	Sequence conflict	232	234	.	.	.	Note=AQA->RQR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23254	UniProtKB	Sequence conflict	243	257	.	.	.	Note=LIKMTTTIGYGSLHA->FDQNDHNHWLRFLRS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23254	UniProtKB	Sequence conflict	383	383	.	.	.	Note=L->LVLPIL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23254	UniProtKB	Sequence conflict	396	396	.	.	.	Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23254	UniProtKB	Sequence conflict	528	538	.	.	.	Note=RQNLPQLEGSS->PDKTCHNWKVAL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23254	UniProtKB	Sequence conflict	639	680	.	.	.	Note=SGKAPEVFKFFGFTPEGVAERAQKTIAFYKGDKLISPLKKAF->PVRHQKSSSSSVSPQKVLLKELKRPLHSIRVTS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23254	UniProtKB	Helix	6	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	32	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	62	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	71	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Turn	91	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	120	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	151	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	157	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	163	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	180	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	191	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKB	
+P23254	UniProtKB	Helix	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	203	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	213	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Turn	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	224	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	242	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Turn	250	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Turn	255	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	263	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	269	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	291	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	302	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	324	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	342	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	358	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Turn	370	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	376	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	384	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	402	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	411	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	418	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	436	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	443	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	447	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	450	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	464	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	472	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Turn	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	486	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	493	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	497	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	504	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	522	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	528	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TRK	
+P23254	UniProtKB	Helix	539	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	547	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	556	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	565	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Turn	578	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	583	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	591	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	599	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	608	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	612	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	623	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Beta strand	628	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	642	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+P23254	UniProtKB	Helix	653	667	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU	
+##sequence-region Q03322 1 224
+Q03322	UniProtKB	Chain	1	224	.	.	.	ID=PRO_0000210277;Note=T-SNARE affecting a late Golgi compartment protein 1	
+Q03322	UniProtKB	Topological domain	1	203	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03322	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03322	UniProtKB	Domain	132	194	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+Q03322	UniProtKB	Region	1	106	.	.	.	Note=Interaction with VPS51;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12377769;Dbxref=PMID:12377769	
+Q03322	UniProtKB	Coiled coil	35	101	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03322	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphothreonine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12006655;Dbxref=PMID:12006655	
+Q03322	UniProtKB	Lipidation	205	205	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15973437;Dbxref=PMID:15973437	
+Q03322	UniProtKB	Lipidation	206	206	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15973437;Dbxref=PMID:15973437	
+Q03322	UniProtKB	Cross-link	183	183	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q03322	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Results in an aktivated t-SNARE that confers endocytosis%2C but not exocytosis. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12006655;Dbxref=PMID:12006655	
+Q03322	UniProtKB	Mutagenesis	205	206	.	.	.	Note=Not palmitoylated%2C rapidly degraded in a TUL1-dependent manner. CC->SS%2CLL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15973437;Dbxref=PMID:15973437	
+Q03322	UniProtKB	Helix	7	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5K	
+Q03322	UniProtKB	Helix	38	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5K	
+Q03322	UniProtKB	Helix	71	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5K	
+##sequence-region P53322 1 534
+P53322	UniProtKB	Chain	1	534	.	.	.	ID=PRO_0000121369;Note=High-affinity nicotinic acid transporter	
+P53322	UniProtKB	Topological domain	1	130	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Topological domain	152	152	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Topological domain	174	187	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Topological domain	209	217	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Transmembrane	218	238	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Topological domain	239	250	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Transmembrane	251	271	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Topological domain	272	323	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Transmembrane	324	344	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Topological domain	345	355	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Transmembrane	356	376	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Topological domain	377	384	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Transmembrane	385	405	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Topological domain	406	410	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Transmembrane	411	431	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Topological domain	432	444	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Transmembrane	445	465	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Topological domain	466	474	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Transmembrane	475	495	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Topological domain	496	534	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53322	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53322	UniProtKB	Cross-link	283	283	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region Q08919 1 783
+Q08919	UniProtKB	Chain	1	783	.	.	.	ID=PRO_0000238622;Note=Uncharacterized protein TRE1	
+Q08919	UniProtKB	Topological domain	1	109	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08919	UniProtKB	Transmembrane	110	127	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08919	UniProtKB	Topological domain	128	783	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08919	UniProtKB	Domain	241	333	.	.	.	Note=PA	
+Q08919	UniProtKB	Glycosylation	139	139	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08919	UniProtKB	Glycosylation	213	213	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08919	UniProtKB	Glycosylation	529	529	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03774 1 444
+Q03774	UniProtKB	Chain	1	444	.	.	.	ID=PRO_0000051295;Note=tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit TRM82	
+Q03774	UniProtKB	Repeat	1	47	.	.	.	Note=WD 1	
+Q03774	UniProtKB	Repeat	48	99	.	.	.	Note=WD 2	
+Q03774	UniProtKB	Repeat	100	147	.	.	.	Note=WD 3	
+Q03774	UniProtKB	Repeat	148	192	.	.	.	Note=WD 4	
+Q03774	UniProtKB	Repeat	193	237	.	.	.	Note=WD 5	
+Q03774	UniProtKB	Repeat	238	279	.	.	.	Note=WD 6	
+Q03774	UniProtKB	Repeat	308	354	.	.	.	Note=WD 7	
+Q03774	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03774	UniProtKB	Beta strand	9	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	14	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	26	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Turn	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	37	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	105	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	114	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Helix	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	126	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	134	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	140	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	152	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	161	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	171	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	191	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	198	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	211	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	222	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	233	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	244	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	254	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Turn	269	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	274	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Helix	281	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Helix	285	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	310	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	317	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	330	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	339	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	345	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	357	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	366	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	383	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Turn	391	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Beta strand	395	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Helix	400	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Turn	418	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q03774	UniProtKB	Helix	424	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+##sequence-region P38334 1 175
+P38334	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000211568;Note=Trafficking protein particle complex subunit 20	
+##sequence-region P32893 1 560
+P32893	UniProtKB	Chain	1	560	.	.	.	ID=PRO_0000084328;Note=Trafficking protein particle complex II-specific subunit 65	
+P32893	UniProtKB	Modified residue	393	393	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32893	UniProtKB	Modified residue	398	398	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q02208 1 771
+Q02208	UniProtKB	Chain	1	771	.	.	.	ID=PRO_0000072621;Note=Topoisomerase 1-associated factor 2	
+Q02208	UniProtKB	Modified residue	397	397	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02208	UniProtKB	Modified residue	405	405	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02208	UniProtKB	Helix	503	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HOI	
+##sequence-region P07213 1 617
+P07213	UniProtKB	Chain	1	617	.	.	.	ID=PRO_0000106340;Note=Mitochondrial import receptor subunit TOM70	
+P07213	UniProtKB	Topological domain	1	10	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07213	UniProtKB	Transmembrane	11	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07213	UniProtKB	Topological domain	31	617	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07213	UniProtKB	Repeat	99	132	.	.	.	Note=TPR 1	
+P07213	UniProtKB	Repeat	134	165	.	.	.	Note=TPR 2	
+P07213	UniProtKB	Repeat	281	315	.	.	.	Note=TPR 3	
+P07213	UniProtKB	Repeat	363	396	.	.	.	Note=TPR 4	
+P07213	UniProtKB	Repeat	397	430	.	.	.	Note=TPR 5	
+P07213	UniProtKB	Repeat	432	464	.	.	.	Note=TPR 6	
+P07213	UniProtKB	Repeat	465	498	.	.	.	Note=TPR 7	
+P07213	UniProtKB	Repeat	505	541	.	.	.	Note=TPR 8	
+P07213	UniProtKB	Repeat	542	575	.	.	.	Note=TPR 9	
+P07213	UniProtKB	Modified residue	174	174	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P07213	UniProtKB	Natural variant	30	30	.	.	.	Note=In strain: SK1%2C V1-09%2C YJM339 and YJM627. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P07213	UniProtKB	Natural variant	68	68	.	.	.	Note=In strain: V1-09 and YJM627. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P07213	UniProtKB	Natural variant	277	277	.	.	.	Note=In strain: YJM1129. N->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P07213	UniProtKB	Natural variant	359	359	.	.	.	Note=In strain: SK1. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P07213	UniProtKB	Natural variant	364	364	.	.	.	Note=In strain: YJM269 and YJM270. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P07213	UniProtKB	Natural variant	385	385	.	.	.	Note=In strain: YJM1129. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P07213	UniProtKB	Natural variant	429	429	.	.	.	Note=In ytrain: V1-09. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P07213	UniProtKB	Sequence conflict	185	185	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07213	UniProtKB	Helix	95	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	115	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	132	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	148	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	166	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	182	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Beta strand	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	204	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	254	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	278	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	297	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Turn	316	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	323	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	346	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	363	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	382	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	385	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	398	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	415	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	432	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Turn	441	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	447	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	466	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	481	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Beta strand	498	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	506	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	523	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	542	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	558	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	575	594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+P07213	UniProtKB	Helix	598	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1	
+##sequence-region P48560 1 102
+P48560	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48560	UniProtKB	Chain	19	80	.	.	.	ID=PRO_0000203371;Note=Protein TOS6	
+P48560	UniProtKB	Propeptide	81	102	.	.	.	ID=PRO_0000372450;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48560	UniProtKB	Compositional bias	21	77	.	.	.	Note=Thr-rich	
+P48560	UniProtKB	Lipidation	80	80	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48560	UniProtKB	Glycosylation	69	69	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P00942 1 248
+P00942	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7005233;Dbxref=PMID:7005233	
+P00942	UniProtKB	Chain	2	248	.	.	.	ID=PRO_0000090169;Note=Triosephosphate isomerase	
+P00942	UniProtKB	Active site	95	95	.	.	.	Note=Electrophile	
+P00942	UniProtKB	Active site	165	165	.	.	.	Note=Proton acceptor	
+P00942	UniProtKB	Binding site	10	10	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12509510;Dbxref=PMID:12509510	
+P00942	UniProtKB	Binding site	12	12	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12509510;Dbxref=PMID:12509510	
+P00942	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00942	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P00942	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P00942	UniProtKB	Cross-link	223	223	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00942	UniProtKB	Beta strand	5	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	17	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Beta strand	36	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	47	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Beta strand	59	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	80	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Beta strand	90	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	96	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	106	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Beta strand	122	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	131	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	139	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Beta strand	160	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Turn	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	178	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	198	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Beta strand	206	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Turn	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	217	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Beta strand	228	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	233	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Helix	239	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+P00942	UniProtKB	Turn	245	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY	
+##sequence-region P40414 1 161
+P40414	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000205693;Note=Tropomyosin-2	
+P40414	UniProtKB	Coiled coil	1	161	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40414	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40414	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40414	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q06451 1 622
+Q06451	UniProtKB	Chain	1	622	.	.	.	ID=PRO_0000262731;Note=Polyamine transporter 3	
+Q06451	UniProtKB	Topological domain	1	182	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	204	215	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	237	245	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	246	266	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	267	275	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	276	296	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	297	305	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	306	326	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	327	335	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	336	356	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	357	416	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	417	437	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	438	446	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	447	467	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	468	487	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	488	508	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	509	512	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	513	533	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	534	550	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	551	571	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	572	583	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Transmembrane	584	604	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Topological domain	605	622	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06451	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06451	UniProtKB	Modified residue	98	98	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06451	UniProtKB	Modified residue	101	101	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06451	UniProtKB	Modified residue	132	132	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P36029 1 618
+P36029	UniProtKB	Chain	1	618	.	.	.	ID=PRO_0000054165;Note=Polyamine transporter TPO5	
+P36029	UniProtKB	Topological domain	1	60	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	61	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	85	90	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	91	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	111	131	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	132	148	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	149	154	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	155	171	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	172	179	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	180	200	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	201	211	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	212	231	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	232	297	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	298	317	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	318	342	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	343	367	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	368	402	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	403	419	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	420	425	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	426	449	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	450	464	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	465	486	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	487	498	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Transmembrane	499	516	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Topological domain	517	618	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36029	UniProtKB	Modified residue	569	569	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q04183 1 1289
+Q04183	UniProtKB	Chain	1	1289	.	.	.	ID=PRO_0000076355;Note=Trafficking protein particle complex II-specific subunit 120	
+Q04183	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04183	UniProtKB	Modified residue	387	387	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04183	UniProtKB	Sequence conflict	435	435	.	.	.	Note=A->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03660 1 1102
+Q03660	UniProtKB	Chain	1	1102	.	.	.	ID=PRO_0000193512;Note=Trafficking protein particle complex II-specific subunit 130	
+##sequence-region P38342 1 320
+P38342	UniProtKB	Chain	1	320	.	.	.	ID=PRO_0000054800;Note=3-ketodihydrosphingosine reductase TSC10	
+P38342	UniProtKB	Transmembrane	280	300	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38342	UniProtKB	Nucleotide binding	11	37	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38342	UniProtKB	Active site	180	180	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38342	UniProtKB	Active site	184	184	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38342	UniProtKB	Binding site	167	167	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38342	UniProtKB	Sequence conflict	255	255	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38342	UniProtKB	Sequence conflict	255	255	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38427 1 1098
+P38427	UniProtKB	Chain	1	1098	.	.	.	ID=PRO_0000122511;Note=Trehalose synthase complex regulatory subunit TSL1	
+P38427	UniProtKB	Repeat	144	150	.	.	.	Note=1	
+P38427	UniProtKB	Repeat	158	164	.	.	.	Note=2	
+P38427	UniProtKB	Region	144	164	.	.	.	Note=2 X 7 AA repeats of R-I-A-S-P-I-Q	
+P38427	UniProtKB	Region	320	812	.	.	.	Note=TPS complex domain	
+P38427	UniProtKB	Compositional bias	42	45	.	.	.	Note=Poly-Gln	
+P38427	UniProtKB	Compositional bias	164	168	.	.	.	Note=Poly-Gln	
+P38427	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38427	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38427	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38427	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38427	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38427	UniProtKB	Modified residue	135	135	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38427	UniProtKB	Modified residue	147	147	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38427	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38427	UniProtKB	Modified residue	229	229	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38427	UniProtKB	Modified residue	251	251	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38427	UniProtKB	Modified residue	303	303	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38427	UniProtKB	Modified residue	815	815	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P50078 1 622
+P50078	UniProtKB	Chain	1	622	.	.	.	ID=PRO_0000072633;Note=Protein TOS2	
+P50078	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53257 1 314
+P53257	UniProtKB	Chain	1	314	.	.	.	ID=PRO_0000090696;Note=Mitochondrial thiamine pyrophosphate carrier 1	
+P53257	UniProtKB	Transmembrane	14	30	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53257	UniProtKB	Transmembrane	84	100	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53257	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53257	UniProtKB	Transmembrane	170	186	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53257	UniProtKB	Transmembrane	217	233	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53257	UniProtKB	Transmembrane	285	302	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53257	UniProtKB	Repeat	14	103	.	.	.	Note=Solcar 1	
+P53257	UniProtKB	Repeat	110	195	.	.	.	Note=Solcar 2	
+P53257	UniProtKB	Repeat	210	310	.	.	.	Note=Solcar 3	
+P53257	UniProtKB	Sequence conflict	66	66	.	.	.	Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q00764 1 495
+Q00764	UniProtKB	Chain	1	495	.	.	.	ID=PRO_0000122502;Note=Alpha%2Calpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit	
+Q00764	UniProtKB	Mutagenesis	223	223	.	.	.	Note=In GLC6-1%3B low glycogen accumulation. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8150278;Dbxref=PMID:8150278	
+Q00764	UniProtKB	Sequence conflict	75	75	.	.	.	Note=K->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00764	UniProtKB	Sequence conflict	101	101	.	.	.	Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00764	UniProtKB	Sequence conflict	104	104	.	.	.	Note=G->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00764	UniProtKB	Sequence conflict	129	130	.	.	.	Note=LA->FG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00764	UniProtKB	Sequence conflict	217	217	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00764	UniProtKB	Sequence conflict	288	288	.	.	.	Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35172 1 780
+P35172	UniProtKB	Chain	1	780	.	.	.	ID=PRO_0000173800;Note=Probable trehalase	
+P35172	UniProtKB	Region	338	339	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35172	UniProtKB	Region	384	386	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35172	UniProtKB	Active site	507	507	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35172	UniProtKB	Active site	703	703	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35172	UniProtKB	Binding site	331	331	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35172	UniProtKB	Binding site	375	375	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35172	UniProtKB	Binding site	384	384	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35172	UniProtKB	Binding site	505	505	.	.	.	Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35172	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35172	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35172	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P35172	UniProtKB	Modified residue	112	112	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q07527 1 1436
+Q07527	UniProtKB	Chain	1	1436	.	.	.	ID=PRO_0000270921;Note=tRNA (guanosine(18)-2'-O)-methyltransferase	
+Q07527	UniProtKB	Region	1365	1367	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13395	
+Q07527	UniProtKB	Region	1409	1418	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13395	
+Q07527	UniProtKB	Binding site	1389	1389	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13395	
+##sequence-region Q02721 1 264
+Q02721	UniProtKB	Chain	1	264	.	.	.	ID=PRO_0000097213;Note=Meiotic recombination protein REC102	
+##sequence-region P34219 1 525
+P34219	UniProtKB	Chain	1	525	.	.	.	ID=PRO_0000197146;Note=Transcriptional regulatory protein TOD6	
+P34219	UniProtKB	Domain	67	124	.	.	.	Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P34219	UniProtKB	DNA binding	97	120	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P34219	UniProtKB	Modified residue	280	280	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34219	UniProtKB	Modified residue	333	333	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34219	UniProtKB	Modified residue	341	341	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34219	UniProtKB	Modified residue	366	366	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P33448 1 61
+P33448	UniProtKB	Chain	1	61	.	.	.	ID=PRO_0000210820;Note=Mitochondrial import receptor subunit TOM6	
+P33448	UniProtKB	Topological domain	1	31	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33448	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33448	UniProtKB	Topological domain	53	61	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33448	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P38811 1 3744
+P38811	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38811	UniProtKB	Chain	2	3744	.	.	.	ID=PRO_0000088854;Note=Transcription-associated protein 1	
+P38811	UniProtKB	Domain	2622	3177	.	.	.	Note=FAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534	
+P38811	UniProtKB	Domain	3414	3711	.	.	.	Note=PI3K/PI4K	
+P38811	UniProtKB	Domain	3712	3744	.	.	.	Note=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535	
+P38811	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38811	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38811	UniProtKB	Modified residue	542	542	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38811	UniProtKB	Mutagenesis	241	241	.	.	.	Note=In TRA1-2%3B when associated with L-604%3B R-2733%3B P-3145%3B S-3222 and G-3302. Defects in its ability to interact with acidic activators. L->S	
+P38811	UniProtKB	Mutagenesis	604	604	.	.	.	Note=In TRA1-2%3B when associated with S-241%3B R-2733%3B P-3145%3B S-3222 and G-3302. Defects in its ability to interact with acidic activators. F->L	
+P38811	UniProtKB	Mutagenesis	2733	2733	.	.	.	Note=In TRA1-2%3B when associated with S-241%3B L-604%3B P-3145%3B S-3222 and G-3302. Defects in its ability to interact with acidic activators. W->R	
+P38811	UniProtKB	Mutagenesis	3145	3145	.	.	.	Note=In TRA1-2%3B when associated with S-241%3B L-604%3B R-2733%3B S-3222 and G-3302. Defects in its ability to interact with acidic activators. S->P	
+P38811	UniProtKB	Mutagenesis	3222	3222	.	.	.	Note=In TRA1-2%3B when associated with S-241%3B L-604%3B R-2733%3B P-3145 and G-3302. Defects in its ability to interact with acidic activators. L->S	
+P38811	UniProtKB	Mutagenesis	3302	3302	.	.	.	Note=In TRA1-2%3B when associated with S-241%3B L-604%3B R-2733%3B P-3145 and S-3222. Defects in its ability to interact with acidic activators. D->G	
+##sequence-region Q08693 1 809
+Q08693	UniProtKB	Chain	1	809	.	.	.	ID=PRO_0000237639;Note=Putative zinc metalloprotease TRE2	
+Q08693	UniProtKB	Topological domain	1	125	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08693	UniProtKB	Transmembrane	126	146	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08693	UniProtKB	Topological domain	147	809	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08693	UniProtKB	Domain	255	349	.	.	.	Note=PA	
+Q08693	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08693	UniProtKB	Glycosylation	669	669	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08693	UniProtKB	Glycosylation	736	736	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P48561 1 642
+P48561	UniProtKB	Chain	1	642	.	.	.	ID=PRO_0000120316;Note=Poly(A) RNA polymerase protein 1	
+P48561	UniProtKB	Domain	368	428	.	.	.	Note=PAP-associated	
+P48561	UniProtKB	Metal binding	233	233	.	.	.	Note=Magnesium or manganese%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48561	UniProtKB	Metal binding	235	235	.	.	.	Note=Magnesium or manganese%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48561	UniProtKB	Modified residue	596	596	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48561	UniProtKB	Modified residue	602	602	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48561	UniProtKB	Sequence conflict	354	355	.	.	.	Note=MH->ID;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P28584 1 889
+P28584	UniProtKB	Chain	1	889	.	.	.	ID=PRO_0000070464;Note=Low-affinity potassium transport protein	
+P28584	UniProtKB	Topological domain	1	51	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	52	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	74	80	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	102	109	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	131	464	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	465	487	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	488	499	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	500	521	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	522	524	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	525	545	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	546	548	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	549	569	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	570	584	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	585	605	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	606	609	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	610	630	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	631	657	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	658	678	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	679	743	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	744	764	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	765	776	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Transmembrane	777	797	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Topological domain	798	889	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Glycosylation	216	216	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Glycosylation	233	233	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28584	UniProtKB	Glycosylation	265	265	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12383 1 476
+Q12383	UniProtKB	Chain	1	476	.	.	.	ID=PRO_0000235932;Note=tRNA:m(4)X modification enzyme TRM13	
+Q12383	UniProtKB	Zinc finger	72	99	.	.	.	Note=CHHC U11-48K-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01141	
+##sequence-region P25040 1 408
+P25040	UniProtKB	Chain	1	408	.	.	.	ID=PRO_0000203487;Note=20S rRNA accumulation protein 4	
+##sequence-region P36164 1 337
+P36164	UniProtKB	Chain	1	337	.	.	.	ID=PRO_0000203226;Note=Golgi apparatus membrane protein TVP38	
+P36164	UniProtKB	Topological domain	1	95	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36164	UniProtKB	Transmembrane	96	116	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36164	UniProtKB	Topological domain	117	137	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36164	UniProtKB	Transmembrane	138	158	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36164	UniProtKB	Topological domain	159	169	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36164	UniProtKB	Transmembrane	170	190	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36164	UniProtKB	Topological domain	191	251	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36164	UniProtKB	Transmembrane	252	272	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36164	UniProtKB	Topological domain	273	286	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36164	UniProtKB	Transmembrane	287	307	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36164	UniProtKB	Topological domain	308	337	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P33122 1 291
+P33122	UniProtKB	Chain	1	291	.	.	.	ID=PRO_0000127495;Note=Serine-rich protein TYE7	
+P33122	UniProtKB	Domain	180	265	.	.	.	Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981	
+P33122	UniProtKB	Compositional bias	63	69	.	.	.	Note=Poly-Ser	
+P33122	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P33122	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P33122	UniProtKB	Mutagenesis	189	189	.	.	.	Note=In SGC1-1%3B suppresses transcriptional defect caused by a GCR1 null mutation. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7739544;Dbxref=PMID:7739544	
+P33122	UniProtKB	Mutagenesis	210	210	.	.	.	Note=In SGC1-2/3/4%3B suppresses transcriptional defect caused by a GCR1 null mutation. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7739544;Dbxref=PMID:7739544	
+##sequence-region P06785 1 304
+P06785	UniProtKB	Chain	1	304	.	.	.	ID=PRO_0000140912;Note=Thymidylate synthase	
+P06785	UniProtKB	Nucleotide binding	157	158	.	.	.	Note=dUMP%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884	
+P06785	UniProtKB	Nucleotide binding	206	209	.	.	.	Note=dUMP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884	
+P06785	UniProtKB	Nucleotide binding	247	249	.	.	.	Note=dUMP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884	
+P06785	UniProtKB	Active site	177	177	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884	
+P06785	UniProtKB	Binding site	30	30	.	.	.	Note=dUMP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884	
+P06785	UniProtKB	Binding site	209	209	.	.	.	Note=5%2C10-methylenetetrahydrofolate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884	
+P06785	UniProtKB	Binding site	217	217	.	.	.	Note=dUMP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884	
+P06785	UniProtKB	Sequence conflict	34	78	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CF16 1 290
+P0CF16	UniProtKB	Chain	1	290	.	.	.	ID=PRO_0000203265;Note=UPF0507 protein YML003W	
+##sequence-region P21734 1 215
+P21734	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000082525;Note=Ubiquitin-conjugating enzyme E2 1	
+P21734	UniProtKB	Active site	88	88	.	.	.	Note=Glycyl thioester intermediate	
+P21734	UniProtKB	Cross-link	93	93	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P21734	UniProtKB	Helix	3	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Helix	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Beta strand	22	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Beta strand	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TTE	
+P21734	UniProtKB	Beta strand	32	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Beta strand	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FXT	
+P21734	UniProtKB	Turn	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Beta strand	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Turn	60	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TTE	
+P21734	UniProtKB	Turn	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Helix	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Turn	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Helix	102	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FXT	
+P21734	UniProtKB	Helix	124	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Helix	134	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY	
+P21734	UniProtKB	Helix	170	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TTE	
+P21734	UniProtKB	Helix	183	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TTE	
+P21734	UniProtKB	Helix	204	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TTE	
+##sequence-region P33296 1 250
+P33296	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000082552;Note=Ubiquitin-conjugating enzyme E2 6	
+P33296	UniProtKB	Topological domain	1	232	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33296	UniProtKB	Transmembrane	233	249	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33296	UniProtKB	Active site	87	87	.	.	.	Note=Glycyl thioester intermediate	
+P33296	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33296	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P33296	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Loss of activity. C->S	
+##sequence-region P36026 1 717
+P36026	UniProtKB	Chain	1	717	.	.	.	ID=PRO_0000080596;Note=Ubiquitin carboxyl-terminal hydrolase 11	
+P36026	UniProtKB	Domain	298	707	.	.	.	Note=USP	
+P36026	UniProtKB	Compositional bias	557	564	.	.	.	Note=Poly-His	
+P36026	UniProtKB	Active site	307	307	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P36026	UniProtKB	Active site	649	649	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+##sequence-region P38237 1 781
+P38237	UniProtKB	Chain	1	781	.	.	.	ID=PRO_0000080599;Note=Ubiquitin carboxyl-terminal hydrolase 14	
+P38237	UniProtKB	Domain	323	781	.	.	.	Note=USP	
+P38237	UniProtKB	Domain	576	626	.	.	.	Note=UBA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
+P38237	UniProtKB	Domain	649	689	.	.	.	Note=UBA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
+P38237	UniProtKB	Zinc finger	190	262	.	.	.	Note=UBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
+P38237	UniProtKB	Compositional bias	92	95	.	.	.	Note=Poly-Asn	
+P38237	UniProtKB	Active site	332	332	.	.	.	Note=Nucleophile	
+P38237	UniProtKB	Active site	737	737	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P38237	UniProtKB	Mutagenesis	332	332	.	.	.	Note=Loss of enzyme activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9305625;Dbxref=PMID:9305625	
+##sequence-region P32571 1 926
+P32571	UniProtKB	Chain	1	926	.	.	.	ID=PRO_0000080589;Note=Ubiquitin carboxyl-terminal hydrolase 4	
+P32571	UniProtKB	Domain	205	328	.	.	.	Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+P32571	UniProtKB	Domain	562	923	.	.	.	Note=USP	
+P32571	UniProtKB	Compositional bias	386	392	.	.	.	Note=Poly-Gln	
+P32571	UniProtKB	Active site	571	571	.	.	.	Note=Nucleophile	
+P32571	UniProtKB	Active site	880	880	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P32571	UniProtKB	Modified residue	443	443	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32571	UniProtKB	Mutagenesis	571	571	.	.	.	Note=Impairs deubiquitination activity and protein sorting into the MVB pathway. C->S%2CA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17376168,ECO:0000269|PubMed:17446860;Dbxref=PMID:17376168,PMID:17446860	
+P32571	UniProtKB	Mutagenesis	826	826	.	.	.	Note=Impairs deubiquitination activity and binding to BRO1%3B when associated with A-827 and A-829. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17446860;Dbxref=PMID:17446860	
+P32571	UniProtKB	Mutagenesis	827	827	.	.	.	Note=Impairs deubiquitination activity and binding to BRO1%3B when associated with A-826 and A-829. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17446860;Dbxref=PMID:17446860	
+P32571	UniProtKB	Mutagenesis	829	829	.	.	.	Note=Impairs deubiquitination activity and binding to BRO1%3B when associated with A-826 and A-827. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17446860;Dbxref=PMID:17446860	
+P32571	UniProtKB	Sequence conflict	327	327	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32571	UniProtKB	Sequence conflict	345	345	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32571	UniProtKB	Sequence conflict	375	378	.	.	.	Note=MLVA->TASW;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32571	UniProtKB	Sequence conflict	383	383	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32571	UniProtKB	Sequence conflict	407	407	.	.	.	Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32571	UniProtKB	Sequence conflict	543	570	.	.	.	Note=LDHTDVTPTSSHNYDLDFAVGLENLGNS->FRSYEMLHQLLLIIMTLISRLVWENLEIP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32571	UniProtKB	Sequence conflict	580	580	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32571	UniProtKB	Sequence conflict	836	836	.	.	.	Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32571	UniProtKB	Sequence conflict	897	897	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40453 1 1071
+P40453	UniProtKB	Chain	1	1071	.	.	.	ID=PRO_0000080592;Note=Ubiquitin carboxyl-terminal hydrolase 7	
+P40453	UniProtKB	Domain	609	1069	.	.	.	Note=USP	
+P40453	UniProtKB	Active site	618	618	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P40453	UniProtKB	Active site	1014	1014	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+##sequence-region P19812 1 1950
+P19812	UniProtKB	Chain	1	1950	.	.	.	ID=PRO_0000056135;Note=E3 ubiquitin-protein ligase UBR1	
+P19812	UniProtKB	Zinc finger	121	194	.	.	.	Note=UBR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00508	
+P19812	UniProtKB	Zinc finger	1220	1324	.	.	.	Note=RING-type%3B atypical	
+P19812	UniProtKB	Region	1117	1219	.	.	.	Note=Interaction with UBC2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257	
+P19812	UniProtKB	Modified residue	296	296	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P19812	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P19812	UniProtKB	Modified residue	1938	1938	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19812	UniProtKB	Mutagenesis	1168	1168	.	.	.	Note=Impairs interaction with UBC2%2C but does not affect degradation of N-end rule substrates. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257	
+P19812	UniProtKB	Mutagenesis	1169	1169	.	.	.	Note=Impairs interaction with UBC2%2C but does not affect degradation of N-end rule substrates. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257	
+P19812	UniProtKB	Mutagenesis	1173	1173	.	.	.	Note=Impairs interaction with UBC2%2C but does not affect degradation of N-end rule substrates. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257	
+P19812	UniProtKB	Mutagenesis	1220	1220	.	.	.	Note=No effect on interaction with UBC2%2C but inhibits degradation of N-end rule substrates. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257	
+P19812	UniProtKB	Mutagenesis	1223	1223	.	.	.	Note=No effect on interaction with UBC2%2C but inhibits degradation of N-end rule substrates. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257	
+P19812	UniProtKB	Mutagenesis	1295	1295	.	.	.	Note=No effect on interaction with UBC2%2C but inhibits degradation of N-end rule substrates. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257	
+P19812	UniProtKB	Mutagenesis	1297	1297	.	.	.	Note=No effect on interaction with UBC2%2C but inhibits degradation of N-end rule substrates. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257	
+P19812	UniProtKB	Mutagenesis	1320	1320	.	.	.	Note=No effect on interaction with UBC2%2C but inhibits degradation of N-end rule substrates. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257	
+P19812	UniProtKB	Beta strand	132	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS	
+P19812	UniProtKB	Turn	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS	
+P19812	UniProtKB	Beta strand	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS	
+P19812	UniProtKB	Turn	149	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS	
+P19812	UniProtKB	Helix	154	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS	
+P19812	UniProtKB	Beta strand	162	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS	
+P19812	UniProtKB	Beta strand	169	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS	
+P19812	UniProtKB	Helix	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS	
+P19812	UniProtKB	Beta strand	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS	
+P19812	UniProtKB	Helix	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS	
+##sequence-region Q07963 1 1872
+Q07963	UniProtKB	Chain	1	1872	.	.	.	ID=PRO_0000056142;Note=E3 ubiquitin-protein ligase UBR2	
+Q07963	UniProtKB	Zinc finger	96	172	.	.	.	Note=UBR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00508	
+Q07963	UniProtKB	Zinc finger	1241	1362	.	.	.	Note=RING-type%3B atypical	
+Q07963	UniProtKB	Region	1134	1240	.	.	.	Note=Interaction with UBC2	
+Q07963	UniProtKB	Modified residue	1218	1218	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07963	UniProtKB	Modified residue	1222	1222	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q07963	UniProtKB	Cross-link	709	709	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region Q04228 1 584
+Q04228	UniProtKB	Chain	1	584	.	.	.	ID=PRO_0000210999;Note=UBX domain-containing protein 2	
+Q04228	UniProtKB	Topological domain	1	80	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04228	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04228	UniProtKB	Topological domain	102	151	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04228	UniProtKB	Transmembrane	152	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04228	UniProtKB	Topological domain	173	584	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04228	UniProtKB	Domain	426	570	.	.	.	Note=UBX	
+##sequence-region Q06682 1 500
+Q06682	UniProtKB	Chain	1	500	.	.	.	ID=PRO_0000211002;Note=UBX domain-containing protein 5	
+Q06682	UniProtKB	Domain	415	493	.	.	.	Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215	
+Q06682	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q03337 1 283
+Q03337	UniProtKB	Chain	1	283	.	.	.	ID=PRO_0000211585;Note=Trafficking protein particle complex subunit 31	
+##sequence-region Q07381 1 788
+Q07381	UniProtKB	Chain	1	788	.	.	.	ID=PRO_0000065671;Note=Ribosome biogenesis protein TSR1	
+Q07381	UniProtKB	Domain	82	254	.	.	.	Note=Bms1-type G	
+Q07381	UniProtKB	Compositional bias	413	496	.	.	.	Note=Glu-rich	
+##sequence-region P20049 1 452
+P20049	UniProtKB	Chain	1	452	.	.	.	ID=PRO_0000119208;Note=Prephenate dehydrogenase [NADP(+)]	
+P20049	UniProtKB	Domain	14	297	.	.	.	Note=Prephenate/arogenate dehydrogenase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00522	
+P20049	UniProtKB	Nucleotide binding	14	43	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20049	UniProtKB	Sequence conflict	38	38	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20049	UniProtKB	Sequence conflict	204	211	.	.	.	Note=IKIYPWTL->DKDSSLDS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20049	UniProtKB	Sequence conflict	312	313	.	.	.	Note=GN->SD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20049	UniProtKB	Sequence conflict	433	452	.	.	.	Note=MIKTILSHSSDRSAAEKRNT->DDKNHSESF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07285 1 380
+P07285	UniProtKB	Chain	1	380	.	.	.	ID=PRO_0000154528;Note=Anthranilate phosphoribosyltransferase	
+##sequence-region Q03784 1 219
+Q03784	UniProtKB	Chain	1	219	.	.	.	ID=PRO_0000211571;Note=Trafficking protein particle complex subunit 23	
+##sequence-region P25372 1 127
+P25372	UniProtKB	Transit peptide	1	21	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25372	UniProtKB	Chain	22	127	.	.	.	ID=PRO_0000034155;Note=Thioredoxin-3%2C mitochondrial	
+P25372	UniProtKB	Domain	22	127	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P25372	UniProtKB	Active site	55	55	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25372	UniProtKB	Active site	58	58	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25372	UniProtKB	Site	49	49	.	.	.	Note=Deprotonates C-terminal active site Cys;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25372	UniProtKB	Site	56	56	.	.	.	Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25372	UniProtKB	Site	57	57	.	.	.	Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25372	UniProtKB	Disulfide bond	55	58	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P25372	UniProtKB	Helix	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3	
+P25372	UniProtKB	Helix	33	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3	
+P25372	UniProtKB	Beta strand	44	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3	
+P25372	UniProtKB	Helix	56	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3	
+P25372	UniProtKB	Helix	62	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3	
+P25372	UniProtKB	Beta strand	75	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3	
+P25372	UniProtKB	Turn	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3	
+P25372	UniProtKB	Helix	86	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3	
+P25372	UniProtKB	Beta strand	96	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3	
+P25372	UniProtKB	Beta strand	107	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3	
+P25372	UniProtKB	Helix	117	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3	
+##sequence-region P29509 1 319
+P29509	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7961686;Dbxref=PMID:7961686	
+P29509	UniProtKB	Chain	2	319	.	.	.	ID=PRO_0000166770;Note=Thioredoxin reductase 1	
+P29509	UniProtKB	Nucleotide binding	11	14	.	.	.	Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561	
+P29509	UniProtKB	Nucleotide binding	40	41	.	.	.	Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561	
+P29509	UniProtKB	Nucleotide binding	295	297	.	.	.	Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561	
+P29509	UniProtKB	Binding site	45	45	.	.	.	Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561	
+P29509	UniProtKB	Binding site	54	54	.	.	.	Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561	
+P29509	UniProtKB	Binding site	87	87	.	.	.	Note=FAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561	
+P29509	UniProtKB	Binding site	145	145	.	.	.	Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561	
+P29509	UniProtKB	Binding site	288	288	.	.	.	Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561	
+P29509	UniProtKB	Modified residue	303	303	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P29509	UniProtKB	Disulfide bond	142	145	.	.	.	Note=Redox-active;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20235561;Dbxref=PMID:20235561	
+P29509	UniProtKB	Sequence conflict	18	18	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29509	UniProtKB	Sequence conflict	101	101	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29509	UniProtKB	Sequence conflict	111	111	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29509	UniProtKB	Sequence conflict	180	196	.	.	.	Note=VFMLVRKDHLRASTIMQ->CLCLSEKTICVLLPLCK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29509	UniProtKB	Beta strand	3	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Helix	13	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Helix	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Helix	64	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	87	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	93	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	110	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Helix	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Turn	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Helix	143	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Helix	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	155	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Helix	164	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Turn	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	177	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	185	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Helix	193	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	210	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Turn	231	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	235	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	242	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Helix	255	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Turn	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D8X	
+P29509	UniProtKB	Beta strand	275	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Beta strand	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Helix	287	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+P29509	UniProtKB	Helix	297	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ	
+##sequence-region P47168 1 421
+P47168	UniProtKB	Chain	1	421	.	.	.	ID=PRO_0000203122;Note=TEL2-interacting protein 2	
+##sequence-region P38962 1 199
+P38962	UniProtKB	Chain	1	199	.	.	.	ID=PRO_0000212837;Note=Golgi apparatus membrane protein TVP23	
+P38962	UniProtKB	Transmembrane	18	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38962	UniProtKB	Transmembrane	43	60	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38962	UniProtKB	Transmembrane	108	128	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38962	UniProtKB	Transmembrane	133	153	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38962	UniProtKB	Glycosylation	63	63	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38962	UniProtKB	Glycosylation	86	86	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38962	UniProtKB	Glycosylation	185	185	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P22803 1 104
+P22803	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7961686;Dbxref=PMID:7961686	
+P22803	UniProtKB	Chain	2	104	.	.	.	ID=PRO_0000120045;Note=Thioredoxin-2	
+P22803	UniProtKB	Domain	2	104	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P22803	UniProtKB	Active site	31	31	.	.	.	Note=Nucleophile	
+P22803	UniProtKB	Active site	34	34	.	.	.	Note=Nucleophile	
+P22803	UniProtKB	Site	25	25	.	.	.	Note=Deprotonates C-terminal active site Cys	
+P22803	UniProtKB	Site	32	32	.	.	.	Note=Contributes to redox potential value	
+P22803	UniProtKB	Site	33	33	.	.	.	Note=Contributes to redox potential value	
+P22803	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P22803	UniProtKB	Disulfide bond	31	34	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00691,ECO:0000269|PubMed:17044062;Dbxref=PMID:17044062	
+P22803	UniProtKB	Cross-link	67	67	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P22803	UniProtKB	Cross-link	97	97	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P22803	UniProtKB	Beta strand	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS	
+P22803	UniProtKB	Helix	8	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS	
+P22803	UniProtKB	Beta strand	19	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS	
+P22803	UniProtKB	Helix	32	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS	
+P22803	UniProtKB	Beta strand	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS	
+P22803	UniProtKB	Turn	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS	
+P22803	UniProtKB	Helix	62	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS	
+P22803	UniProtKB	Beta strand	72	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS	
+P22803	UniProtKB	Beta strand	83	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS	
+P22803	UniProtKB	Helix	93	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS	
+##sequence-region P38254 1 753
+P38254	UniProtKB	Chain	1	753	.	.	.	ID=PRO_0000212448;Note=Probable tubulin--tyrosine ligase PBY1	
+P38254	UniProtKB	Domain	343	734	.	.	.	Note=TTL;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00568	
+P38254	UniProtKB	Sequence conflict	352	355	.	.	.	Note=HALK->TPE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38254	UniProtKB	Sequence conflict	450	450	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38254	UniProtKB	Sequence conflict	450	450	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38254	UniProtKB	Sequence conflict	563	563	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P29340 1 183
+P29340	UniProtKB	Chain	1	183	.	.	.	ID=PRO_0000082558;Note=Ubiquitin-conjugating enzyme E2-21 kDa	
+P29340	UniProtKB	Active site	115	115	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133	
+P29340	UniProtKB	Helix	16	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Turn	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Turn	42	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Beta strand	47	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Beta strand	60	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BWF	
+P29340	UniProtKB	Turn	72	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Beta strand	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Turn	86	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Beta strand	94	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Turn	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Helix	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Turn	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Helix	130	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Helix	152	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P29340	UniProtKB	Helix	163	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+##sequence-region Q12094 1 313
+Q12094	UniProtKB	Chain	1	313	.	.	.	ID=PRO_0000094426;Note=Ribosome biogenesis protein TSR3	
+Q12094	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12094	UniProtKB	Modified residue	289	289	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q08747 1 228
+Q08747	UniProtKB	Chain	1	228	.	.	.	ID=PRO_0000245507;Note=Upstream activation factor subunit UAF30	
+Q08747	UniProtKB	Domain	120	194	.	.	.	Note=SWIB	
+Q08747	UniProtKB	Modified residue	218	218	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08747	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08747	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P14682 1 295
+P14682	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000082541;Note=Ubiquitin-conjugating enzyme E2-34 kDa	
+P14682	UniProtKB	Compositional bias	191	289	.	.	.	Note=Asp/Glu-rich (acidic)	
+P14682	UniProtKB	Active site	95	95	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133	
+P14682	UniProtKB	Modified residue	186	186	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14682	UniProtKB	Modified residue	282	282	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14682	UniProtKB	Modified residue	292	292	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P40032 1 644
+P40032	UniProtKB	Chain	1	644	.	.	.	ID=PRO_0000206670;Note=Prolyl 3%2C4-dihydroxylase TPA1	
+P40032	UniProtKB	Domain	141	247	.	.	.	Note=Fe2OG dioxygenase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00805	
+P40032	UniProtKB	Metal binding	159	159	.	.	.	Note=Iron;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00805,ECO:0000269|PubMed:20040577;Dbxref=PMID:20040577	
+P40032	UniProtKB	Metal binding	161	161	.	.	.	Note=Iron;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00805,ECO:0000269|PubMed:20040577;Dbxref=PMID:20040577	
+P40032	UniProtKB	Metal binding	227	227	.	.	.	Note=Iron;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00805,ECO:0000269|PubMed:20040577;Dbxref=PMID:20040577	
+P40032	UniProtKB	Binding site	173	173	.	.	.	Note=2-oxoglutarate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00805,ECO:0000269|PubMed:20040577;Dbxref=PMID:20040577	
+P40032	UniProtKB	Binding site	238	238	.	.	.	Note=2-oxoglutarate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00805,ECO:0000269|PubMed:20040577;Dbxref=PMID:20040577	
+P40032	UniProtKB	Modified residue	607	607	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40032	UniProtKB	Mutagenesis	159	161	.	.	.	Note=Loss of function. HDD->ADN%2CADA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20630870,ECO:0000269|PubMed:24550462;Dbxref=PMID:20630870,PMID:24550462	
+P40032	UniProtKB	Mutagenesis	159	159	.	.	.	Note=Loss of function. H->A	
+P40032	UniProtKB	Helix	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	32	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	37	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	56	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	64	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	81	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	86	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	111	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	123	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	139	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MGU	
+P40032	UniProtKB	Beta strand	145	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	155	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	166	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	214	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Turn	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	238	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NHK	
+P40032	UniProtKB	Helix	259	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	269	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT4	
+P40032	UniProtKB	Helix	278	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	294	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	332	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	344	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	349	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	363	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	373	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	396	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Turn	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	415	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	419	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT1	
+P40032	UniProtKB	Helix	428	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	443	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Turn	461	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	466	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	481	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	492	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	497	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Turn	507	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Helix	521	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	527	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Turn	546	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	555	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	588	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	596	604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	609	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+P40032	UniProtKB	Beta strand	623	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7	
+##sequence-region P31688 1 896
+P31688	UniProtKB	Chain	1	896	.	.	.	ID=PRO_0000122509;Note=Trehalose-phosphatase	
+P31688	UniProtKB	Region	1	554	.	.	.	Note=Glycosyltransferase	
+P31688	UniProtKB	Sequence conflict	48	48	.	.	.	Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31688	UniProtKB	Sequence conflict	289	289	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31688	UniProtKB	Sequence conflict	542	542	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31688	UniProtKB	Sequence conflict	546	546	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31688	UniProtKB	Sequence conflict	549	549	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38426 1 1054
+P38426	UniProtKB	Chain	1	1054	.	.	.	ID=PRO_0000122510;Note=Trehalose synthase complex regulatory subunit TPS3	
+P38426	UniProtKB	Region	287	778	.	.	.	Note=Glycosyltransferase	
+P38426	UniProtKB	Compositional bias	125	249	.	.	.	Note=Ser-rich	
+P38426	UniProtKB	Modified residue	148	148	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38426	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38426	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P38426	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38426	UniProtKB	Modified residue	267	267	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38426	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38426	UniProtKB	Modified residue	960	960	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38426	UniProtKB	Sequence conflict	186	186	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38426	UniProtKB	Sequence conflict	765	765	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38426	UniProtKB	Sequence conflict	834	834	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38426	UniProtKB	Sequence conflict	902	902	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P46959 1 383
+P46959	UniProtKB	Chain	1	383	.	.	.	ID=PRO_0000087437;Note=tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRM61	
+P46959	UniProtKB	Region	121	124	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000269,ECO:0000312;evidence=ECO:0000269|PubMed:27582183,ECO:0000312|PDB:5ERG;Dbxref=PMID:27582183	
+P46959	UniProtKB	Region	168	169	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000269,ECO:0000312;evidence=ECO:0000269|PubMed:27582183,ECO:0000312|PDB:5ERG;Dbxref=PMID:27582183	
+P46959	UniProtKB	Binding site	94	94	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000269,ECO:0000312;evidence=ECO:0000269|PubMed:27582183,ECO:0000312|PDB:5ERG;Dbxref=PMID:27582183	
+P46959	UniProtKB	Binding site	139	139	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000269,ECO:0000312;evidence=ECO:0000269|PubMed:27582183,ECO:0000312|PDB:5ERG;Dbxref=PMID:27582183	
+P46959	UniProtKB	Binding site	144	144	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96FX7	
+P46959	UniProtKB	Binding site	203	203	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000269,ECO:0000312;evidence=ECO:0000269|PubMed:27582183,ECO:0000312|PDB:5ERG;Dbxref=PMID:27582183	
+P46959	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46959	UniProtKB	Beta strand	18	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	27	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Helix	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Turn	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	58	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	71	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Helix	80	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Helix	96	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	113	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Helix	123	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	133	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Helix	142	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Turn	158	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	162	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Helix	169	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	197	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Helix	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Helix	211	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	224	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Helix	233	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	249	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Helix	271	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	341	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Beta strand	357	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+P46959	UniProtKB	Helix	371	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ	
+##sequence-region P38238 1 310
+P38238	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000155587;Note=tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase	
+P38238	UniProtKB	Active site	164	164	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162	
+P38238	UniProtKB	Binding site	55	55	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162	
+P38238	UniProtKB	Binding site	57	57	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162	
+P38238	UniProtKB	Binding site	83	83	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162	
+P38238	UniProtKB	Binding site	99	99	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162	
+P38238	UniProtKB	Binding site	124	124	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162	
+##sequence-region P49957 1 279
+P49957	UniProtKB	Chain	1	279	.	.	.	ID=PRO_0000203262;Note=tRNA (carboxymethyluridine(34)-5-O)-methyltransferase	
+##sequence-region Q12009 1 286
+Q12009	UniProtKB	Chain	1	286	.	.	.	ID=PRO_0000171437;Note=tRNA (guanine-N(7)-)-methyltransferase	
+Q12009	UniProtKB	Region	126	127	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q12009	UniProtKB	Region	161	162	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q12009	UniProtKB	Region	259	261	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q12009	UniProtKB	Active site	184	184	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12009	UniProtKB	Binding site	103	103	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03055,ECO:0000269|PubMed:18184583;Dbxref=PMID:18184583	
+Q12009	UniProtKB	Binding site	181	181	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03055,ECO:0000269|PubMed:18184583;Dbxref=PMID:18184583	
+Q12009	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12009	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12009	UniProtKB	Helix	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Helix	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q12009	UniProtKB	Helix	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Helix	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Turn	88	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q12009	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q12009	UniProtKB	Beta strand	97	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Helix	108	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Beta strand	120	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Helix	129	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Beta strand	147	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU	
+Q12009	UniProtKB	Turn	151	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Beta strand	155	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Helix	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Beta strand	175	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Helix	199	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Beta strand	209	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Helix	222	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Beta strand	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Helix	243	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Helix	250	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Helix	260	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+Q12009	UniProtKB	Beta strand	273	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV	
+##sequence-region P00912 1 224
+P00912	UniProtKB	Chain	1	224	.	.	.	ID=PRO_0000154337;Note=N-(5'-phosphoribosyl)anthranilate isomerase	
+P00912	UniProtKB	Natural variant	48	48	.	.	.	Note=In strain: CLIB 556 haplotype Ha2 and CLIB 630 haplotype Ha2. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P00912	UniProtKB	Natural variant	172	172	.	.	.	Note=In strain: CLIB 556 haplotype Ha1. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P00912	UniProtKB	Natural variant	212	212	.	.	.	Note=In strain: CLIB 95%2C CLIB 382%2C CLIB 388%2C CLIB 556 haplotype Ha2%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 haplotype Ha2 and YIIc17 haplotype Ha1. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+##sequence-region Q03860 1 143
+Q03860	UniProtKB	Chain	1	143	.	.	.	ID=PRO_0000240392;Note=Golgi apparatus membrane protein TVP15	
+Q03860	UniProtKB	Topological domain	1	10	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03860	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03860	UniProtKB	Topological domain	32	35	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03860	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03860	UniProtKB	Topological domain	57	67	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03860	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03860	UniProtKB	Topological domain	89	89	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03860	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03860	UniProtKB	Topological domain	111	143	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03860	UniProtKB	Compositional bias	133	141	.	.	.	Note=Poly-Asp	
+##sequence-region P53250 1 332
+P53250	UniProtKB	Chain	1	332	.	.	.	ID=PRO_0000214953;Note=Twinfilin-1	
+P53250	UniProtKB	Domain	5	132	.	.	.	Note=ADF-H 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00599	
+P53250	UniProtKB	Domain	173	300	.	.	.	Note=ADF-H 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00599	
+P53250	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53250	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P00899 1 507
+P00899	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7483834;Dbxref=PMID:7483834	
+P00899	UniProtKB	Chain	2	507	.	.	.	ID=PRO_0000154134;Note=Anthranilate synthase component 1	
+P00899	UniProtKB	Region	280	282	.	.	.	Note=Tryptophan binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897	
+P00899	UniProtKB	Region	316	317	.	.	.	Note=Chorismate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897	
+P00899	UniProtKB	Region	466	468	.	.	.	Note=Chorismate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897	
+P00899	UniProtKB	Metal binding	343	343	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897	
+P00899	UniProtKB	Metal binding	481	481	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897	
+P00899	UniProtKB	Binding site	65	65	.	.	.	Note=Tryptophan;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897	
+P00899	UniProtKB	Binding site	431	431	.	.	.	Note=Chorismate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897	
+P00899	UniProtKB	Binding site	452	452	.	.	.	Note=Chorismate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897	
+P00899	UniProtKB	Binding site	468	468	.	.	.	Note=Chorismate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897	
+P00899	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00899	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00899	UniProtKB	Sequence conflict	204	212	.	.	.	Note=TDDSSPIPY->DRRFLANTI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00899	UniProtKB	Sequence conflict	220	220	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00899	UniProtKB	Sequence conflict	223	238	.	.	.	Note=TFESNVGKEGYENHVS->LLNRMWARKVTKITSP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00899	UniProtKB	Sequence conflict	262	268	.	.	.	Note=TSLHPFN->SRYILSIFTD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00899	UniProtKB	Sequence conflict	276	276	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00899	UniProtKB	Sequence conflict	323	323	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00899	UniProtKB	Sequence conflict	330	330	.	.	.	Note=L->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00899	UniProtKB	Sequence conflict	401	402	.	.	.	Note=SI->TN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00899	UniProtKB	Sequence conflict	461	507	.	.	.	Note=AYLQAGGGIVYDSDEYDEYVETMNKMMANHSTIVQAEELWADIVGSA->LTCKLAVVLFTIQLSTMNMLETMNNDGQSQYYCASRRIVGRYRRISLKRAFSVFFPLDDIFIVFE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00937 1 484
+P00937	UniProtKB	Chain	1	484	.	.	.	ID=PRO_0000056866;Note=Multifunctional tryptophan biosynthesis protein	
+P00937	UniProtKB	Domain	13	207	.	.	.	Note=Glutamine amidotransferase type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P00937	UniProtKB	Region	64	66	.	.	.	Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00900	
+P00937	UniProtKB	Region	142	143	.	.	.	Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00900	
+P00937	UniProtKB	Region	215	484	.	.	.	Note=Indole-3-glycerol phosphate synthase	
+P00937	UniProtKB	Active site	92	92	.	.	.	Note=Nucleophile%3B for GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P00937	UniProtKB	Active site	181	181	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P00937	UniProtKB	Active site	183	183	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P00937	UniProtKB	Binding site	96	96	.	.	.	Note=Glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00900	
+P00937	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00937	UniProtKB	Sequence conflict	32	32	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00937	UniProtKB	Sequence conflict	63	65	.	.	.	Note=PGP->LGL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00937	UniProtKB	Sequence conflict	129	129	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00937	UniProtKB	Sequence conflict	170	170	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00937	UniProtKB	Sequence conflict	236	236	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00931 1 707
+P00931	UniProtKB	Chain	1	707	.	.	.	ID=PRO_0000098726;Note=Tryptophan synthase	
+P00931	UniProtKB	Region	1	297	.	.	.	Note=Tryptophan synthase alpha chain	
+P00931	UniProtKB	Region	298	707	.	.	.	Note=Tryptophan synthase beta chain	
+P00931	UniProtKB	Active site	50	50	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00931	UniProtKB	Active site	61	61	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00931	UniProtKB	Modified residue	384	384	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00931	UniProtKB	Modified residue	540	540	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00931	UniProtKB	Modified residue	683	683	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q3E790 1 80
+Q3E790	UniProtKB	Chain	1	80	.	.	.	ID=PRO_0000076358;Note=Serine palmitoyltransferase-regulating protein TSC3	
+Q3E790	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04767 1 167
+Q04767	UniProtKB	Chain	1	167	.	.	.	ID=PRO_0000203281;Note=Golgi apparatus membrane protein TVP18	
+Q04767	UniProtKB	Transmembrane	23	43	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04767	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04767	UniProtKB	Transmembrane	98	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04767	UniProtKB	Transmembrane	121	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04767	UniProtKB	Modified residue	146	146	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04767	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q04767	UniProtKB	Glycosylation	22	22	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q99394 1 268
+Q99394	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q99394	UniProtKB	Chain	2	268	.	.	.	ID=PRO_0000211589;Note=Trafficking protein particle complex subunit 33	
+Q99394	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q04120 1 196
+Q04120	UniProtKB	Chain	1	196	.	.	.	ID=PRO_0000135096;Note=Peroxiredoxin TSA2	
+Q04120	UniProtKB	Domain	3	161	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+Q04120	UniProtKB	Active site	48	48	.	.	.	Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26894543;Dbxref=PMID:26894543	
+Q04120	UniProtKB	Modified residue	174	174	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P34760	
+Q04120	UniProtKB	Disulfide bond	48	48	.	.	.	Note=Interchain (with C-171)%3B in linked form;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:5EPT,ECO:0000269|PubMed:26894543;Dbxref=PMID:26894543	
+Q04120	UniProtKB	Disulfide bond	171	171	.	.	.	Note=Interchain (with C-48)%3B in linked form;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:5EPT,ECO:0000269|PubMed:26894543;Dbxref=PMID:26894543	
+Q04120	UniProtKB	Cross-link	14	14	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P34760	
+Q04120	UniProtKB	Cross-link	89	89	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P34760	
+Q04120	UniProtKB	Cross-link	132	132	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P34760	
+Q04120	UniProtKB	Mutagenesis	48	48	.	.	.	Note=No activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10681558;Dbxref=PMID:10681558	
+Q04120	UniProtKB	Beta strand	13	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Beta strand	21	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Helix	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Beta strand	33	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Beta strand	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Helix	48	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Helix	59	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Beta strand	67	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Helix	77	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Turn	88	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Helix	107	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Turn	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Beta strand	124	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Beta strand	133	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Helix	149	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Turn	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+Q04120	UniProtKB	Helix	187	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB	
+##sequence-region Q06672 1 205
+Q06672	UniProtKB	Chain	1	205	.	.	.	ID=PRO_0000076359;Note=Pre-rRNA-processing protein TSR2	
+Q06672	UniProtKB	Compositional bias	153	179	.	.	.	Note=Asp-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36097 1 1038
+P36097	UniProtKB	Chain	1	1038	.	.	.	ID=PRO_0000203185;Note=TEL2-interacting protein 1	
+P36097	UniProtKB	Modified residue	817	817	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P16649 1 713
+P16649	UniProtKB	Chain	1	713	.	.	.	ID=PRO_0000051312;Note=General transcriptional corepressor TUP1	
+P16649	UniProtKB	Repeat	342	371	.	.	.	Note=WD 1	
+P16649	UniProtKB	Repeat	441	471	.	.	.	Note=WD 2	
+P16649	UniProtKB	Repeat	483	513	.	.	.	Note=WD 3	
+P16649	UniProtKB	Repeat	524	555	.	.	.	Note=WD 4	
+P16649	UniProtKB	Repeat	574	604	.	.	.	Note=WD 5	
+P16649	UniProtKB	Repeat	628	658	.	.	.	Note=WD 6	
+P16649	UniProtKB	Repeat	670	706	.	.	.	Note=WD 7	
+P16649	UniProtKB	Compositional bias	97	118	.	.	.	Note=Gln-rich	
+P16649	UniProtKB	Compositional bias	181	198	.	.	.	Note=Poly-Gln	
+P16649	UniProtKB	Compositional bias	399	409	.	.	.	Note=Thr-rich	
+P16649	UniProtKB	Modified residue	439	439	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P16649	UniProtKB	Sequence conflict	75	75	.	.	.	Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16649	UniProtKB	Sequence conflict	100	100	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16649	UniProtKB	Sequence conflict	685	685	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16649	UniProtKB	Sequence conflict	685	685	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16649	UniProtKB	Turn	19	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP9	
+P16649	UniProtKB	Helix	27	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP9	
+P16649	UniProtKB	Beta strand	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Helix	300	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	307	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	314	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	322	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	333	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	349	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	356	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	367	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Turn	372	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	377	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	445	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	455	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	467	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Turn	472	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	476	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	488	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	497	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	507	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Turn	514	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	518	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	529	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	541	546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	551	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Turn	556	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	561	565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	579	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	588	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	598	604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	622	627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	633	638	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Helix	640	642	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	644	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	652	658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Turn	659	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	664	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	675	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	691	697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+P16649	UniProtKB	Beta strand	700	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ	
+##sequence-region P32356 1 751
+P32356	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32356	UniProtKB	Chain	2	751	.	.	.	ID=PRO_0000173798;Note=Neutral trehalase	
+P32356	UniProtKB	Region	309	310	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32356	UniProtKB	Region	355	357	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32356	UniProtKB	Active site	478	478	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32356	UniProtKB	Active site	674	674	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32356	UniProtKB	Binding site	302	302	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32356	UniProtKB	Binding site	346	346	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32356	UniProtKB	Binding site	355	355	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32356	UniProtKB	Binding site	476	476	.	.	.	Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32356	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32356	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32356	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32356	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32356	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P32356	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:19779198	
+P32356	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P32356	UniProtKB	Modified residue	83	83	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P32356	UniProtKB	Sequence conflict	514	515	.	.	.	Note=CD->NN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32356	UniProtKB	Sequence conflict	712	712	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32356	UniProtKB	Sequence conflict	712	712	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32356	UniProtKB	Sequence conflict	723	724	.	.	.	Note=HA->YE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32356	UniProtKB	Sequence conflict	723	724	.	.	.	Note=HA->YE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32356	UniProtKB	Sequence conflict	727	728	.	.	.	Note=AL->EI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32356	UniProtKB	Sequence conflict	727	728	.	.	.	Note=AL->EI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38816 1 342
+P38816	UniProtKB	Transit peptide	1	23	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38816	UniProtKB	Chain	24	342	.	.	.	ID=PRO_0000030303;Note=Thioredoxin reductase 2%2C mitochondrial	
+P38816	UniProtKB	Nucleotide binding	34	37	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509	
+P38816	UniProtKB	Nucleotide binding	56	68	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509	
+P38816	UniProtKB	Nucleotide binding	63	64	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509	
+P38816	UniProtKB	Nucleotide binding	311	320	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509	
+P38816	UniProtKB	Nucleotide binding	318	320	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509	
+P38816	UniProtKB	Binding site	68	68	.	.	.	Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509	
+P38816	UniProtKB	Binding site	77	77	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509	
+P38816	UniProtKB	Binding site	110	110	.	.	.	Note=FAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509	
+P38816	UniProtKB	Binding site	168	168	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509	
+P38816	UniProtKB	Binding site	311	311	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509	
+P38816	UniProtKB	Disulfide bond	165	168	.	.	.	Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509	
+##sequence-region P53044 1 361
+P53044	UniProtKB	Chain	1	361	.	.	.	ID=PRO_0000194989;Note=Ubiquitin fusion degradation protein 1	
+P53044	UniProtKB	Region	27	28	.	.	.	Note=Monoubiquitin-binding	
+P53044	UniProtKB	Region	30	32	.	.	.	Note=Monoubiquitin-binding	
+P53044	UniProtKB	Region	99	101	.	.	.	Note=Monoubiquitin-binding	
+P53044	UniProtKB	Site	37	37	.	.	.	Note=Monoubiquitin-binding	
+P53044	UniProtKB	Site	39	39	.	.	.	Note=Monoubiquitin-binding	
+P53044	UniProtKB	Site	109	109	.	.	.	Note=Monoubiquitin-binding	
+P53044	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53044	UniProtKB	Mutagenesis	94	94	.	.	.	Note=In UFD1-1%3B grows more slowly. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P53044	UniProtKB	Beta strand	19	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Helix	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Turn	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Helix	40	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Beta strand	45	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Helix	52	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Beta strand	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Turn	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Beta strand	79	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Helix	98	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Beta strand	111	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Beta strand	123	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Helix	131	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Helix	140	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Beta strand	154	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Beta strand	167	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+P53044	UniProtKB	Beta strand	192	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1	
+##sequence-region P33202 1 1483
+P33202	UniProtKB	Chain	1	1483	.	.	.	ID=PRO_0000194998;Note=Ubiquitin fusion degradation protein 4	
+P33202	UniProtKB	Domain	1376	1483	.	.	.	Note=HECT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104	
+P33202	UniProtKB	Region	1007	1081	.	.	.	Note=K-box	
+P33202	UniProtKB	Compositional bias	898	901	.	.	.	Note=Poly-Glu	
+P33202	UniProtKB	Active site	1450	1450	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104	
+P33202	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33202	UniProtKB	Cross-link	349	349	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P26370 1 528
+P26370	UniProtKB	Chain	1	528	.	.	.	ID=PRO_0000114986;Note=Transcriptional activator protein UGA3	
+P26370	UniProtKB	DNA binding	17	44	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P26370	UniProtKB	Motif	55	62	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P26370	UniProtKB	Mutagenesis	224	224	.	.	.	Note=Constitutive activity%3B when associated with R-451. G->R	
+P26370	UniProtKB	Mutagenesis	451	451	.	.	.	Note=Loss of activity. Constitutive activity%3B when associated with R-224. G->R	
+##sequence-region P36137 1 443
+P36137	UniProtKB	Signal peptide	1	27	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36137	UniProtKB	Chain	28	443	.	.	.	ID=PRO_0000203212;Note=Protein UIP5	
+P36137	UniProtKB	Topological domain	28	398	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36137	UniProtKB	Transmembrane	399	420	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36137	UniProtKB	Topological domain	421	443	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q02724 1 621
+Q02724	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q02724	UniProtKB	Chain	2	621	.	.	.	ID=PRO_0000101731;Note=Ubiquitin-like-specific protease 1	
+Q02724	UniProtKB	Region	432	621	.	.	.	Note=Protease;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882122;Dbxref=PMID:10882122	
+Q02724	UniProtKB	Active site	514	514	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882122;Dbxref=PMID:10882122	
+Q02724	UniProtKB	Active site	531	531	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882122;Dbxref=PMID:10882122	
+Q02724	UniProtKB	Active site	580	580	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882122;Dbxref=PMID:10882122	
+Q02724	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q02724	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q02724	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q02724	UniProtKB	Modified residue	179	179	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q02724	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02724	UniProtKB	Helix	409	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Beta strand	426	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Beta strand	433	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Helix	437	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Helix	441	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Helix	451	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Beta strand	468	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Helix	474	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Helix	484	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Turn	487	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Helix	492	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Helix	498	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Beta strand	502	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Turn	511	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Beta strand	514	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Turn	522	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Beta strand	526	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Helix	539	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Beta strand	558	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Beta strand	565	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Beta strand	575	578	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Helix	580	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Helix	601	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+Q02724	UniProtKB	Turn	617	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV	
+##sequence-region Q05776 1 175
+Q05776	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000271269;Note=Protein UPS1%2C mitochondrial	
+Q05776	UniProtKB	Domain	2	172	.	.	.	Note=PRELI/MSF1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00158	
+Q05776	UniProtKB	Region	1	80	.	.	.	Note=Required for mitochondrial targeting;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16754953;Dbxref=PMID:16754953	
+Q05776	UniProtKB	Binding site	26	26	.	.	.	Note=Phosphatidic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513	
+Q05776	UniProtKB	Binding site	58	58	.	.	.	Note=Phosphatidic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513	
+Q05776	UniProtKB	Binding site	148	148	.	.	.	Note=Phosphatidic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Binding site	152	152	.	.	.	Note=Phosphatidic acid;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26071601,ECO:0000269|PubMed:26235513;Dbxref=PMID:26071601,PMID:26235513	
+Q05776	UniProtKB	Mutagenesis	23	23	.	.	.	Note=Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	25	25	.	.	.	Note=Nearly abolishes phosphatidic acid transfer activity. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513	
+Q05776	UniProtKB	Mutagenesis	25	25	.	.	.	Note=No effect on phosphatidic acid transfer activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513	
+Q05776	UniProtKB	Mutagenesis	33	33	.	.	.	Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-58%3B E-61%3B E-148 and E-155. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	42	42	.	.	.	Note=Impairs interaction with MDM35. Reduces ability to complement the mitochondrial defects of UPS1-deficient cells. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	50	50	.	.	.	Note=Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Decreases phosphatidic acid transfer activity and impairs cardiolipin biosynthesis. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071602;Dbxref=PMID:26071602	
+Q05776	UniProtKB	Mutagenesis	58	58	.	.	.	Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-33%3B E-61%3B E-148 and E-155. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	61	61	.	.	.	Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-33%3B E-58%3B E-148 and E-155. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	61	61	.	.	.	Note=Nearly abolishes phosphatidic acid transfer activity%3B when associated with E-155. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513	
+Q05776	UniProtKB	Mutagenesis	62	62	.	.	.	Note=Decreases phosphatidic acid binding and impairs cardiolipin biosynthesis%3B when associated with A-65. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071602;Dbxref=PMID:26071602	
+Q05776	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Decreases phosphatidic acid binding and impairs cardiolipin biosynthesis%3B when associated with A-62. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071602;Dbxref=PMID:26071602	
+Q05776	UniProtKB	Mutagenesis	77	77	.	.	.	Note=Impairs interaction with MDM35. Reduces ability to complement the mitochondrial defects of UPS1-deficient cells. W->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Failure to complement the mitochondrial defects of UPS1-deficient cells. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	84	84	.	.	.	Note=Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	96	96	.	.	.	Note=Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Failure to complement the mitochondrial defects of UPS1-deficient cells. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-144. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Failure to complement the mitochondrial defects of UPS1-deficient cells. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	144	144	.	.	.	Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-104. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	148	148	.	.	.	Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-33%3B E-58%3B E-61 and E-155. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	155	155	.	.	.	Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-33%3B E-58%3B E-61 and E-148. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601	
+Q05776	UniProtKB	Mutagenesis	155	155	.	.	.	Note=Nearly abolishes phosphatidic acid transfer activity%3B when associated with E-61. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513	
+Q05776	UniProtKB	Beta strand	2	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Helix	15	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Beta strand	34	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Beta strand	50	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Turn	64	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Beta strand	75	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Turn	86	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Beta strand	90	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Turn	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Beta strand	105	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Turn	116	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Beta strand	120	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Helix	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+Q05776	UniProtKB	Helix	137	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+##sequence-region P28274 1 579
+P28274	UniProtKB	Chain	1	579	.	.	.	ID=PRO_0000138283;Note=CTP synthase 1	
+P28274	UniProtKB	Domain	305	559	.	.	.	Note=Glutamine amidotransferase type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P28274	UniProtKB	Active site	404	404	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P28274	UniProtKB	Active site	535	535	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P28274	UniProtKB	Active site	537	537	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P28274	UniProtKB	Cross-link	422	422	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P28274	UniProtKB	Sequence conflict	307	307	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28274	UniProtKB	Sequence conflict	418	418	.	.	.	Note=V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38627 1 578
+P38627	UniProtKB	Chain	1	578	.	.	.	ID=PRO_0000138284;Note=CTP synthase 2	
+P38627	UniProtKB	Domain	305	564	.	.	.	Note=Glutamine amidotransferase type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P38627	UniProtKB	Active site	404	404	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P38627	UniProtKB	Active site	537	537	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P38627	UniProtKB	Active site	539	539	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P38627	UniProtKB	Mutagenesis	161	161	.	.	.	Note=Increases the specific activity 2-fold and decreases sensitivity to CTP product inhibition 5-fold. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9668079;Dbxref=PMID:9668079	
+P38627	UniProtKB	Mutagenesis	233	233	.	.	.	Note=No effect on activity and product inhibition by CTP. H->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9668079;Dbxref=PMID:9668079	
+P38627	UniProtKB	Sequence conflict	96	97	.	.	.	Note=HV->QL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38627	UniProtKB	Sequence conflict	204	204	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38627	UniProtKB	Sequence conflict	440	446	.	.	.	Note=QVVIYMP->PSSHIHA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38627	UniProtKB	Sequence conflict	557	563	.	.	.	Note=AASGTLG->QLRHTC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05946 1 817
+Q05946	UniProtKB	Chain	1	817	.	.	.	ID=PRO_0000051320;Note=U3 small nucleolar RNA-associated protein 13	
+Q05946	UniProtKB	Repeat	59	100	.	.	.	Note=WD 1	
+Q05946	UniProtKB	Repeat	102	139	.	.	.	Note=WD 2	
+Q05946	UniProtKB	Repeat	142	187	.	.	.	Note=WD 3	
+Q05946	UniProtKB	Repeat	191	233	.	.	.	Note=WD 4	
+Q05946	UniProtKB	Repeat	238	280	.	.	.	Note=WD 5	
+Q05946	UniProtKB	Repeat	386	425	.	.	.	Note=WD 6	
+Q05946	UniProtKB	Repeat	432	476	.	.	.	Note=WD 7	
+Q05946	UniProtKB	Repeat	489	528	.	.	.	Note=WD 8	
+Q05946	UniProtKB	Repeat	531	572	.	.	.	Note=WD 9	
+Q05946	UniProtKB	Repeat	573	614	.	.	.	Note=WD 10	
+Q05946	UniProtKB	Repeat	616	654	.	.	.	Note=WD 11	
+Q05946	UniProtKB	Repeat	664	705	.	.	.	Note=WD 12	
+##sequence-region Q04305 1 513
+Q04305	UniProtKB	Chain	1	513	.	.	.	ID=PRO_0000051328;Note=U3 small nucleolar RNA-associated protein 15	
+Q04305	UniProtKB	Repeat	37	78	.	.	.	Note=WD 1	
+Q04305	UniProtKB	Repeat	79	118	.	.	.	Note=WD 2	
+Q04305	UniProtKB	Repeat	124	162	.	.	.	Note=WD 3	
+Q04305	UniProtKB	Repeat	166	206	.	.	.	Note=WD 4	
+Q04305	UniProtKB	Repeat	210	247	.	.	.	Note=WD 5	
+Q04305	UniProtKB	Repeat	250	294	.	.	.	Note=WD 6	
+##sequence-region P40362 1 594
+P40362	UniProtKB	Chain	1	594	.	.	.	ID=PRO_0000051330;Note=U3 small nucleolar RNA-associated protein 18	
+P40362	UniProtKB	Repeat	246	285	.	.	.	Note=WD 1	
+P40362	UniProtKB	Repeat	290	334	.	.	.	Note=WD 2	
+P40362	UniProtKB	Repeat	463	504	.	.	.	Note=WD 3	
+P40362	UniProtKB	Repeat	513	554	.	.	.	Note=WD 4	
+P40362	UniProtKB	Repeat	560	593	.	.	.	Note=WD 5	
+P40362	UniProtKB	Region	101	190	.	.	.	Note=Interaction with UTP21;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+P40362	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40362	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P35194 1 2493
+P35194	UniProtKB	Chain	1	2493	.	.	.	ID=PRO_0000202465;Note=U3 small nucleolar RNA-associated protein 20	
+P35194	UniProtKB	Repeat	227	264	.	.	.	Note=HEAT 1	
+P35194	UniProtKB	Repeat	495	532	.	.	.	Note=HEAT 2	
+P35194	UniProtKB	Repeat	576	613	.	.	.	Note=HEAT 3	
+P35194	UniProtKB	Repeat	845	882	.	.	.	Note=HEAT 4	
+P35194	UniProtKB	Repeat	1176	1214	.	.	.	Note=HEAT 5	
+P35194	UniProtKB	Repeat	1216	1252	.	.	.	Note=HEAT 6	
+P35194	UniProtKB	Repeat	1342	1380	.	.	.	Note=HEAT 7	
+P35194	UniProtKB	Repeat	1393	1430	.	.	.	Note=HEAT 8	
+P35194	UniProtKB	Repeat	1480	1520	.	.	.	Note=HEAT 9	
+P35194	UniProtKB	Repeat	1522	1558	.	.	.	Note=HEAT 10	
+P35194	UniProtKB	Repeat	1588	1625	.	.	.	Note=HEAT 11	
+P35194	UniProtKB	Repeat	1630	1667	.	.	.	Note=HEAT 12	
+P35194	UniProtKB	Repeat	1890	1927	.	.	.	Note=HEAT 13	
+P35194	UniProtKB	Repeat	1953	1992	.	.	.	Note=HEAT 14	
+P35194	UniProtKB	Repeat	2120	2157	.	.	.	Note=HEAT 15	
+P35194	UniProtKB	Repeat	2358	2397	.	.	.	Note=HEAT 16	
+P35194	UniProtKB	Sequence conflict	2440	2440	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40498 1 721
+P40498	UniProtKB	Chain	1	721	.	.	.	ID=PRO_0000202974;Note=U3 small nucleolar RNA-associated protein 25	
+P40498	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40498	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40498	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q02354 1 440
+Q02354	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000205765;Note=U3 small nucleolar RNA-associated protein 6	
+Q02354	UniProtKB	Repeat	87	119	.	.	.	Note=HAT 1	
+Q02354	UniProtKB	Repeat	124	156	.	.	.	Note=HAT 2	
+Q02354	UniProtKB	Repeat	159	191	.	.	.	Note=HAT 3	
+Q02354	UniProtKB	Sequence conflict	138	140	.	.	.	Note=KLH->SA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08474 1 114
+Q08474	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000065758;Note=Vacuolar morphogenesis protein 10	
+##sequence-region P16140 1 517
+P16140	UniProtKB	Chain	1	517	.	.	.	ID=PRO_0000144648;Note=V-type proton ATPase subunit B	
+P16140	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956	
+P16140	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P16140	UniProtKB	Modified residue	503	503	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P16140	UniProtKB	Modified residue	504	504	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P16140	UniProtKB	Modified residue	511	511	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P16140	UniProtKB	Modified residue	515	515	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P16140	UniProtKB	Cross-link	14	14	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P16140	UniProtKB	Cross-link	508	508	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P16140	UniProtKB	Sequence conflict	14	14	.	.	.	Note=K->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16140	UniProtKB	Sequence conflict	79	79	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16140	UniProtKB	Sequence conflict	227	227	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16140	UniProtKB	Sequence conflict	500	517	.	.	.	Note=DTRSSGKKKDASQEESLI->TQEAPVRRRTPAKKNL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38358 1 474
+P38358	UniProtKB	Chain	1	474	.	.	.	ID=PRO_0000173423;Note=Vacuolar basic amino acid transporter 2	
+P38358	UniProtKB	Topological domain	1	33	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	55	62	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	63	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	86	97	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	119	121	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	143	167	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	189	196	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	197	217	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	218	238	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	239	259	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	260	273	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	274	294	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	295	303	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	304	324	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	325	331	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	332	352	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	353	375	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	376	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	397	447	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Transmembrane	448	468	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Topological domain	469	474	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38358	UniProtKB	Glycosylation	420	420	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04602 1 768
+Q04602	UniProtKB	Chain	1	768	.	.	.	ID=PRO_0000252272;Note=Vacuolar basic amino acid transporter 4	
+Q04602	UniProtKB	Topological domain	1	252	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	253	273	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	274	282	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	283	305	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	306	311	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	312	331	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	332	334	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	335	357	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	358	375	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	376	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	397	406	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	407	427	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	428	447	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	448	468	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	469	481	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	482	502	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	503	522	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	523	543	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	544	562	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	563	583	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	584	587	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	588	608	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	609	617	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	618	638	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	639	653	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	654	674	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	675	734	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Transmembrane	735	755	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Topological domain	756	768	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Coiled coil	9	40	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04602	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q04602	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04602	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04602	UniProtKB	Modified residue	192	192	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04602	UniProtKB	Glycosylation	480	480	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04602	UniProtKB	Glycosylation	553	553	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39538 1 1254
+P39538	UniProtKB	Chain	1	1254	.	.	.	ID=PRO_0000080597;Note=Ubiquitin carboxyl-terminal hydrolase 12	
+P39538	UniProtKB	Domain	97	199	.	.	.	Note=DUSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00613	
+P39538	UniProtKB	Domain	364	1110	.	.	.	Note=USP	
+P39538	UniProtKB	Active site	373	373	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P39538	UniProtKB	Active site	1068	1068	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P39538	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39538	UniProtKB	Modified residue	1160	1160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q01477 1 912
+Q01477	UniProtKB	Chain	1	912	.	.	.	ID=PRO_0000080588;Note=Ubiquitin carboxyl-terminal hydrolase 3	
+Q01477	UniProtKB	Domain	460	911	.	.	.	Note=USP	
+Q01477	UniProtKB	Active site	469	469	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+Q01477	UniProtKB	Active site	861	861	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+Q01477	UniProtKB	Beta strand	208	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+Q01477	UniProtKB	Helix	214	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+##sequence-region P39967 1 754
+P39967	UniProtKB	Chain	1	754	.	.	.	ID=PRO_0000080594;Note=Ubiquitin carboxyl-terminal hydrolase 9	
+P39967	UniProtKB	Domain	134	667	.	.	.	Note=USP	
+P39967	UniProtKB	Active site	143	143	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P39967	UniProtKB	Active site	618	618	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+##sequence-region Q12229 1 455
+Q12229	UniProtKB	Chain	1	455	.	.	.	ID=PRO_0000211000;Note=UBX domain-containing protein 3	
+Q12229	UniProtKB	Domain	356	455	.	.	.	Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215	
+##sequence-region P47049 1 396
+P47049	UniProtKB	Chain	1	396	.	.	.	ID=PRO_0000211003;Note=UBX domain-containing protein 6	
+P47049	UniProtKB	Domain	186	264	.	.	.	Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215	
+P47049	UniProtKB	Modified residue	369	369	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40554 1 99
+P40554	UniProtKB	Chain	1	99	.	.	.	ID=PRO_0000203002;Note=Ubiquitin-related modifier 1	
+P40554	UniProtKB	Modified residue	99	99	.	.	.	Note=1-thioglycine;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03048,ECO:0000269|PubMed:18491921,ECO:0000269|PubMed:19145231,ECO:0000269|PubMed:19151091;Dbxref=PMID:18491921,PMID:19145231,PMID:19151091	
+P40554	UniProtKB	Cross-link	99	99	.	.	.	Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03048	
+P40554	UniProtKB	Mutagenesis	98	99	.	.	.	Note=Abolishes thiocarboxylation and function in 2-Thiolation of tRNA. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19151091;Dbxref=PMID:19151091	
+P40554	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Abolishes URM1 conjugate formation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10713047;Dbxref=PMID:10713047	
+P40554	UniProtKB	Beta strand	2	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL	
+P40554	UniProtKB	Helix	12	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL	
+P40554	UniProtKB	Turn	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL	
+P40554	UniProtKB	Beta strand	21	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL	
+P40554	UniProtKB	Helix	34	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL	
+P40554	UniProtKB	Helix	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL	
+P40554	UniProtKB	Helix	52	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL	
+P40554	UniProtKB	Beta strand	56	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PKO	
+P40554	UniProtKB	Beta strand	65	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL	
+P40554	UniProtKB	Helix	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL	
+P40554	UniProtKB	Helix	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL	
+P40554	UniProtKB	Beta strand	89	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL	
+##sequence-region Q04500 1 899
+Q04500	UniProtKB	Chain	1	899	.	.	.	ID=PRO_0000065742;Note=U3 small nucleolar RNA-associated protein 14	
+Q04500	UniProtKB	Nucleotide binding	260	267	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04500	UniProtKB	Compositional bias	162	168	.	.	.	Note=Poly-Ser	
+Q04500	UniProtKB	Compositional bias	179	182	.	.	.	Note=Poly-Glu	
+Q04500	UniProtKB	Compositional bias	704	712	.	.	.	Note=Poly-Lys	
+Q04500	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04500	UniProtKB	Modified residue	35	35	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04500	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04500	UniProtKB	Modified residue	423	423	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04500	UniProtKB	Modified residue	424	424	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04500	UniProtKB	Modified residue	488	488	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q04500	UniProtKB	Modified residue	500	500	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q04500	UniProtKB	Modified residue	562	562	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04500	UniProtKB	Modified residue	668	668	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+Q04500	UniProtKB	Modified residue	738	738	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q12339 1 254
+Q12339	UniProtKB	Chain	1	254	.	.	.	ID=PRO_0000245250;Note=rRNA-processing protein UTP23	
+Q12339	UniProtKB	Compositional bias	188	239	.	.	.	Note=Lys-rich	
+Q12339	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12339	UniProtKB	Helix	4	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Beta strand	24	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Helix	32	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Helix	45	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Beta strand	57	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Helix	63	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Helix	75	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Beta strand	84	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Beta strand	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Helix	99	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Beta strand	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Helix	124	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Beta strand	138	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Beta strand	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+Q12339	UniProtKB	Helix	153	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7	
+##sequence-region P43123 1 477
+P43123	UniProtKB	Chain	1	477	.	.	.	ID=PRO_0000185773;Note=UDP-N-acetylglucosamine pyrophosphorylase	
+P43123	UniProtKB	Region	109	112	.	.	.	Note=UTP binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P43123	UniProtKB	Motif	109	112	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43123	UniProtKB	Motif	302	303	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43123	UniProtKB	Binding site	123	123	.	.	.	Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P43123	UniProtKB	Binding site	194	194	.	.	.	Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P43123	UniProtKB	Binding site	221	221	.	.	.	Note=UTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P43123	UniProtKB	Binding site	222	222	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43123	UniProtKB	Binding site	252	252	.	.	.	Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P43123	UniProtKB	Binding site	377	377	.	.	.	Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P43123	UniProtKB	Binding site	409	409	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43123	UniProtKB	Modified residue	218	218	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43123	UniProtKB	Modified residue	461	461	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43123	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Decrease of activity. G->A	
+P43123	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Loss of activity. G->A	
+P43123	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Decrease of activity. G->A	
+P43123	UniProtKB	Mutagenesis	115	115	.	.	.	Note=Decrease of activity. T->A	
+P43123	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Loss of activity. R->A	
+P43123	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Decrease of activity. L->A	
+P43123	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Decrease of activity. P->A	
+P43123	UniProtKB	Mutagenesis	123	123	.	.	.	Note=Loss of activity. K->A	
+##sequence-region P52490 1 153
+P52490	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000082565;Note=Ubiquitin-conjugating enzyme E2 13	
+P52490	UniProtKB	Active site	87	87	.	.	.	Note=Glycyl thioester intermediate	
+P52490	UniProtKB	Cross-link	92	92	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P52490	UniProtKB	Mutagenesis	55	55	.	.	.	Note=Strongly reduces MMS2 binding and interferes with error-free DNA repair. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11440714;Dbxref=PMID:11440714	
+P52490	UniProtKB	Mutagenesis	81	81	.	.	.	Note=Abolishes ubiquitin chain elongation. No effect on thioester formation at the active site. D->R	
+P52490	UniProtKB	Mutagenesis	110	110	.	.	.	Note=Lowers rate of ubiquitin chain elongation. No effect on thioester formation at the active site. A->R	
+P52490	UniProtKB	Helix	6	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Beta strand	23	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Beta strand	31	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Turn	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Beta strand	50	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Turn	60	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Beta strand	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Helix	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Turn	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Helix	101	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Helix	126	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Helix	133	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P52490	UniProtKB	Beta strand	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+##sequence-region Q02159 1 165
+Q02159	UniProtKB	Chain	1	165	.	.	.	ID=PRO_0000082554;Note=Ubiquitin-conjugating enzyme E2 7	
+Q02159	UniProtKB	Active site	89	89	.	.	.	Note=Glycyl thioester intermediate	
+Q02159	UniProtKB	Cross-link	89	89	.	.	.	Note=Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17310239;Dbxref=PMID:17310239	
+Q02159	UniProtKB	Mutagenesis	39	39	.	.	.	Note=No effect%3B when associated with S-141. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17310239;Dbxref=PMID:17310239	
+Q02159	UniProtKB	Mutagenesis	81	81	.	.	.	Note=Impairs degradation of UBC7-substrates%2C but does not prevent protein degradation. N->A	
+Q02159	UniProtKB	Mutagenesis	89	89	.	.	.	Note=Prevents polyubiquitin chain attachment and protein degradation. C->A%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17310239;Dbxref=PMID:17310239	
+Q02159	UniProtKB	Mutagenesis	141	141	.	.	.	Note=No effect%3B when associated with S-39. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17310239;Dbxref=PMID:17310239	
+Q02159	UniProtKB	Helix	2	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Beta strand	24	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Beta strand	33	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Turn	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Beta strand	53	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Turn	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Beta strand	70	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Beta strand	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UCZ	
+Q02159	UniProtKB	Turn	105	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UCZ	
+Q02159	UniProtKB	Helix	116	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Helix	138	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+Q02159	UniProtKB	Helix	148	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+##sequence-region Q12059 1 462
+Q12059	UniProtKB	Chain	1	462	.	.	.	ID=PRO_0000194962;Note=NEDD8-activating enzyme E1 regulatory subunit	
+##sequence-region Q08562 1 1619
+Q08562	UniProtKB	Chain	1	1619	.	.	.	ID=PRO_0000268702;Note=ATP-dependent helicase ULS1	
+Q08562	UniProtKB	Domain	956	1157	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q08562	UniProtKB	Domain	1447	1606	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q08562	UniProtKB	Nucleotide binding	969	976	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q08562	UniProtKB	Zinc finger	1330	1386	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q08562	UniProtKB	Motif	7	10	.	.	.	Note=SUMO interacting motif%3B type a 1	
+Q08562	UniProtKB	Motif	371	378	.	.	.	Note=SUMO interacting motif%3B type b 1	
+Q08562	UniProtKB	Motif	470	473	.	.	.	Note=SUMO interacting motif%3B type a 2	
+Q08562	UniProtKB	Motif	543	550	.	.	.	Note=SUMO interacting motif%3B type b 2	
+Q08562	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q03010 1 460
+Q03010	UniProtKB	Chain	1	460	.	.	.	ID=PRO_0000051315;Note=Transcriptional regulatory protein UME1	
+Q03010	UniProtKB	Repeat	233	271	.	.	.	Note=WD 1	
+Q03010	UniProtKB	Repeat	276	316	.	.	.	Note=WD 2	
+Q03010	UniProtKB	Repeat	339	379	.	.	.	Note=WD 3	
+Q03010	UniProtKB	Repeat	411	451	.	.	.	Note=WD 4	
+Q03010	UniProtKB	Motif	14	22	.	.	.	Note=NEE-box	
+##sequence-region P25386 1 1790
+P25386	UniProtKB	Chain	1	1790	.	.	.	ID=PRO_0000065730;Note=Intracellular protein transport protein USO1	
+P25386	UniProtKB	Repeat	45	89	.	.	.	Note=ARM 1	
+P25386	UniProtKB	Repeat	127	170	.	.	.	Note=ARM 2	
+P25386	UniProtKB	Repeat	173	213	.	.	.	Note=ARM 3	
+P25386	UniProtKB	Repeat	215	260	.	.	.	Note=ARM 4	
+P25386	UniProtKB	Repeat	261	312	.	.	.	Note=ARM 5	
+P25386	UniProtKB	Repeat	314	362	.	.	.	Note=ARM 6	
+P25386	UniProtKB	Repeat	363	429	.	.	.	Note=ARM 7	
+P25386	UniProtKB	Repeat	431	512	.	.	.	Note=ARM 8	
+P25386	UniProtKB	Repeat	543	584	.	.	.	Note=ARM 9	
+P25386	UniProtKB	Repeat	586	630	.	.	.	Note=ARM 10	
+P25386	UniProtKB	Region	1	724	.	.	.	Note=Globular head	
+P25386	UniProtKB	Region	465	487	.	.	.	Note=Charged (hyper-hydrophilic)	
+P25386	UniProtKB	Region	991	1790	.	.	.	Note=Dispensable for the protein function	
+P25386	UniProtKB	Coiled coil	725	1790	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25386	UniProtKB	Compositional bias	1172	1786	.	.	.	Note=Asp/Glu-rich (acidic)	
+P25386	UniProtKB	Modified residue	1770	1770	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25386	UniProtKB	Sequence conflict	390	391	.	.	.	Note=NG->TA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25386	UniProtKB	Sequence conflict	725	725	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25386	UniProtKB	Sequence conflict	847	847	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25386	UniProtKB	Sequence conflict	924	924	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25386	UniProtKB	Sequence conflict	1253	1253	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25386	UniProtKB	Sequence conflict	1319	1319	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25386	UniProtKB	Sequence conflict	1461	1461	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25386	UniProtKB	Sequence conflict	1581	1581	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25386	UniProtKB	Sequence conflict	1600	1600	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25386	UniProtKB	Sequence conflict	1661	1661	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25386	UniProtKB	Sequence conflict	1772	1772	.	.	.	Note=D->DEEDDEE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P42945 1 1769
+P42945	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P42945	UniProtKB	Chain	2	1769	.	.	.	ID=PRO_0000186207;Note=U3 small nucleolar RNA-associated protein 10	
+P42945	UniProtKB	Repeat	1729	1767	.	.	.	Note=HEAT	
+P42945	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q06078 1 939
+Q06078	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06078	UniProtKB	Chain	2	939	.	.	.	ID=PRO_0000051480;Note=U3 small nucleolar RNA-associated protein 21	
+Q06078	UniProtKB	Repeat	40	71	.	.	.	Note=WD 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	81	111	.	.	.	Note=WD 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	119	158	.	.	.	Note=WD 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	168	201	.	.	.	Note=WD 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	208	245	.	.	.	Note=WD 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	252	287	.	.	.	Note=WD 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	295	347	.	.	.	Note=WD 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	354	388	.	.	.	Note=WD 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	415	454	.	.	.	Note=WD 9;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	463	497	.	.	.	Note=WD 10;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	505	541	.	.	.	Note=WD 11;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	546	581	.	.	.	Note=WD 12;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	583	624	.	.	.	Note=WD 13;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Repeat	626	664	.	.	.	Note=WD 14;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140	
+Q06078	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06078	UniProtKB	Modified residue	772	772	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06078	UniProtKB	Beta strand	22	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	40	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	47	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	58	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Turn	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	82	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	89	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	97	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	105	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	113	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	118	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	127	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	135	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	152	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Turn	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	165	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	179	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	188	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Turn	193	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	198	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	209	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	220	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Turn	235	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	239	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	251	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	263	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	273	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Turn	278	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	282	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Helix	293	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	299	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	307	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	315	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	341	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	353	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	365	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	375	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	386	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	414	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Turn	422	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	430	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	438	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Turn	445	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	449	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	458	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	463	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	474	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	482	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Turn	489	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	494	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	505	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	516	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	524	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	536	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	546	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Turn	553	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	557	562	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	567	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Turn	572	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	576	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	588	593	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	597	604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	607	613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Turn	614	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	619	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	629	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	640	647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+Q06078	UniProtKB	Beta strand	649	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX	
+##sequence-region P53254 1 1237
+P53254	UniProtKB	Chain	1	1237	.	.	.	ID=PRO_0000215651;Note=U3 small nucleolar RNA-associated protein 22	
+P53254	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P53254	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53254	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53254	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53254	UniProtKB	Helix	82	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	118	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	146	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	182	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	187	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	201	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	216	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	223	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	248	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	252	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	266	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	290	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	305	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	330	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	342	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	359	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	381	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	390	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	402	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	410	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	418	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	435	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	439	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	455	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	467	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	470	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	476	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	482	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	502	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	507	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	519	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	523	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	536	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	539	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	549	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	558	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	575	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	578	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	596	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	603	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	606	609	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	611	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	621	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	627	633	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	640	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	650	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	653	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	663	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	673	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	677	689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	695	697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	699	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	711	713	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	716	718	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	725	742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	750	755	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	758	761	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	779	786	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	796	817	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	821	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	838	843	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	849	855	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	859	869	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	872	874	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	875	889	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	892	903	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	909	922	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	926	928	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	931	943	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	954	967	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	970	972	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	1014	1030	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	1034	1036	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	1051	1055	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	1058	1078	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	1082	1088	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	1097	1103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	1109	1113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	1136	1142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	1145	1157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	1158	1160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	1161	1165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	1169	1172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Turn	1174	1177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	1179	1186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	1188	1190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	1204	1214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	1216	1227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Helix	1228	1230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P53254	UniProtKB	Beta strand	1231	1236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+##sequence-region Q04177 1 643
+Q04177	UniProtKB	Chain	1	643	.	.	.	ID=PRO_0000051318;Note=U3 small nucleolar RNA-associated protein 5	
+Q04177	UniProtKB	Repeat	14	54	.	.	.	Note=WD 1	
+Q04177	UniProtKB	Repeat	55	98	.	.	.	Note=WD 2	
+Q04177	UniProtKB	Repeat	186	225	.	.	.	Note=WD 3	
+Q04177	UniProtKB	Repeat	227	266	.	.	.	Note=WD 4	
+Q04177	UniProtKB	Repeat	340	389	.	.	.	Note=WD 5	
+Q04177	UniProtKB	Repeat	471	511	.	.	.	Note=WD 6	
+Q04177	UniProtKB	Compositional bias	568	643	.	.	.	Note=Glu-rich	
+##sequence-region P53276 1 713
+P53276	UniProtKB	Chain	1	713	.	.	.	ID=PRO_0000065743;Note=U3 small nucleolar RNA-associated protein 8	
+P53276	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53276	UniProtKB	Modified residue	148	148	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53276	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P21373 1 530
+P21373	UniProtKB	Chain	1	530	.	.	.	ID=PRO_0000120716;Note=NAD(+) kinase	
+P21373	UniProtKB	Modified residue	499	499	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P21373	UniProtKB	Modified residue	503	503	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P21373	UniProtKB	Sequence conflict	337	337	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35127 1 236
+P35127	UniProtKB	Chain	1	236	.	.	.	ID=PRO_0000211073;Note=Ubiquitin carboxyl-terminal hydrolase YUH1	
+P35127	UniProtKB	Region	10	15	.	.	.	Note=Interaction with ubiquitin	
+P35127	UniProtKB	Region	149	157	.	.	.	Note=Interaction with ubiquitin	
+P35127	UniProtKB	Region	219	228	.	.	.	Note=Interaction with ubiquitin	
+P35127	UniProtKB	Active site	90	90	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10091	
+P35127	UniProtKB	Active site	166	166	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10091	
+P35127	UniProtKB	Site	84	84	.	.	.	Note=Transition state stabilizer	
+P35127	UniProtKB	Site	181	181	.	.	.	Note=Important for enzyme activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35127	UniProtKB	Helix	15	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Beta strand	31	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Helix	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Beta strand	54	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Helix	90	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Helix	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Helix	111	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Beta strand	126	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Helix	132	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Helix	146	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Beta strand	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Beta strand	164	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Beta strand	174	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Beta strand	189	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Helix	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Helix	205	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+P35127	UniProtKB	Beta strand	227	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX	
+##sequence-region Q01476 1 1272
+Q01476	UniProtKB	Chain	1	1272	.	.	.	ID=PRO_0000080586;Note=Ubiquitin carboxyl-terminal hydrolase 2	
+Q01476	UniProtKB	Domain	736	1258	.	.	.	Note=USP	
+Q01476	UniProtKB	Active site	745	745	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+Q01476	UniProtKB	Active site	1209	1209	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+Q01476	UniProtKB	Modified residue	907	907	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q01476	UniProtKB	Sequence conflict	658	665	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43593 1 499
+P43593	UniProtKB	Chain	1	499	.	.	.	ID=PRO_0000080591;Note=Ubiquitin carboxyl-terminal hydrolase 6	
+P43593	UniProtKB	Domain	6	80	.	.	.	Note=Ubiquitin-like	
+P43593	UniProtKB	Domain	109	497	.	.	.	Note=USP	
+P43593	UniProtKB	Active site	118	118	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P43593	UniProtKB	Active site	447	447	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P43593	UniProtKB	Modified residue	389	389	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P43593	UniProtKB	Modified residue	470	470	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43593	UniProtKB	Helix	118	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	131	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	154	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	182	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	193	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	210	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	227	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Turn	231	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	235	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	246	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	257	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	272	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	297	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	307	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	317	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Turn	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	325	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	337	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	342	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	347	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	390	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	426	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	445	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	461	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	468	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	474	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Helix	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+P43593	UniProtKB	Beta strand	488	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV	
+##sequence-region P50102 1 471
+P50102	UniProtKB	Chain	1	471	.	.	.	ID=PRO_0000080593;Note=Ubiquitin carboxyl-terminal hydrolase 8	
+P50102	UniProtKB	Domain	137	468	.	.	.	Note=USP	
+P50102	UniProtKB	Zinc finger	44	105	.	.	.	Note=UBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
+P50102	UniProtKB	Active site	146	146	.	.	.	Note=Nucleophile	
+P50102	UniProtKB	Active site	427	427	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P50102	UniProtKB	Mutagenesis	46	46	.	.	.	Note=Lowers histone H2B deubiquitination activity%3B when associated with A-49. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657441;Dbxref=PMID:15657441	
+P50102	UniProtKB	Mutagenesis	49	49	.	.	.	Note=Lowers histone H2B deubiquitination activity%3B when associated with A-46. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657441;Dbxref=PMID:15657441	
+P50102	UniProtKB	Mutagenesis	77	77	.	.	.	Note=Lowers histone H2B deubiquitination activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657441;Dbxref=PMID:15657441	
+P50102	UniProtKB	Mutagenesis	146	146	.	.	.	Note=Lowers histone H2B deubiquitination activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657441;Dbxref=PMID:15657441	
+P50102	UniProtKB	Mutagenesis	419	419	.	.	.	Note=Lowers histone H2B deubiquitination activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657441;Dbxref=PMID:15657441	
+P50102	UniProtKB	Helix	5	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	14	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	36	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	54	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Turn	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	73	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	85	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Turn	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Turn	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	112	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	118	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	146	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	159	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	169	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Turn	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	183	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	214	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	231	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	238	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	260	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FK5	
+P50102	UniProtKB	Helix	274	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	281	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Turn	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	297	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	316	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	327	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FJC	
+P50102	UniProtKB	Turn	337	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FJC	
+P50102	UniProtKB	Beta strand	346	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	356	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	369	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M99	
+P50102	UniProtKB	Beta strand	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	384	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	389	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	409	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	425	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Turn	435	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FIP	
+P50102	UniProtKB	Beta strand	439	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	446	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Helix	452	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P50102	UniProtKB	Beta strand	460	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+##sequence-region P54730 1 416
+P54730	UniProtKB	Chain	1	416	.	.	.	ID=PRO_0000211001;Note=UBX domain-containing protein 4	
+P54730	UniProtKB	Domain	273	350	.	.	.	Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215	
+##sequence-region P36135 1 365
+P36135	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36135	UniProtKB	Chain	18	365	.	.	.	ID=PRO_0000194002;Note=Probable secreted beta-glucosidase UTH1	
+P36135	UniProtKB	Compositional bias	89	103	.	.	.	Note=Poly-Ser	
+##sequence-region Q12220 1 943
+Q12220	UniProtKB	Chain	1	943	.	.	.	ID=PRO_0000050955;Note=U3 small nucleolar RNA-associated protein 12	
+Q12220	UniProtKB	Repeat	77	107	.	.	.	Note=WD 1	
+Q12220	UniProtKB	Repeat	119	149	.	.	.	Note=WD 2	
+Q12220	UniProtKB	Repeat	161	190	.	.	.	Note=WD 3	
+Q12220	UniProtKB	Repeat	202	230	.	.	.	Note=WD 4	
+Q12220	UniProtKB	Repeat	389	418	.	.	.	Note=WD 5	
+Q12220	UniProtKB	Repeat	428	458	.	.	.	Note=WD 6	
+Q12220	UniProtKB	Repeat	471	501	.	.	.	Note=WD 7	
+Q12220	UniProtKB	Repeat	571	601	.	.	.	Note=WD 8	
+Q12220	UniProtKB	Repeat	613	643	.	.	.	Note=WD 9	
+Q12220	UniProtKB	Repeat	655	685	.	.	.	Note=WD 10	
+##sequence-region Q06679 1 776
+Q06679	UniProtKB	Chain	1	776	.	.	.	ID=PRO_0000051317;Note=U3 small nucleolar RNA-associated protein 4	
+Q06679	UniProtKB	Repeat	35	40	.	.	.	Note=WD 1	
+Q06679	UniProtKB	Repeat	132	169	.	.	.	Note=WD 2	
+Q06679	UniProtKB	Repeat	178	214	.	.	.	Note=WD 3	
+Q06679	UniProtKB	Repeat	230	266	.	.	.	Note=WD 4	
+Q06679	UniProtKB	Repeat	271	308	.	.	.	Note=WD 5	
+Q06679	UniProtKB	Repeat	417	452	.	.	.	Note=WD 6	
+##sequence-region P38882 1 575
+P38882	UniProtKB	Chain	1	575	.	.	.	ID=PRO_0000065744;Note=U3 small nucleolar RNA-associated protein 9	
+P38882	UniProtKB	Modified residue	547	547	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38882	UniProtKB	Modified residue	564	564	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P25591 1 423
+P25591	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25591	UniProtKB	Chain	2	423	.	.	.	ID=PRO_0000202554;Note=vacuole-related protein 17	
+P25591	UniProtKB	Region	110	170	.	.	.	Note=MYO2-binding	
+P25591	UniProtKB	Region	290	380	.	.	.	Note=VAC8-binding	
+P25591	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25591	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442	
+P25591	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442	
+P25591	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442	
+P25591	UniProtKB	Modified residue	248	248	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442	
+P25591	UniProtKB	Modified residue	269	269	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25591	UniProtKB	Mutagenesis	119	119	.	.	.	Note=Impairs phosphorylation%3B when associated with A-149%3B A-178 and A-248. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442	
+P25591	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Impairs phosphorylation%3B when associated with A-119%3B A-178 and A-248. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442	
+P25591	UniProtKB	Mutagenesis	178	178	.	.	.	Note=Impairs phosphorylation%3B when associated with A-119%3B A-149 and A-248. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442	
+P25591	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Stabilizes VAC17 whose protein levels are about 10-fold higher than wild-type. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442	
+P25591	UniProtKB	Mutagenesis	248	248	.	.	.	Note=Impairs phosphorylation%3B when associated with A-119%3B A-149 and A-178. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442	
+##sequence-region Q07468 1 1049
+Q07468	UniProtKB	Chain	1	1049	.	.	.	ID=PRO_0000065903;Note=Vacuolar morphogenesis protein 6	
+Q07468	UniProtKB	Repeat	730	896	.	.	.	Note=CHCR	
+##sequence-region P17255 1 1071
+P17255	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:11884132,ECO:0000269|Ref.6;Dbxref=PMID:22814378,PMID:11884132	
+P17255	UniProtKB	Chain	2	283	.	.	.	ID=PRO_0000002458;Note=V-type proton ATPase catalytic subunit A%2C 1st part	
+P17255	UniProtKB	Chain	284	737	.	.	.	ID=PRO_0000002459;Note=Endonuclease PI-SceI	
+P17255	UniProtKB	Chain	738	1071	.	.	.	ID=PRO_0000002460;Note=V-type proton ATPase catalytic subunit A%2C 2nd part	
+P17255	UniProtKB	Domain	494	642	.	.	.	Note=DOD-type homing endonuclease;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00273	
+P17255	UniProtKB	Nucleotide binding	257	264	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17255	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.6;Dbxref=PMID:22814378	
+P17255	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P17255	UniProtKB	Modified residue	858	858	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P17255	UniProtKB	Modified residue	928	928	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P17255	UniProtKB	Mutagenesis	284	284	.	.	.	Note=Reduces splicing reaction speed. Inhibits splicing%3B when associated with N-362%3B S-737 and S-738 in X10SSS VDE. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10828056,ECO:0000269|PubMed:11884132,ECO:0000269|PubMed:1417861;Dbxref=PMID:10828056,PMID:11884132,PMID:1417861	
+P17255	UniProtKB	Mutagenesis	362	362	.	.	.	Note=Inhibits splicing%3B when associated with S-284%3B S-737 and S-738 in X10SSS VDE. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11884132;Dbxref=PMID:11884132	
+P17255	UniProtKB	Mutagenesis	737	737	.	.	.	Note=Inhibits splicing%3B when associated with S-284%3B N-362 and S-738 in X10SSS VDE. N->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10828056,ECO:0000269|PubMed:11884132;Dbxref=PMID:10828056,PMID:11884132	
+P17255	UniProtKB	Mutagenesis	738	738	.	.	.	Note=Reduces splicing reaction speed. Inhibits splicing%3B when associated with S-284%3B N-362 and S-737 in X10SSS VDE. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11884132,ECO:0000269|PubMed:1417861;Dbxref=PMID:11884132,PMID:1417861	
+P17255	UniProtKB	Sequence conflict	875	875	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17255	UniProtKB	Beta strand	290	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Helix	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	309	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	315	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	325	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0	
+P17255	UniProtKB	Beta strand	347	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0	
+P17255	UniProtKB	Beta strand	355	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	363	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	372	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	382	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	398	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDE	
+P17255	UniProtKB	Beta strand	402	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Helix	415	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Helix	420	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	434	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Helix	444	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Helix	452	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	459	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Turn	471	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Beta strand	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDE	
+P17255	UniProtKB	Beta strand	485	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Helix	488	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Beta strand	506	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0	
+P17255	UniProtKB	Helix	516	528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Beta strand	531	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LWT	
+P17255	UniProtKB	Beta strand	534	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0	
+P17255	UniProtKB	Beta strand	538	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UM2	
+P17255	UniProtKB	Turn	541	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0	
+P17255	UniProtKB	Beta strand	544	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0	
+P17255	UniProtKB	Turn	556	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LWT	
+P17255	UniProtKB	Helix	570	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Beta strand	579	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Helix	588	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Helix	595	609	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Beta strand	610	613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0	
+P17255	UniProtKB	Beta strand	619	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Helix	627	639	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Beta strand	643	650	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Helix	654	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Beta strand	657	659	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0	
+P17255	UniProtKB	Beta strand	661	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Helix	672	678	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Turn	684	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA	
+P17255	UniProtKB	Helix	693	695	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	700	702	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	704	719	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	721	723	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0	
+P17255	UniProtKB	Beta strand	727	729	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+P17255	UniProtKB	Beta strand	733	735	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP	
+##sequence-region P38152 1 299
+P38152	UniProtKB	Chain	1	299	.	.	.	ID=PRO_0000090653;Note=Tricarboxylate transport protein	
+P38152	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38152	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38152	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38152	UniProtKB	Transmembrane	174	193	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38152	UniProtKB	Transmembrane	215	235	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38152	UniProtKB	Transmembrane	272	291	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38152	UniProtKB	Repeat	10	97	.	.	.	Note=Solcar 1	
+P38152	UniProtKB	Repeat	109	199	.	.	.	Note=Solcar 2	
+P38152	UniProtKB	Repeat	212	297	.	.	.	Note=Solcar 3	
+P38152	UniProtKB	Sequence conflict	97	97	.	.	.	Note=M->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38152	UniProtKB	Sequence conflict	101	101	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04235 1 462
+Q04235	UniProtKB	Chain	1	462	.	.	.	ID=PRO_0000203264;Note=tRNA wybutosine-synthesizing protein 2	
+Q04235	UniProtKB	Region	305	306	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01021	
+Q04235	UniProtKB	Binding site	257	257	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01021	
+Q04235	UniProtKB	Binding site	264	264	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01021	
+##sequence-region P06104 1 172
+P06104	UniProtKB	Chain	1	172	.	.	.	ID=PRO_0000082540;Note=Ubiquitin-conjugating enzyme E2 2	
+P06104	UniProtKB	Compositional bias	150	172	.	.	.	Note=Asp/Glu-rich (acidic tail)	
+P06104	UniProtKB	Active site	88	88	.	.	.	Note=Glycyl thioester intermediate	
+P06104	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphoserine%3B by SGV1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:16307922;Dbxref=PMID:18407956,PMID:16307922	
+P06104	UniProtKB	Mutagenesis	1	9	.	.	.	Note=Prevents H3K4me3 formation. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12077605,ECO:0000269|PubMed:8436296;Dbxref=PMID:12077605,PMID:8436296	
+P06104	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Loss of activity. C->A%2CV;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12077605,ECO:0000269|PubMed:2157209;Dbxref=PMID:12077605,PMID:2157209	
+P06104	UniProtKB	Helix	4	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Beta strand	24	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Beta strand	32	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Turn	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Beta strand	52	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Turn	61	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Beta strand	69	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Beta strand	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Helix	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Turn	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Helix	102	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Helix	124	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+P06104	UniProtKB	Helix	134	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62	
+##sequence-region P39944 1 805
+P39944	UniProtKB	Chain	1	805	.	.	.	ID=PRO_0000080590;Note=Ubiquitin carboxyl-terminal hydrolase 5	
+P39944	UniProtKB	Domain	159	283	.	.	.	Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+P39944	UniProtKB	Domain	446	804	.	.	.	Note=USP	
+P39944	UniProtKB	Active site	455	455	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P39944	UniProtKB	Active site	761	761	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+##sequence-region P38349 1 436
+P38349	UniProtKB	Chain	1	436	.	.	.	ID=PRO_0000211004;Note=UBX domain-containing protein 7	
+P38349	UniProtKB	Domain	212	290	.	.	.	Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215	
+P38349	UniProtKB	Modified residue	388	388	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38349	UniProtKB	Cross-link	19	19	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P47108 1 1174
+P47108	UniProtKB	Chain	1	1174	.	.	.	ID=PRO_0000203094;Note=Nucleolar pre-ribosomal-associated protein 2	
+##sequence-region P53146 1 245
+P53146	UniProtKB	Chain	1	245	.	.	.	ID=PRO_0000215584;Note=Protein transport protein USE1	
+P53146	UniProtKB	Topological domain	1	218	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53146	UniProtKB	Transmembrane	219	239	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53146	UniProtKB	Topological domain	240	245	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53146	UniProtKB	Mutagenesis	183	183	.	.	.	Note=In USE1-0%3B slows down protein transport from the endoplasmic reticulum to the Golgi at 37 degrees Celsius. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12853481;Dbxref=PMID:12853481	
+##sequence-region P53177 1 273
+P53177	UniProtKB	Chain	1	273	.	.	.	ID=PRO_0000202769;Note=tRNA wybutosine-synthesizing protein 3	
+P53177	UniProtKB	Modified residue	26	26	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53177	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P22515 1 1024
+P22515	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P22515	UniProtKB	Chain	2	1024	.	.	.	ID=PRO_0000194977;Note=Ubiquitin-activating enzyme E1 1	
+P22515	UniProtKB	Repeat	27	164	.	.	.	Note=1-1	
+P22515	UniProtKB	Repeat	425	579	.	.	.	Note=1-2	
+P22515	UniProtKB	Nucleotide binding	544	545	.	.	.	Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24816100;Dbxref=PMID:24816100	
+P22515	UniProtKB	Region	27	579	.	.	.	Note=2 approximate repeats	
+P22515	UniProtKB	Active site	600	600	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10132,ECO:0000269|PubMed:24816100;Dbxref=PMID:24816100	
+P22515	UniProtKB	Binding site	444	444	.	.	.	Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24816100;Dbxref=PMID:24816100	
+P22515	UniProtKB	Binding site	470	470	.	.	.	Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24816100;Dbxref=PMID:24816100	
+P22515	UniProtKB	Binding site	481	481	.	.	.	Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24816100;Dbxref=PMID:24816100	
+P22515	UniProtKB	Binding site	494	494	.	.	.	Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24816100;Dbxref=PMID:24816100	
+P22515	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P22515	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P22515	UniProtKB	Modified residue	914	914	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22515	UniProtKB	Cross-link	595	595	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P22515	UniProtKB	Cross-link	608	608	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P22515	UniProtKB	Mutagenesis	912	912	.	.	.	Note=Strongly reduces formation of the thioester intermediate with ubiquitin%3B when associated with P-914. I->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18662542;Dbxref=PMID:18662542	
+P22515	UniProtKB	Mutagenesis	914	914	.	.	.	Note=Strongly reduces formation of the thioester intermediate with ubiquitin%3B when associated with P-912. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18662542;Dbxref=PMID:18662542	
+P22515	UniProtKB	Mutagenesis	1004	1004	.	.	.	Note=Strongly reduces formation of the thioester intermediate with ubiquitin. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18662542;Dbxref=PMID:18662542	
+P22515	UniProtKB	Mutagenesis	1014	1014	.	.	.	Note=Strongly reduces formation of the thioester intermediate with ubiquitin%3B when associated with K-1016. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18662542;Dbxref=PMID:18662542	
+P22515	UniProtKB	Mutagenesis	1016	1016	.	.	.	Note=Strongly reduces formation of the thioester intermediate with ubiquitin%3B when associated with K-1014. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18662542;Dbxref=PMID:18662542	
+P22515	UniProtKB	Sequence conflict	526	526	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22515	UniProtKB	Sequence conflict	736	736	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22515	UniProtKB	Helix	16	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	28	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	38	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	46	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	61	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	73	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	91	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	117	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	124	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	134	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	150	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	160	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	171	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	183	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	194	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	210	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	220	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	231	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	244	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	254	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	269	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	283	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	288	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Turn	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	316	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Turn	334	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	345	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Turn	354	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	360	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	387	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	394	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Turn	400	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Turn	407	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	418	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	426	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	436	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	444	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Turn	457	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	465	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	476	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	487	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	494	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	507	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Turn	510	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	513	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	522	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Turn	525	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	530	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	537	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	546	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	563	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	572	578	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Turn	580	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	586	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	599	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	609	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	626	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	640	647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	651	663	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	669	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	686	694	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	704	708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	725	742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	755	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	797	802	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	808	811	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	830	844	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	852	859	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	867	885	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	891	893	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	896	900	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Turn	901	904	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	905	909	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	916	919	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	922	925	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Turn	926	928	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	930	936	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	939	950	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	953	959	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	962	966	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	971	977	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Helix	982	990	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	1000	1008	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P22515	UniProtKB	Beta strand	1019	1023	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+##sequence-region Q99344 1 299
+Q99344	UniProtKB	Chain	1	299	.	.	.	ID=PRO_0000194950;Note=NEDD8-activating enzyme E1 catalytic subunit	
+Q99344	UniProtKB	Nucleotide binding	12	37	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99344	UniProtKB	Active site	168	168	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10132	
+Q99344	UniProtKB	Sequence conflict	33	33	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P52492 1 156
+P52492	UniProtKB	Chain	1	156	.	.	.	ID=PRO_0000082559;Note=Ubiquitin-conjugating enzyme E2-18 kDa	
+P52492	UniProtKB	Active site	93	93	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133	
+##sequence-region P52491 1 188
+P52491	UniProtKB	Chain	1	188	.	.	.	ID=PRO_0000082501;Note=NEDD8-conjugating enzyme UBC12	
+P52491	UniProtKB	Active site	115	115	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133	
+P52491	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21940857;Dbxref=PMID:21940857	
+P52491	UniProtKB	Helix	1	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Beta strand	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Helix	27	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Beta strand	45	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Beta strand	63	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Beta strand	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Turn	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Beta strand	80	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Turn	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Beta strand	96	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Beta strand	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Helix	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Turn	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Helix	129	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Helix	151	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+P52491	UniProtKB	Helix	161	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U	
+##sequence-region P15732 1 148
+P15732	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000082546;Note=Ubiquitin-conjugating enzyme E2-16 kDa	
+P15732	UniProtKB	Active site	86	86	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133	
+P15732	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15731	
+P15732	UniProtKB	Cross-link	91	91	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15731	
+##sequence-region P38187 1 747
+P38187	UniProtKB	Chain	1	747	.	.	.	ID=PRO_0000080598;Note=Ubiquitin carboxyl-terminal hydrolase 13	
+P38187	UniProtKB	Domain	140	668	.	.	.	Note=USP	
+P38187	UniProtKB	Active site	149	149	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P38187	UniProtKB	Active site	619	619	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P38187	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38187	UniProtKB	Sequence conflict	180	180	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25037 1 809
+P25037	UniProtKB	Chain	1	809	.	.	.	ID=PRO_0000080585;Note=Ubiquitin carboxyl-terminal hydrolase 1	
+P25037	UniProtKB	Domain	101	738	.	.	.	Note=USP	
+P25037	UniProtKB	Active site	110	110	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P25037	UniProtKB	Active site	697	697	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P25037	UniProtKB	Modified residue	530	530	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25037	UniProtKB	Modified residue	531	531	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25037	UniProtKB	Modified residue	555	555	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25037	UniProtKB	Modified residue	618	618	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25037	UniProtKB	Modified residue	638	638	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25037	UniProtKB	Modified residue	652	652	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25037	UniProtKB	Modified residue	653	653	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25037	UniProtKB	Modified residue	654	654	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25037	UniProtKB	Modified residue	670	670	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P25037	UniProtKB	Modified residue	755	755	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25037	UniProtKB	Sequence conflict	418	418	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38290 1 277
+P38290	UniProtKB	Chain	1	277	.	.	.	ID=PRO_0000065713;Note=Ubiquitin-conjugating enzyme suppressor 1	
+##sequence-region P32861 1 499
+P32861	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32861	UniProtKB	Chain	2	499	.	.	.	ID=PRO_0000185765;Note=UTP--glucose-1-phosphate uridylyltransferase	
+P32861	UniProtKB	Region	109	112	.	.	.	Note=UTP binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P32861	UniProtKB	Region	111	112	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16851	
+P32861	UniProtKB	Region	244	246	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16851	
+P32861	UniProtKB	Region	448	499	.	.	.	Note=Oligomerization	
+P32861	UniProtKB	Active site	388	388	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32861	UniProtKB	Metal binding	123	123	.	.	.	Note=Magnesium;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32861	UniProtKB	Metal binding	246	246	.	.	.	Note=Magnesium;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32861	UniProtKB	Binding site	123	123	.	.	.	Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P32861	UniProtKB	Binding site	186	186	.	.	.	Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P32861	UniProtKB	Binding site	215	215	.	.	.	Note=UTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P32861	UniProtKB	Binding site	216	216	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16851	
+P32861	UniProtKB	Binding site	246	246	.	.	.	Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P32861	UniProtKB	Binding site	388	388	.	.	.	Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P32861	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32861	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32861	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32861	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32861	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32861	UniProtKB	Modified residue	369	369	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23865587;Dbxref=PMID:23865587	
+P32861	UniProtKB	Helix	23	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	49	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Turn	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	104	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	134	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	154	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Turn	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	164	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	180	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Turn	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	202	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	216	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	219	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	228	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	239	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	247	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	254	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	266	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	283	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	290	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	304	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Turn	310	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	315	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	325	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	364	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	371	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	375	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	381	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	390	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	401	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	407	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	420	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	425	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Helix	430	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	446	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	462	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	477	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+P32861	UniProtKB	Beta strand	484	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K	
+##sequence-region P38709 1 493
+P38709	UniProtKB	Chain	1	493	.	.	.	ID=PRO_0000185766;Note=Probable UTP--glucose-1-phosphate uridylyltransferase	
+P38709	UniProtKB	Region	105	108	.	.	.	Note=UTP binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P38709	UniProtKB	Region	107	108	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16851	
+P38709	UniProtKB	Region	240	242	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16851	
+P38709	UniProtKB	Binding site	181	181	.	.	.	Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P38709	UniProtKB	Binding site	211	211	.	.	.	Note=UTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+P38709	UniProtKB	Binding site	242	242	.	.	.	Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3	
+##sequence-region P38293 1 148
+P38293	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000065720;Note=Proteasome maturation factor UMP1	
+##sequence-region Q08960 1 810
+Q08960	UniProtKB	Chain	1	810	.	.	.	ID=PRO_0000217861;Note=S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase	
+Q08960	UniProtKB	Domain	205	360	.	.	.	Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088	
+Q08960	UniProtKB	Nucleotide binding	211	215	.	.	.	Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088	
+Q08960	UniProtKB	Nucleotide binding	304	337	.	.	.	Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088	
+Q08960	UniProtKB	Metal binding	479	479	.	.	.	Note=Iron-sulfur (4Fe-4S-S-AdoMet)	
+Q08960	UniProtKB	Metal binding	483	483	.	.	.	Note=Iron-sulfur (4Fe-4S-S-AdoMet)	
+Q08960	UniProtKB	Metal binding	486	486	.	.	.	Note=Iron-sulfur (4Fe-4S-S-AdoMet)	
+Q08960	UniProtKB	Cross-link	496	496	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+Q08960	UniProtKB	Mutagenesis	479	479	.	.	.	Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16642040;Dbxref=PMID:16642040	
+Q08960	UniProtKB	Mutagenesis	483	483	.	.	.	Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16642040;Dbxref=PMID:16642040	
+Q08960	UniProtKB	Mutagenesis	486	486	.	.	.	Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16642040;Dbxref=PMID:16642040	
+Q08960	UniProtKB	Mutagenesis	532	532	.	.	.	Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16642040;Dbxref=PMID:16642040	
+Q08960	UniProtKB	Mutagenesis	550	550	.	.	.	Note=Loss of function. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16642040;Dbxref=PMID:16642040	
+##sequence-region Q08282 1 695
+Q08282	UniProtKB	Chain	1	695	.	.	.	ID=PRO_0000226146;Note=tRNA wybutosine-synthesizing protein 4	
+Q08282	UniProtKB	Region	146	147	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q08282	UniProtKB	Region	196	197	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q08282	UniProtKB	Active site	88	88	.	.	.	Note=Proton donor%3B for both methylation and methoxycarbonylation activities;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19287006;Dbxref=PMID:19287006	
+Q08282	UniProtKB	Active site	229	229	.	.	.	Note=Proton acceptor%3B for methoxycarbonylation activity;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19287006;Dbxref=PMID:19287006	
+Q08282	UniProtKB	Binding site	38	38	.	.	.	Note=S-adenosyl-L-methionine	
+Q08282	UniProtKB	Binding site	88	88	.	.	.	Note=S-adenosyl-L-methionine	
+Q08282	UniProtKB	Binding site	115	115	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen	
+Q08282	UniProtKB	Binding site	224	224	.	.	.	Note=S-adenosyl-L-methionine	
+Q08282	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Loss of function. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19287006;Dbxref=PMID:19287006	
+Q08282	UniProtKB	Sequence conflict	417	417	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08282	UniProtKB	Helix	7	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	17	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	30	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	67	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	79	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	107	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	121	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	131	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	137	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	148	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	162	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	188	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	200	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Turn	210	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	217	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	232	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	245	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	264	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	282	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	289	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	303	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	309	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	318	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	333	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	343	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	352	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZW9	
+Q08282	UniProtKB	Turn	358	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	375	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	392	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	400	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	406	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	414	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	424	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	444	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Turn	449	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	453	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	460	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	471	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Turn	475	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	479	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	490	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZW9	
+Q08282	UniProtKB	Beta strand	494	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	503	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	509	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZW9	
+Q08282	UniProtKB	Beta strand	514	519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Turn	520	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	524	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	533	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	539	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZW9	
+Q08282	UniProtKB	Beta strand	543	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Turn	548	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	552	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	569	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	584	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	593	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	601	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	609	613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Turn	624	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	627	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Turn	633	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	637	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	645	650	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	659	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	668	671	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	674	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Helix	677	679	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZZK	
+Q08282	UniProtKB	Beta strand	682	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+Q08282	UniProtKB	Beta strand	688	692	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA	
+##sequence-region P38820 1 440
+P38820	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000120587;Note=Adenylyltransferase and sulfurtransferase UBA4	
+P38820	UniProtKB	Domain	339	438	.	.	.	Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049	
+P38820	UniProtKB	Nucleotide binding	105	109	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049	
+P38820	UniProtKB	Nucleotide binding	166	167	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049	
+P38820	UniProtKB	Compositional bias	214	219	.	.	.	Note=Poly-Pro	
+P38820	UniProtKB	Active site	225	225	.	.	.	Note=Glycyl thioester intermediate%3B for adenylyltransferase activity	
+P38820	UniProtKB	Active site	397	397	.	.	.	Note=Cysteine persulfide intermediate%3B for sulfurtransferase activity	
+P38820	UniProtKB	Metal binding	208	208	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049	
+P38820	UniProtKB	Metal binding	211	211	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049	
+P38820	UniProtKB	Metal binding	286	286	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049	
+P38820	UniProtKB	Metal binding	289	289	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049	
+P38820	UniProtKB	Binding site	77	77	.	.	.	Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049	
+P38820	UniProtKB	Binding site	98	98	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049	
+P38820	UniProtKB	Binding site	122	122	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049	
+P38820	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38820	UniProtKB	Modified residue	326	326	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38820	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Abolishes adenylyltransferase activity but not sulfurtransferase activity. C->A%2CS;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10713047,ECO:0000269|PubMed:18491921,ECO:0000269|PubMed:19145231,ECO:0000269|PubMed:19151091;Dbxref=PMID:10713047,PMID:18491921,PMID:19145231,PMID:19151091	
+P38820	UniProtKB	Mutagenesis	397	397	.	.	.	Note=Abolishes sulfurtransferase activity but not adenylyltransferase activity. C->A%2CS;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18491921,ECO:0000269|PubMed:19145231,ECO:0000269|PubMed:19151091;Dbxref=PMID:18491921,PMID:19145231,PMID:19151091	
+##sequence-region P15731 1 148
+P15731	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000082545;Note=Ubiquitin-conjugating enzyme E2 4	
+P15731	UniProtKB	Active site	86	86	.	.	.	Note=Glycyl thioester intermediate	
+P15731	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P15731	UniProtKB	Cross-link	91	91	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P15731	UniProtKB	Helix	2	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ	
+P15731	UniProtKB	Beta strand	20	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ	
+P15731	UniProtKB	Beta strand	30	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ	
+P15731	UniProtKB	Beta strand	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE	
+P15731	UniProtKB	Turn	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE	
+P15731	UniProtKB	Beta strand	50	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ	
+P15731	UniProtKB	Turn	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ	
+P15731	UniProtKB	Beta strand	67	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ	
+P15731	UniProtKB	Helix	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ	
+P15731	UniProtKB	Turn	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ	
+P15731	UniProtKB	Helix	100	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ	
+P15731	UniProtKB	Helix	122	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ	
+P15731	UniProtKB	Helix	132	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ	
+##sequence-region P28263 1 218
+P28263	UniProtKB	Chain	1	218	.	.	.	ID=PRO_0000082555;Note=Ubiquitin-conjugating enzyme E2-24 kDa	
+P28263	UniProtKB	Active site	85	85	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133	
+##sequence-region P34223 1 423
+P34223	UniProtKB	Chain	1	423	.	.	.	ID=PRO_0000210998;Note=UBX domain-containing protein 1	
+P34223	UniProtKB	Domain	232	297	.	.	.	Note=SEP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00732	
+P34223	UniProtKB	Domain	344	421	.	.	.	Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215	
+P34223	UniProtKB	Modified residue	128	128	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34223	UniProtKB	Modified residue	210	210	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34223	UniProtKB	Modified residue	224	224	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34223	UniProtKB	Modified residue	315	315	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P34223	UniProtKB	Modified residue	321	321	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34223	UniProtKB	Modified residue	322	322	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34223	UniProtKB	Modified residue	331	331	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34223	UniProtKB	Cross-link	241	241	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P34223	UniProtKB	Sequence conflict	223	223	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04511 1 668
+Q04511	UniProtKB	Chain	1	668	.	.	.	ID=PRO_0000119970;Note=Ubiquitin ligase complex F-box protein UFO1	
+Q04511	UniProtKB	Domain	5	51	.	.	.	Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080	
+Q04511	UniProtKB	Domain	547	566	.	.	.	Note=UIM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+Q04511	UniProtKB	Domain	583	602	.	.	.	Note=UIM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+Q04511	UniProtKB	Domain	651	668	.	.	.	Note=UIM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+Q04511	UniProtKB	Modified residue	511	511	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04511	UniProtKB	Modified residue	514	514	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P40537 1 1034
+P40537	UniProtKB	Chain	1	1034	.	.	.	ID=PRO_0000101732;Note=Ubiquitin-like-specific protease 2	
+P40537	UniProtKB	Modified residue	788	788	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40537	UniProtKB	Modified residue	903	903	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40537	UniProtKB	Modified residue	983	983	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40537	UniProtKB	Modified residue	984	984	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40537	UniProtKB	Helix	832	839	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5V1A	
+##sequence-region Q12151 1 913
+Q12151	UniProtKB	Chain	1	913	.	.	.	ID=PRO_0000114988;Note=Sterol uptake control protein 2	
+Q12151	UniProtKB	DNA binding	50	80	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+Q12151	UniProtKB	Coiled coil	303	346	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12151	UniProtKB	Coiled coil	440	472	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12151	UniProtKB	Compositional bias	222	353	.	.	.	Note=Gln-rich	
+Q12151	UniProtKB	Compositional bias	885	888	.	.	.	Note=Poly-Gly	
+Q12151	UniProtKB	Modified residue	122	122	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12151	UniProtKB	Modified residue	519	519	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12151	UniProtKB	Mutagenesis	888	888	.	.	.	Note=Increased aerobic expression of DAN1. G->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11238402,ECO:0000269|PubMed:3059715,ECO:0000269|PubMed:9696767;Dbxref=PMID:11238402,PMID:3059715,PMID:9696767	
+Q12151	UniProtKB	Mutagenesis	888	888	.	.	.	Note=In upc2-1%3B increases aerobic sterol synthesis and uptake. Increases also aerobic expression of DAN1 and sensibility to NaCl and LiCl. G->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11238402,ECO:0000269|PubMed:3059715,ECO:0000269|PubMed:9696767;Dbxref=PMID:11238402,PMID:3059715,PMID:9696767	
+Q12151	UniProtKB	Helix	607	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	621	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	632	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	638	645	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	647	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	670	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	687	692	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	695	711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	732	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	756	759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Turn	767	769	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Beta strand	773	776	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Beta strand	784	787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	788	790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Beta strand	795	797	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	800	811	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	817	824	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	825	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	831	839	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Helix	842	861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+Q12151	UniProtKB	Turn	871	873	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N	
+##sequence-region P36096 1 758
+P36096	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Chain	27	758	.	.	.	ID=PRO_0000056409;Note=Transmembrane E3 ubiquitin-protein ligase 1	
+P36096	UniProtKB	Topological domain	27	398	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Transmembrane	399	419	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Topological domain	420	431	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Transmembrane	432	452	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Topological domain	453	458	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Transmembrane	459	479	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Topological domain	480	523	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Transmembrane	524	544	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Topological domain	545	553	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Transmembrane	554	574	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Topological domain	575	602	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Transmembrane	603	623	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Topological domain	624	635	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Transmembrane	636	656	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Topological domain	657	758	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36096	UniProtKB	Zinc finger	699	752	.	.	.	Note=RING-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+##sequence-region Q06412 1 1307
+Q06412	UniProtKB	Chain	1	1307	.	.	.	ID=PRO_0000080979;Note=Rho1 guanine nucleotide exchange factor TUS1	
+Q06412	UniProtKB	Domain	467	657	.	.	.	Note=DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00062	
+Q06412	UniProtKB	Domain	715	877	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+Q06412	UniProtKB	Domain	938	1279	.	.	.	Note=CNH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00795	
+Q06412	UniProtKB	Compositional bias	105	110	.	.	.	Note=Poly-Pro	
+Q06412	UniProtKB	Compositional bias	227	230	.	.	.	Note=Poly-Pro	
+##sequence-region P38319 1 544
+P38319	UniProtKB	Chain	1	544	.	.	.	ID=PRO_0000212490;Note=Tyrosyl-DNA phosphodiesterase 1	
+P38319	UniProtKB	Region	312	316	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NUW8	
+P38319	UniProtKB	Active site	182	182	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16751265;Dbxref=PMID:16751265	
+P38319	UniProtKB	Active site	432	432	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17707402;Dbxref=PMID:17707402	
+P38319	UniProtKB	Binding site	184	184	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NUW8	
+P38319	UniProtKB	Binding site	434	434	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NUW8	
+P38319	UniProtKB	Site	467	467	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NUW8	
+P38319	UniProtKB	Mutagenesis	182	182	.	.	.	Note=Loss of activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16751265;Dbxref=PMID:16751265	
+P38319	UniProtKB	Mutagenesis	432	432	.	.	.	Note=Strongly reduced release of the covalent intermediate with DNA that is formed during the enzyme reaction%2C leading to the accumulation of toxic adducts. No effect on bleomycin sensitivity. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17707402;Dbxref=PMID:17707402	
+P38319	UniProtKB	Mutagenesis	432	432	.	.	.	Note=Interferes with the hydrolysis of the covalent intermediate with DNA that is formed during the enzyme reaction. No effect on bleomycin sensitivity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17707402;Dbxref=PMID:17707402	
+P38319	UniProtKB	Beta strand	81	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Turn	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	105	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	114	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	126	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	139	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	159	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	168	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	185	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	193	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	206	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	215	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	232	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	247	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	254	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	263	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	269	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	277	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ3	
+P38319	UniProtKB	Helix	282	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Turn	294	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	301	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	311	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	319	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	325	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	330	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	336	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ8	
+P38319	UniProtKB	Helix	356	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	368	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	386	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	398	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	401	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Turn	419	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Turn	424	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	434	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	454	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	468	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	474	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	479	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	489	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	492	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	498	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Helix	503	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	516	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+P38319	UniProtKB	Beta strand	523	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ3	
+P38319	UniProtKB	Turn	530	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7	
+##sequence-region P53874 1 792
+P53874	UniProtKB	Chain	1	792	.	.	.	ID=PRO_0000080595;Note=Ubiquitin carboxyl-terminal hydrolase 10	
+P53874	UniProtKB	Domain	362	733	.	.	.	Note=USP	
+P53874	UniProtKB	Compositional bias	127	130	.	.	.	Note=Poly-Ser	
+P53874	UniProtKB	Compositional bias	138	144	.	.	.	Note=Poly-Glu	
+P53874	UniProtKB	Compositional bias	252	255	.	.	.	Note=Poly-Glu	
+P53874	UniProtKB	Compositional bias	302	309	.	.	.	Note=Poly-Glu	
+P53874	UniProtKB	Compositional bias	556	562	.	.	.	Note=Poly-Ser	
+P53874	UniProtKB	Active site	371	371	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10093	
+P53874	UniProtKB	Active site	691	691	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10093	
+P53874	UniProtKB	Sequence conflict	310	310	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P08067 1 215
+P08067	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion	
+P08067	UniProtKB	Chain	31	215	.	.	.	ID=PRO_0000030683;Note=Cytochrome b-c1 complex subunit Rieske%2C mitochondrial	
+P08067	UniProtKB	Transmembrane	49	82	.	.	.	Note=Helical	
+P08067	UniProtKB	Domain	123	214	.	.	.	Note=Rieske;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00628	
+P08067	UniProtKB	Metal binding	159	159	.	.	.	Note=Iron-sulfur (2Fe-2S)	
+P08067	UniProtKB	Metal binding	161	161	.	.	.	Note=Iron-sulfur (2Fe-2S)%3B via pros nitrogen	
+P08067	UniProtKB	Metal binding	178	178	.	.	.	Note=Iron-sulfur (2Fe-2S)	
+P08067	UniProtKB	Metal binding	181	181	.	.	.	Note=Iron-sulfur (2Fe-2S)%3B via pros nitrogen	
+P08067	UniProtKB	Disulfide bond	164	180	.	.	.	Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00628,ECO:0000269|PubMed:18390544;Dbxref=PMID:18390544	
+P08067	UniProtKB	Mutagenesis	157	157	.	.	.	Note=Loss of activity. G->D	
+P08067	UniProtKB	Mutagenesis	159	159	.	.	.	Note=Loss of activity. C->S	
+P08067	UniProtKB	Mutagenesis	161	161	.	.	.	Note=Loss of activity. H->R	
+P08067	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Partial loss of activity. G->D	
+P08067	UniProtKB	Mutagenesis	164	164	.	.	.	Note=Loss of activity. C->S	
+P08067	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Partial loss of activity. P->L	
+P08067	UniProtKB	Mutagenesis	178	178	.	.	.	Note=Loss of activity. C->S%2CY	
+P08067	UniProtKB	Mutagenesis	179	179	.	.	.	Note=Partial loss of activity. P->L	
+P08067	UniProtKB	Mutagenesis	180	180	.	.	.	Note=Loss of activity. C->S	
+P08067	UniProtKB	Mutagenesis	181	181	.	.	.	Note=Loss of activity. H->R	
+P08067	UniProtKB	Mutagenesis	183	183	.	.	.	Note=Loss of activity. S->L	
+P08067	UniProtKB	Mutagenesis	184	184	.	.	.	Note=No loss of activity. H->R	
+P08067	UniProtKB	Mutagenesis	186	186	.	.	.	Note=Partial loss of activity. D->N	
+P08067	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Loss of activity. G->D	
+P08067	UniProtKB	Mutagenesis	195	195	.	.	.	Note=No loss of activity. P->S	
+P08067	UniProtKB	Mutagenesis	196	196	.	.	.	Note=No loss of activity. A->T	
+P08067	UniProtKB	Mutagenesis	203	203	.	.	.	Note=Loss of activity. P->S	
+P08067	UniProtKB	Turn	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Beta strand	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EZV	
+P08067	UniProtKB	Helix	51	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Helix	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Beta strand	94	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Helix	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Beta strand	106	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Beta strand	114	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Helix	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Helix	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Turn	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Beta strand	152	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Turn	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Beta strand	167	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Turn	171	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Beta strand	175	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Turn	179	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Beta strand	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Beta strand	191	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Beta strand	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08067	UniProtKB	Beta strand	211	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+##sequence-region P41834 1 346
+P41834	UniProtKB	Chain	1	346	.	.	.	ID=PRO_0000210283;Note=Syntaxin UFE1	
+P41834	UniProtKB	Topological domain	1	324	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41834	UniProtKB	Transmembrane	325	342	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41834	UniProtKB	Topological domain	343	346	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41834	UniProtKB	Domain	255	317	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+##sequence-region P0CF17 1 737
+P0CF17	UniProtKB	Chain	1	737	.	.	.	ID=PRO_0000393363;Note=UPF0507 protein YML002W	
+P0CF17	UniProtKB	Domain	1	83	.	.	.	Note=VPS9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00550	
+P0CF17	UniProtKB	Sequence conflict	32	32	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P52488 1 636
+P52488	UniProtKB	Chain	1	636	.	.	.	ID=PRO_0000194979;Note=Ubiquitin-activating enzyme E1-like	
+P52488	UniProtKB	Nucleotide binding	28	33	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52488	UniProtKB	Nucleotide binding	60	63	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52488	UniProtKB	Nucleotide binding	121	126	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52488	UniProtKB	Motif	619	622	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52488	UniProtKB	Active site	177	177	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10132	
+P52488	UniProtKB	Metal binding	162	162	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52488	UniProtKB	Metal binding	165	165	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52488	UniProtKB	Metal binding	435	435	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52488	UniProtKB	Metal binding	438	438	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52488	UniProtKB	Binding site	52	52	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52488	UniProtKB	Binding site	76	76	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52488	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Loss of function. C->A%2CS	
+P52488	UniProtKB	Beta strand	442	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+P52488	UniProtKB	Helix	450	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+P52488	UniProtKB	Helix	458	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+P52488	UniProtKB	Beta strand	473	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+P52488	UniProtKB	Turn	480	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+P52488	UniProtKB	Beta strand	484	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+P52488	UniProtKB	Turn	493	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+P52488	UniProtKB	Turn	499	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+P52488	UniProtKB	Beta strand	509	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+P52488	UniProtKB	Beta strand	518	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+P52488	UniProtKB	Beta strand	525	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+P52488	UniProtKB	Beta strand	535	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONG	
+P52488	UniProtKB	Beta strand	549	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH	
+##sequence-region P50623 1 157
+P50623	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P50623	UniProtKB	Chain	2	157	.	.	.	ID=PRO_0000082556;Note=SUMO-conjugating enzyme UBC9	
+P50623	UniProtKB	Active site	93	93	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133	
+P50623	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P50623	UniProtKB	Helix	4	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Beta strand	25	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Beta strand	36	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Turn	52	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Beta strand	56	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Turn	66	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Beta strand	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Helix	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Turn	99	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Helix	109	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Helix	131	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+P50623	UniProtKB	Helix	141	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD	
+##sequence-region P0CG63 1 381
+P0CG63	UniProtKB	Chain	1	76	.	.	.	ID=PRO_0000396306;Note=Ubiquitin	
+P0CG63	UniProtKB	Chain	77	152	.	.	.	ID=PRO_0000396307;Note=Ubiquitin	
+P0CG63	UniProtKB	Chain	153	228	.	.	.	ID=PRO_0000396308;Note=Ubiquitin	
+P0CG63	UniProtKB	Chain	229	304	.	.	.	ID=PRO_0000396309;Note=Ubiquitin	
+P0CG63	UniProtKB	Chain	305	380	.	.	.	ID=PRO_0000396310;Note=Ubiquitin	
+P0CG63	UniProtKB	Propeptide	381	381	.	.	.	ID=PRO_0000396311	
+P0CG63	UniProtKB	Domain	1	76	.	.	.	Note=Ubiquitin-like 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+P0CG63	UniProtKB	Domain	77	152	.	.	.	Note=Ubiquitin-like 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+P0CG63	UniProtKB	Domain	153	228	.	.	.	Note=Ubiquitin-like 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+P0CG63	UniProtKB	Domain	229	304	.	.	.	Note=Ubiquitin-like 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+P0CG63	UniProtKB	Domain	305	380	.	.	.	Note=Ubiquitin-like 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+P0CG63	UniProtKB	Cross-link	76	76	.	.	.	Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)	
+P0CG63	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P0CG63	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P0CG63	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P0CG63	UniProtKB	Sequence conflict	352	352	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CG63	UniProtKB	Beta strand	2	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	12	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Helix	23	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Turn	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	41	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	52	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L10	
+P0CG63	UniProtKB	Helix	56	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	66	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	88	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	101	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	143	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	157	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Helix	163	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Helix	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Helix	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	184	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	207	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	227	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W	
+P0CG63	UniProtKB	Beta strand	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7	
+P0CG63	UniProtKB	Beta strand	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7	
+P0CG63	UniProtKB	Helix	251	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7	
+P0CG63	UniProtKB	Helix	266	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7	
+P0CG63	UniProtKB	Beta strand	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7	
+P0CG63	UniProtKB	Beta strand	274	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7	
+P0CG63	UniProtKB	Helix	285	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7	
+P0CG63	UniProtKB	Beta strand	294	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7	
+P0CG63	UniProtKB	Beta strand	306	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E	
+P0CG63	UniProtKB	Turn	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q0W	
+P0CG63	UniProtKB	Beta strand	316	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E	
+P0CG63	UniProtKB	Beta strand	323	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q0W	
+P0CG63	UniProtKB	Helix	327	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E	
+P0CG63	UniProtKB	Turn	342	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E	
+P0CG63	UniProtKB	Beta strand	345	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E	
+P0CG63	UniProtKB	Beta strand	351	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ	
+P0CG63	UniProtKB	Beta strand	358	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OLM	
+P0CG63	UniProtKB	Helix	361	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E	
+P0CG63	UniProtKB	Beta strand	370	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E	
+P0CG63	UniProtKB	Helix	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JT4	
+##sequence-region P50101 1 1230
+P50101	UniProtKB	Chain	1	1230	.	.	.	ID=PRO_0000080600;Note=Ubiquitin carboxyl-terminal hydrolase 15	
+P50101	UniProtKB	Domain	39	179	.	.	.	Note=MATH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00129	
+P50101	UniProtKB	Domain	205	536	.	.	.	Note=USP	
+P50101	UniProtKB	Active site	214	214	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+P50101	UniProtKB	Active site	465	465	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+##sequence-region Q02863 1 499
+Q02863	UniProtKB	Chain	1	499	.	.	.	ID=PRO_0000080601;Note=Ubiquitin carboxyl-terminal hydrolase 16	
+Q02863	UniProtKB	Domain	53	497	.	.	.	Note=USP	
+Q02863	UniProtKB	Active site	62	62	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+Q02863	UniProtKB	Active site	407	407	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
+##sequence-region P32837 1 571
+P32837	UniProtKB	Chain	1	571	.	.	.	ID=PRO_0000054161;Note=GABA-specific permease	
+P32837	UniProtKB	Topological domain	1	73	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	95	105	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	127	153	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	154	174	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	175	198	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	220	228	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	229	249	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	250	271	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	272	292	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	293	312	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	313	333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	334	364	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	365	385	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	386	416	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	417	437	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	438	441	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	442	462	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	463	482	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	483	503	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	504	514	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Transmembrane	515	535	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32837	UniProtKB	Topological domain	536	571	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03327 1 502
+Q03327	UniProtKB	Chain	1	502	.	.	.	ID=PRO_0000270985;Note=Mitochondrial fusion and transport protein UGO1	
+Q03327	UniProtKB	Topological domain	1	293	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03327	UniProtKB	Transmembrane	294	314	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03327	UniProtKB	Topological domain	315	502	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03327	UniProtKB	Repeat	288	383	.	.	.	Note=Solcar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03327	UniProtKB	Region	1	294	.	.	.	Note=Binds FZO1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087460;Dbxref=PMID:15087460	
+Q03327	UniProtKB	Region	312	502	.	.	.	Note=Binds MGM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087460;Dbxref=PMID:15087460	
+Q03327	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03327	UniProtKB	Sequence conflict	114	114	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03327	UniProtKB	Sequence conflict	114	114	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39547 1 235
+P39547	UniProtKB	Chain	1	235	.	.	.	ID=PRO_0000207528;Note=ULP1-interacting protein 3	
+P39547	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39547	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39547	UniProtKB	Cross-link	11	11	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P39547	UniProtKB	Cross-link	218	218	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q04006 1 179
+Q04006	UniProtKB	Chain	1	179	.	.	.	ID=PRO_0000253834;Note=Protein UPS3%2C mitochondrial	
+Q04006	UniProtKB	Domain	1	175	.	.	.	Note=PRELI/MSF1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00158	
+##sequence-region P12887 1 359
+P12887	UniProtKB	Transit peptide	1	21	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12887	UniProtKB	Chain	22	359	.	.	.	ID=PRO_0000036085;Note=Uracil-DNA glycosylase	
+P12887	UniProtKB	Active site	162	162	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03166	
+P12887	UniProtKB	Sequence conflict	173	173	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P18562 1 216
+P18562	UniProtKB	Chain	1	216	.	.	.	ID=PRO_0000120788;Note=Uracil phosphoribosyltransferase	
+P18562	UniProtKB	Nucleotide binding	75	78	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998	
+P18562	UniProtKB	Region	137	145	.	.	.	Note=5-phospho-alpha-D-ribose 1-diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998	
+P18562	UniProtKB	Region	207	209	.	.	.	Note=Uracil binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998	
+P18562	UniProtKB	Binding site	32	32	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998	
+P18562	UniProtKB	Binding site	41	41	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998	
+P18562	UniProtKB	Binding site	77	77	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18562	UniProtKB	Binding site	85	85	.	.	.	Note=5-phospho-alpha-D-ribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998	
+P18562	UniProtKB	Binding site	102	102	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998	
+P18562	UniProtKB	Binding site	110	110	.	.	.	Note=5-phospho-alpha-D-ribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998	
+P18562	UniProtKB	Binding site	131	131	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998	
+P18562	UniProtKB	Binding site	137	137	.	.	.	Note=5-phospho-alpha-D-ribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998	
+P18562	UniProtKB	Binding site	201	201	.	.	.	Note=Ribose-5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18562	UniProtKB	Binding site	202	202	.	.	.	Note=Uracil%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998	
+P18562	UniProtKB	Binding site	208	208	.	.	.	Note=5-phospho-alpha-D-ribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18562	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P18562	UniProtKB	Mutagenesis	26	26	.	.	.	Note=In FUR1-8%3B causes resistance to 5-fluorouracil (5FU). R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2189783;Dbxref=PMID:2189783	
+P18562	UniProtKB	Mutagenesis	99	99	.	.	.	Note=In FUR1-5%3B causes resistance to 5-fluorouracil (5FU). R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1913872;Dbxref=PMID:1913872	
+P18562	UniProtKB	Mutagenesis	106	106	.	.	.	Note=In FUR1-7%3B causes resistance to 5-fluorouracil (5FU). I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2189783;Dbxref=PMID:2189783	
+P18562	UniProtKB	Mutagenesis	173	173	.	.	.	Note=In FUR1-9%3B causes resistance to 5-fluorouracil (5FU). E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2189783;Dbxref=PMID:2189783	
+P18562	UniProtKB	Sequence conflict	104	104	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04411 1 772
+Q04411	UniProtKB	Chain	1	772	.	.	.	ID=PRO_0000253827;Note=Uracil catabolism protein 2	
+Q04411	UniProtKB	DNA binding	72	101	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P27515 1 501
+P27515	UniProtKB	Chain	1	501	.	.	.	ID=PRO_0000164462;Note=Uridine kinase	
+P27515	UniProtKB	Nucleotide binding	63	70	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27515	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P27515	UniProtKB	Modified residue	276	276	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32366 1 345
+P32366	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000119360;Note=V-type proton ATPase subunit d	
+P32366	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378	
+P32366	UniProtKB	Sequence conflict	32	32	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40003 1 282
+P40003	UniProtKB	Chain	1	282	.	.	.	ID=PRO_0000202618;Note=Biogenesis of lysosome-related organelles complex 1 subunit VAB2	
+P40003	UniProtKB	Coiled coil	64	140	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06708 1 880
+Q06708	UniProtKB	Chain	1	880	.	.	.	ID=PRO_0000065756;Note=Vacuole morphology and inheritance protein 14	
+Q06708	UniProtKB	Repeat	82	119	.	.	.	Note=HEAT 1	
+Q06708	UniProtKB	Repeat	243	280	.	.	.	Note=HEAT 2	
+Q06708	UniProtKB	Repeat	388	425	.	.	.	Note=HEAT 3	
+Q06708	UniProtKB	Repeat	429	466	.	.	.	Note=HEAT 4	
+Q06708	UniProtKB	Repeat	517	554	.	.	.	Note=HEAT 5	
+Q06708	UniProtKB	Modified residue	767	767	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06708	UniProtKB	Modified residue	805	805	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06708	UniProtKB	Modified residue	867	867	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06708	UniProtKB	Mutagenesis	56	56	.	.	.	Note=Loss of interaction with ATG18 and VAC7. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19037259;Dbxref=PMID:19037259	
+Q06708	UniProtKB	Mutagenesis	61	61	.	.	.	Note=Loss of interaction with ATG18 and VAC7. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19037259;Dbxref=PMID:19037259	
+Q06708	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Loss of interaction with ATG18 and VAC7. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19037259;Dbxref=PMID:19037259	
+Q06708	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Loss of interaction with ATG18%2C FAB1 and VAC7. No loss of interaction with FIG4. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19037259;Dbxref=PMID:19037259	
+##sequence-region Q99385 1 411
+Q99385	UniProtKB	Chain	1	411	.	.	.	ID=PRO_0000209504;Note=Vacuolar calcium ion transporter	
+Q99385	UniProtKB	Topological domain	1	30	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Transmembrane	31	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Topological domain	54	59	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Transmembrane	60	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Topological domain	83	91	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Transmembrane	92	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Topological domain	115	126	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Transmembrane	127	146	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Topological domain	147	160	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Transmembrane	161	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Topological domain	184	203	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Transmembrane	204	226	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Topological domain	227	252	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Transmembrane	253	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Topological domain	276	287	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Transmembrane	288	310	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Topological domain	311	319	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Transmembrane	320	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Topological domain	343	348	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Transmembrane	349	371	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Topological domain	372	380	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Transmembrane	381	398	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Topological domain	399	411	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99385	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q99385	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q99385	UniProtKB	Natural variant	204	204	.	.	.	Note=In manganese-resistant mutant 2. S->A	
+Q99385	UniProtKB	Natural variant	208	208	.	.	.	Note=In manganese-resistant mutant 1. L->P	
+Q99385	UniProtKB	Natural variant	383	383	.	.	.	Note=In VCX1-D1. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8628289;Dbxref=PMID:8628289	
+Q99385	UniProtKB	Helix	25	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	41	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	46	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	60	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	91	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	104	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Turn	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	119	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	136	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	158	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	193	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Turn	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	223	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	250	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	275	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	286	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	294	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	315	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	333	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	354	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+Q99385	UniProtKB	Helix	378	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C	
+##sequence-region P53058 1 206
+P53058	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53058	UniProtKB	Chain	20	206	.	.	.	ID=PRO_0000202704;Note=Protein VEL1	
+P53058	UniProtKB	Glycosylation	26	26	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53058	UniProtKB	Glycosylation	48	48	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53058	UniProtKB	Glycosylation	91	91	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53058	UniProtKB	Glycosylation	139	139	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53058	UniProtKB	Glycosylation	152	152	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P54860 1 961
+P54860	UniProtKB	Chain	1	961	.	.	.	ID=PRO_0000194997;Note=E4 ubiquitin-protein ligase UFD2	
+P54860	UniProtKB	Domain	880	954	.	.	.	Note=U-box	
+P54860	UniProtKB	Sequence conflict	102	102	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54860	UniProtKB	Sequence conflict	102	102	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54860	UniProtKB	Sequence conflict	677	677	.	.	.	Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54860	UniProtKB	Sequence conflict	677	677	.	.	.	Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54860	UniProtKB	Helix	1	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	10	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	16	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M63	
+P54860	UniProtKB	Helix	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	39	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	56	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	80	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	84	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	113	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	123	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	128	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	144	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	171	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	188	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	211	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	228	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Turn	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	243	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	276	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	294	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	309	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	324	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Turn	339	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	347	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	356	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	361	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	381	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	397	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	407	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	429	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	463	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	485	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJ0	
+P54860	UniProtKB	Turn	490	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJ0	
+P54860	UniProtKB	Beta strand	507	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJ0	
+P54860	UniProtKB	Helix	512	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	523	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	529	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Turn	548	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	555	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	575	589	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	601	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	608	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	625	627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	633	635	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	637	654	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	656	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	670	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	720	754	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	756	759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	762	780	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	782	785	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	792	795	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	799	812	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Turn	813	815	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	817	825	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Turn	827	829	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	832	842	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	843	846	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJ0	
+P54860	UniProtKB	Helix	851	878	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	883	885	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Turn	888	890	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	895	899	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Turn	901	903	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Beta strand	906	908	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	909	916	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Turn	923	925	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	931	933	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P54860	UniProtKB	Helix	938	952	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+##sequence-region P32772 1 223
+P32772	UniProtKB	Chain	1	223	.	.	.	ID=PRO_0000065718;Note=Protein UGX2	
+##sequence-region Q08926 1 304
+Q08926	UniProtKB	Chain	1	304	.	.	.	ID=PRO_0000270927;Note=ULP1-interacting protein 4	
+Q08926	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:18407956,PMID:19779198	
+Q08926	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+Q08926	UniProtKB	Modified residue	205	205	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:18407956,PMID:19779198	
+##sequence-region P43604 1 169
+P43604	UniProtKB	Chain	1	169	.	.	.	ID=PRO_0000202692;Note=Unfolded protein response-inducible protein 1	
+##sequence-region P39001 1 836
+P39001	UniProtKB	Chain	1	836	.	.	.	ID=PRO_0000114987;Note=Transcriptional regulatory protein UME6	
+P39001	UniProtKB	DNA binding	771	798	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P39001	UniProtKB	Region	508	594	.	.	.	Note=SIN3-binding	
+P39001	UniProtKB	Modified residue	114	114	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39001	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39001	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39001	UniProtKB	Modified residue	228	228	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39001	UniProtKB	Modified residue	316	316	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39001	UniProtKB	Modified residue	318	318	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39001	UniProtKB	Modified residue	645	645	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39001	UniProtKB	Mutagenesis	99	109	.	.	.	Note=Impairs meiotic genes expression%2C sporulation and interactions with IME1 and RIM11%2C and abolishes phosphorylation. TPVHTPSGSPS->APVHAPAGAPA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372955;Dbxref=PMID:9372955	
+P39001	UniProtKB	Mutagenesis	99	107	.	.	.	Note=Impairs meiotic genes expression and sporulation%2C reduces the interaction with IME1%2C and abolishes phosphorylation. TPVHTPSGS->APVHAPSGA	
+P39001	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Impairs meiotic genes expression and sporulation%2C reduces interactions with IME1 and RIM11%2C and reduces phosphorylation. T->N%2CA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10891485,ECO:0000269|PubMed:9372955;Dbxref=PMID:10891485,PMID:9372955	
+P39001	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Impairs meiotic genes expression and sporulation%2C reduces interaction with IME%2C and reduces phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891485;Dbxref=PMID:10891485	
+P39001	UniProtKB	Mutagenesis	107	107	.	.	.	Note=Impairs meiotic genes expression and sporulation%2C reduces interaction with IME%2C and reduces phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891485;Dbxref=PMID:10891485	
+P39001	UniProtKB	Mutagenesis	523	523	.	.	.	Note=Impairs SIN3-binding and gene repression activity. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941	
+P39001	UniProtKB	Mutagenesis	524	524	.	.	.	Note=Impairs gene repression activity. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941	
+P39001	UniProtKB	Mutagenesis	525	525	.	.	.	Note=Impairs gene repression activity. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941	
+P39001	UniProtKB	Mutagenesis	526	526	.	.	.	Note=Impairs gene repression activity. V->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941	
+P39001	UniProtKB	Mutagenesis	527	527	.	.	.	Note=Impairs SIN3-binding and gene repression activity. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941	
+P39001	UniProtKB	Mutagenesis	528	528	.	.	.	Note=Impairs SIN3-binding and gene repression activity. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941	
+P39001	UniProtKB	Mutagenesis	530	530	.	.	.	Note=Impairs SIN3-binding and gene repression activity. M->T%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941	
+P39001	UniProtKB	Mutagenesis	635	635	.	.	.	Note=Impairs gene repression activity. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941	
+P39001	UniProtKB	Sequence conflict	101	101	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39001	UniProtKB	Sequence conflict	363	363	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39001	UniProtKB	Sequence conflict	443	443	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39001	UniProtKB	Sequence conflict	465	465	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P48412 1 387
+P48412	UniProtKB	Chain	1	387	.	.	.	ID=PRO_0000215298;Note=Nonsense-mediated mRNA decay protein 3	
+P48412	UniProtKB	Motif	15	31	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48412	UniProtKB	Motif	58	75	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48412	UniProtKB	Motif	284	300	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48412	UniProtKB	Sequence conflict	26	26	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35200 1 230
+P35200	UniProtKB	Chain	1	230	.	.	.	ID=PRO_0000096596;Note=Protein UPS2%2C mitochondrial	
+P35200	UniProtKB	Domain	1	175	.	.	.	Note=PRELI/MSF1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00158	
+##sequence-region Q12208 1 290
+Q12208	UniProtKB	Chain	1	290	.	.	.	ID=PRO_0000262872;Note=U6 snRNA phosphodiesterase	
+Q12208	UniProtKB	Active site	133	133	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12208	UniProtKB	Active site	231	231	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12208	UniProtKB	Mutagenesis	133	133	.	.	.	Note=Cannot restore cell growth in USB1 depleted cells. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22899009,ECO:0000269|PubMed:23190533;Dbxref=PMID:22899009,PMID:23190533	
+Q12208	UniProtKB	Mutagenesis	231	231	.	.	.	Note=Cannot restore cell growth in USB1 depleted cells. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22899009,ECO:0000269|PubMed:23190533;Dbxref=PMID:22899009,PMID:23190533	
+##sequence-region P34247 1 250
+P34247	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000211052;Note=U3 small nucleolar RNA-associated protein 11	
+##sequence-region Q02931 1 896
+Q02931	UniProtKB	Chain	1	896	.	.	.	ID=PRO_0000051088;Note=NET1-associated nuclear protein 1	
+Q02931	UniProtKB	Repeat	295	334	.	.	.	Note=WD 1	
+Q02931	UniProtKB	Repeat	490	542	.	.	.	Note=WD 2	
+Q02931	UniProtKB	Repeat	552	595	.	.	.	Note=WD 3	
+Q02931	UniProtKB	Repeat	605	645	.	.	.	Note=WD 4	
+##sequence-region P40055 1 554
+P40055	UniProtKB	Chain	1	554	.	.	.	ID=PRO_0000051319;Note=U3 small nucleolar RNA-associated protein 7	
+P40055	UniProtKB	Repeat	108	149	.	.	.	Note=WD 1	
+P40055	UniProtKB	Repeat	230	269	.	.	.	Note=WD 2	
+P40055	UniProtKB	Repeat	272	311	.	.	.	Note=WD 3	
+P40055	UniProtKB	Repeat	314	351	.	.	.	Note=WD 4	
+##sequence-region P32630 1 166
+P32630	UniProtKB	Chain	1	166	.	.	.	ID=PRO_0000065747;Note=Protein UTR5	
+P32630	UniProtKB	Sequence conflict	1	20	.	.	.	Note=MSRYGKNLVHYIIVEHDDQR->MRDSNVKISVFPCALYNRGNTTIN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39111 1 118
+P39111	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000144812;Note=V-type proton ATPase subunit F	
+P39111	UniProtKB	Helix	2	4	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND	
+P39111	UniProtKB	Beta strand	7	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9	
+P39111	UniProtKB	Helix	14	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9	
+P39111	UniProtKB	Turn	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9	
+P39111	UniProtKB	Turn	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9	
+P39111	UniProtKB	Beta strand	37	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9	
+P39111	UniProtKB	Turn	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9	
+P39111	UniProtKB	Helix	47	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9	
+P39111	UniProtKB	Beta strand	62	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9	
+P39111	UniProtKB	Helix	71	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9	
+P39111	UniProtKB	Helix	78	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9	
+P39111	UniProtKB	Beta strand	86	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9	
+P39111	UniProtKB	Helix	108	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND	
+##sequence-region Q12063 1 375
+Q12063	UniProtKB	Chain	1	375	.	.	.	ID=PRO_0000242134;Note=Dehydrodolichyl diphosphate synthase complex subunit NUS1	
+Q12063	UniProtKB	Transmembrane	97	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12063	UniProtKB	Mutagenesis	372	372	.	.	.	Note=Loss of function. N->H	
+##sequence-region P34241 1 1764
+P34241	UniProtKB	Chain	1	1764	.	.	.	ID=PRO_0000203190;Note=Nucleolar pre-ribosomal-associated protein 1	
+##sequence-region P23202 1 354
+P23202	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P23202	UniProtKB	Chain	2	354	.	.	.	ID=PRO_0000186013;Note=Transcriptional regulator URE2	
+P23202	UniProtKB	Domain	112	196	.	.	.	Note=GST N-terminal	
+P23202	UniProtKB	Domain	205	354	.	.	.	Note=GST C-terminal	
+P23202	UniProtKB	Region	2	89	.	.	.	Note=Prion domain (PrD)	
+P23202	UniProtKB	Region	164	165	.	.	.	Note=Glutathione binding	
+P23202	UniProtKB	Region	180	181	.	.	.	Note=Glutathione binding	
+P23202	UniProtKB	Binding site	124	124	.	.	.	Note=Glutathione;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11695904;Dbxref=PMID:11695904	
+P23202	UniProtKB	Binding site	151	151	.	.	.	Note=Glutathione;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11695904;Dbxref=PMID:11695904	
+P23202	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P23202	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Reduces glutaredoxin activity. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19321443;Dbxref=PMID:19321443	
+P23202	UniProtKB	Mutagenesis	124	124	.	.	.	Note=Abolishes glutaredoxin activity. N->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19321443;Dbxref=PMID:19321443	
+P23202	UniProtKB	Mutagenesis	313	313	.	.	.	Note=Destroys protein function. F->S	
+P23202	UniProtKB	Helix	101	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Beta strand	111	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Helix	123	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Beta strand	139	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Turn	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Helix	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Helix	154	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Beta strand	167	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Turn	171	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Beta strand	176	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Helix	181	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Helix	206	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Helix	224	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Beta strand	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6W	
+P23202	UniProtKB	Helix	242	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Turn	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0B	
+P23202	UniProtKB	Helix	279	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6W	
+P23202	UniProtKB	Beta strand	285	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6W	
+P23202	UniProtKB	Helix	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6W	
+P23202	UniProtKB	Helix	293	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6W	
+P23202	UniProtKB	Helix	308	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Helix	314	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Helix	320	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Helix	327	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Helix	332	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+P23202	UniProtKB	Helix	345	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D	
+##sequence-region Q03714 1 838
+Q03714	UniProtKB	Chain	1	838	.	.	.	ID=PRO_0000114926;Note=U1 SNP1-associating protein 1	
+Q03714	UniProtKB	Topological domain	1	536	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03714	UniProtKB	Transmembrane	537	559	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03714	UniProtKB	Topological domain	560	563	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03714	UniProtKB	Transmembrane	564	583	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03714	UniProtKB	Topological domain	584	838	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03714	UniProtKB	Domain	259	318	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+Q03714	UniProtKB	Region	31	240	.	.	.	Note=Required for ERAD-L function	
+Q03714	UniProtKB	Region	319	418	.	.	.	Note=Important for HRD1 oligomer formation	
+Q03714	UniProtKB	Region	345	535	.	.	.	Note=Interaction with HRD1	
+Q03714	UniProtKB	Region	437	490	.	.	.	Note=Required for ERAD-L function and HRD1 oligomer formation	
+Q03714	UniProtKB	Region	584	838	.	.	.	Note=Interaction with DER1	
+Q03714	UniProtKB	Modified residue	374	374	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03714	UniProtKB	Modified residue	376	376	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03714	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P41807 1 478
+P41807	UniProtKB	Chain	1	478	.	.	.	ID=PRO_0000124202;Note=V-type proton ATPase subunit H	
+P41807	UniProtKB	Helix	11	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	27	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	38	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	77	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	90	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Beta strand	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	111	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	136	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Turn	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	158	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	168	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	180	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	197	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	207	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	239	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	257	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	268	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	284	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Beta strand	299	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	305	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	318	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	333	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	355	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	372	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	377	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	385	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	390	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	393	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	414	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	435	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	438	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	446	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+P41807	UniProtKB	Helix	459	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8	
+##sequence-region P25515 1 160
+P25515	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000071762;Note=V-type proton ATPase subunit c	
+P25515	UniProtKB	Topological domain	1	8	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25515	UniProtKB	Transmembrane	9	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25515	UniProtKB	Topological domain	32	53	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25515	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25515	UniProtKB	Topological domain	75	90	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25515	UniProtKB	Transmembrane	91	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25515	UniProtKB	Topological domain	113	124	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25515	UniProtKB	Transmembrane	125	150	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25515	UniProtKB	Topological domain	151	160	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25515	UniProtKB	Site	137	137	.	.	.	Note=Essential for proton translocation	
+P25515	UniProtKB	Mutagenesis	137	137	.	.	.	Note=Partial inactivation. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1825730;Dbxref=PMID:1825730	
+P25515	UniProtKB	Mutagenesis	137	137	.	.	.	Note=Inactivation. E->Q%2CV%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1825730;Dbxref=PMID:1825730	
+##sequence-region P36172 1 582
+P36172	UniProtKB	Chain	1	582	.	.	.	ID=PRO_0000173427;Note=Vacuolar basic amino acid transporter 5	
+P36172	UniProtKB	Topological domain	1	44	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	66	80	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	102	104	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	126	132	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	133	153	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	154	160	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	182	191	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	192	212	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	213	256	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	257	277	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	278	287	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	288	308	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	309	329	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	330	350	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	351	372	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	394	401	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	402	422	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	423	430	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	431	451	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	452	469	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	470	492	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	493	539	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Transmembrane	540	560	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Topological domain	561	582	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36172	UniProtKB	Glycosylation	70	70	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36172	UniProtKB	Glycosylation	423	423	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P04840 1 283
+P04840	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+P04840	UniProtKB	Chain	2	283	.	.	.	ID=PRO_0000050524;Note=Mitochondrial outer membrane protein porin 1	
+P04840	UniProtKB	Modified residue	109	109	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:19779198	
+P04840	UniProtKB	Modified residue	117	117	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04840	UniProtKB	Mutagenesis	19	19	.	.	.	Note=2.5-fold reduction in steepness of voltage dependence. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.9	
+P04840	UniProtKB	Mutagenesis	51	51	.	.	.	Note=2-fold increase in steepness of voltage dependence. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.9	
+P04840	UniProtKB	Mutagenesis	61	61	.	.	.	Note=Alters the selectivity of VDAC. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2478533;Dbxref=PMID:2478533	
+P04840	UniProtKB	Sequence conflict	118	118	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04840	UniProtKB	Sequence conflict	118	118	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04840	UniProtKB	Sequence conflict	203	207	.	.	.	Note=GAKAT->AKATM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40157 1 782
+P40157	UniProtKB	Chain	1	782	.	.	.	ID=PRO_0000065827;Note=Vacuolar import and degradation protein 27	
+P40157	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40157	UniProtKB	Modified residue	195	195	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40157	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40157	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P40157	UniProtKB	Modified residue	486	486	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q06685 1 1146
+Q06685	UniProtKB	Chain	1	1146	.	.	.	ID=PRO_0000270924;Note=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase	
+Q06685	UniProtKB	Nucleotide binding	402	405	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Nucleotide binding	412	414	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Nucleotide binding	487	489	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Region	197	198	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Region	377	378	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Region	492	495	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Region	530	597	.	.	.	Note=Polyphosphoinositide-binding domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6PFW1	
+Q06685	UniProtKB	Binding site	278	278	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Binding site	351	351	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Binding site	358	358	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Binding site	377	377	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Binding site	414	414	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Binding site	428	428	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Binding site	430	430	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Binding site	475	475	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314	
+Q06685	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06685	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06685	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06685	UniProtKB	Modified residue	895	895	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06685	UniProtKB	Modified residue	1107	1107	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06685	UniProtKB	Mutagenesis	487	487	.	.	.	Note=Abolishes enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17412958;Dbxref=PMID:17412958	
+Q06685	UniProtKB	Mutagenesis	548	548	.	.	.	Note=Does not affect enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17412958;Dbxref=PMID:17412958	
+##sequence-region Q04311 1 632
+Q04311	UniProtKB	Chain	1	632	.	.	.	ID=PRO_0000244435;Note=Protein VMS1	
+Q04311	UniProtKB	Repeat	470	500	.	.	.	Note=ANK 1	
+Q04311	UniProtKB	Repeat	504	530	.	.	.	Note=ANK 2	
+Q04311	UniProtKB	Zinc finger	72	96	.	.	.	Note=C2H2-type	
+Q04311	UniProtKB	Coiled coil	544	582	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04311	UniProtKB	Coiled coil	608	632	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04311	UniProtKB	Sequence conflict	170	170	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38067 1 497
+P38067	UniProtKB	Chain	1	497	.	.	.	ID=PRO_0000056568;Note=Succinate-semialdehyde dehydrogenase [NADP(+)]	
+P38067	UniProtKB	Active site	264	264	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007	
+P38067	UniProtKB	Active site	298	298	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007	
+P38067	UniProtKB	Site	164	164	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04179 1 340
+Q04179	UniProtKB	Chain	1	340	.	.	.	ID=PRO_0000206812;Note=Uridine nucleosidase	
+Q04179	UniProtKB	Active site	254	254	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04179	UniProtKB	Mutagenesis	254	254	.	.	.	Note=Reduces the Vmax 30-fold%2C but does not change the KM in a uridine hydrolase assay. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12111094;Dbxref=PMID:12111094	
+##sequence-region Q3E7B6 1 73
+Q3E7B6	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000071737;Note=V-type proton ATPase subunit e	
+Q3E7B6	UniProtKB	Transmembrane	4	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E7B6	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39968 1 578
+P39968	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+P39968	UniProtKB	Chain	2	578	.	.	.	ID=PRO_0000064302;Note=Vacuolar protein 8	
+P39968	UniProtKB	Repeat	37	75	.	.	.	Note=ARM 1	
+P39968	UniProtKB	Repeat	76	114	.	.	.	Note=ARM 2	
+P39968	UniProtKB	Repeat	116	155	.	.	.	Note=ARM 3	
+P39968	UniProtKB	Repeat	157	196	.	.	.	Note=ARM 4	
+P39968	UniProtKB	Repeat	198	237	.	.	.	Note=ARM 5	
+P39968	UniProtKB	Repeat	239	280	.	.	.	Note=ARM 6	
+P39968	UniProtKB	Repeat	282	321	.	.	.	Note=ARM 7	
+P39968	UniProtKB	Repeat	323	363	.	.	.	Note=ARM 8	
+P39968	UniProtKB	Repeat	407	446	.	.	.	Note=ARM 9	
+P39968	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39968	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39968	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9490720;Dbxref=PMID:9490720	
+P39968	UniProtKB	Lipidation	4	4	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9490720;Dbxref=PMID:9490720	
+P39968	UniProtKB	Lipidation	5	5	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9490720;Dbxref=PMID:9490720	
+P39968	UniProtKB	Lipidation	7	7	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9490720;Dbxref=PMID:9490720	
+P39968	UniProtKB	Cross-link	77	77	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P39968	UniProtKB	Cross-link	515	515	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P39968	UniProtKB	Mutagenesis	4	7	.	.	.	Note=In VAC8-3%3B not palmitoylated. CCSC->GTSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9490720;Dbxref=PMID:9490720	
+##sequence-region P32912 1 316
+P32912	UniProtKB	Chain	1	316	.	.	.	ID=PRO_0000065760;Note=Vacuolar morphogenesis protein 7	
+P32912	UniProtKB	Domain	1	124	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
+P32912	UniProtKB	Domain	250	312	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+P32912	UniProtKB	Coiled coil	168	186	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32912	UniProtKB	Beta strand	16	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD	
+P32912	UniProtKB	Beta strand	27	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD	
+P32912	UniProtKB	Beta strand	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD	
+P32912	UniProtKB	Helix	42	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD	
+P32912	UniProtKB	Helix	82	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD	
+P32912	UniProtKB	Helix	92	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD	
+P32912	UniProtKB	Helix	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD	
+P32912	UniProtKB	Helix	112	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD	
+##sequence-region Q05934 1 901
+Q05934	UniProtKB	Chain	1	901	.	.	.	ID=PRO_0000270928;Note=Vacuolar import and degradation protein 22	
+Q05934	UniProtKB	Transmembrane	381	401	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Zinc finger	66	122	.	.	.	Note=BED-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00027	
+Q05934	UniProtKB	Compositional bias	643	722	.	.	.	Note=Asn-rich	
+Q05934	UniProtKB	Glycosylation	21	21	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Glycosylation	242	242	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Glycosylation	291	291	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Glycosylation	540	540	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Glycosylation	645	645	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Glycosylation	649	649	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Glycosylation	652	652	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Glycosylation	662	662	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Glycosylation	669	669	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Glycosylation	673	673	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Glycosylation	688	688	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05934	UniProtKB	Glycosylation	722	722	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12241 1 283
+Q12241	UniProtKB	Chain	1	283	.	.	.	ID=PRO_0000210280;Note=Syntaxin VAM3	
+Q12241	UniProtKB	Topological domain	1	261	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12241	UniProtKB	Transmembrane	262	282	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12241	UniProtKB	Topological domain	283	283	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12241	UniProtKB	Domain	190	252	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+Q12241	UniProtKB	Coiled coil	28	48	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12241	UniProtKB	Coiled coil	84	111	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12241	UniProtKB	Coiled coil	169	189	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12241	UniProtKB	Compositional bias	174	179	.	.	.	Note=Poly-Gln	
+Q12241	UniProtKB	Compositional bias	268	271	.	.	.	Note=Poly-Ile	
+Q12241	UniProtKB	Helix	25	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7	
+Q12241	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7	
+Q12241	UniProtKB	Helix	58	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7	
+Q12241	UniProtKB	Helix	68	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7	
+Q12241	UniProtKB	Helix	84	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7	
+Q12241	UniProtKB	Helix	89	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7	
+##sequence-region P23642 1 535
+P23642	UniProtKB	Chain	1	535	.	.	.	ID=PRO_0000193672;Note=Mannan polymerase I complex VAN1 subunit	
+P23642	UniProtKB	Topological domain	1	64	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23642	UniProtKB	Transmembrane	65	81	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P23642	UniProtKB	Topological domain	82	535	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23642	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P23642	UniProtKB	Glycosylation	215	215	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23642	UniProtKB	Glycosylation	251	251	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23642	UniProtKB	Mutagenesis	361	361	.	.	.	Note=Reduced activity of the M-Pol I complex. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12235155;Dbxref=PMID:12235155	
+P23642	UniProtKB	Sequence conflict	87	87	.	.	.	Note=M->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23642	UniProtKB	Sequence conflict	140	140	.	.	.	Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23642	UniProtKB	Sequence conflict	281	281	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32610 1 256
+P32610	UniProtKB	Chain	1	256	.	.	.	ID=PRO_0000144244;Note=V-type proton ATPase subunit D	
+P32610	UniProtKB	Helix	29	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND	
+P32610	UniProtKB	Helix	79	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND	
+P32610	UniProtKB	Beta strand	91	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND	
+P32610	UniProtKB	Beta strand	104	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND	
+P32610	UniProtKB	Beta strand	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND	
+P32610	UniProtKB	Helix	128	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND	
+P32610	UniProtKB	Helix	177	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND	
+##sequence-region P48836 1 114
+P48836	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P48836	UniProtKB	Chain	2	114	.	.	.	ID=PRO_0000192916;Note=V-type proton ATPase subunit G	
+P48836	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P48836	UniProtKB	Helix	4	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P48836	UniProtKB	Helix	70	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DL0	
+P48836	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P48836	UniProtKB	Helix	77	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P48836	UniProtKB	Helix	91	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+##sequence-region P32319 1 1579
+P32319	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32319	UniProtKB	Chain	22	1579	.	.	.	ID=PRO_0000022037;Note=Vacuolar protein sorting/targeting protein VPS10	
+P32319	UniProtKB	Topological domain	22	1397	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32319	UniProtKB	Transmembrane	1398	1414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32319	UniProtKB	Topological domain	1415	1579	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32319	UniProtKB	Repeat	57	68	.	.	.	Note=BNR 1	
+P32319	UniProtKB	Repeat	101	112	.	.	.	Note=BNR 2	
+P32319	UniProtKB	Repeat	179	190	.	.	.	Note=BNR 3	
+P32319	UniProtKB	Repeat	415	426	.	.	.	Note=BNR 4	
+P32319	UniProtKB	Repeat	487	498	.	.	.	Note=BNR 5	
+P32319	UniProtKB	Repeat	533	544	.	.	.	Note=BNR 6	
+P32319	UniProtKB	Repeat	764	775	.	.	.	Note=BNR 7	
+P32319	UniProtKB	Repeat	861	872	.	.	.	Note=BNR 8	
+P32319	UniProtKB	Repeat	1143	1154	.	.	.	Note=BNR 9	
+P32319	UniProtKB	Repeat	1184	1195	.	.	.	Note=BNR 10	
+P32319	UniProtKB	Glycosylation	96	96	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32319	UniProtKB	Glycosylation	170	170	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32319	UniProtKB	Glycosylation	447	447	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32319	UniProtKB	Glycosylation	793	793	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32319	UniProtKB	Glycosylation	1010	1010	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32319	UniProtKB	Glycosylation	1303	1303	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32319	UniProtKB	Sequence conflict	19	19	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	38	38	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	54	54	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	74	74	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	94	99	.	.	.	Note=AMNGSY->SMYESR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	119	126	.	.	.	Note=GESISPRE->EKNISSRG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	152	153	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	165	167	.	.	.	Note=QFE->APV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	202	202	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	214	214	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	283	283	.	.	.	Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	378	378	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	410	410	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	426	426	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	774	774	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	1089	1089	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	1266	1266	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	1476	1476	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32319	UniProtKB	Sequence conflict	1557	1557	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32913 1 551
+P32913	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000065892;Note=Vacuolar protein sorting-associated protein 17	
+P32913	UniProtKB	Domain	108	227	.	.	.	Note=PX	
+P32913	UniProtKB	Coiled coil	359	385	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32913	UniProtKB	Modified residue	544	544	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32913	UniProtKB	Sequence conflict	25	25	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32913	UniProtKB	Sequence conflict	30	30	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32913	UniProtKB	Sequence conflict	62	62	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32913	UniProtKB	Sequence conflict	68	68	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32913	UniProtKB	Sequence conflict	90	90	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32913	UniProtKB	Sequence conflict	402	402	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04272 1 221
+Q04272	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+Q04272	UniProtKB	Chain	2	221	.	.	.	ID=PRO_0000211515;Note=Vacuolar protein sorting-associated protein 20	
+Q04272	UniProtKB	Coiled coil	72	178	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04272	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9748261;Dbxref=PMID:9748261	
+Q04272	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Loss of membrane association. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12194857;Dbxref=PMID:12194857	
+Q04272	UniProtKB	Helix	171	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FVL	
+##sequence-region Q05919 1 439
+Q05919	UniProtKB	Chain	1	439	.	.	.	ID=PRO_0000065900;Note=Vacuolar protein sorting-associated protein 38	
+Q05919	UniProtKB	Coiled coil	223	255	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05919	UniProtKB	Sequence conflict	55	55	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39702 1 1274
+P39702	UniProtKB	Chain	1	1274	.	.	.	ID=PRO_0000055901;Note=Vacuolar protein sorting-associated protein 8	
+P39702	UniProtKB	Repeat	75	119	.	.	.	Note=WD 1	
+P39702	UniProtKB	Repeat	131	170	.	.	.	Note=WD 2	
+P39702	UniProtKB	Repeat	193	233	.	.	.	Note=WD 3	
+P39702	UniProtKB	Repeat	507	665	.	.	.	Note=CHCR 1	
+P39702	UniProtKB	Repeat	915	1092	.	.	.	Note=CHCR 2	
+P39702	UniProtKB	Zinc finger	1198	1266	.	.	.	Note=RING-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P39702	UniProtKB	Compositional bias	40	43	.	.	.	Note=Poly-Ser	
+P39702	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P32842 1 164
+P32842	UniProtKB	Chain	1	164	.	.	.	ID=PRO_0000071788;Note=V-type proton ATPase subunit c'	
+P32842	UniProtKB	Topological domain	1	14	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32842	UniProtKB	Transmembrane	15	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32842	UniProtKB	Topological domain	38	59	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32842	UniProtKB	Transmembrane	60	80	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32842	UniProtKB	Topological domain	81	98	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32842	UniProtKB	Transmembrane	99	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32842	UniProtKB	Topological domain	121	132	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32842	UniProtKB	Transmembrane	133	158	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32842	UniProtKB	Topological domain	159	164	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32842	UniProtKB	Site	145	145	.	.	.	Note=Essential for proton translocation	
+P32842	UniProtKB	Mutagenesis	145	145	.	.	.	Note=Partial inactivation. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9030535;Dbxref=PMID:9030535	
+P32842	UniProtKB	Mutagenesis	145	145	.	.	.	Note=Inactivation. E->L%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9030535;Dbxref=PMID:9030535	
+P32842	UniProtKB	Sequence conflict	27	35	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38329 1 1120
+P38329	UniProtKB	Chain	1	1120	.	.	.	ID=PRO_0000202520;Note=Vacuolar cation-chloride cotransporter 1	
+P38329	UniProtKB	Topological domain	1	62	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	84	85	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	107	145	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	167	193	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	194	214	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	215	221	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	222	242	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	243	283	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	284	304	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	305	317	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	318	338	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	339	360	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	361	381	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	382	393	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	394	414	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	415	430	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	431	451	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	452	462	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	463	482	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	483	487	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Transmembrane	488	506	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38329	UniProtKB	Topological domain	507	1120	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P38329	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38329	UniProtKB	Modified residue	654	654	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38329	UniProtKB	Modified residue	915	915	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38329	UniProtKB	Modified residue	918	918	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40522 1 640
+P40522	UniProtKB	Chain	1	640	.	.	.	ID=PRO_0000202988;Note=Transcription factor VHR1	
+P40522	UniProtKB	Modified residue	409	409	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q08438 1 674
+Q08438	UniProtKB	Chain	1	674	.	.	.	ID=PRO_0000182038;Note=Phosphopantothenoylcysteine decarboxylase subunit VHS3	
+Q08438	UniProtKB	Compositional bias	580	661	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+Q08438	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q08438	UniProtKB	Mutagenesis	459	459	.	.	.	Note=Does not strongly affect the phosphatase inhibitor function but abolishes PPCDC activity. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15192104,ECO:0000269|PubMed:19915539;Dbxref=PMID:15192104,PMID:19915539	
+##sequence-region P53285 1 467
+P53285	UniProtKB	Chain	1	467	.	.	.	ID=PRO_0000065906;Note=Vacuolar protein sorting-associated protein 62	
+P53285	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53285	UniProtKB	Glycosylation	74	74	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53285	UniProtKB	Glycosylation	145	145	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53142 1 486
+P53142	UniProtKB	Chain	1	486	.	.	.	ID=PRO_0000050462;Note=Vacuolar protein sorting-associated protein 73	
+P53142	UniProtKB	Topological domain	1	26	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	48	90	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	112	119	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	141	146	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	168	178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	200	208	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	230	305	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	306	326	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	327	342	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	343	363	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	364	366	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	367	387	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	388	396	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	397	417	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	418	432	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	433	453	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	454	454	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Transmembrane	455	475	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53142	UniProtKB	Topological domain	476	486	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06525 1 465
+Q06525	UniProtKB	Chain	1	465	.	.	.	ID=PRO_0000244477;Note=Pre-mRNA-splicing factor URN1	
+Q06525	UniProtKB	Domain	1	32	.	.	.	Note=WW;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224	
+Q06525	UniProtKB	Domain	212	266	.	.	.	Note=FF	
+Q06525	UniProtKB	Compositional bias	119	192	.	.	.	Note=Glu-rich	
+Q06525	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06525	UniProtKB	Helix	216	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC	
+Q06525	UniProtKB	Turn	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC	
+Q06525	UniProtKB	Helix	235	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC	
+Q06525	UniProtKB	Beta strand	242	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC	
+Q06525	UniProtKB	Helix	247	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC	
+Q06525	UniProtKB	Helix	253	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC	
+##sequence-region Q12132 1 391
+Q12132	UniProtKB	Chain	1	391	.	.	.	ID=PRO_0000255973;Note=Nutrient and stress factor 1	
+Q12132	UniProtKB	Zinc finger	41	66	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q12132	UniProtKB	Zinc finger	72	95	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q12132	UniProtKB	Compositional bias	102	134	.	.	.	Note=Ser-rich	
+Q12132	UniProtKB	Compositional bias	185	197	.	.	.	Note=Poly-Gln	
+Q12132	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12132	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53950 1 1165
+P53950	UniProtKB	Chain	1	1165	.	.	.	ID=PRO_0000065757;Note=Vacuolar segregation protein 7	
+P53950	UniProtKB	Topological domain	1	919	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53950	UniProtKB	Transmembrane	920	940	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53950	UniProtKB	Topological domain	941	1165	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53950	UniProtKB	Compositional bias	277	412	.	.	.	Note=Asn-rich	
+P53950	UniProtKB	Compositional bias	469	485	.	.	.	Note=Gln-rich	
+P53950	UniProtKB	Compositional bias	1085	1119	.	.	.	Note=Asp-rich	
+P53950	UniProtKB	Modified residue	164	164	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53950	UniProtKB	Glycosylation	1020	1020	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53950	UniProtKB	Glycosylation	1099	1099	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40041 1 505
+P40041	UniProtKB	Chain	1	505	.	.	.	ID=PRO_0000202632;Note=Transcription factor VHR2	
+##sequence-region P23968 1 213
+P23968	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000071780;Note=V-type proton ATPase subunit c''	
+P23968	UniProtKB	Topological domain	1	14	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23968	UniProtKB	Transmembrane	15	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23968	UniProtKB	Topological domain	36	61	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23968	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23968	UniProtKB	Topological domain	83	100	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23968	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23968	UniProtKB	Topological domain	122	145	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23968	UniProtKB	Transmembrane	146	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23968	UniProtKB	Topological domain	168	179	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23968	UniProtKB	Transmembrane	180	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23968	UniProtKB	Topological domain	206	213	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23968	UniProtKB	Site	108	108	.	.	.	Note=Essential for proton translocation	
+P23968	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Partial inactivation. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9030535;Dbxref=PMID:9030535	
+P23968	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Inactivation. E->L%2CQ%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9030535;Dbxref=PMID:9030535	
+##sequence-region P40478 1 281
+P40478	UniProtKB	Chain	1	281	.	.	.	ID=PRO_0000050525;Note=Mitochondrial outer membrane protein porin 2	
+##sequence-region O13549 1 108
+O13549	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000299780;Note=Uncharacterized protein VPS63	
+##sequence-region P47161 1 811
+P47161	UniProtKB	Chain	1	811	.	.	.	ID=PRO_0000174138;Note=Vacuolar protein sorting-associated protein 70	
+P47161	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47161	UniProtKB	Metal binding	445	445	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47161	UniProtKB	Metal binding	456	456	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47161	UniProtKB	Metal binding	456	456	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47161	UniProtKB	Metal binding	522	522	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47161	UniProtKB	Metal binding	607	607	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47161	UniProtKB	Glycosylation	55	55	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47161	UniProtKB	Glycosylation	237	237	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47161	UniProtKB	Glycosylation	568	568	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47161	UniProtKB	Glycosylation	599	599	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47161	UniProtKB	Glycosylation	670	670	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P37370 1 817
+P37370	UniProtKB	Chain	1	817	.	.	.	ID=PRO_0000065929;Note=Verprolin	
+P37370	UniProtKB	Domain	30	47	.	.	.	Note=WH2 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00406	
+P37370	UniProtKB	Domain	87	106	.	.	.	Note=WH2 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00406	
+P37370	UniProtKB	Compositional bias	5	14	.	.	.	Note=Poly-Pro	
+P37370	UniProtKB	Compositional bias	239	245	.	.	.	Note=Poly-Pro	
+P37370	UniProtKB	Compositional bias	349	357	.	.	.	Note=Poly-Pro	
+P37370	UniProtKB	Compositional bias	396	406	.	.	.	Note=Poly-Pro	
+P37370	UniProtKB	Compositional bias	424	431	.	.	.	Note=Poly-Pro	
+P37370	UniProtKB	Compositional bias	462	468	.	.	.	Note=Poly-Ser	
+P37370	UniProtKB	Compositional bias	704	708	.	.	.	Note=Poly-Pro	
+P37370	UniProtKB	Modified residue	519	519	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P37370	UniProtKB	Modified residue	762	762	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P37370	UniProtKB	Glycosylation	109	109	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37370	UniProtKB	Glycosylation	212	212	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37370	UniProtKB	Glycosylation	337	337	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37370	UniProtKB	Glycosylation	383	383	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37370	UniProtKB	Glycosylation	784	784	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37370	UniProtKB	Glycosylation	796	796	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37370	UniProtKB	Sequence conflict	308	308	.	.	.	Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37370	UniProtKB	Sequence conflict	350	350	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37370	UniProtKB	Sequence conflict	689	689	.	.	.	Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37370	UniProtKB	Sequence conflict	710	817	.	.	.	Note=PSTMDTGTSNSPSKNLKQRLFSTGGSTLQHKHNTHTNQPDVDVGRYTIGGSNSIVGAKSGNERIVIDDSRFKWTNVSQMPKPRPFQNKTKLYPSGKGSSVPLDLTLFT->HLRWIPVPLIAPVKTLNNGYFLQVDRRCNTSIIRIQINQMLM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03631 1 944
+Q03631	UniProtKB	Chain	1	944	.	.	.	ID=PRO_0000115004;Note=Weak acid resistance protein 1	
+Q03631	UniProtKB	DNA binding	76	109	.	.	.	Note=Zn(2)-C6 fungal-type	
+Q03631	UniProtKB	Modified residue	128	128	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03631	UniProtKB	Mutagenesis	368	368	.	.	.	Note=Causes hyperactivity with constitutive induction of PDR12. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18621731;Dbxref=PMID:18621731	
+Q03631	UniProtKB	Mutagenesis	452	452	.	.	.	Note=Causes hyperactivity with constitutive induction of PDR12. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18621731;Dbxref=PMID:18621731	
+Q03631	UniProtKB	Mutagenesis	463	463	.	.	.	Note=Causes hyperactivity with constitutive induction of PDR12. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18621731;Dbxref=PMID:18621731	
+Q03631	UniProtKB	Mutagenesis	640	640	.	.	.	Note=Causes hyperactivity with constitutive induction of PDR12. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18621731;Dbxref=PMID:18621731	
+Q03631	UniProtKB	Mutagenesis	703	703	.	.	.	Note=Causes hyperactivitywith constitutive induction of PDR12. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18621731;Dbxref=PMID:18621731	
+Q03631	UniProtKB	Mutagenesis	762	762	.	.	.	Note=Causes hyperactivity with constitutive induction of PDR12. K->R%2CN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17509074,ECO:0000269|PubMed:18621731;Dbxref=PMID:17509074,PMID:18621731	
+Q03631	UniProtKB	Mutagenesis	763	763	.	.	.	Note=Causes hyperactivity with constitutive induction of PDR12. F->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17509074;Dbxref=PMID:17509074	
+Q03631	UniProtKB	Mutagenesis	764	764	.	.	.	Note=Causes hypersensitivity to sorbate through its inability to induce PDR12. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17509074;Dbxref=PMID:17509074	
+##sequence-region P31412 1 392
+P31412	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6	
+P31412	UniProtKB	Chain	2	392	.	.	.	ID=PRO_0000209358;Note=V-type proton ATPase subunit C	
+P31412	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6	
+P31412	UniProtKB	Mutagenesis	255	255	.	.	.	Note=Is rapidly degraded and disrupts stable ATPase assembly. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11777935;Dbxref=PMID:11777935	
+P31412	UniProtKB	Beta strand	9	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	30	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Beta strand	43	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	61	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Beta strand	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	107	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Turn	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	127	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Turn	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Turn	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Beta strand	189	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	203	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Beta strand	213	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DL0	
+P31412	UniProtKB	Beta strand	223	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Beta strand	229	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	243	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Beta strand	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	264	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Beta strand	325	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	337	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Helix	349	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+P31412	UniProtKB	Beta strand	384	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L	
+##sequence-region P22203 1 233
+P22203	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378	
+P22203	UniProtKB	Chain	2	233	.	.	.	ID=PRO_0000117310;Note=V-type proton ATPase subunit E	
+P22203	UniProtKB	Region	8	20	.	.	.	Note=Interaction with VMA5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15751969;Dbxref=PMID:15751969	
+P22203	UniProtKB	Region	19	38	.	.	.	Note=Interaction with VMA10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15751969;Dbxref=PMID:15751969	
+P22203	UniProtKB	Coiled coil	15	45	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22203	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378	
+P22203	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Reduces ATPase activity by 11%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227	
+P22203	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Reduces ATPase activity by 73%25. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227	
+P22203	UniProtKB	Mutagenesis	9	9	.	.	.	Note=Increases ATPase activity 1.4-fold. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227	
+P22203	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Reduces ATPase activity by 88%25. Prevents assembly of V1 subunits at the membrane. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227	
+P22203	UniProtKB	Mutagenesis	145	145	.	.	.	Note=In VMA4-1%3B is rapidly degraded at 37 degrees Celsius. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9660816;Dbxref=PMID:9660816	
+P22203	UniProtKB	Mutagenesis	160	160	.	.	.	Note=Reduces ATPase activity by 22%25. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227	
+P22203	UniProtKB	Mutagenesis	202	202	.	.	.	Note=Increases ATPase activity 2.1-fold by increasing Vmax for ATP hydrolysis 2-fold. Reduces ATPase activity by 90%25 and produces structurally aberrant V-ATPase complexes%3B when associated with A-233. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227	
+P22203	UniProtKB	Mutagenesis	230	230	.	.	.	Note=Increases ATPase activity 1.3-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227	
+P22203	UniProtKB	Mutagenesis	233	233	.	.	.	Note=Reduces ATPase activity by 74%25. Reduces ATPase activity by 90%25 and produces structurally aberrant V-ATPase complexes%3B when associated with A-202. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227	
+P22203	UniProtKB	Sequence conflict	97	98	.	.	.	Note=DG->ER;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22203	UniProtKB	Helix	10	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P22203	UniProtKB	Helix	114	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P22203	UniProtKB	Beta strand	135	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P22203	UniProtKB	Turn	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P22203	UniProtKB	Helix	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P22203	UniProtKB	Helix	153	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P22203	UniProtKB	Turn	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P22203	UniProtKB	Beta strand	171	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P22203	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P22203	UniProtKB	Beta strand	185	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P22203	UniProtKB	Beta strand	198	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+P22203	UniProtKB	Helix	203	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA	
+##sequence-region Q04301 1 562
+Q04301	UniProtKB	Chain	1	562	.	.	.	ID=PRO_0000173428;Note=Vacuolar basic amino acid transporter 1	
+Q04301	UniProtKB	Topological domain	1	30	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	31	51	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	52	100	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	122	131	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	153	166	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	167	187	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	188	190	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	191	211	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	212	232	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	254	255	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	256	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	277	292	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	293	313	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	314	331	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	332	352	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	353	365	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	366	386	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	387	419	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	420	440	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	441	448	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	449	469	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	470	528	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Transmembrane	529	549	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Topological domain	550	562	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Glycosylation	123	123	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Glycosylation	324	324	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04301	UniProtKB	Glycosylation	504	504	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25594 1 458
+P25594	UniProtKB	Chain	1	458	.	.	.	ID=PRO_0000173424;Note=Vacuolar basic amino acid transporter 3	
+P25594	UniProtKB	Topological domain	1	9	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Topological domain	31	36	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Transmembrane	37	57	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Topological domain	58	67	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Topological domain	89	132	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Transmembrane	133	153	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Topological domain	154	163	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Topological domain	185	205	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Transmembrane	206	226	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Topological domain	227	248	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Transmembrane	249	269	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Topological domain	270	277	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Transmembrane	278	298	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Topological domain	299	306	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Transmembrane	307	327	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Topological domain	328	415	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Transmembrane	416	436	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Topological domain	437	458	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25594	UniProtKB	Glycosylation	195	195	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03785 1 461
+Q03785	UniProtKB	Chain	1	461	.	.	.	ID=PRO_0000086789;Note=Serine/threonine-protein kinase VHS1	
+Q03785	UniProtKB	Domain	12	337	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03785	UniProtKB	Nucleotide binding	18	26	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03785	UniProtKB	Active site	185	185	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q03785	UniProtKB	Binding site	41	41	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region P53262 1 265
+P53262	UniProtKB	Signal peptide	1	24	.	.	.	.	
+P53262	UniProtKB	Chain	25	265	.	.	.	ID=PRO_0000042985;Note=V0 assembly protein 1	
+P53262	UniProtKB	Topological domain	25	223	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53262	UniProtKB	Transmembrane	224	244	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53262	UniProtKB	Topological domain	245	265	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53262	UniProtKB	Motif	262	265	.	.	.	Note=ER retention motif	
+P53262	UniProtKB	Glycosylation	69	69	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53262	UniProtKB	Glycosylation	104	104	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53262	UniProtKB	Glycosylation	172	172	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32563 1 840
+P32563	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.6;Dbxref=PMID:22814378	
+P32563	UniProtKB	Chain	2	840	.	.	.	ID=PRO_0000119224;Note=V-type proton ATPase subunit a%2C vacuolar isoform	
+P32563	UniProtKB	Topological domain	2	404	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Transmembrane	405	423	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Topological domain	424	425	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Transmembrane	426	442	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Topological domain	443	456	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Transmembrane	457	486	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Topological domain	487	534	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Transmembrane	535	554	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Topological domain	555	572	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Transmembrane	573	593	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Topological domain	594	636	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Transmembrane	637	656	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Topological domain	657	719	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Transmembrane	720	744	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Topological domain	745	765	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Transmembrane	766	804	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Topological domain	805	840	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Coiled coil	117	145	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32563	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.6;Dbxref=PMID:22814378	
+P32563	UniProtKB	Mutagenesis	425	425	.	.	.	Note=Reduces assembly of V-ATPase complexes and reduces ATPase activity of the assembled complexes. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8798414;Dbxref=PMID:8798414	
+P32563	UniProtKB	Mutagenesis	538	538	.	.	.	Note=Reduces assembly of V-ATPase complexes. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8798414;Dbxref=PMID:8798414	
+P32563	UniProtKB	Mutagenesis	593	593	.	.	.	Note=Reduces ATPase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8798414;Dbxref=PMID:8798414	
+P32563	UniProtKB	Mutagenesis	634	634	.	.	.	Note=Reduces subunit stability. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8798414;Dbxref=PMID:8798414	
+P32563	UniProtKB	Mutagenesis	729	729	.	.	.	Note=Reduces ATPase activity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970	
+P32563	UniProtKB	Mutagenesis	735	735	.	.	.	Note=Reduces subunit stability. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8798414;Dbxref=PMID:8798414	
+P32563	UniProtKB	Mutagenesis	739	739	.	.	.	Note=Reduces ATPase activity. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970	
+P32563	UniProtKB	Mutagenesis	743	743	.	.	.	Note=Reduces ATPase activity. H->A%2CE%2CY;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8798414,ECO:0000269|PubMed:9506970;Dbxref=PMID:8798414,PMID:9506970	
+P32563	UniProtKB	Mutagenesis	746	746	.	.	.	Note=Reduces ATPase activity. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970	
+P32563	UniProtKB	Mutagenesis	780	780	.	.	.	Note=Reduces assembly of V-ATPase complexes. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970	
+P32563	UniProtKB	Mutagenesis	789	789	.	.	.	Note=Abolishes ATPase activity and proton transport%2C but does not affect complex assembly. E->A%2CD%2CH%2CQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8798414,ECO:0000269|PubMed:9506970;Dbxref=PMID:8798414,PMID:9506970	
+P32563	UniProtKB	Mutagenesis	800	800	.	.	.	Note=Reduces assembly of V-ATPase complexes. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970	
+P32563	UniProtKB	Mutagenesis	802	802	.	.	.	Note=Reduces assembly of V-ATPase complexes. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970	
+P32563	UniProtKB	Mutagenesis	803	803	.	.	.	Note=Reduces ATPase activity. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970	
+P32563	UniProtKB	Mutagenesis	803	803	.	.	.	Note=Reduces assembly of V-ATPase complexes. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970	
+P32563	UniProtKB	Mutagenesis	809	809	.	.	.	Note=Reduces assembly of V-ATPase complexes. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970	
+P32563	UniProtKB	Mutagenesis	814	814	.	.	.	Note=Reduces assembly of V-ATPase complexes. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970	
+P32563	UniProtKB	Beta strand	723	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVJ	
+P32563	UniProtKB	Helix	729	747	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JTW	
+##sequence-region P47142 1 202
+P47142	UniProtKB	Chain	1	202	.	.	.	ID=PRO_0000215221;Note=Vacuolar protein-sorting-associated protein 25	
+P47142	UniProtKB	Helix	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Helix	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Helix	20	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Beta strand	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Beta strand	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Turn	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Helix	87	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Beta strand	102	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Beta strand	120	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Helix	128	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Helix	151	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Turn	164	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Helix	170	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Helix	182	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Beta strand	187	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+P47142	UniProtKB	Beta strand	196	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4	
+##sequence-region P38959 1 992
+P38959	UniProtKB	Chain	1	992	.	.	.	ID=PRO_0000212827;Note=Vacuolar protein sorting-associated protein 41	
+P38959	UniProtKB	Repeat	114	152	.	.	.	Note=WD 1	
+P38959	UniProtKB	Repeat	153	192	.	.	.	Note=WD 2	
+P38959	UniProtKB	Repeat	194	234	.	.	.	Note=WD 3	
+P38959	UniProtKB	Repeat	240	280	.	.	.	Note=WD 4	
+P38959	UniProtKB	Repeat	324	366	.	.	.	Note=WD 5	
+P38959	UniProtKB	Repeat	753	901	.	.	.	Note=CHCR	
+P38959	UniProtKB	Compositional bias	79	94	.	.	.	Note=Poly-Asp	
+P38959	UniProtKB	Compositional bias	239	244	.	.	.	Note=Poly-Lys	
+P38959	UniProtKB	Modified residue	26	26	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38959	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38959	UniProtKB	Sequence conflict	424	424	.	.	.	Note=K->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38932 1 577
+P38932	UniProtKB	Chain	1	577	.	.	.	ID=PRO_0000206316;Note=Vacuolar protein sorting-associated protein 45	
+P38932	UniProtKB	Sequence conflict	136	136	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38932	UniProtKB	Sequence conflict	239	239	.	.	.	Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12071 1 889
+Q12071	UniProtKB	Chain	1	889	.	.	.	ID=PRO_0000148737;Note=Vacuolar protein sorting-associated protein 54	
+Q12071	UniProtKB	Coiled coil	286	321	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12071	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12071	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12071	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P47111 1 140
+P47111	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000215201;Note=Vacuolar protein sorting-associated protein 55	
+P47111	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47111	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47111	UniProtKB	Topological domain	33	37	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47111	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47111	UniProtKB	Topological domain	59	76	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47111	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47111	UniProtKB	Topological domain	98	107	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47111	UniProtKB	Transmembrane	108	128	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47111	UniProtKB	Topological domain	129	140	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47111	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q12016 1 184
+Q12016	UniProtKB	Chain	1	184	.	.	.	ID=PRO_0000174187;Note=Vacuolar protein sorting-associated protein 68	
+Q12016	UniProtKB	Transmembrane	26	46	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12016	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12016	UniProtKB	Transmembrane	115	135	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12016	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12016	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q12016	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956	
+Q12016	UniProtKB	Glycosylation	52	52	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06385 1 345
+Q06385	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000123823;Note=Vacuolar protein sorting-associated protein 74	
+Q06385	UniProtKB	Region	197	208	.	.	.	Note=Beta-hairpin required for oligomerization	
+Q06385	UniProtKB	Binding site	88	88	.	.	.	Note=PtdIns4P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06385	UniProtKB	Binding site	97	97	.	.	.	Note=PtdIns4P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06385	UniProtKB	Binding site	178	178	.	.	.	Note=PtdIns4P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06385	UniProtKB	Binding site	181	181	.	.	.	Note=PtdIns4P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06385	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06385	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:22889169;Dbxref=PMID:22889169	
+Q06385	UniProtKB	Mutagenesis	6	8	.	.	.	Note=Loss of coatomer-binding. RRR->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22889169;Dbxref=PMID:22889169	
+Q06385	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Alters phosphorylation but has not effect on Golgi enzymes localization. S->A	
+Q06385	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Abolishes phosphoinositide binding and Golgi localization%3B when associated with A-97. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20026658;Dbxref=PMID:20026658	
+Q06385	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Abolishes phosphoinositide binding and Golgi localization%3B when associated with A-88. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20026658;Dbxref=PMID:20026658	
+Q06385	UniProtKB	Mutagenesis	178	178	.	.	.	Note=Abolishes phosphoinositide binding and Golgi localization%3B when associated with A-181. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20026658;Dbxref=PMID:20026658	
+Q06385	UniProtKB	Mutagenesis	181	181	.	.	.	Note=Abolishes phosphoinositide binding and Golgi localization%3B when associated with A-178. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20026658;Dbxref=PMID:20026658	
+Q06385	UniProtKB	Helix	69	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Beta strand	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	90	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Beta strand	109	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	116	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Beta strand	126	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	139	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	156	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Turn	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	170	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	180	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Beta strand	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Beta strand	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	214	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Beta strand	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	248	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	266	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	274	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Beta strand	292	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Beta strand	303	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	310	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Helix	325	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+Q06385	UniProtKB	Turn	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH	
+##sequence-region Q07655 1 649
+Q07655	UniProtKB	Chain	1	649	.	.	.	ID=PRO_0000262756;Note=Protein WHI4	
+Q07655	UniProtKB	Domain	533	625	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q07655	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07655	UniProtKB	Modified residue	206	206	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07655	UniProtKB	Modified residue	258	258	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07655	UniProtKB	Modified residue	283	283	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40080 1 203
+P40080	UniProtKB	Chain	1	203	.	.	.	ID=PRO_0000202649;Note=VPS4-associated protein 1	
+P40080	UniProtKB	Coiled coil	121	157	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40080	UniProtKB	Helix	189	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FVK	
+##sequence-region P41806 1 77
+P41806	UniProtKB	Chain	1	77	.	.	.	ID=PRO_0000065875;Note=Vacuolar ATPase assembly integral membrane protein VMA21	
+P41806	UniProtKB	Topological domain	1	13	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03058	
+P41806	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03058	
+P41806	UniProtKB	Topological domain	35	38	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03058	
+P41806	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03058	
+P41806	UniProtKB	Topological domain	60	77	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03058	
+P41806	UniProtKB	Motif	74	77	.	.	.	Note=Prevents secretion from ER	
+P41806	UniProtKB	Mutagenesis	74	75	.	.	.	Note=Mislocalizes to the vacuole membrane and stay associated with the V0 sector after transport out of the ER. KK->QQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15356264,ECO:0000269|PubMed:7841520;Dbxref=PMID:15356264,PMID:7841520	
+P41806	UniProtKB	Mutagenesis	74	74	.	.	.	Note=Secretion from ER. K->Q	
+P41806	UniProtKB	Mutagenesis	75	75	.	.	.	Note=Secretion from ER. K->Q	
+P41806	UniProtKB	Sequence conflict	70	70	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P42839 1 908
+P42839	UniProtKB	Chain	1	908	.	.	.	ID=PRO_0000209505;Note=Low affinity vacuolar monovalent cation/H(+) antiporter	
+P42839	UniProtKB	Topological domain	1	244	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	245	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	266	408	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	409	429	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	430	494	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	495	515	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	516	530	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	531	551	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	552	560	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	561	581	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	582	587	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	588	608	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	609	626	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	627	647	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	648	686	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	687	707	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	708	746	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	747	767	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	768	783	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	784	804	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	805	816	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	817	837	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	838	851	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	852	872	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	873	885	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Transmembrane	886	906	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Topological domain	907	908	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42839	UniProtKB	Modified residue	26	26	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P42839	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P42839	UniProtKB	Modified residue	33	33	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P42839	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P42839	UniProtKB	Modified residue	118	118	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P42839	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P42839	UniProtKB	Glycosylation	361	361	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39904 1 641
+P39904	UniProtKB	Chain	1	641	.	.	.	ID=PRO_0000213318;Note=Vacuolar protein sorting-associated protein 52	
+P39904	UniProtKB	Coiled coil	81	110	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39904	UniProtKB	Modified residue	602	602	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39904	UniProtKB	Sequence conflict	204	209	.	.	.	Note=KRLIIS->EKTYYF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03913 1 190
+Q03913	UniProtKB	Chain	1	190	.	.	.	ID=PRO_0000299779;Note=Putative uncharacterized protein VPS61	
+Q03913	UniProtKB	Transmembrane	152	174	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03433 1 280
+Q03433	UniProtKB	Chain	1	280	.	.	.	ID=PRO_0000173557;Note=Vacuolar protein sorting-associated protein 71	
+Q03433	UniProtKB	Zinc finger	244	277	.	.	.	Note=HIT-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00453	
+##sequence-region P54787 1 451
+P54787	UniProtKB	Chain	1	451	.	.	.	ID=PRO_0000191324;Note=Vacuolar protein sorting-associated protein 9	
+P54787	UniProtKB	Domain	170	312	.	.	.	Note=VPS9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00550	
+P54787	UniProtKB	Domain	408	451	.	.	.	Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468	
+P54787	UniProtKB	Motif	229	237	.	.	.	Note=GBH motif I	
+P54787	UniProtKB	Motif	249	257	.	.	.	Note=GBH motif II	
+P54787	UniProtKB	Motif	287	295	.	.	.	Note=GBH motif III	
+P54787	UniProtKB	Compositional bias	332	341	.	.	.	Note=Glu/Lys-rich	
+P54787	UniProtKB	Modified residue	375	375	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P54787	UniProtKB	Sequence conflict	172	172	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54787	UniProtKB	Sequence conflict	305	305	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54787	UniProtKB	Sequence conflict	305	305	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54787	UniProtKB	Sequence conflict	314	314	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54787	UniProtKB	Sequence conflict	314	314	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54787	UniProtKB	Sequence conflict	327	327	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54787	UniProtKB	Sequence conflict	327	327	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54787	UniProtKB	Sequence conflict	345	345	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54787	UniProtKB	Sequence conflict	345	345	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54787	UniProtKB	Helix	401	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P3Q	
+P54787	UniProtKB	Helix	425	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P3Q	
+P54787	UniProtKB	Helix	441	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P3Q	
+P54787	UniProtKB	Helix	445	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P3Q	
+##sequence-region Q06263 1 330
+Q06263	UniProtKB	Chain	1	330	.	.	.	ID=PRO_0000065933;Note=Vacuolar protein sorting-associated protein VTA1	
+Q06263	UniProtKB	Region	1	167	.	.	.	Note=Interaction with DID2	
+Q06263	UniProtKB	Region	37	68	.	.	.	Note=Interaction with VSP60;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16505166;Dbxref=PMID:16505166	
+Q06263	UniProtKB	Region	280	330	.	.	.	Note=Dimerization	
+Q06263	UniProtKB	Region	290	330	.	.	.	Note=Interaction with VSP4	
+Q06263	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06263	UniProtKB	Modified residue	195	195	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06263	UniProtKB	Modified residue	233	233	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06263	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Abolishes interaction with VSP60 and DID2. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651	
+Q06263	UniProtKB	Mutagenesis	152	152	.	.	.	Note=Abolishes interaction with VSP60 and DID2. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651	
+Q06263	UniProtKB	Mutagenesis	299	299	.	.	.	Note=Abolishes interaction with VSP4. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16505166;Dbxref=PMID:16505166	
+Q06263	UniProtKB	Mutagenesis	302	302	.	.	.	Note=Abolishes interaction with VSP4. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16505166;Dbxref=PMID:16505166	
+Q06263	UniProtKB	Mutagenesis	303	303	.	.	.	Note=Abolishes interaction with VSP4%2C no effect on dimerization. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651	
+Q06263	UniProtKB	Mutagenesis	306	306	.	.	.	Note=Diminishes interaction with VSP4. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16505166;Dbxref=PMID:16505166	
+Q06263	UniProtKB	Mutagenesis	310	310	.	.	.	Note=Abolishes interaction with VSP4%2C no effect on dimerization. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651	
+Q06263	UniProtKB	Mutagenesis	311	311	.	.	.	Note=Abolishes interaction with VSP4 and dimerization. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651	
+Q06263	UniProtKB	Mutagenesis	312	312	.	.	.	Note=Abolishes interaction with VSP4 and dimerization. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651	
+Q06263	UniProtKB	Mutagenesis	320	320	.	.	.	Note=Abolishes dimerization. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651	
+Q06263	UniProtKB	Mutagenesis	322	322	.	.	.	Note=No effect on interaction with VSP4. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16505166;Dbxref=PMID:16505166	
+Q06263	UniProtKB	Mutagenesis	327	327	.	.	.	Note=Abolishes dimerization. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651	
+Q06263	UniProtKB	Sequence conflict	12	12	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06263	UniProtKB	Helix	1	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK	
+Q06263	UniProtKB	Helix	21	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK	
+Q06263	UniProtKB	Helix	43	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK	
+Q06263	UniProtKB	Turn	62	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H7P	
+Q06263	UniProtKB	Helix	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LUH	
+Q06263	UniProtKB	Turn	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK	
+Q06263	UniProtKB	Helix	81	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK	
+Q06263	UniProtKB	Helix	86	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK	
+Q06263	UniProtKB	Helix	115	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK	
+Q06263	UniProtKB	Helix	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK	
+Q06263	UniProtKB	Helix	141	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK	
+Q06263	UniProtKB	Helix	280	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKL	
+Q06263	UniProtKB	Turn	309	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKL	
+Q06263	UniProtKB	Helix	313	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKL	
+##sequence-region P47165 1 209
+P47165	UniProtKB	Chain	1	209	.	.	.	ID=PRO_0000066042;Note=Xanthine phosphoribosyltransferase 1	
+P47165	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53076 1 958
+P53076	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53076	UniProtKB	Chain	2	958	.	.	.	ID=PRO_0000065829;Note=Vacuolar import and degradation protein 30	
+P53076	UniProtKB	Domain	390	592	.	.	.	Note=B30.2/SPRY;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00548	
+P53076	UniProtKB	Domain	710	742	.	.	.	Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126	
+P53076	UniProtKB	Domain	769	826	.	.	.	Note=CTLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00058	
+P53076	UniProtKB	Compositional bias	165	185	.	.	.	Note=Poly-Asp	
+P53076	UniProtKB	Compositional bias	450	453	.	.	.	Note=Poly-Ser	
+P53076	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53076	UniProtKB	Modified residue	147	147	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53076	UniProtKB	Modified residue	246	246	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53076	UniProtKB	Modified residue	248	248	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53076	UniProtKB	Modified residue	277	277	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P22219 1 1454
+P22219	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+P22219	UniProtKB	Chain	2	1454	.	.	.	ID=PRO_0000086802;Note=Serine/threonine-protein kinase VPS15	
+P22219	UniProtKB	Domain	27	300	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22219	UniProtKB	Repeat	460	497	.	.	.	Note=HEAT 1	
+P22219	UniProtKB	Repeat	576	613	.	.	.	Note=HEAT 2	
+P22219	UniProtKB	Repeat	615	652	.	.	.	Note=HEAT 3	
+P22219	UniProtKB	Repeat	654	691	.	.	.	Note=HEAT 4	
+P22219	UniProtKB	Repeat	1078	1118	.	.	.	Note=WD 1	
+P22219	UniProtKB	Repeat	1126	1165	.	.	.	Note=WD 2	
+P22219	UniProtKB	Repeat	1229	1268	.	.	.	Note=WD 3	
+P22219	UniProtKB	Repeat	1275	1315	.	.	.	Note=WD 4	
+P22219	UniProtKB	Repeat	1344	1382	.	.	.	Note=WD 5	
+P22219	UniProtKB	Repeat	1422	1453	.	.	.	Note=WD 6	
+P22219	UniProtKB	Nucleotide binding	33	41	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22219	UniProtKB	Active site	147	147	.	.	.	Note=Proton acceptor	
+P22219	UniProtKB	Binding site	54	54	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22219	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716	
+P22219	UniProtKB	Mutagenesis	2	2	.	.	.	Note=No myristoylation%2C but still membrane-association and normal activity. G->A%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716	
+P22219	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Loss of activity. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716	
+P22219	UniProtKB	Mutagenesis	147	147	.	.	.	Note=Loss of activity. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716	
+P22219	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Loss of activity. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716	
+P22219	UniProtKB	Mutagenesis	151	151	.	.	.	Note=Modest effect on activity and normal CPY sorting. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716	
+P22219	UniProtKB	Mutagenesis	165	165	.	.	.	Note=Loss of activity. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1988155;Dbxref=PMID:1988155	
+P22219	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Loss of activity. No activation of VPS34 kinase activity. E->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1988155,ECO:0000269|PubMed:8387919;Dbxref=PMID:1988155,PMID:8387919	
+P22219	UniProtKB	Sequence conflict	134	134	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22219	UniProtKB	Sequence conflict	134	134	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22219	UniProtKB	Sequence conflict	443	443	.	.	.	Note=L->PV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22219	UniProtKB	Sequence conflict	610	610	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22219	UniProtKB	Sequence conflict	851	851	.	.	.	Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22219	UniProtKB	Sequence conflict	851	851	.	.	.	Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22219	UniProtKB	Sequence conflict	851	851	.	.	.	Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22219	UniProtKB	Helix	1034	1036	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Helix	1046	1048	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Helix	1050	1052	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Helix	1064	1066	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1070	1075	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Turn	1077	1080	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1083	1089	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1091	1093	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1095	1100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1103	1109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Helix	1110	1114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1122	1126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1131	1136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1140	1147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1150	1162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1165	1178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Helix	1179	1182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1188	1195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1200	1206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1209	1215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Turn	1216	1218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1221	1226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Helix	1229	1231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1234	1239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1245	1250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1255	1259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Turn	1260	1263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1264	1270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1275	1282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Turn	1284	1286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1290	1297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1300	1306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Turn	1307	1310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1311	1321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Helix	1325	1328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Helix	1335	1337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Helix	1346	1349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1352	1355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1358	1363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Helix	1364	1366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1368	1373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Helix	1377	1379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1381	1384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1392	1399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1402	1408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1427	1445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+P22219	UniProtKB	Beta strand	1450	1454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE	
+##sequence-region P21576 1 704
+P21576	UniProtKB	Chain	1	704	.	.	.	ID=PRO_0000206588;Note=Vacuolar protein sorting-associated protein 1	
+P21576	UniProtKB	Domain	26	336	.	.	.	Note=Dynamin-type G	
+P21576	UniProtKB	Domain	618	704	.	.	.	Note=GED;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00720	
+P21576	UniProtKB	Nucleotide binding	36	43	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21576	UniProtKB	Nucleotide binding	178	182	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21576	UniProtKB	Nucleotide binding	247	250	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21576	UniProtKB	Modified residue	579	579	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P21576	UniProtKB	Modified residue	599	599	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P21576	UniProtKB	Sequence conflict	33	33	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21576	UniProtKB	Sequence conflict	111	111	.	.	.	Note=N->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21576	UniProtKB	Sequence conflict	141	141	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02767 1 242
+Q02767	UniProtKB	Chain	1	242	.	.	.	ID=PRO_0000120958;Note=Vacuolar protein sorting-associated protein 28	
+Q02767	UniProtKB	Domain	11	125	.	.	.	Note=VPS28 N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00645	
+Q02767	UniProtKB	Domain	148	242	.	.	.	Note=VPS28 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00642	
+Q02767	UniProtKB	Region	148	242	.	.	.	Note=Interaction with VSP36 and VPS20;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16749904;Dbxref=PMID:16749904	
+Q02767	UniProtKB	Mutagenesis	40	40	.	.	.	Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVB)%3B when associated with D-44. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894	
+Q02767	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVB)%3B when associated with D-40. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894	
+Q02767	UniProtKB	Mutagenesis	228	231	.	.	.	Note=Abolishes interaction with VPS20. FDLE->ASLA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16749904;Dbxref=PMID:16749904	
+Q02767	UniProtKB	Sequence conflict	193	193	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02767	UniProtKB	Beta strand	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+Q02767	UniProtKB	Helix	14	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M	
+Q02767	UniProtKB	Beta strand	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+Q02767	UniProtKB	Helix	31	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M	
+Q02767	UniProtKB	Helix	64	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M	
+Q02767	UniProtKB	Turn	85	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M	
+Q02767	UniProtKB	Helix	89	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M	
+Q02767	UniProtKB	Helix	109	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M	
+Q02767	UniProtKB	Helix	150	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U	
+Q02767	UniProtKB	Helix	174	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U	
+Q02767	UniProtKB	Helix	199	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U	
+Q02767	UniProtKB	Helix	220	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U	
+##sequence-region P22543 1 875
+P22543	UniProtKB	Chain	1	875	.	.	.	ID=PRO_0000088818;Note=Phosphatidylinositol 3-kinase VPS34	
+P22543	UniProtKB	Domain	14	188	.	.	.	Note=C2 PI3K-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00880	
+P22543	UniProtKB	Domain	293	526	.	.	.	Note=PIK helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00878	
+P22543	UniProtKB	Domain	619	873	.	.	.	Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269	
+P22543	UniProtKB	Mutagenesis	731	731	.	.	.	Note=Loss of kinase activity and no vacuolar carboxypeptidase Y (PCR1) sorting to the vacuole. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8385367;Dbxref=PMID:8385367	
+P22543	UniProtKB	Mutagenesis	736	736	.	.	.	Note=Loss of kinase activity and no vacuolar carboxypeptidase Y (PCR1) sorting to the vacuole. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8385367;Dbxref=PMID:8385367	
+P22543	UniProtKB	Mutagenesis	749	749	.	.	.	Note=Loss of kinase activity and no vacuolar carboxypeptidase Y (PCR1) sorting to the vacuole. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8385367;Dbxref=PMID:8385367	
+##sequence-region Q06696 1 566
+Q06696	UniProtKB	Chain	1	566	.	.	.	ID=PRO_0000215227;Note=Vacuolar protein-sorting-associated protein 36	
+Q06696	UniProtKB	Domain	7	96	.	.	.	Note=GLUE N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00828	
+Q06696	UniProtKB	Domain	255	288	.	.	.	Note=GLUE C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00828	
+Q06696	UniProtKB	Zinc finger	114	151	.	.	.	Note=RanBP2-type 1%3B degenerate	
+Q06696	UniProtKB	Zinc finger	177	205	.	.	.	Note=RanBP2-type 2	
+Q06696	UniProtKB	Mutagenesis	187	188	.	.	.	Note=Abolishes ubiquitin-binding and vacuole sorting of ubiquitinated proteins. TF->GS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15029239;Dbxref=PMID:15029239	
+Q06696	UniProtKB	Beta strand	23	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY	
+Q06696	UniProtKB	Beta strand	43	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY	
+Q06696	UniProtKB	Helix	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY	
+Q06696	UniProtKB	Beta strand	67	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY	
+Q06696	UniProtKB	Helix	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY	
+Q06696	UniProtKB	Beta strand	74	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY	
+Q06696	UniProtKB	Beta strand	82	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY	
+Q06696	UniProtKB	Beta strand	89	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY	
+Q06696	UniProtKB	Beta strand	116	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U	
+Q06696	UniProtKB	Turn	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U	
+Q06696	UniProtKB	Beta strand	126	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U	
+Q06696	UniProtKB	Turn	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U	
+Q06696	UniProtKB	Helix	152	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U	
+Q06696	UniProtKB	Helix	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U	
+Q06696	UniProtKB	Beta strand	256	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY	
+Q06696	UniProtKB	Helix	266	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY	
+##sequence-region Q92331 1 675
+Q92331	UniProtKB	Chain	1	675	.	.	.	ID=PRO_0000213804;Note=Vacuolar protein sorting-associated protein 5	
+Q92331	UniProtKB	Domain	279	394	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
+Q92331	UniProtKB	Binding site	320	320	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92331	UniProtKB	Binding site	346	346	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92331	UniProtKB	Binding site	360	360	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92331	UniProtKB	Sequence conflict	376	376	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04338 1 217
+Q04338	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+Q04338	UniProtKB	Chain	2	217	.	.	.	ID=PRO_0000218232;Note=t-SNARE VTI1	
+Q04338	UniProtKB	Topological domain	2	194	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04338	UniProtKB	Transmembrane	195	215	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04338	UniProtKB	Topological domain	216	217	.	.	.	Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04338	UniProtKB	Domain	124	186	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+Q04338	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+Q04338	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q04338	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04338	UniProtKB	Mutagenesis	130	130	.	.	.	Note=In VTI1-2%3B exhibits defects in TGN to PVC transport at nonpermissive temperature%3B when associated with T-151. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565	
+Q04338	UniProtKB	Mutagenesis	141	141	.	.	.	Note=In VTI1-12%3B blocks constitutively the traffic from the late Golgi to the vacuole and blocks the transport to the cis-Golgi compartment at nonpermissive temperature%3B when associated with R-158. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565	
+Q04338	UniProtKB	Mutagenesis	145	145	.	.	.	Note=In VTI1-11%3B displays a block in traffic to the PVC and an additional defect in retrograde traffic to the cis-Golgi%3B when associated with F-155. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565	
+Q04338	UniProtKB	Mutagenesis	145	145	.	.	.	Note=In VTI1-1%3B exhibits defects in TGN to PVC transport at nonpermissive temperature%3B when associated with R-148. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565	
+Q04338	UniProtKB	Mutagenesis	148	148	.	.	.	Note=In VTI1-1%3B exhibits defects in TGN to PVC transport at nonpermissive temperature%3B when associated with K-145. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565	
+Q04338	UniProtKB	Mutagenesis	151	151	.	.	.	Note=In VTI1-2%3B exhibits defects in TGN to PVC transport at nonpermissive temperature%3B when associated with P-130. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565	
+Q04338	UniProtKB	Mutagenesis	155	155	.	.	.	Note=In VTI1-11%3B displays a block in traffic to the PVC and an additional defect in retrograde traffic to the cis-Golgi%3B when associated with G-145. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565	
+Q04338	UniProtKB	Mutagenesis	158	158	.	.	.	Note=In VTI1-12%3B blocks constitutively the traffic from the late Golgi to the vacuole and blocks the transport to the cis-Golgi compartment at nonpermissive temperature%3B when associated with S-141. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565	
+Q04338	UniProtKB	Helix	4	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONJ	
+Q04338	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONJ	
+Q04338	UniProtKB	Helix	31	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONJ	
+Q04338	UniProtKB	Helix	66	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONJ	
+Q04338	UniProtKB	Helix	88	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONJ	
+##sequence-region P40151 1 587
+P40151	UniProtKB	Chain	1	587	.	.	.	ID=PRO_0000084788;Note=DNA-dependent ATPase MGS1	
+P40151	UniProtKB	Zinc finger	11	34	.	.	.	Note=UBZ-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40151	UniProtKB	Nucleotide binding	177	184	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40151	UniProtKB	Nucleotide binding	179	185	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072	
+##sequence-region P39102 1 459
+P39102	UniProtKB	Chain	1	459	.	.	.	ID=PRO_0000071121;Note=DnaJ protein homolog XDJ1	
+P39102	UniProtKB	Domain	7	79	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P39102	UniProtKB	Repeat	159	166	.	.	.	Note=CXXCXGXG motif	
+P39102	UniProtKB	Repeat	181	188	.	.	.	Note=CXXCXGXG motif	
+P39102	UniProtKB	Repeat	208	215	.	.	.	Note=CXXCXGXG motif	
+P39102	UniProtKB	Repeat	228	235	.	.	.	Note=CXXCXGXG motif	
+P39102	UniProtKB	Zinc finger	146	240	.	.	.	Note=CR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00546	
+P39102	UniProtKB	Sequence conflict	119	119	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39102	UniProtKB	Sequence conflict	448	448	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38759 1 282
+P38759	UniProtKB	Chain	1	282	.	.	.	ID=PRO_0000058305;Note=Vacuolar protein sorting-associated protein 29	
+##sequence-region O13584 1 106
+O13584	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000299782;Note=Putative uncharacterized protein VPS69	
+O13584	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13584	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40438 1 1549
+P40438	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40438	UniProtKB	Chain	22	1549	.	.	.	ID=PRO_0000014329;Note=VPS10 homolog 1	
+P40438	UniProtKB	Topological domain	22	1369	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40438	UniProtKB	Transmembrane	1370	1390	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40438	UniProtKB	Topological domain	1391	1549	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40438	UniProtKB	Repeat	57	68	.	.	.	Note=BNR 1	
+P40438	UniProtKB	Repeat	101	112	.	.	.	Note=BNR 2	
+P40438	UniProtKB	Repeat	159	170	.	.	.	Note=BNR 3	
+P40438	UniProtKB	Repeat	228	239	.	.	.	Note=BNR 4	
+P40438	UniProtKB	Repeat	393	404	.	.	.	Note=BNR 5	
+P40438	UniProtKB	Repeat	465	476	.	.	.	Note=BNR 6	
+P40438	UniProtKB	Repeat	511	522	.	.	.	Note=BNR 7	
+P40438	UniProtKB	Repeat	740	751	.	.	.	Note=BNR 8	
+P40438	UniProtKB	Repeat	837	848	.	.	.	Note=BNR 9	
+P40438	UniProtKB	Repeat	1040	1051	.	.	.	Note=BNR 10	
+P40438	UniProtKB	Repeat	1119	1130	.	.	.	Note=BNR 11	
+P40438	UniProtKB	Repeat	1160	1171	.	.	.	Note=BNR 12	
+P40438	UniProtKB	Glycosylation	479	479	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40438	UniProtKB	Glycosylation	769	769	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40438	UniProtKB	Glycosylation	986	986	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40890 1 1549
+P40890	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40890	UniProtKB	Chain	22	1549	.	.	.	ID=PRO_0000014331;Note=VPS10 homolog 2	
+P40890	UniProtKB	Topological domain	22	1369	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40890	UniProtKB	Transmembrane	1370	1390	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40890	UniProtKB	Topological domain	1391	1549	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40890	UniProtKB	Repeat	57	68	.	.	.	Note=BNR 1	
+P40890	UniProtKB	Repeat	101	112	.	.	.	Note=BNR 2	
+P40890	UniProtKB	Repeat	159	170	.	.	.	Note=BNR 3	
+P40890	UniProtKB	Repeat	228	239	.	.	.	Note=BNR 4	
+P40890	UniProtKB	Repeat	393	404	.	.	.	Note=BNR 5	
+P40890	UniProtKB	Repeat	465	476	.	.	.	Note=BNR 6	
+P40890	UniProtKB	Repeat	511	522	.	.	.	Note=BNR 7	
+P40890	UniProtKB	Repeat	740	751	.	.	.	Note=BNR 8	
+P40890	UniProtKB	Repeat	837	848	.	.	.	Note=BNR 9	
+P40890	UniProtKB	Repeat	1040	1051	.	.	.	Note=BNR 10	
+P40890	UniProtKB	Repeat	1119	1130	.	.	.	Note=BNR 11	
+P40890	UniProtKB	Repeat	1160	1171	.	.	.	Note=BNR 12	
+P40890	UniProtKB	Glycosylation	479	479	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40890	UniProtKB	Glycosylation	769	769	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40890	UniProtKB	Glycosylation	986	986	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08831 1 523
+Q08831	UniProtKB	Chain	1	523	.	.	.	ID=PRO_0000081458;Note=Protein VTS1	
+Q08831	UniProtKB	Domain	451	512	.	.	.	Note=SAM	
+Q08831	UniProtKB	Compositional bias	74	178	.	.	.	Note=Gln-rich	
+Q08831	UniProtKB	Compositional bias	374	384	.	.	.	Note=His-rich	
+Q08831	UniProtKB	Mutagenesis	467	467	.	.	.	Note=Loss of RNA-binding. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12858164;Dbxref=PMID:12858164	
+Q08831	UniProtKB	Mutagenesis	498	498	.	.	.	Note=Loss of RNA-binding. A->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12858164;Dbxref=PMID:12858164	
+Q08831	UniProtKB	Helix	444	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D	
+Q08831	UniProtKB	Helix	450	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D	
+Q08831	UniProtKB	Helix	456	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D	
+Q08831	UniProtKB	Helix	466	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D	
+Q08831	UniProtKB	Helix	469	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D	
+Q08831	UniProtKB	Helix	477	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D	
+Q08831	UniProtKB	Helix	485	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D	
+Q08831	UniProtKB	Helix	496	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D	
+Q08831	UniProtKB	Helix	520	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D	
+##sequence-region P12611 1 486
+P12611	UniProtKB	Chain	1	486	.	.	.	ID=PRO_0000065967;Note=Growth regulation protein	
+P12611	UniProtKB	Sequence conflict	216	216	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P34761 1 661
+P34761	UniProtKB	Chain	1	661	.	.	.	ID=PRO_0000082005;Note=Protein WHI3	
+P34761	UniProtKB	Domain	538	625	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P34761	UniProtKB	Compositional bias	247	277	.	.	.	Note=Gln-rich	
+P34761	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40463 1 436
+P40463	UniProtKB	Chain	1	436	.	.	.	ID=PRO_0000065812;Note=Protein VHS2	
+P40463	UniProtKB	Compositional bias	386	424	.	.	.	Note=Asn-rich	
+P40463	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40463	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40463	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40463	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40463	UniProtKB	Modified residue	299	299	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40463	UniProtKB	Modified residue	301	301	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40463	UniProtKB	Modified residue	303	303	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40463	UniProtKB	Modified residue	325	325	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q12045 1 647
+Q12045	UniProtKB	Chain	1	647	.	.	.	ID=PRO_0000270929;Note=Spindle pole body-associated protein VIK1	
+Q12045	UniProtKB	Coiled coil	202	350	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12045	UniProtKB	Helix	353	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	376	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Helix	383	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	390	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Turn	394	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	398	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Turn	402	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	407	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	411	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Turn	416	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Helix	421	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Helix	430	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	443	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Helix	454	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Helix	470	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	475	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	486	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ETP	
+Q12045	UniProtKB	Beta strand	490	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	506	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	514	518	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	521	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Helix	526	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Turn	532	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	546	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	570	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Helix	580	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Helix	599	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Beta strand	614	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Helix	622	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+Q12045	UniProtKB	Helix	625	638	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A	
+##sequence-region P32341 1 215
+P32341	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000065874;Note=Vacuolar ATPase assembly integral membrane protein VPH2	
+P32341	UniProtKB	Topological domain	1	134	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32341	UniProtKB	Transmembrane	135	155	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32341	UniProtKB	Topological domain	156	167	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32341	UniProtKB	Transmembrane	168	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32341	UniProtKB	Topological domain	187	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07878 1 3144
+Q07878	UniProtKB	Chain	1	3144	.	.	.	ID=PRO_0000065887;Note=Vacuolar protein sorting-associated protein 13	
+Q07878	UniProtKB	Modified residue	1364	1364	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07878	UniProtKB	Modified residue	1382	1382	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07878	UniProtKB	Modified residue	1715	1715	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q07878	UniProtKB	Modified residue	1729	1729	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07878	UniProtKB	Modified residue	1731	1731	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q03390 1 229
+Q03390	UniProtKB	Chain	1	229	.	.	.	ID=PRO_0000211507;Note=Vacuolar protein-sorting-associated protein 60	
+Q03390	UniProtKB	Region	128	159	.	.	.	Note=Interaction with VTA1	
+Q03390	UniProtKB	Coiled coil	9	155	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03390	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03390	UniProtKB	Mutagenesis	144	148	.	.	.	Note=Abolishes interaction with VTA1 and reduces endosomal localization. IEQGD->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194652;Dbxref=PMID:18194652	
+Q03390	UniProtKB	Helix	129	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LUH	
+Q03390	UniProtKB	Helix	140	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LUH	
+Q03390	UniProtKB	Helix	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LUH	
+Q03390	UniProtKB	Helix	168	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LUH	
+##sequence-region P53853 1 264
+P53853	UniProtKB	Chain	1	264	.	.	.	ID=PRO_0000185675;Note=Vacuolar protein sorting-associated protein 75	
+P53853	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53853	UniProtKB	Helix	7	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Helix	57	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Beta strand	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DM7	
+P53853	UniProtKB	Helix	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Helix	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Helix	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Beta strand	83	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Beta strand	103	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Turn	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Beta strand	119	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Beta strand	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Beta strand	138	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Helix	150	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Turn	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Beta strand	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Helix	166	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Helix	179	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Beta strand	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Beta strand	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Helix	197	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Helix	208	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7	
+P53853	UniProtKB	Helix	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66	
+P53853	UniProtKB	Turn	227	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q68	
+##sequence-region Q12215 1 556
+Q12215	UniProtKB	Signal peptide	1	38	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12215	UniProtKB	Chain	39	556	.	.	.	ID=PRO_0000041485;Note=Cell wall integrity and stress response component 3	
+Q12215	UniProtKB	Topological domain	39	384	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12215	UniProtKB	Transmembrane	385	405	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12215	UniProtKB	Topological domain	406	556	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12215	UniProtKB	Domain	39	132	.	.	.	Note=WSC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00558	
+Q12215	UniProtKB	Compositional bias	137	348	.	.	.	Note=Ser/Thr-rich	
+Q12215	UniProtKB	Glycosylation	84	84	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12215	UniProtKB	Glycosylation	367	367	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12215	UniProtKB	Glycosylation	370	370	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03944 1 604
+Q03944	UniProtKB	Chain	1	604	.	.	.	ID=PRO_0000065907;Note=Vacuolar protein sorting-associated protein 64	
+Q03944	UniProtKB	Topological domain	1	578	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03944	UniProtKB	Transmembrane	579	598	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03944	UniProtKB	Topological domain	599	604	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03944	UniProtKB	Domain	185	257	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+Q03944	UniProtKB	Coiled coil	404	563	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08924 1 1013
+Q08924	UniProtKB	Chain	1	1013	.	.	.	ID=PRO_0000234366;Note=Regulator of Ty1 transposition protein 10	
+Q08924	UniProtKB	Repeat	5	41	.	.	.	Note=WD 1	
+Q08924	UniProtKB	Repeat	45	84	.	.	.	Note=WD 2	
+Q08924	UniProtKB	Repeat	132	174	.	.	.	Note=WD 3	
+Q08924	UniProtKB	Repeat	177	216	.	.	.	Note=WD 4	
+Q08924	UniProtKB	Repeat	219	258	.	.	.	Note=WD 5	
+Q08924	UniProtKB	Repeat	269	308	.	.	.	Note=WD 6	
+Q08924	UniProtKB	Repeat	465	504	.	.	.	Note=WD 7	
+Q08924	UniProtKB	Repeat	586	625	.	.	.	Note=WD 8	
+Q08924	UniProtKB	Repeat	652	702	.	.	.	Note=WD 9	
+Q08924	UniProtKB	Repeat	709	747	.	.	.	Note=WD 10	
+Q08924	UniProtKB	Repeat	761	804	.	.	.	Note=WD 11	
+Q08924	UniProtKB	Repeat	811	852	.	.	.	Note=WD 12	
+Q08924	UniProtKB	Repeat	880	928	.	.	.	Note=WD 13	
+Q08924	UniProtKB	Repeat	934	973	.	.	.	Note=WD 14	
+Q08924	UniProtKB	Repeat	975	1013	.	.	.	Note=WD 15	
+##sequence-region P38739 1 605
+P38739	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38739	UniProtKB	Chain	27	605	.	.	.	ID=PRO_0000041486;Note=Cell wall integrity and stress response component 4	
+P38739	UniProtKB	Transmembrane	415	435	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38739	UniProtKB	Domain	27	110	.	.	.	Note=WSC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00558	
+P38739	UniProtKB	Compositional bias	116	317	.	.	.	Note=Ser/Thr-rich	
+P38739	UniProtKB	Glycosylation	340	340	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38739	UniProtKB	Glycosylation	386	386	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38739	UniProtKB	Glycosylation	389	389	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38739	UniProtKB	Glycosylation	398	398	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38739	UniProtKB	Glycosylation	479	479	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38739	UniProtKB	Glycosylation	553	553	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38739	UniProtKB	Glycosylation	583	583	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43582 1 211
+P43582	UniProtKB	Chain	1	211	.	.	.	ID=PRO_0000076096;Note=WW domain-containing protein WWM1	
+P43582	UniProtKB	Domain	9	43	.	.	.	Note=WW;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224	
+P43582	UniProtKB	Compositional bias	40	121	.	.	.	Note=Pro-rich	
+P43582	UniProtKB	Compositional bias	64	123	.	.	.	Note=Gln-rich	
+P43582	UniProtKB	Compositional bias	135	208	.	.	.	Note=Gly-rich	
+P43582	UniProtKB	Compositional bias	164	210	.	.	.	Note=Asp-rich	
+P43582	UniProtKB	Modified residue	75	75	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43582	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43582	UniProtKB	Cross-link	50	50	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P43582	UniProtKB	Cross-link	60	60	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P40489 1 647
+P40489	UniProtKB	Chain	1	647	.	.	.	ID=PRO_0000066004;Note=Transcriptional repressor XBP1	
+P40489	UniProtKB	Domain	282	395	.	.	.	Note=HTH APSES-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630	
+P40489	UniProtKB	DNA binding	318	339	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630	
+P40489	UniProtKB	Sequence conflict	106	107	.	.	.	Note=LL->FV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07993 1 356
+Q07993	UniProtKB	Chain	1	356	.	.	.	ID=PRO_0000270925;Note=D-xylulose reductase	
+Q07993	UniProtKB	Nucleotide binding	179	184	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07993	UniProtKB	Metal binding	44	44	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07993	UniProtKB	Metal binding	69	69	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07993	UniProtKB	Metal binding	155	155	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53241 1 593
+P53241	UniProtKB	Chain	1	593	.	.	.	ID=PRO_0000121372;Note=Vitamin H transporter	
+P53241	UniProtKB	Topological domain	1	121	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Topological domain	143	166	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Transmembrane	167	187	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Topological domain	188	190	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Transmembrane	191	211	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Topological domain	212	224	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Transmembrane	225	245	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Topological domain	246	291	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Transmembrane	292	312	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Topological domain	313	361	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Transmembrane	362	382	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Topological domain	383	408	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Transmembrane	409	429	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Topological domain	430	432	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Transmembrane	433	453	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Topological domain	454	460	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Transmembrane	461	481	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Topological domain	482	492	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Transmembrane	493	513	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Topological domain	514	526	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Transmembrane	527	547	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Topological domain	548	593	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53241	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53241	UniProtKB	Modified residue	33	33	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53241	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40547 1 921
+P40547	UniProtKB	Chain	1	921	.	.	.	ID=PRO_0000065828;Note=Vacuolar import and degradation protein 28	
+P40547	UniProtKB	Modified residue	226	226	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38784 1 181
+P38784	UniProtKB	Chain	1	181	.	.	.	ID=PRO_0000065876;Note=Vacuolar ATPase assembly protein VMA22	
+P38784	UniProtKB	Alternative sequence	1	5	.	.	.	ID=VSP_058123;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38735 1 1592
+P38735	UniProtKB	Chain	1	1592	.	.	.	ID=PRO_0000093465;Note=ABC transporter ATP-binding protein/permease VMR1	
+P38735	UniProtKB	Topological domain	1	33	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	55	74	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	96	100	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	122	131	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	153	170	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	192	329	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	330	350	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	351	379	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	380	400	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	401	465	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	466	486	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	487	489	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	490	510	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	511	572	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	573	593	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	594	614	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	615	635	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	636	989	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	990	1010	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	1011	1051	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	1052	1072	.	.	.	Note=Helical%3B Name%3D13;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	1073	1115	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	1116	1136	.	.	.	Note=Helical%3B Name%3D14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	1137	1137	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	1138	1158	.	.	.	Note=Helical%3B Name%3D15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	1159	1229	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	1230	1250	.	.	.	Note=Helical%3B Name%3D16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	1251	1252	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Transmembrane	1253	1273	.	.	.	Note=Helical%3B Name%3D17;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Topological domain	1274	1592	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38735	UniProtKB	Domain	338	632	.	.	.	Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Domain	664	908	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P38735	UniProtKB	Domain	981	1282	.	.	.	Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P38735	UniProtKB	Domain	1323	1572	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P38735	UniProtKB	Nucleotide binding	702	709	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P38735	UniProtKB	Nucleotide binding	1357	1364	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P38735	UniProtKB	Glycosylation	11	11	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38735	UniProtKB	Glycosylation	370	370	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P20795 1 691
+P20795	UniProtKB	Chain	1	691	.	.	.	ID=PRO_0000206311;Note=Vacuolar protein sorting-associated protein 33	
+P20795	UniProtKB	Modified residue	626	626	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P34110 1 944
+P34110	UniProtKB	Chain	1	944	.	.	.	ID=PRO_0000065899;Note=Vacuolar protein sorting-associated protein 35	
+P34110	UniProtKB	Modified residue	846	846	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34110	UniProtKB	Modified residue	848	848	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34110	UniProtKB	Modified residue	868	868	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34110	UniProtKB	Sequence conflict	14	20	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P34110	UniProtKB	Sequence conflict	661	661	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P23643 1 1011
+P23643	UniProtKB	Chain	1	1011	.	.	.	ID=PRO_0000065904;Note=Vacuolar protein sorting-associated protein 3	
+P23643	UniProtKB	Domain	143	418	.	.	.	Note=CNH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00795	
+##sequence-region P52917 1 437
+P52917	UniProtKB	Chain	1	437	.	.	.	ID=PRO_0000084760;Note=Vacuolar protein sorting-associated protein 4	
+P52917	UniProtKB	Domain	3	80	.	.	.	Note=MIT	
+P52917	UniProtKB	Nucleotide binding	173	180	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52917	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Inhibits membrane protein sorting to the vacuole. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928862;Dbxref=PMID:17928862	
+P52917	UniProtKB	Mutagenesis	179	179	.	.	.	Note=No ATP hydrolysis. Missorting of vacuolar proteins. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9155008;Dbxref=PMID:9155008	
+P52917	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Abolishes oligomerization. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18272179;Dbxref=PMID:18272179	
+P52917	UniProtKB	Mutagenesis	233	233	.	.	.	Note=Defective in ATP hydrolysis. Missorting of vacuolar proteins. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9155008;Dbxref=PMID:9155008	
+P52917	UniProtKB	Sequence conflict	32	32	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P52917	UniProtKB	Helix	3	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FVK	
+P52917	UniProtKB	Helix	26	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FVK	
+P52917	UniProtKB	Helix	50	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FVK	
+P52917	UniProtKB	Beta strand	123	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	139	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	150	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Beta strand	168	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Beta strand	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	179	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Beta strand	193	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	199	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Turn	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	210	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Beta strand	225	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	234	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Turn	244	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIH	
+P52917	UniProtKB	Helix	250	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	261	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Beta strand	270	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	284	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Beta strand	292	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	301	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Beta strand	313	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKO	
+P52917	UniProtKB	Helix	321	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Turn	330	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	336	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	349	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Beta strand	358	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Beta strand	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Beta strand	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHV	
+P52917	UniProtKB	Beta strand	383	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	388	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	393	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QP9	
+P52917	UniProtKB	Helix	403	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Helix	421	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE	
+P52917	UniProtKB	Beta strand	433	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIH	
+##sequence-region Q02725 1 835
+Q02725	UniProtKB	Chain	1	835	.	.	.	ID=PRO_0000065936;Note=Vacuolar transporter chaperone 3	
+Q02725	UniProtKB	Topological domain	1	709	.	.	.	Note=Cytoplasmic	
+Q02725	UniProtKB	Transmembrane	710	727	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02725	UniProtKB	Topological domain	728	735	.	.	.	Note=Vacuolar	
+Q02725	UniProtKB	Transmembrane	736	756	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02725	UniProtKB	Topological domain	757	778	.	.	.	Note=Cytoplasmic	
+Q02725	UniProtKB	Transmembrane	779	799	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02725	UniProtKB	Topological domain	800	835	.	.	.	Note=Vacuolar	
+Q02725	UniProtKB	Domain	1	145	.	.	.	Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714	
+Q02725	UniProtKB	Region	126	133	.	.	.	Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:27080106;Dbxref=PMID:27080106	
+Q02725	UniProtKB	Coiled coil	385	413	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02725	UniProtKB	Site	22	22	.	.	.	Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43585	
+Q02725	UniProtKB	Site	26	26	.	.	.	Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43585	
+Q02725	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q02725	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02725	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02725	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02725	UniProtKB	Modified residue	195	195	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02725	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q02725	UniProtKB	Modified residue	270	270	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q02725	UniProtKB	Modified residue	274	274	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q02725	UniProtKB	Modified residue	589	589	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q02725	UniProtKB	Modified residue	592	592	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+Q02725	UniProtKB	Modified residue	621	621	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q02725	UniProtKB	Modified residue	622	622	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P47075 1 721
+P47075	UniProtKB	Chain	1	721	.	.	.	ID=PRO_0000065937;Note=Vacuolar transporter chaperone 4	
+P47075	UniProtKB	Topological domain	1	630	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253	
+P47075	UniProtKB	Transmembrane	631	651	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47075	UniProtKB	Transmembrane	652	672	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47075	UniProtKB	Topological domain	673	699	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253	
+P47075	UniProtKB	Transmembrane	700	720	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47075	UniProtKB	Topological domain	721	721	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253	
+P47075	UniProtKB	Domain	1	148	.	.	.	Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714	
+P47075	UniProtKB	Region	126	133	.	.	.	Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:27080106;Dbxref=PMID:27080106	
+P47075	UniProtKB	Site	22	22	.	.	.	Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43585	
+P47075	UniProtKB	Site	26	26	.	.	.	Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43585	
+P47075	UniProtKB	Cross-link	75	75	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P47075	UniProtKB	Helix	2	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIG	
+P47075	UniProtKB	Helix	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT	
+P47075	UniProtKB	Helix	22	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT	
+P47075	UniProtKB	Turn	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT	
+P47075	UniProtKB	Helix	42	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT	
+P47075	UniProtKB	Beta strand	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIQ	
+P47075	UniProtKB	Helix	96	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT	
+P47075	UniProtKB	Helix	143	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT	
+P47075	UniProtKB	Helix	160	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT	
+P47075	UniProtKB	Turn	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT	
+P47075	UniProtKB	Beta strand	195	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Helix	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Helix	208	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Beta strand	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3R	
+P47075	UniProtKB	Helix	232	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Beta strand	236	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Helix	248	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Beta strand	261	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Beta strand	275	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Helix	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Beta strand	293	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Helix	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Helix	304	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Beta strand	310	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIG	
+P47075	UniProtKB	Helix	314	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Helix	329	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Beta strand	352	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Beta strand	369	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Turn	393	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3R	
+P47075	UniProtKB	Beta strand	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Helix	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Beta strand	417	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Beta strand	423	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Helix	439	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Beta strand	447	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3Q	
+P47075	UniProtKB	Beta strand	450	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIG	
+P47075	UniProtKB	Helix	458	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+P47075	UniProtKB	Turn	467	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T	
+##sequence-region Q12416 1 295
+Q12416	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000262757;Note=G1-specific transcriptional repressor WHI5	
+Q12416	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15210110;Dbxref=PMID:15210110	
+Q12416	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12416	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15210110;Dbxref=PMID:19779198,PMID:15210110	
+Q12416	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15210110;Dbxref=PMID:19779198,PMID:15210110	
+Q12416	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12416	UniProtKB	Modified residue	113	113	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12416	UniProtKB	Modified residue	115	115	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12416	UniProtKB	Modified residue	154	154	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12416	UniProtKB	Modified residue	156	156	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12416	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15210110;Dbxref=PMID:15210110	
+Q12416	UniProtKB	Modified residue	262	262	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15210110;Dbxref=PMID:15210110	
+Q12416	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12416	UniProtKB	Modified residue	290	290	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38838 1 269
+P38838	UniProtKB	Chain	1	269	.	.	.	ID=PRO_0000202919;Note=DNA-dependent metalloprotease WSS1	
+P38838	UniProtKB	Domain	20	221	.	.	.	Note=WLM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00730	
+P38838	UniProtKB	Region	161	208	.	.	.	Note=Required and sufficient for binding to DNA	
+P38838	UniProtKB	Motif	152	160	.	.	.	Note=SHP box	
+P38838	UniProtKB	Motif	209	219	.	.	.	Note=VCP-interaction motif (VIM)	
+P38838	UniProtKB	Motif	247	254	.	.	.	Note=SUMO interaction motif 1 (SIM)	
+P38838	UniProtKB	Motif	266	269	.	.	.	Note=SUMO interaction motif 2 (SIM)	
+P38838	UniProtKB	Active site	116	116	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P38838	UniProtKB	Metal binding	115	115	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P38838	UniProtKB	Metal binding	119	119	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P38838	UniProtKB	Metal binding	125	125	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P38838	UniProtKB	Mutagenesis	115	115	.	.	.	Note=In wss1-pd%3B loss of function%3B when associated with A-119. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20516210;Dbxref=PMID:20516210	
+P38838	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24998930;Dbxref=PMID:24998930	
+P38838	UniProtKB	Mutagenesis	119	119	.	.	.	Note=In wss1-pd%3B loss of function%3B when associated with A-115. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20516210;Dbxref=PMID:20516210	
+##sequence-region Q12363 1 437
+Q12363	UniProtKB	Chain	1	437	.	.	.	ID=PRO_0000051463;Note=Transcriptional modulator WTM1	
+Q12363	UniProtKB	Repeat	103	144	.	.	.	Note=WD 1	
+Q12363	UniProtKB	Repeat	221	259	.	.	.	Note=WD 2	
+Q12363	UniProtKB	Repeat	264	304	.	.	.	Note=WD 3	
+Q12363	UniProtKB	Repeat	326	366	.	.	.	Note=WD 4	
+Q12363	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12363	UniProtKB	Modified residue	200	200	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12363	UniProtKB	Modified residue	370	370	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12363	UniProtKB	Modified residue	406	406	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P36095 1 224
+P36095	UniProtKB	Chain	1	224	.	.	.	ID=PRO_0000211487;Note=Vacuolar protein-sorting-associated protein 24	
+P36095	UniProtKB	Cross-link	203	203	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P40343 1 622
+P40343	UniProtKB	Chain	1	622	.	.	.	ID=PRO_0000065893;Note=Vacuolar protein sorting-associated protein 27	
+P40343	UniProtKB	Domain	18	149	.	.	.	Note=VHS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00218	
+P40343	UniProtKB	Domain	258	277	.	.	.	Note=UIM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+P40343	UniProtKB	Domain	301	320	.	.	.	Note=UIM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+P40343	UniProtKB	Zinc finger	170	230	.	.	.	Note=FYVE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
+P40343	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956	
+P40343	UniProtKB	Modified residue	495	495	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40343	UniProtKB	Modified residue	613	613	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40343	UniProtKB	Cross-link	294	294	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40343	UniProtKB	Mutagenesis	185	186	.	.	.	Note=Decreases the association to PtdIns(3)P containing membranes. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12006563;Dbxref=PMID:12006563	
+P40343	UniProtKB	Mutagenesis	193	193	.	.	.	Note=Decreases the association to PtdIns(3)P containing membranes. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12006563;Dbxref=PMID:12006563	
+P40343	UniProtKB	Mutagenesis	270	270	.	.	.	Note=Reduces strongly the ubiquitin-binding activity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11988742;Dbxref=PMID:11988742	
+P40343	UniProtKB	Mutagenesis	313	313	.	.	.	Note=Reduces strongly the ubiquitin-binding activity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11988742;Dbxref=PMID:11988742	
+P40343	UniProtKB	Sequence conflict	321	322	.	.	.	Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40343	UniProtKB	Turn	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY	
+P40343	UniProtKB	Turn	193	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY	
+P40343	UniProtKB	Helix	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY	
+P40343	UniProtKB	Beta strand	206	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY	
+P40343	UniProtKB	Helix	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY	
+P40343	UniProtKB	Beta strand	215	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY	
+P40343	UniProtKB	Helix	223	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY	
+P40343	UniProtKB	Beta strand	251	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q0V	
+P40343	UniProtKB	Helix	259	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q0V	
+P40343	UniProtKB	Helix	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q0W	
+P40343	UniProtKB	Helix	304	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O06	
+P40343	UniProtKB	Helix	352	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW	
+P40343	UniProtKB	Turn	375	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW	
+P40343	UniProtKB	Helix	381	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW	
+##sequence-region P36116 1 164
+P36116	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36116	UniProtKB	Chain	2	164	.	.	.	ID=PRO_0000065905;Note=Vacuolar protein sorting-associated protein 51	
+P36116	UniProtKB	Coiled coil	73	164	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36116	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36116	UniProtKB	Helix	16	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5K	
+##sequence-region P47061 1 822
+P47061	UniProtKB	Chain	1	822	.	.	.	ID=PRO_0000215193;Note=Vacuolar protein sorting-associated protein 53	
+P47061	UniProtKB	Coiled coil	34	58	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47061	UniProtKB	Coiled coil	460	484	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47061	UniProtKB	Helix	567	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+P47061	UniProtKB	Helix	571	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+P47061	UniProtKB	Beta strand	605	608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+P47061	UniProtKB	Helix	615	638	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+P47061	UniProtKB	Helix	639	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+P47061	UniProtKB	Helix	653	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+P47061	UniProtKB	Helix	683	693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+P47061	UniProtKB	Helix	700	710	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+P47061	UniProtKB	Helix	716	729	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+P47061	UniProtKB	Helix	746	750	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+P47061	UniProtKB	Helix	752	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+P47061	UniProtKB	Helix	768	776	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4	
+##sequence-region O13554 1 104
+O13554	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000299781;Note=Putative uncharacterized protein VPS65	
+O13554	UniProtKB	Transmembrane	4	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13554	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03388 1 795
+Q03388	UniProtKB	Chain	1	795	.	.	.	ID=PRO_0000065909;Note=Vacuolar protein sorting-associated protein 72	
+Q03388	UniProtKB	Region	1	281	.	.	.	Note=Interaction with HTZ1	
+Q03388	UniProtKB	Coiled coil	28	63	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03388	UniProtKB	Coiled coil	121	150	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03388	UniProtKB	Coiled coil	204	281	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03388	UniProtKB	Compositional bias	57	85	.	.	.	Note=Asp-rich	
+Q03388	UniProtKB	Compositional bias	315	343	.	.	.	Note=Lys-rich	
+Q03388	UniProtKB	Modified residue	425	425	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P40046 1 129
+P40046	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378	
+P40046	UniProtKB	Chain	2	129	.	.	.	ID=PRO_0000065934;Note=Vacuolar transporter chaperone 1	
+P40046	UniProtKB	Topological domain	2	32	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253	
+P40046	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40046	UniProtKB	Topological domain	54	59	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253	
+P40046	UniProtKB	Transmembrane	60	80	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40046	UniProtKB	Topological domain	81	98	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253	
+P40046	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40046	UniProtKB	Topological domain	120	129	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253	
+P40046	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378	
+##sequence-region P43585 1 828
+P43585	UniProtKB	Chain	1	828	.	.	.	ID=PRO_0000065935;Note=Vacuolar transporter chaperone 2	
+P43585	UniProtKB	Topological domain	1	693	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43585	UniProtKB	Transmembrane	694	716	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43585	UniProtKB	Topological domain	717	727	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43585	UniProtKB	Transmembrane	728	748	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43585	UniProtKB	Topological domain	749	766	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43585	UniProtKB	Transmembrane	767	787	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43585	UniProtKB	Topological domain	788	828	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43585	UniProtKB	Domain	1	146	.	.	.	Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714	
+P43585	UniProtKB	Region	127	134	.	.	.	Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106	
+P43585	UniProtKB	Site	22	22	.	.	.	Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106	
+P43585	UniProtKB	Site	26	26	.	.	.	Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106	
+P43585	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P43585	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P43585	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P43585	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P43585	UniProtKB	Modified residue	583	583	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P43585	UniProtKB	Modified residue	615	615	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P43585	UniProtKB	Modified residue	616	616	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P43585	UniProtKB	Modified residue	620	620	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43585	UniProtKB	Modified residue	626	626	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43585	UniProtKB	Modified residue	657	657	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P43585	UniProtKB	Mutagenesis	22	22	.	.	.	Note=Decreases affinity for inositol polyphosphate. Strongly decreases affinity for inositol polyphosphate%3B when associated with A-26 and A-131. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106	
+P43585	UniProtKB	Mutagenesis	26	26	.	.	.	Note=Decreases affinity for inositol polyphosphate. Strongly decreases affinity for inositol polyphosphate%3B when associated with F-22 and A-131. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106	
+P43585	UniProtKB	Mutagenesis	127	127	.	.	.	Note=Abolishes inositol polyphosphate binding%3B when associated with A-130 and A-134. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106	
+P43585	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Abolishes inositol polyphosphate binding%3B when associated with A-127 and A-134. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106	
+P43585	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Decreases affinity for inositol polyphosphate. Strongly decreases affinity for inositol polyphosphate%3B when associated with F-22 and A-26. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106	
+P43585	UniProtKB	Mutagenesis	134	134	.	.	.	Note=Abolishes inositol polyphosphate binding%3B when associated with A-127 and A-130. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106	
+P43585	UniProtKB	Beta strand	204	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Helix	212	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Beta strand	278	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Helix	289	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Beta strand	303	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Helix	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Beta strand	318	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Beta strand	336	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Helix	345	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Helix	348	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Helix	358	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Helix	374	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Beta strand	397	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Beta strand	416	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Beta strand	434	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Beta strand	444	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Beta strand	452	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Turn	457	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Helix	463	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Beta strand	466	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Beta strand	471	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Helix	503	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Helix	522	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+P43585	UniProtKB	Helix	532	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O	
+##sequence-region P53832 1 503
+P53832	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53832	UniProtKB	Chain	24	503	.	.	.	ID=PRO_0000041484;Note=Cell wall integrity and stress response component 2	
+P53832	UniProtKB	Topological domain	24	325	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53832	UniProtKB	Transmembrane	326	346	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53832	UniProtKB	Topological domain	347	503	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53832	UniProtKB	Domain	25	118	.	.	.	Note=WSC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00558	
+P53832	UniProtKB	Compositional bias	121	319	.	.	.	Note=Ser/Thr-rich	
+P53832	UniProtKB	Modified residue	402	402	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53832	UniProtKB	Modified residue	455	455	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53832	UniProtKB	Modified residue	458	458	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P33418 1 1100
+P33418	UniProtKB	Chain	1	1100	.	.	.	ID=PRO_0000084460;Note=Exportin-T	
+##sequence-region Q12206 1 467
+Q12206	UniProtKB	Chain	1	467	.	.	.	ID=PRO_0000051464;Note=Transcriptional modulator WTM2	
+Q12206	UniProtKB	Repeat	244	282	.	.	.	Note=WD 1	
+Q12206	UniProtKB	Repeat	287	327	.	.	.	Note=WD 2	
+Q12206	UniProtKB	Repeat	349	389	.	.	.	Note=WD 3	
+Q12206	UniProtKB	Compositional bias	87	98	.	.	.	Note=Poly-Asp	
+##sequence-region P42826 1 600
+P42826	UniProtKB	Chain	1	600	.	.	.	ID=PRO_0000059563;Note=Xylulose kinase	
+P42826	UniProtKB	Nucleotide binding	505	506	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42826	UniProtKB	Binding site	110	110	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42826	UniProtKB	Binding site	184	184	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42826	UniProtKB	Binding site	299	299	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42826	UniProtKB	Binding site	300	300	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42826	UniProtKB	Binding site	383	383	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42826	UniProtKB	Binding site	509	509	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42826	UniProtKB	Modified residue	244	244	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P42826	UniProtKB	Sequence conflict	497	502	.	.	.	Note=PERTFF->QKGLFL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33301 1 854
+P33301	UniProtKB	Chain	1	854	.	.	.	ID=PRO_0000066050;Note=DNA repair protein XRS2	
+P33301	UniProtKB	Compositional bias	836	843	.	.	.	Note=Poly-Asp	
+P33301	UniProtKB	Modified residue	349	349	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P33301	UniProtKB	Modified residue	533	533	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P33301	UniProtKB	Modified residue	534	534	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P33301	UniProtKB	Modified residue	553	553	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33301	UniProtKB	Modified residue	555	555	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q02792 1 1006
+Q02792	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7608167;Dbxref=PMID:7608167	
+Q02792	UniProtKB	Chain	2	1006	.	.	.	ID=PRO_0000071399;Note=5'-3' exoribonuclease 2	
+Q02792	UniProtKB	Repeat	955	958	.	.	.	Note=1-1	
+Q02792	UniProtKB	Repeat	961	964	.	.	.	Note=2-1	
+Q02792	UniProtKB	Repeat	972	975	.	.	.	Note=2-2	
+Q02792	UniProtKB	Repeat	975	978	.	.	.	Note=3-1	
+Q02792	UniProtKB	Repeat	984	986	.	.	.	Note=3-2	
+Q02792	UniProtKB	Repeat	996	999	.	.	.	Note=1-2	
+Q02792	UniProtKB	Region	492	529	.	.	.	Note=Required for retention in the nucleus	
+Q02792	UniProtKB	Region	955	999	.	.	.	Note=2 X 4 AA repeats of S-R-Y-D%2C N-N-N-Y%2C Y-S-G-N	
+Q02792	UniProtKB	Coiled coil	256	287	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02792	UniProtKB	Coiled coil	453	544	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02792	UniProtKB	Compositional bias	933	1004	.	.	.	Note=Asn-rich	
+Q02792	UniProtKB	Modified residue	574	574	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02792	UniProtKB	Mutagenesis	235	235	.	.	.	Note=Abrogates exonuclease activity and impairs termination of transcription by RNA polymerase II. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15565157;Dbxref=PMID:15565157	
+Q02792	UniProtKB	Mutagenesis	518	518	.	.	.	Note=Causes mislocalization to the cytoplasm and suppresses the requirement for XRN1 function. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672	
+Q02792	UniProtKB	Mutagenesis	520	520	.	.	.	Note=Suppresses the requirement for XRN1 function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672	
+Q02792	UniProtKB	Mutagenesis	534	534	.	.	.	Note=Causes mislocalization to the cytoplasm%3B when associated with A-535 and A-537. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672	
+Q02792	UniProtKB	Mutagenesis	535	535	.	.	.	Note=Causes mislocalization to the cytoplasm%3B when associated with A-534 and A-537. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672	
+Q02792	UniProtKB	Mutagenesis	535	535	.	.	.	Note=Causes mislocalization to the cytoplasm and suppresses the requirement for XRN1 function. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672	
+Q02792	UniProtKB	Mutagenesis	537	537	.	.	.	Note=Causes mislocalization to the cytoplasm%3B when associated with A-534 and A-535. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672	
+Q02792	UniProtKB	Mutagenesis	537	537	.	.	.	Note=Causes mislocalization to the cytoplasm and suppresses the requirement for XRN1 function. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672	
+Q02792	UniProtKB	Mutagenesis	683	683	.	.	.	Note=In allele TAP1-1%3B activates transcription of the promoter-defective yeast SUP4 tRNA(Tyr) allele SUP4A53T61. Y->H	
+##sequence-region P30822 1 1084
+P30822	UniProtKB	Chain	1	1084	.	.	.	ID=PRO_0000204710;Note=Exportin-1	
+P30822	UniProtKB	Domain	34	100	.	.	.	Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115	
+P30822	UniProtKB	Modified residue	1080	1080	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P30822	UniProtKB	Helix	1	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Beta strand	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DIF	
+P30822	UniProtKB	Helix	13	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	28	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	61	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	84	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	105	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	112	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Turn	130	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	137	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Turn	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	149	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Turn	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	176	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Beta strand	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HB2	
+P30822	UniProtKB	Helix	208	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Turn	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	227	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Beta strand	231	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	234	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	241	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	246	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	269	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	297	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	308	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	327	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	337	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	356	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Turn	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	417	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	421	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Beta strand	443	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Beta strand	451	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	459	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	462	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	480	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Beta strand	497	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAZ	
+P30822	UniProtKB	Helix	502	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Turn	515	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	521	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	545	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	563	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	570	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	589	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	608	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Beta strand	617	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DHA	
+P30822	UniProtKB	Helix	621	627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	629	633	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Beta strand	634	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HB3	
+P30822	UniProtKB	Helix	638	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	658	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	670	685	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	689	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	693	713	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	714	717	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	718	746	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	748	752	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	754	776	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	780	786	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	788	801	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	804	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	809	822	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	823	825	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	827	845	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Beta strand	849	852	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	853	869	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	872	875	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	879	893	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	898	918	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	922	944	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Beta strand	945	947	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	949	951	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	952	967	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Turn	978	980	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HB2	
+P30822	UniProtKB	Helix	987	1002	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	1008	1020	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Turn	1021	1023	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	1025	1038	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Beta strand	1041	1043	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	1046	1050	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P30822	UniProtKB	Helix	1051	1054	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYG	
+P30822	UniProtKB	Turn	1055	1057	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P30822	UniProtKB	Helix	1079	1081	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VYC	
+##sequence-region Q03308 1 798
+Q03308	UniProtKB	Chain	1	798	.	.	.	ID=PRO_0000065891;Note=Vacuolar protein sorting-associated protein 16	
+Q03308	UniProtKB	Sequence conflict	100	100	.	.	.	Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03308	UniProtKB	Sequence conflict	170	170	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03308	UniProtKB	Sequence conflict	326	340	.	.	.	Note=AIEILKNFVLEKGVL->QLNIKEFCLREGCT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36017 1 210
+P36017	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000121325;Note=Vacuolar protein sorting-associated protein 21	
+P36017	UniProtKB	Nucleotide binding	14	21	.	.	.	Note=GTP	
+P36017	UniProtKB	Nucleotide binding	62	66	.	.	.	Note=GTP	
+P36017	UniProtKB	Nucleotide binding	120	123	.	.	.	Note=GTP	
+P36017	UniProtKB	Motif	36	44	.	.	.	Note=Effector region;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36017	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36017	UniProtKB	Modified residue	210	210	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36017	UniProtKB	Lipidation	208	208	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36017	UniProtKB	Lipidation	210	210	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36017	UniProtKB	Mutagenesis	21	21	.	.	.	Note=Locks VPS21 in its GDP-bound form by abolishing binding to GTP. S->L%2CN;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10021387,ECO:0000269|PubMed:10329739,ECO:0000269|PubMed:8137814;Dbxref=PMID:10021387,PMID:10329739,PMID:8137814	
+P36017	UniProtKB	Mutagenesis	66	66	.	.	.	Note=Abolishes GTP hydrolysis. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10021387;Dbxref=PMID:10021387	
+P36017	UniProtKB	Beta strand	6	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Helix	20	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Beta strand	40	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Beta strand	54	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Helix	67	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Helix	73	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Beta strand	81	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Helix	92	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Beta strand	114	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Helix	122	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Helix	135	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Beta strand	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Turn	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+P36017	UniProtKB	Helix	160	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0	
+##sequence-region Q03897 1 1148
+Q03897	UniProtKB	Chain	1	1148	.	.	.	ID=PRO_0000253807;Note=Maintenance of telomere capping protein 5	
+Q03897	UniProtKB	Repeat	63	106	.	.	.	Note=WD 1	
+Q03897	UniProtKB	Repeat	112	152	.	.	.	Note=WD 2	
+Q03897	UniProtKB	Repeat	156	195	.	.	.	Note=WD 3	
+Q03897	UniProtKB	Repeat	199	239	.	.	.	Note=WD 4	
+Q03897	UniProtKB	Repeat	299	348	.	.	.	Note=WD 5	
+Q03897	UniProtKB	Domain	432	543	.	.	.	Note=RWD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00179	
+Q03897	UniProtKB	Modified residue	759	759	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38189 1 126
+P38189	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000202453;Note=Putative uncharacterized membrane protein YBL062W	
+P38189	UniProtKB	Topological domain	1	9	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38189	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38189	UniProtKB	Topological domain	31	73	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38189	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38189	UniProtKB	Topological domain	95	126	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38216 1 128
+P38216	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38216	UniProtKB	Chain	2	128	.	.	.	ID=PRO_0000202469;Note=Uncharacterized protein YBR016W	
+P38216	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38216	UniProtKB	Cross-link	32	32	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P38239 1 180
+P38239	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38239	UniProtKB	Chain	2	180	.	.	.	ID=PRO_0000056335;Note=Uncharacterized RING finger protein YBR062C	
+P38239	UniProtKB	Zinc finger	109	153	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P38239	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P38243 1 211
+P38243	UniProtKB	Chain	1	211	.	.	.	ID=PRO_0000202478;Note=Uncharacterized protein YBR071W	
+P38243	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38243	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38243	UniProtKB	Modified residue	186	186	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32386 1 1661
+P32386	UniProtKB	Chain	1	1661	.	.	.	ID=PRO_0000093447;Note=ATP-dependent bile acid permease	
+P32386	UniProtKB	Topological domain	1	33	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	55	74	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	96	133	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	134	154	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	155	166	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	167	187	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	188	205	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	206	226	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	227	345	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	346	366	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	367	393	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	394	414	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	415	495	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	496	516	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	517	519	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	520	540	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	541	602	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	603	623	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	624	644	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	645	665	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	666	1053	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	1054	1074	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	1075	1114	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	1115	1135	.	.	.	Note=Helical%3B Name%3D13;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	1136	1178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	1179	1199	.	.	.	Note=Helical%3B Name%3D14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	1200	1200	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	1201	1221	.	.	.	Note=Helical%3B Name%3D15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	1222	1292	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	1293	1313	.	.	.	Note=Helical%3B Name%3D16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	1314	1315	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Transmembrane	1316	1336	.	.	.	Note=Helical%3B Name%3D17;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Topological domain	1337	1661	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32386	UniProtKB	Domain	354	662	.	.	.	Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Domain	694	935	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P32386	UniProtKB	Domain	1026	1345	.	.	.	Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P32386	UniProtKB	Domain	1381	1636	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P32386	UniProtKB	Nucleotide binding	729	736	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P32386	UniProtKB	Nucleotide binding	1415	1422	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P32386	UniProtKB	Modified residue	936	936	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32386	UniProtKB	Modified residue	940	940	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32386	UniProtKB	Modified residue	955	955	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32386	UniProtKB	Glycosylation	6	6	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32386	UniProtKB	Glycosylation	97	97	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32386	UniProtKB	Sequence conflict	172	174	.	.	.	Note=TIT->QIH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32386	UniProtKB	Sequence conflict	188	189	.	.	.	Note=LR->FS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38109 1 508
+P38109	UniProtKB	Chain	1	508	.	.	.	ID=PRO_0000120563;Note=Putative serine carboxypeptidase YBR139W	
+P38109	UniProtKB	Active site	219	219	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38109	UniProtKB	Active site	415	415	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38109	UniProtKB	Active site	474	474	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q96VG8 1 41
+Q96VG8	UniProtKB	Chain	1	41	.	.	.	ID=PRO_0000299836;Note=Putative uncharacterized protein YCR038W-A	
+##sequence-region P25383 1 438
+P25383	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000203495;Note=Transposon Ty2-C Gag polyprotein	
+P25383	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279282;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25383	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000279283;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25383	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25383	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25383	UniProtKB	Sequence conflict	174	174	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25383	UniProtKB	Sequence conflict	174	174	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25349 1 247
+P25349	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000200768;Note=Flavoprotein-like protein YCP4	
+P25349	UniProtKB	Propeptide	245	247	.	.	.	ID=PRO_0000366191;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25349	UniProtKB	Domain	4	193	.	.	.	Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088	
+P25349	UniProtKB	Modified residue	244	244	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25349	UniProtKB	Lipidation	243	243	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+P25349	UniProtKB	Lipidation	244	244	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25617 1 290
+P25617	UniProtKB	Chain	1	290	.	.	.	ID=PRO_0000202563;Note=Uncharacterized protein YCR016W	
+P25617	UniProtKB	Compositional bias	52	98	.	.	.	Note=Lys-rich	
+##sequence-region P25351 1 611
+P25351	UniProtKB	Chain	1	611	.	.	.	ID=PRO_0000173425;Note=Uncharacterized membrane protein YCR023C	
+P25351	UniProtKB	Topological domain	1	89	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Topological domain	111	152	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Topological domain	174	199	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Topological domain	221	353	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Transmembrane	354	372	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Topological domain	373	413	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Transmembrane	414	434	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Topological domain	435	442	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Transmembrane	443	463	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Topological domain	464	542	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Transmembrane	543	563	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Topological domain	564	611	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25351	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P25351	UniProtKB	Modified residue	603	603	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P25361 1 127
+P25361	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000202568;Note=Uncharacterized protein YCR043C	
+##sequence-region P25639 1 631
+P25639	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Chain	21	631	.	.	.	ID=PRO_0000014313;Note=Uncharacterized membrane protein YCR061W	
+P25639	UniProtKB	Topological domain	21	105	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Topological domain	127	131	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Topological domain	153	170	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Topological domain	192	322	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Transmembrane	323	343	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Topological domain	344	351	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Transmembrane	352	372	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Topological domain	373	407	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Transmembrane	408	428	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Topological domain	429	451	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Transmembrane	452	472	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Topological domain	473	529	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Transmembrane	530	550	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Topological domain	551	598	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Transmembrane	599	619	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Topological domain	620	631	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Modified residue	219	219	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25639	UniProtKB	Glycosylation	87	87	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Glycosylation	98	98	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25639	UniProtKB	Cross-link	250	250	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q12489 1 107
+Q12489	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12489	UniProtKB	Chain	2	107	.	.	.	ID=PRO_0000248456;Note=Cysteine-rich and transmembrane domain-containing protein YDL012C	
+Q12489	UniProtKB	Transmembrane	82	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12489	UniProtKB	Compositional bias	37	80	.	.	.	Note=Gln-rich	
+Q12489	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12489	UniProtKB	Cross-link	13	13	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q03205 1 200
+Q03205	UniProtKB	Chain	1	200	.	.	.	ID=PRO_0000242648;Note=Uncharacterized protein YDR042C	
+##sequence-region Q07438 1 124
+Q07438	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000299854;Note=Putative uncharacterized protein YDL071C	
+##sequence-region Q03193 1 310
+Q03193	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000244443;Note=Uncharacterized membrane protein YDR090C	
+Q03193	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Topological domain	28	36	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Transmembrane	37	57	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Topological domain	58	61	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Topological domain	83	96	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Transmembrane	97	117	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Topological domain	118	131	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Topological domain	153	164	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Transmembrane	165	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Topological domain	186	191	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Transmembrane	192	212	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Topological domain	213	310	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Domain	5	69	.	.	.	Note=PQ-loop 1	
+Q03193	UniProtKB	Domain	138	194	.	.	.	Note=PQ-loop 2	
+Q03193	UniProtKB	Modified residue	229	229	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03193	UniProtKB	Glycosylation	251	251	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03193	UniProtKB	Glycosylation	259	259	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07589 1 356
+Q07589	UniProtKB	Chain	1	356	.	.	.	ID=PRO_0000202587;Note=Uncharacterized protein YDL144C	
+##sequence-region P0C2I2 1 1755
+P0C2I2	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279025;Note=Transposon Ty1-DR5 Gag-Pol polyprotein	
+P0C2I2	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279026;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I2	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279027;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I2	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279028;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I2	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279029;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I2	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I2	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0C2I2	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+P0C2I2	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I2	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+P0C2I2	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I2	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0C2I2	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P0C2I2	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I2	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I2	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I2	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I2	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I2	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I2	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I2	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I2	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I2	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I2	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12307 1 118
+Q12307	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000299860;Note=Putative uncharacterized protein YDL162C	
+##sequence-region Q12257 1 170
+Q12257	UniProtKB	Chain	1	170	.	.	.	ID=PRO_0000207658;Note=IMPACT family member YDL177C	
+##sequence-region P48569 1 320
+P48569	UniProtKB	Chain	1	320	.	.	.	ID=PRO_0000202590;Note=Uncharacterized protein YDL183C	
+##sequence-region Q03482 1 75
+Q03482	UniProtKB	Chain	1	75	.	.	.	ID=PRO_0000253837;Note=Cysteine-rich and transmembrane domain-containing protein YDR210W	
+Q03482	UniProtKB	Transmembrane	52	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03482	UniProtKB	Repeat	4	13	.	.	.	Note=1	
+Q03482	UniProtKB	Repeat	14	23	.	.	.	Note=2	
+Q03482	UniProtKB	Repeat	24	33	.	.	.	Note=3	
+Q03482	UniProtKB	Region	4	33	.	.	.	Note=3 X 10 AA tandem repeats of Q-Q-G-Y-Y-Q-Q-G-P-P	
+Q03482	UniProtKB	Compositional bias	3	49	.	.	.	Note=Gln-rich	
+Q03482	UniProtKB	Compositional bias	55	73	.	.	.	Note=Cys-rich	
+##sequence-region Q12472 1 1770
+Q12472	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000279284;Note=Transposon Ty2-DR1 Gag-Pol polyprotein	
+Q12472	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279285;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12472	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000279286;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12472	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000279287;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12472	UniProtKB	Chain	1233	1770	.	.	.	ID=PRO_0000279288;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12472	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12472	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12472	UniProtKB	Domain	1625	1767	.	.	.	Note=RNase H Ty1/copia-type	
+Q12472	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12472	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+Q12472	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12472	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12472	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12472	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12472	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12472	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12472	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12472	UniProtKB	Metal binding	1625	1625	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12472	UniProtKB	Metal binding	1667	1667	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12472	UniProtKB	Metal binding	1700	1700	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12472	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12472	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12472	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03780 1 787
+Q03780	UniProtKB	Chain	1	787	.	.	.	ID=PRO_0000253839;Note=Uncharacterized protein YDR239C	
+Q03780	UniProtKB	Compositional bias	151	155	.	.	.	Note=Poly-Pro	
+Q03780	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03780	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03780	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03780	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03780	UniProtKB	Modified residue	342	342	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03780	UniProtKB	Modified residue	345	345	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03780	UniProtKB	Modified residue	390	390	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03780	UniProtKB	Modified residue	477	477	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q03780	UniProtKB	Modified residue	492	492	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03780	UniProtKB	Modified residue	546	546	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03780	UniProtKB	Modified residue	683	683	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03780	UniProtKB	Modified residue	699	699	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P0C5L8 1 45
+P0C5L8	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C5L8	UniProtKB	Chain	20	45	.	.	.	ID=PRO_0000309016;Note=Putative uncharacterized protein YDL240C-A	
+##sequence-region Q03788 1 91
+Q03788	UniProtKB	Chain	1	91	.	.	.	ID=PRO_0000299878;Note=Putative uncharacterized protein YDR250C	
+Q03788	UniProtKB	Transmembrane	12	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGP6 1 47
+Q8TGP6	UniProtKB	Chain	1	47	.	.	.	ID=PRO_0000299886;Note=Putative uncharacterized protein YDR354C-A	
+##sequence-region Q04069 1 103
+Q04069	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000299892;Note=Putative uncharacterized protein YDR431W	
+Q04069	UniProtKB	Transmembrane	37	57	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P87273 1 111
+P87273	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000299902;Note=Putative uncharacterized protein YDR521W	
+P87273	UniProtKB	Transmembrane	18	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87273	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZE8 1 133
+A0A023PZE8	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000430985;Note=Uncharacterized protein YDR157W	
+##sequence-region Q2V2P8 1 89
+Q2V2P8	UniProtKB	Chain	1	89	.	.	.	ID=PRO_0000253848;Note=Uncharacterized protein YDR374W-A	
+##sequence-region Q02217 1 200
+Q02217	UniProtKB	Chain	1	200	.	.	.	ID=PRO_0000299907;Note=Putative uncharacterized protein YEL034C-A	
+Q02217	UniProtKB	Transmembrane	7	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02217	UniProtKB	Sequence conflict	138	139	.	.	.	Note=VD->TS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02217	UniProtKB	Sequence conflict	170	170	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40102 1 141
+P40102	UniProtKB	Chain	1	141	.	.	.	ID=PRO_0000202663;Note=Uncharacterized protein YER187W	
+##sequence-region P40001 1 126
+P40001	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000202616;Note=Uncharacterized protein YEL008W	
+##sequence-region P34225 1 687
+P34225	UniProtKB	Chain	1	687	.	.	.	ID=PRO_0000120222;Note=Guanine-nucleotide exchange factor YEL1	
+P34225	UniProtKB	Domain	61	266	.	.	.	Note=SEC7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00189	
+P34225	UniProtKB	Domain	412	551	.	.	.	Note=PH	
+P34225	UniProtKB	Modified residue	290	290	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34225	UniProtKB	Modified residue	293	293	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P34225	UniProtKB	Modified residue	299	299	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40062 1 109
+P40062	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000202643;Note=Putative uncharacterized protein YER097W	
+##sequence-region Q04210 1 160
+Q04210	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000203275;Note=Endoplasmic reticulum transmembrane protein 2	
+Q04210	UniProtKB	Topological domain	1	2	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04210	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04210	UniProtKB	Topological domain	24	45	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04210	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04210	UniProtKB	Topological domain	67	103	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04210	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04210	UniProtKB	Topological domain	125	160	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04210	UniProtKB	Motif	157	160	.	.	.	Note=Di-lysine motif	
+##sequence-region A0A023PZD0 1 216
+A0A023PZD0	UniProtKB	Chain	1	216	.	.	.	ID=PRO_0000431012;Note=Putative uncharacterized protein YFR036W-A	
+A0A023PZD0	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZD0	UniProtKB	Compositional bias	11	16	.	.	.	Note=Poly-Phe;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZD0	UniProtKB	Compositional bias	38	189	.	.	.	Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016	
+##sequence-region P43576 1 117
+P43576	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000202677;Note=Uncharacterized protein YFL019C	
+##sequence-region P43539 1 102
+P43539	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000202668;Note=Uncharacterized protein YFL065C	
+##sequence-region P43537 1 175
+P43537	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000202667;Note=Uncharacterized membrane protein YFL067W	
+P43537	UniProtKB	Topological domain	1	2	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43537	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43537	UniProtKB	Topological domain	24	151	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43537	UniProtKB	Transmembrane	152	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43537	UniProtKB	Topological domain	173	175	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43590 1 535
+P43590	UniProtKB	Chain	1	535	.	.	.	ID=PRO_0000185099;Note=Uncharacterized peptidase YFR006W	
+P43590	UniProtKB	Transmembrane	8	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43590	UniProtKB	Metal binding	316	316	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43590	UniProtKB	Metal binding	327	327	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43590	UniProtKB	Metal binding	327	327	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43590	UniProtKB	Metal binding	412	412	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43590	UniProtKB	Metal binding	452	452	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43590	UniProtKB	Metal binding	493	493	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43590	UniProtKB	Metal binding	493	493	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43590	UniProtKB	Cross-link	50	50	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P43590	UniProtKB	Sequence conflict	326	326	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43591 1 353
+P43591	UniProtKB	Chain	1	353	.	.	.	ID=PRO_0000202683;Note=ATP-dependent kinase YFH7	
+P43591	UniProtKB	Nucleotide binding	31	39	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43591	UniProtKB	Helix	4	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Turn	18	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	25	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	37	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	84	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Turn	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	109	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	121	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	155	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	161	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	168	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	178	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Turn	182	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	192	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	222	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	237	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Turn	244	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	248	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	262	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	275	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Turn	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	290	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	299	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	319	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Turn	330	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Helix	335	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+P43591	UniProtKB	Beta strand	347	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8	
+##sequence-region Q03186 1 124
+Q03186	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000299918;Note=Putative uncharacterized protein YFL012W-A	
+Q03186	UniProtKB	Transmembrane	83	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGP0 1 49
+Q8TGP0	UniProtKB	Chain	1	49	.	.	.	ID=PRO_0000299921;Note=Putative uncharacterized protein YGL063C-A	
+##sequence-region Q3E816 1 71
+Q3E816	UniProtKB	Chain	1	71	.	.	.	ID=PRO_0000245383;Note=Uncharacterized protein YGR121W-A	
+##sequence-region Q3E744 1 92
+Q3E744	UniProtKB	Chain	1	92	.	.	.	ID=PRO_0000245385;Note=Uncharacterized protein YGR161W-C	
+##sequence-region P0CX96 1 160
+P0CX96	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000410453;Note=UPF0479 membrane protein YGR296C-B	
+P0CX96	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX96	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX96	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region P53265 1 400
+P53265	UniProtKB	Chain	1	400	.	.	.	ID=PRO_0000202814;Note=Uncharacterized protein YGR111W	
+##sequence-region P53270 1 476
+P53270	UniProtKB	Chain	1	476	.	.	.	ID=PRO_0000202817;Note=Uncharacterized protein YGR117C	
+P53270	UniProtKB	Domain	7	39	.	.	.	Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126	
+##sequence-region P53273 1 1036
+P53273	UniProtKB	Chain	1	1036	.	.	.	ID=PRO_0000202819;Note=Uncharacterized vacuolar membrane protein YGR125W	
+P53273	UniProtKB	Topological domain	1	213	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	235	236	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	237	257	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	258	269	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	270	290	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	291	300	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	301	321	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	322	338	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	339	359	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	360	375	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	376	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	397	405	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	406	426	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	427	473	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	474	494	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	495	515	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	516	536	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	537	546	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	547	567	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	568	568	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	569	589	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	590	604	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	605	625	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	626	664	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Transmembrane	665	685	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Topological domain	686	1036	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53273	UniProtKB	Domain	660	781	.	.	.	Note=STAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00198	
+P53273	UniProtKB	Modified residue	42	42	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198	
+P53273	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53273	UniProtKB	Modified residue	130	130	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53273	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53273	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53273	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53273	UniProtKB	Modified residue	152	152	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53273	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53273	UniProtKB	Modified residue	842	842	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53273	UniProtKB	Modified residue	847	847	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P48236 1 432
+P48236	UniProtKB	Chain	1	432	.	.	.	ID=PRO_0000202829;Note=Uncharacterized membrane protein YGR149W	
+P48236	UniProtKB	Topological domain	1	110	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Topological domain	132	132	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Transmembrane	133	153	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Topological domain	154	162	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Transmembrane	163	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Topological domain	184	187	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Topological domain	209	221	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Transmembrane	222	242	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Topological domain	243	319	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Transmembrane	320	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Topological domain	343	346	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Transmembrane	347	369	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Topological domain	370	432	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48236	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P42942 1 411
+P42942	UniProtKB	Chain	1	411	.	.	.	ID=PRO_0000122467;Note=Uncharacterized GTP-binding protein YGR210C	
+P42942	UniProtKB	Domain	5	274	.	.	.	Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P42942	UniProtKB	Nucleotide binding	11	18	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P42942	UniProtKB	Nucleotide binding	83	87	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+##sequence-region P53321 1 146
+P53321	UniProtKB	Chain	1	146	.	.	.	ID=PRO_0000202861;Note=Putative uncharacterized protein YGR259C	
+##sequence-region P53340 1 73
+P53340	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000202873;Note=Putative uncharacterized protein YGR291C	
+##sequence-region Q8TGT4 1 77
+Q8TGT4	UniProtKB	Chain	1	77	.	.	.	ID=PRO_0000245398;Note=Uncharacterized protein YHR213W-A	
+Q8TGT4	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX91 1 67
+P0CX91	UniProtKB	Chain	1	67	.	.	.	ID=PRO_0000410450;Note=Uncharacterized protein YHR212W-A	
+##sequence-region P0C5N4 1 26
+P0C5N4	UniProtKB	Chain	1	26	.	.	.	ID=PRO_0000309032;Note=Uncharacterized protein YHR073C-B	
+##sequence-region P38750 1 627
+P38750	UniProtKB	Chain	1	627	.	.	.	ID=PRO_0000094729;Note=Uncharacterized transporter YHL008C	
+P38750	UniProtKB	Topological domain	1	32	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Topological domain	54	66	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Transmembrane	67	87	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Topological domain	88	113	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Topological domain	135	165	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Transmembrane	166	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Topological domain	187	192	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Transmembrane	193	213	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Topological domain	214	218	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Transmembrane	219	239	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Topological domain	240	245	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Transmembrane	246	266	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Topological domain	267	627	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38750	UniProtKB	Modified residue	305	305	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38750	UniProtKB	Modified residue	546	546	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38750	UniProtKB	Modified residue	588	588	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38726 1 115
+P38726	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000202877;Note=Putative UPF0377 protein YHL045W	
+P38726	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38708 1 688
+P38708	UniProtKB	Chain	1	688	.	.	.	ID=PRO_0000139355;Note=Putative proline--tRNA ligase YHR020W	
+P38708	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38708	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38708	UniProtKB	Modified residue	655	655	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38763 1 256
+P38763	UniProtKB	Chain	1	256	.	.	.	ID=PRO_0000202890;Note=Uncharacterized protein YHR022C	
+P38763	UniProtKB	Nucleotide binding	29	36	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38780 1 354
+P38780	UniProtKB	Chain	1	354	.	.	.	ID=PRO_0000202896;Note=Uncharacterized protein YHR054C	
+##sequence-region P38808 1 164
+P38808	UniProtKB	Chain	1	164	.	.	.	ID=PRO_0000202906;Note=Putative uncharacterized protein YHR095W	
+P38808	UniProtKB	Compositional bias	111	119	.	.	.	Note=Poly-Lys	
+##sequence-region P38716 1 378
+P38716	UniProtKB	Chain	1	378	.	.	.	ID=PRO_0000114766;Note=Uncharacterized trans-sulfuration enzyme YHR112C	
+P38716	UniProtKB	Modified residue	198	198	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38835 1 850
+P38835	UniProtKB	Chain	1	850	.	.	.	ID=PRO_0000202917;Note=PH domain-containing protein YHR131C	
+P38835	UniProtKB	Domain	194	306	.	.	.	Note=PH	
+P38835	UniProtKB	Compositional bias	318	339	.	.	.	Note=Arg-rich	
+P38835	UniProtKB	Compositional bias	796	845	.	.	.	Note=Asp-rich	
+##sequence-region P38864 1 112
+P38864	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000202931;Note=Uncharacterized protein YHR173C	
+##sequence-region P40514 1 678
+P40514	UniProtKB	Chain	1	678	.	.	.	ID=PRO_0000202981;Note=Uncharacterized protein YIL067C	
+P40514	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40514	UniProtKB	Transmembrane	245	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40514	UniProtKB	Transmembrane	317	337	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40514	UniProtKB	Transmembrane	340	360	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40514	UniProtKB	Transmembrane	371	391	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40514	UniProtKB	Transmembrane	405	425	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40514	UniProtKB	Transmembrane	443	463	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40514	UniProtKB	Transmembrane	475	495	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40514	UniProtKB	Transmembrane	519	539	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40514	UniProtKB	Sequence conflict	644	644	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40500 1 205
+P40500	UniProtKB	Chain	1	205	.	.	.	ID=PRO_0000202976;Note=Uncharacterized membrane protein YIL089W	
+P40500	UniProtKB	Topological domain	1	63	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40500	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40500	UniProtKB	Topological domain	85	124	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40500	UniProtKB	Transmembrane	125	145	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40500	UniProtKB	Topological domain	146	205	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40490 1 117
+P40490	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000202968;Note=Putative uncharacterized protein YIL100W	
+##sequence-region P40461 1 129
+P40461	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000202959;Note=Putative uncharacterized protein YIL141W	
+##sequence-region P40588 1 61
+P40588	UniProtKB	Chain	1	61	.	.	.	ID=PRO_0000207535;Note=Putative uncharacterized protein YIR044C	
+##sequence-region Q3E827 1 93
+Q3E827	UniProtKB	Chain	1	93	.	.	.	ID=PRO_0000245415;Note=Uncharacterized protein YJR005C-A	
+Q3E827	UniProtKB	Coiled coil	20	83	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGN2 1 85
+Q8TGN2	UniProtKB	Chain	1	85	.	.	.	ID=PRO_0000299764;Note=Putative uncharacterized protein YJL020W-A	
+Q8TGN2	UniProtKB	Compositional bias	5	17	.	.	.	Note=Poly-Ser	
+Q8TGN2	UniProtKB	Compositional bias	66	83	.	.	.	Note=Poly-Ser	
+##sequence-region Q3E737 1 44
+Q3E737	UniProtKB	Chain	1	44	.	.	.	ID=PRO_0000245414;Note=Uncharacterized protein YJL047C-A	
+##sequence-region P47106 1 120
+P47106	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000203092;Note=Putative uncharacterized protein YJR038C	
+P47106	UniProtKB	Transmembrane	26	46	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47106	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E743 1 109
+Q3E743	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000245416;Note=Uncharacterized protein YJR112W-A	
+Q3E743	UniProtKB	Transmembrane	90	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E7A3 1 74
+Q3E7A3	UniProtKB	Chain	1	74	.	.	.	ID=PRO_0000245409;Note=Uncharacterized protein YJL133C-A	
+Q3E7A3	UniProtKB	Transmembrane	8	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47131 1 105
+P47131	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000203105;Note=TMEM14 protein homolog YJR085C	
+P47131	UniProtKB	Transmembrane	26	46	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47131	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47131	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47059 1 104
+P47059	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000203070;Note=Putative uncharacterized protein YJL032W	
+##sequence-region P46991 1 170
+P46991	UniProtKB	Chain	1	170	.	.	.	ID=PRO_0000203024;Note=Putative uncharacterized membrane protein YJL175W	
+P46991	UniProtKB	Topological domain	1	15	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46991	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46991	UniProtKB	Topological domain	37	76	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46991	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46991	UniProtKB	Topological domain	98	119	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46991	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46991	UniProtKB	Topological domain	141	170	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39541 1 233
+P39541	UniProtKB	Chain	1	233	.	.	.	ID=PRO_0000203018;Note=Putative uncharacterized protein YJL195C	
+P39541	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39541	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39541	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39529 1 758
+P39529	UniProtKB	Chain	1	758	.	.	.	ID=PRO_0000114999;Note=Putative transcriptional regulatory protein YJL206C	
+P39529	UniProtKB	DNA binding	47	73	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P36074 1 111
+P36074	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000203157;Note=Putative uncharacterized protein YKL111C	
+##sequence-region P36050 1 127
+P36050	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000203141;Note=Putative uncharacterized protein YKL169C	
+##sequence-region P34238 1 112
+P34238	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000203138;Note=Putative uncharacterized protein YKL177W	
+##sequence-region P34231 1 750
+P34231	UniProtKB	Chain	1	750	.	.	.	ID=PRO_0000203136;Note=Uncharacterized protein YKL187C	
+P34231	UniProtKB	Modified residue	675	675	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P34231	UniProtKB	Modified residue	678	678	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:19779198	
+P34231	UniProtKB	Glycosylation	61	61	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	84	84	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	154	154	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	176	176	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	197	197	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	207	207	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	241	241	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	267	267	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	293	293	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	299	299	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	312	312	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	335	335	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	351	351	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	373	373	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	389	389	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	519	519	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	709	709	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	714	714	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Glycosylation	724	724	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34231	UniProtKB	Cross-link	697	697	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region Q07978 1 186
+Q07978	UniProtKB	Chain	1	186	.	.	.	ID=PRO_0000247174;Note=Putative uncharacterized protein YLR031W	
+##sequence-region Q07986 1 203
+Q07986	UniProtKB	Chain	1	203	.	.	.	ID=PRO_0000203232;Note=Uncharacterized protein YLR036C	
+Q07986	UniProtKB	Transmembrane	60	80	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07986	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07986	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07986	UniProtKB	Nucleotide binding	192	199	.	.	.	Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07988 1 224
+Q07988	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07988	UniProtKB	Chain	26	203	.	.	.	ID=PRO_0000247442;Note=Cell wall protein YLR040C	
+Q07988	UniProtKB	Propeptide	204	224	.	.	.	ID=PRO_0000247443;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07988	UniProtKB	Lipidation	203	203	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07988	UniProtKB	Glycosylation	148	148	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07988	UniProtKB	Glycosylation	181	181	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07988	UniProtKB	Glycosylation	191	191	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGR1 1 33
+Q8TGR1	UniProtKB	Chain	1	33	.	.	.	ID=PRO_0000299613;Note=Putative uncharacterized protein YLR120W-A	
+##sequence-region Q12088 1 1755
+Q12088	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279094;Note=Transposon Ty1-LR1 Gag-Pol polyprotein	
+Q12088	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279095;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12088	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279096;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12088	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279097;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12088	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279098;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12088	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12088	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12088	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q12088	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12088	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q12088	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12088	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q12088	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q12088	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12088	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12088	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12088	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12088	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12088	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12088	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12088	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12088	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12088	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12088	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04501 1 128
+Q04501	UniProtKB	Chain	1	128	.	.	.	ID=PRO_0000203245;Note=Putative uncharacterized protein YML090W	
+Q04501	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04501	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04501	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03675 1 126
+Q03675	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000203269;Note=Uncharacterized protein YMR007W	
+##sequence-region Q03687 1 405
+Q03687	UniProtKB	Chain	1	405	.	.	.	ID=PRO_0000203270;Note=Uncharacterized membrane protein YMR010W	
+Q03687	UniProtKB	Topological domain	1	51	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Topological domain	73	76	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Topological domain	98	103	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Topological domain	125	178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Topological domain	200	223	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Transmembrane	224	244	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Topological domain	245	254	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Topological domain	276	299	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Transmembrane	300	320	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03687	UniProtKB	Topological domain	321	405	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05131 1 434
+Q05131	UniProtKB	Chain	1	434	.	.	.	ID=PRO_0000203274;Note=Uncharacterized membrane protein YMR034C	
+Q05131	UniProtKB	Topological domain	1	15	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Topological domain	37	50	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Topological domain	72	87	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Topological domain	109	118	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Topological domain	140	149	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Topological domain	171	199	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Topological domain	221	234	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Transmembrane	235	255	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Topological domain	256	264	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Transmembrane	265	285	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Topological domain	286	327	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Transmembrane	328	348	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Topological domain	349	362	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Transmembrane	363	383	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Topological domain	384	434	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05131	UniProtKB	Modified residue	425	425	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q04276 1 118
+Q04276	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000203283;Note=Uncharacterized protein YMR082C	
+##sequence-region Q04299 1 284
+Q04299	UniProtKB	Chain	1	284	.	.	.	ID=PRO_0000203285;Note=Probable ADP-ribose 1''-phosphate phosphatase YML087W	
+Q04299	UniProtKB	Domain	34	230	.	.	.	Note=Macro;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00490	
+Q04299	UniProtKB	Active site	80	80	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04299	UniProtKB	Active site	90	90	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04299	UniProtKB	Active site	145	145	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04299	UniProtKB	Binding site	23	23	.	.	.	Note=Substrate	
+Q04299	UniProtKB	Binding site	55	55	.	.	.	Note=Substrate	
+Q04299	UniProtKB	Binding site	80	80	.	.	.	Note=Substrate	
+Q04299	UniProtKB	Binding site	90	90	.	.	.	Note=Substrate	
+Q04299	UniProtKB	Binding site	148	148	.	.	.	Note=Substrate	
+Q04299	UniProtKB	Binding site	195	195	.	.	.	Note=Substrate	
+Q04299	UniProtKB	Disulfide bond	128	136	.	.	.	.	
+Q04299	UniProtKB	Beta strand	18	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	26	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Beta strand	47	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	54	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Beta strand	73	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	89	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	100	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Turn	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Beta strand	121	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	125	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Beta strand	140	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Beta strand	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	167	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Beta strand	186	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Beta strand	193	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXZ	
+Q04299	UniProtKB	Helix	202	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	219	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	224	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	245	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	258	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Turn	266	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+Q04299	UniProtKB	Helix	271	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR	
+##sequence-region Q03177 1 834
+Q03177	UniProtKB	Chain	1	834	.	.	.	ID=PRO_0000051481;Note=WD repeat-containing protein YMR102C	
+Q03177	UniProtKB	Repeat	171	210	.	.	.	Note=WD 1	
+Q03177	UniProtKB	Repeat	276	314	.	.	.	Note=WD 2	
+Q03177	UniProtKB	Repeat	316	356	.	.	.	Note=WD 3	
+Q03177	UniProtKB	Repeat	358	398	.	.	.	Note=WD 4	
+Q03177	UniProtKB	Repeat	423	468	.	.	.	Note=WD 5	
+Q03177	UniProtKB	Modified residue	528	528	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q03177	UniProtKB	Modified residue	771	771	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53846 1 198
+P53846	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000203382;Note=Uncharacterized ORAOV1 family protein YNL260C	
+##sequence-region P53842 1 139
+P53842	UniProtKB	Chain	1	139	.	.	.	ID=PRO_0000203380;Note=Putative uncharacterized protein YNL266W	
+P53842	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53842	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53842	UniProtKB	Compositional bias	25	33	.	.	.	Note=Poly-Ser	
+##sequence-region Q3E7A8 1 72
+Q3E7A8	UniProtKB	Chain	1	72	.	.	.	ID=PRO_0000247798;Note=Uncharacterized protein YNL162W-A	
+##sequence-region P53825 1 131
+P53825	UniProtKB	Chain	1	131	.	.	.	ID=PRO_0000203363;Note=Putative uncharacterized protein YNL324W	
+P53825	UniProtKB	Transmembrane	61	81	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53825	UniProtKB	Transmembrane	102	122	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53964 1 284
+P53964	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53964	UniProtKB	Chain	25	284	.	.	.	ID=PRO_0000014340;Note=Uncharacterized membrane protein YNL033W	
+P53964	UniProtKB	Topological domain	25	84	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53964	UniProtKB	Transmembrane	85	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53964	UniProtKB	Topological domain	105	284	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53964	UniProtKB	Glycosylation	270	270	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08216 1 224
+Q08216	UniProtKB	Chain	1	224	.	.	.	ID=PRO_0000299690;Note=Putative uncharacterized protein YOL046C	
+##sequence-region Q08448 1 450
+Q08448	UniProtKB	Chain	1	450	.	.	.	ID=PRO_0000237649;Note=Putative lipase YOR059C	
+Q08448	UniProtKB	Transmembrane	269	289	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08448	UniProtKB	Active site	90	90	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037	
+##sequence-region Q08238 1 132
+Q08238	UniProtKB	Chain	1	132	.	.	.	ID=PRO_0000262742;Note=Putative uncharacterized membrane protein YOL079W	
+Q08238	UniProtKB	Topological domain	1	18	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258	
+Q08238	UniProtKB	Transmembrane	19	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08238	UniProtKB	Topological domain	40	49	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258	
+Q08238	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08238	UniProtKB	Topological domain	71	77	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258	
+Q08238	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08238	UniProtKB	Topological domain	99	132	.	.	.	Note=Extracellular;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12524434,ECO:0000269|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258	
+##sequence-region Q99247 1 1116
+Q99247	UniProtKB	Chain	1	1116	.	.	.	ID=PRO_0000235919;Note=Uncharacterized WD repeat-containing protein YOL087C	
+Q99247	UniProtKB	Repeat	21	62	.	.	.	Note=WD 1	
+Q99247	UniProtKB	Repeat	91	132	.	.	.	Note=WD 2	
+Q99247	UniProtKB	Repeat	160	200	.	.	.	Note=WD 3	
+Q99247	UniProtKB	Repeat	219	262	.	.	.	Note=WD 4	
+Q99247	UniProtKB	Repeat	266	305	.	.	.	Note=WD 5	
+Q99247	UniProtKB	Repeat	387	426	.	.	.	Note=WD 6	
+Q99247	UniProtKB	Repeat	428	466	.	.	.	Note=WD 7	
+Q99247	UniProtKB	Compositional bias	364	374	.	.	.	Note=Poly-His	
+Q99247	UniProtKB	Modified residue	668	668	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q99247	UniProtKB	Modified residue	693	693	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q12496 1 1037
+Q12496	UniProtKB	Chain	1	1037	.	.	.	ID=PRO_0000178013;Note=Uncharacterized protein YOL098C	
+##sequence-region Q92393 1 1755
+Q92393	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279161;Note=Transposon Ty1-OR Gag-Pol polyprotein	
+Q92393	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279162;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92393	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279163;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92393	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279164;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92393	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279165;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92393	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q92393	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q92393	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q92393	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92393	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q92393	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92393	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q92393	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q92393	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q92393	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q92393	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q92393	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q92393	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q92393	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q92393	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q92393	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q92393	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92393	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92393	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92393	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region Q3E7A5 1 60
+Q3E7A5	UniProtKB	Chain	1	60	.	.	.	ID=PRO_0000245278;Note=Uncharacterized protein YOL164W-A	
+##sequence-region Q08634 1 303
+Q08634	UniProtKB	Chain	1	303	.	.	.	ID=PRO_0000237669;Note=Uncharacterized protein YOR238W	
+##sequence-region O14468 1 76
+O14468	UniProtKB	Chain	1	76	.	.	.	ID=PRO_0000245285;Note=Uncharacterized protein YOR304C-A	
+##sequence-region P0C5R1 1 69
+P0C5R1	UniProtKB	Chain	1	69	.	.	.	ID=PRO_0000309059;Note=Putative uncharacterized protein YOR329W-A	
+P0C5R1	UniProtKB	Transmembrane	39	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12182 1 319
+Q12182	UniProtKB	Chain	1	319	.	.	.	ID=PRO_0000245289;Note=Uncharacterized protein YOR342C	
+##sequence-region Q08844 1 703
+Q08844	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Chain	25	703	.	.	.	ID=PRO_0000252268;Note=Uncharacterized membrane protein YOR365C	
+Q08844	UniProtKB	Topological domain	25	203	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Topological domain	225	238	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Transmembrane	239	259	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Topological domain	260	374	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Transmembrane	375	395	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Topological domain	396	415	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Transmembrane	416	438	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Topological domain	439	452	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Transmembrane	453	473	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Topological domain	474	516	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Transmembrane	517	537	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Topological domain	538	545	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Transmembrane	546	566	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Topological domain	567	571	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Transmembrane	572	592	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Topological domain	593	605	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Transmembrane	606	626	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Topological domain	627	703	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Glycosylation	43	43	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Glycosylation	87	87	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08844	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5R4 1 46
+P0C5R4	UniProtKB	Chain	1	46	.	.	.	ID=PRO_0000309062;Note=Uncharacterized protein YOL083C-A	
+##sequence-region P53049 1 1477
+P53049	UniProtKB	Chain	1	1477	.	.	.	ID=PRO_0000093450;Note=Oligomycin resistance ATP-dependent permease YOR1	
+P53049	UniProtKB	Topological domain	1	206	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	207	227	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	228	249	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	250	270	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	271	328	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	329	349	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	350	357	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	358	370	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	371	433	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	434	454	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	455	478	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	479	499	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	500	615	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	616	636	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	637	892	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	893	913	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	914	940	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	941	961	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	962	1027	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	1028	1048	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	1049	1117	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	1118	1138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	1139	1141	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Transmembrane	1142	1162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Topological domain	1163	1477	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Domain	207	493	.	.	.	Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Domain	581	808	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P53049	UniProtKB	Domain	897	1175	.	.	.	Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P53049	UniProtKB	Domain	1213	1464	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P53049	UniProtKB	Nucleotide binding	621	628	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P53049	UniProtKB	Nucleotide binding	1247	1254	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P53049	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P53049	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53049	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53049	UniProtKB	Glycosylation	661	661	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Glycosylation	759	759	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53049	UniProtKB	Glycosylation	799	799	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12486 1 218
+Q12486	UniProtKB	Chain	1	218	.	.	.	ID=PRO_0000237658;Note=Putative uncharacterized hydrolase YOR131C	
+##sequence-region Q12251 1 326
+Q12251	UniProtKB	Chain	1	326	.	.	.	ID=PRO_0000243949;Note=Uncharacterized mitochondrial carrier YPR011C	
+Q12251	UniProtKB	Transmembrane	24	40	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12251	UniProtKB	Transmembrane	84	104	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12251	UniProtKB	Transmembrane	126	143	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12251	UniProtKB	Transmembrane	195	213	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12251	UniProtKB	Transmembrane	237	254	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12251	UniProtKB	Transmembrane	297	316	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12251	UniProtKB	Repeat	20	107	.	.	.	Note=Solcar 1	
+Q12251	UniProtKB	Repeat	120	219	.	.	.	Note=Solcar 2	
+Q12251	UniProtKB	Repeat	231	322	.	.	.	Note=Solcar 3	
+##sequence-region Q12079 1 277
+Q12079	UniProtKB	Chain	1	277	.	.	.	ID=PRO_0000252275;Note=Uncharacterized membrane protein YPR027C	
+Q12079	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12079	UniProtKB	Topological domain	22	84	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12079	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12079	UniProtKB	Topological domain	106	277	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12079	UniProtKB	Glycosylation	155	155	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12079	UniProtKB	Glycosylation	265	265	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q6Q5F3 1 151
+Q6Q5F3	UniProtKB	Chain	1	151	.	.	.	ID=PRO_0000299818;Note=Uncharacterized protein YPR053C	
+##sequence-region Q12194 1 479
+Q12194	UniProtKB	Chain	1	479	.	.	.	ID=PRO_0000203492;Note=Uncharacterized protein YPL066W	
+##sequence-region Q02864 1 156
+Q02864	UniProtKB	Chain	1	156	.	.	.	ID=PRO_0000238643;Note=Uncharacterized protein YPL071C	
+Q02864	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region O13585 1 888
+O13585	UniProtKB	Chain	1	888	.	.	.	ID=PRO_0000257825;Note=Dilute domain-containing protein YPR089W	
+O13585	UniProtKB	Domain	360	745	.	.	.	Note=Dilute;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00503	
+##sequence-region Q06089 1 161
+Q06089	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000252300;Note=Uncharacterized mitochondrial outer membrane protein YPR098C	
+Q06089	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06089	UniProtKB	Transmembrane	60	80	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06089	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E751 1 87
+Q3E751	UniProtKB	Chain	1	87	.	.	.	ID=PRO_0000238648;Note=Uncharacterized protein YPL119C-A	
+Q3E751	UniProtKB	Transmembrane	21	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13566 1 144
+O13566	UniProtKB	Chain	1	144	.	.	.	ID=PRO_0000299825;Note=Putative uncharacterized protein YPR123C	
+O13566	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13566	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13566	UniProtKB	Transmembrane	83	103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13566	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13568 1 135
+O13568	UniProtKB	Chain	1	135	.	.	.	ID=PRO_0000299827;Note=Putative uncharacterized protein YPR130C	
+O13568	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C2J0 1 1756
+P0C2J0	UniProtKB	Chain	1	1756	.	.	.	ID=PRO_0000279179;Note=Transposon Ty1-PR2 Gag-Pol polyprotein	
+P0C2J0	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279180;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J0	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279181;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J0	UniProtKB	Chain	583	1218	.	.	.	ID=PRO_0000279182;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J0	UniProtKB	Chain	1219	1756	.	.	.	ID=PRO_0000279183;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J0	UniProtKB	Domain	660	836	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J0	UniProtKB	Domain	1339	1477	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0C2J0	UniProtKB	Domain	1611	1753	.	.	.	Note=RNase H Ty1/copia-type	
+P0C2J0	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J0	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+P0C2J0	UniProtKB	Motif	1179	1213	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J0	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0C2J0	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P0C2J0	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J0	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J0	UniProtKB	Metal binding	1347	1347	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J0	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J0	UniProtKB	Metal binding	1429	1429	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J0	UniProtKB	Metal binding	1611	1611	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J0	UniProtKB	Metal binding	1653	1653	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J0	UniProtKB	Metal binding	1686	1686	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J0	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J0	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J0	UniProtKB	Site	1218	1219	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q06537 1 140
+Q06537	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000244638;Note=Uncharacterized protein YPR153W	
+Q06537	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06537	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06537	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06537	UniProtKB	Glycosylation	27	27	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13575 1 123
+O13575	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000299833;Note=Putative uncharacterized protein YPR177C	
+O13575	UniProtKB	Compositional bias	11	20	.	.	.	Note=Poly-Ser	
+##sequence-region P0C5R9 1 85
+P0C5R9	UniProtKB	Chain	1	85	.	.	.	ID=PRO_0000309067;Note=Uncharacterized protein YPR170W-B	
+P0C5R9	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C5R9	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P18961 1 677
+P18961	UniProtKB	Chain	1	677	.	.	.	ID=PRO_0000086836;Note=Serine/threonine-protein kinase YPK2/YKR2	
+P18961	UniProtKB	Domain	344	599	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P18961	UniProtKB	Domain	600	670	.	.	.	Note=AGC-kinase C-terminal	
+P18961	UniProtKB	Nucleotide binding	350	358	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P18961	UniProtKB	Compositional bias	35	57	.	.	.	Note=His-rich	
+P18961	UniProtKB	Active site	467	467	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P18961	UniProtKB	Binding site	373	373	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P18961	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P18961	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12688	
+P18961	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P18961	UniProtKB	Modified residue	499	499	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P18961	UniProtKB	Modified residue	501	501	.	.	.	Note=Phosphothreonine%3B by PKH2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732	
+P18961	UniProtKB	Modified residue	641	641	.	.	.	Note=Phosphoserine%3B by TOR2;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000269|PubMed:16055732;Dbxref=PMID:17330950,PMID:16055732	
+P18961	UniProtKB	Modified residue	650	650	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P18961	UniProtKB	Modified residue	659	659	.	.	.	Note=Phosphothreonine%3B by TOR2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732	
+P18961	UniProtKB	Modified residue	669	669	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P18961	UniProtKB	Mutagenesis	239	239	.	.	.	Note=Rescues growth of cells compromised in TORC2%2C but not TORC1 function. Restores SLT2 activation and suppresses actin cytoskeleton organization defect in TOR2 mutant cells. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732	
+P18961	UniProtKB	Mutagenesis	373	373	.	.	.	Note=No kinase activity. K->R%2CA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12221112,ECO:0000269|PubMed:15840588;Dbxref=PMID:12221112,PMID:15840588	
+P18961	UniProtKB	Mutagenesis	641	641	.	.	.	Note=Reduced kinase activity%3B when associated with A-659. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732	
+P18961	UniProtKB	Mutagenesis	659	659	.	.	.	Note=Reduced kinase activity%3B when associated with A-641. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732	
+##sequence-region P32939 1 208
+P32939	UniProtKB	Chain	1	208	.	.	.	ID=PRO_0000121320;Note=GTP-binding protein YPT7	
+P32939	UniProtKB	Nucleotide binding	15	22	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32939	UniProtKB	Nucleotide binding	64	68	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32939	UniProtKB	Nucleotide binding	126	129	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32939	UniProtKB	Motif	37	45	.	.	.	Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32939	UniProtKB	Modified residue	208	208	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32939	UniProtKB	Lipidation	206	206	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32939	UniProtKB	Lipidation	208	208	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32939	UniProtKB	Cross-link	147	147	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32939	UniProtKB	Beta strand	8	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Helix	21	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Beta strand	46	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Beta strand	58	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Helix	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY2	
+P32939	UniProtKB	Turn	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY2	
+P32939	UniProtKB	Helix	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY2	
+P32939	UniProtKB	Beta strand	84	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Helix	94	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Helix	100	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Turn	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Beta strand	121	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Helix	139	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Beta strand	154	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Turn	159	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+P32939	UniProtKB	Helix	165	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3	
+##sequence-region P36036 1 203
+P36036	UniProtKB	Chain	1	203	.	.	.	ID=PRO_0000082033;Note=RNA annealing protein YRA2	
+P36036	UniProtKB	Domain	64	138	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P36036	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P38079 1 344
+P38079	UniProtKB	Chain	1	344	.	.	.	ID=PRO_0000196286;Note=Protein YRO2	
+P38079	UniProtKB	Topological domain	1	34	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Topological domain	56	62	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Topological domain	84	119	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Topological domain	141	141	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Topological domain	163	172	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Topological domain	194	202	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Transmembrane	203	223	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Topological domain	224	238	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Transmembrane	239	259	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Topological domain	260	344	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38079	UniProtKB	Compositional bias	304	331	.	.	.	Note=Lys-rich	
+P38079	UniProtKB	Compositional bias	334	344	.	.	.	Note=Glu-rich	
+P38079	UniProtKB	Modified residue	293	293	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38079	UniProtKB	Modified residue	341	341	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:18407956,PMID:19779198	
+P38079	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956;Dbxref=PMID:17761666,PMID:18407956	
+P38079	UniProtKB	Cross-link	286	286	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region P39703 1 215
+P39703	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000202411;Note=Putative uncharacterized protein YAL004W	
+P39703	UniProtKB	Sequence conflict	17	17	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38215 1 129
+P38215	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38215	UniProtKB	Chain	21	129	.	.	.	ID=PRO_0000014310;Note=Putative uncharacterized protein YBR013C	
+##sequence-region P38223 1 100
+P38223	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000202473;Note=Uncharacterized protein YBR032W	
+##sequence-region P38277 1 524
+P38277	UniProtKB	Chain	1	524	.	.	.	ID=PRO_0000202493;Note=Uncharacterized protein YBR138C	
+P38277	UniProtKB	Sequence conflict	122	122	.	.	.	Note=L->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38277	UniProtKB	Sequence conflict	122	122	.	.	.	Note=L->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q96VH3 1 125
+Q96VH3	UniProtKB	Chain	1	125	.	.	.	ID=PRO_0000248447;Note=Putative uncharacterized protein YCL021W-A	
+Q96VH3	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q2V2Q2 1 79
+Q2V2Q2	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q2V2Q2	UniProtKB	Chain	19	55	.	.	.	ID=PRO_0000248449;Note=Uncharacterized protein YCL048W-A	
+Q2V2Q2	UniProtKB	Propeptide	56	79	.	.	.	ID=PRO_0000253885;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q2V2Q2	UniProtKB	Lipidation	55	55	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q2V2Q2	UniProtKB	Glycosylation	25	25	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q2V2Q2	UniProtKB	Glycosylation	30	30	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q2V2Q2	UniProtKB	Glycosylation	35	35	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q2V2Q2	UniProtKB	Glycosylation	40	40	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39109 1 1515
+P39109	UniProtKB	Chain	1	1515	.	.	.	ID=PRO_0000093449;Note=Metal resistance protein YCF1	
+P39109	UniProtKB	Topological domain	1	32	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	54	73	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	95	99	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	121	130	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	152	169	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	170	190	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	191	278	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	279	299	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	300	345	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	346	366	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	367	422	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	423	443	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	444	446	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	447	467	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	468	530	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	531	551	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	552	572	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	573	593	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	594	943	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	944	964	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	965	1001	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	1002	1023	.	.	.	Note=Helical%3B Name%3D13;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	1024	1066	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	1067	1087	.	.	.	Note=Helical%3B Name%3D14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	1088	1088	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	1089	1109	.	.	.	Note=Helical%3B Name%3D15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	1110	1180	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	1181	1201	.	.	.	Note=Helical%3B Name%3D16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	1202	1205	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Transmembrane	1206	1226	.	.	.	Note=Helical%3B Name%3D17;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Topological domain	1227	1515	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39109	UniProtKB	Domain	287	590	.	.	.	Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Domain	626	853	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P39109	UniProtKB	Domain	951	1235	.	.	.	Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P39109	UniProtKB	Domain	1272	1507	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P39109	UniProtKB	Nucleotide binding	663	670	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P39109	UniProtKB	Nucleotide binding	1306	1313	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P39109	UniProtKB	Modified residue	251	251	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39109	UniProtKB	Modified residue	873	873	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39109	UniProtKB	Modified residue	903	903	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P39109	UniProtKB	Modified residue	908	908	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P39109	UniProtKB	Modified residue	911	911	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P39109	UniProtKB	Modified residue	914	914	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39109	UniProtKB	Mutagenesis	713	713	.	.	.	Note=Loss of function. Missing	
+P39109	UniProtKB	Mutagenesis	908	908	.	.	.	Note=Loss of function. S->A	
+P39109	UniProtKB	Sequence conflict	680	680	.	.	.	Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P37264 1 122
+P37264	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000202555;Note=Putative uncharacterized protein YCL065W	
+P37264	UniProtKB	Transmembrane	21	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37264	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37264	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12316 1 1755
+Q12316	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279069;Note=Transposon Ty1-GR3 Gag-Pol polyprotein	
+Q12316	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279070;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12316	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279071;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12316	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279072;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12316	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279073;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12316	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12316	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12316	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q12316	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12316	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q12316	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12316	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q12316	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q12316	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12316	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12316	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12316	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12316	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12316	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12316	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12316	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12316	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12316	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12316	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12316	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region P53227 1 271
+P53227	UniProtKB	Chain	1	271	.	.	.	ID=PRO_0000202794;Note=Uncharacterized protein YGR042W	
+##sequence-region Q8TGT7 1 37
+Q8TGT7	UniProtKB	Chain	1	37	.	.	.	ID=PRO_0000245388;Note=Uncharacterized protein YGR204C-A	
+##sequence-region P53234 1 283
+P53234	UniProtKB	Chain	1	283	.	.	.	ID=PRO_0000202799;Note=Uncharacterized protein YGR053C	
+##sequence-region P0CX64 1 1770
+P0CX64	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000409809;Note=Transposon Ty2-GR2 Gag-Pol polyprotein	
+P0CX64	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000409810;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX64	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000409811;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX64	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000409812;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX64	UniProtKB	Chain	1233	1770	.	.	.	ID=PRO_0000409813;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX64	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX64	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0CX64	UniProtKB	Domain	1625	1767	.	.	.	Note=RNase H Ty1/copia-type	
+P0CX64	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX64	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+P0CX64	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX64	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX64	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX64	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX64	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX64	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX64	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX64	UniProtKB	Metal binding	1625	1625	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX64	UniProtKB	Metal binding	1667	1667	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX64	UniProtKB	Metal binding	1700	1700	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX64	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX64	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX64	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P48238 1 217
+P48238	UniProtKB	Chain	1	217	.	.	.	ID=PRO_0000202832;Note=Uncharacterized protein YGR153W	
+P48238	UniProtKB	Sequence conflict	158	158	.	.	.	Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48238	UniProtKB	Sequence conflict	158	158	.	.	.	Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q3E750 1 60
+Q3E750	UniProtKB	Chain	1	60	.	.	.	ID=PRO_0000245379;Note=Uncharacterized protein YGL041C-B	
+Q3E750	UniProtKB	Transmembrane	19	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53302 1 121
+P53302	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000202841;Note=Putative uncharacterized protein YGR190C	
+##sequence-region P50083 1 69
+P50083	UniProtKB	Chain	1	69	.	.	.	ID=PRO_0000202849;Note=Putative uncharacterized protein YGR226C	
+P50083	UniProtKB	Transmembrane	13	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53326 1 701
+P53326	UniProtKB	Chain	1	701	.	.	.	ID=PRO_0000202864;Note=Uncharacterized protein YGR266W	
+##sequence-region P53162 1 154
+P53162	UniProtKB	Chain	1	154	.	.	.	ID=PRO_0000202763;Note=Putative uncharacterized protein YGL069C	
+##sequence-region P53161 1 119
+P53161	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000202762;Note=Putative uncharacterized protein YGL072C	
+P53161	UniProtKB	Transmembrane	30	50	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12222 1 375
+Q12222	UniProtKB	Chain	1	375	.	.	.	ID=PRO_0000086159;Note=Glycogen synthase kinase-3 homolog YGK3	
+Q12222	UniProtKB	Domain	41	329	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12222	UniProtKB	Nucleotide binding	47	55	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12222	UniProtKB	Active site	173	173	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q12222	UniProtKB	Binding site	74	74	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12222	UniProtKB	Modified residue	211	211	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P53113 1 225
+P53113	UniProtKB	Chain	1	225	.	.	.	ID=PRO_0000202733;Note=Putative uncharacterized protein YGL152C	
+P53113	UniProtKB	Transmembrane	40	60	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53113	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53113	UniProtKB	Transmembrane	151	171	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53113	UniProtKB	Transmembrane	176	196	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53106 1 192
+P53106	UniProtKB	Chain	1	192	.	.	.	ID=PRO_0000202729;Note=Putative uncharacterized protein YGL165C	
+P53106	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46945 1 554
+P46945	UniProtKB	Chain	1	554	.	.	.	ID=PRO_0000202727;Note=Uncharacterized protein YGL176C	
+##sequence-region P53098 1 57
+P53098	UniProtKB	Chain	1	57	.	.	.	ID=PRO_0000202724;Note=Putative uncharacterized protein YGL188C	
+##sequence-region P53087 1 161
+P53087	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000202718;Note=Putative uncharacterized protein YGL214W	
+P53087	UniProtKB	Transmembrane	76	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53069 1 104
+P53069	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000202709;Note=Putative uncharacterized protein YGL239C	
+P53069	UniProtKB	Transmembrane	80	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53056 1 76
+P53056	UniProtKB	Chain	1	76	.	.	.	ID=PRO_0000202703;Note=Putative UPF0377 protein YGL260W	
+##sequence-region Q8TGT6 1 29
+Q8TGT6	UniProtKB	Chain	1	29	.	.	.	ID=PRO_0000245394;Note=Uncharacterized protein YHR022C-A	
+##sequence-region A0A023PZH9 1 153
+A0A023PZH9	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000431019;Note=Putative uncharacterized protein YHL034W-A	
+A0A023PZH9	UniProtKB	Compositional bias	5	56	.	.	.	Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016	
+##sequence-region Q3E746 1 53
+Q3E746	UniProtKB	Chain	1	53	.	.	.	ID=PRO_0000245395;Note=Uncharacterized protein YHR086W-A	
+##sequence-region P38893 1 341
+P38893	UniProtKB	Chain	1	341	.	.	.	ID=PRO_0000197448;Note=Uncharacterized isomerase YHR210C	
+P38893	UniProtKB	Active site	175	175	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10126	
+P38893	UniProtKB	Active site	306	306	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38893	UniProtKB	Binding site	70	70	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38893	UniProtKB	Binding site	239	239	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q8TGN6 1 216
+Q8TGN6	UniProtKB	Chain	1	216	.	.	.	ID=PRO_0000299928;Note=Putative uncharacterized protein YHR137C-A	
+##sequence-region P38898 1 153
+P38898	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000202946;Note=Putative uncharacterized protein YHR217C	
+##sequence-region P38900 1 624
+P38900	UniProtKB	Chain	1	624	.	.	.	ID=PRO_0000202948;Note=Putative uncharacterized protein YHR219W	
+##sequence-region A0A023PXF5 1 105
+A0A023PXF5	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000430969;Note=Putative uncharacterized helicase-like protein YHR218W-A	
+A0A023PXF5	UniProtKB	Domain	2	42	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+##sequence-region P38752 1 130
+P38752	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000202884;Note=Uncharacterized protein YHL005C	
+P38752	UniProtKB	Transmembrane	15	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38733 1 133
+P38733	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38733	UniProtKB	Chain	23	133	.	.	.	ID=PRO_0000202880;Note=Uncharacterized protein YHL037C	
+P38733	UniProtKB	Glycosylation	111	111	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PYH8 1 122
+A0A023PYH8	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000431034;Note=Putative uncharacterized protein YIL047C-A	
+##sequence-region Q8TGN4 1 89
+Q8TGN4	UniProtKB	Chain	1	89	.	.	.	ID=PRO_0000299758;Note=Putative uncharacterized protein YIL021C-A	
+##sequence-region A0A023PZK4 1 127
+A0A023PZK4	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000431041;Note=Putative uncharacterized protein YIR030W-A	
+##sequence-region Q99219 1 290
+Q99219	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12173	
+Q99219	UniProtKB	Chain	2	290	.	.	.	ID=PRO_0000279376;Note=Transposon Ty3-I Gag polyprotein	
+Q99219	UniProtKB	Chain	2	207	.	.	.	ID=PRO_0000279377;Note=Capsid protein	
+Q99219	UniProtKB	Peptide	208	233	.	.	.	ID=PRO_0000279378;Note=Spacer peptide p3	
+Q99219	UniProtKB	Chain	234	290	.	.	.	ID=PRO_0000279379;Note=Nucleocapsid protein p9	
+Q99219	UniProtKB	Zinc finger	265	282	.	.	.	Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+Q99219	UniProtKB	Site	207	208	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q99219	UniProtKB	Site	233	234	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q99219	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12173	
+##sequence-region P53845 1 314
+P53845	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53845	UniProtKB	Chain	2	314	.	.	.	ID=PRO_0000203381;Note=Protein transport protein YIF1	
+P53845	UniProtKB	Topological domain	2	153	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53845	UniProtKB	Transmembrane	154	174	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53845	UniProtKB	Topological domain	175	188	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53845	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53845	UniProtKB	Topological domain	210	217	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53845	UniProtKB	Transmembrane	218	238	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53845	UniProtKB	Topological domain	239	243	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53845	UniProtKB	Transmembrane	244	264	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53845	UniProtKB	Topological domain	265	293	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53845	UniProtKB	Transmembrane	294	313	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53845	UniProtKB	Topological domain	314	314	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53845	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P40440 1 109
+P40440	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000050407;Note=Putative transporter-like protein YIL171W	
+P40440	UniProtKB	Topological domain	1	56	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40440	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40440	UniProtKB	Topological domain	78	109	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40440	UniProtKB	Glycosylation	87	87	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40570 1 242
+P40570	UniProtKB	Chain	1	242	.	.	.	ID=PRO_0000203004;Note=Putative uncharacterized protein YIR014W	
+P40570	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40570	UniProtKB	Transmembrane	152	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40575 1 100
+P40575	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000203006;Note=Uncharacterized protein YIR020C	
+##sequence-region P40579 1 254
+P40579	UniProtKB	Chain	1	254	.	.	.	ID=PRO_0000054870;Note=Uncharacterized oxidoreductase YIR035C	
+P40579	UniProtKB	Nucleotide binding	6	30	.	.	.	Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40579	UniProtKB	Active site	150	150	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001	
+P40579	UniProtKB	Binding site	137	137	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40579	UniProtKB	Beta strand	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	13	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Beta strand	30	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	38	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Beta strand	52	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	62	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Beta strand	81	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Turn	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	100	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	112	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Beta strand	131	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	148	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	157	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Beta strand	171	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Turn	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	200	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	219	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Beta strand	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+P40579	UniProtKB	Helix	247	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV	
+##sequence-region P40584 1 110
+P40584	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000203008;Note=Putative UPF0377 protein YIR040C	
+##sequence-region P47101 1 745
+P47101	UniProtKB	Chain	1	745	.	.	.	ID=PRO_0000203090;Note=UPF0508 protein YJR030C	
+P47101	UniProtKB	Compositional bias	680	736	.	.	.	Note=Ser-rich	
+P47101	UniProtKB	Natural variant	742	745	.	.	.	Note=In strain: VP102-10A. LRNM->HVKTKADVWKPSRVGYTDIFSQEYKGIVVAIKFVICSDAEGTLYPREYNSRLHDIKRLGRTGLSFTDKKEAYLLEFKNQDVVDHVHKLILPFNTSWQSN	
+##sequence-region Q8TGJ8 1 73
+Q8TGJ8	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000299763;Note=Putative uncharacterized protein YJL026C-A	
+##sequence-region Q3E837 1 39
+Q3E837	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E837	UniProtKB	Chain	22	39	.	.	.	ID=PRO_0000245413;Note=Uncharacterized protein YJL052C-A	
+##sequence-region P0CT86 1 78
+P0CT86	UniProtKB	Chain	1	78	.	.	.	ID=PRO_0000435366;Note=Uncharacterized protein YJR107C-A	
+##sequence-region P47098 1 1755
+P47098	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000199563;Note=Transposon Ty1-JR1 Gag-Pol polyprotein	
+P47098	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279082;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47098	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279083;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47098	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279084;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47098	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279085;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47098	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47098	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P47098	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+P47098	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47098	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+P47098	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47098	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P47098	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P47098	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47098	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47098	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47098	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47098	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47098	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47098	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47098	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47098	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47098	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47098	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47098	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region P47137 1 282
+P47137	UniProtKB	Chain	1	282	.	.	.	ID=PRO_0000124679;Note=Uncharacterized oxidoreductase YJR096W	
+P47137	UniProtKB	Active site	50	50	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47137	UniProtKB	Binding site	115	115	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47137	UniProtKB	Site	81	81	.	.	.	Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q8TGT3 1 32
+Q8TGT3	UniProtKB	Chain	1	32	.	.	.	ID=PRO_0000245411;Note=Uncharacterized protein YJL077W-B	
+##sequence-region P47173 1 342
+P47173	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000203126;Note=Uncharacterized protein YJR142W	
+P47173	UniProtKB	Domain	155	309	.	.	.	Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794	
+##sequence-region P47080 1 104
+P47080	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000203079;Note=Uncharacterized protein YJL007C	
+P47080	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47073 1 94
+P47073	UniProtKB	Chain	1	94	.	.	.	ID=PRO_0000203076;Note=Putative uncharacterized protein YJL015C	
+##sequence-region P47072 1 561
+P47072	UniProtKB	Chain	1	561	.	.	.	ID=PRO_0000203075;Note=Uncharacterized protein YJL016W	
+P47072	UniProtKB	Modified residue	514	514	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P47048 1 450
+P47048	UniProtKB	Chain	1	450	.	.	.	ID=PRO_0000203065;Note=Uncharacterized protein YJL049W	
+##sequence-region P47044 1 245
+P47044	UniProtKB	Chain	1	245	.	.	.	ID=PRO_0000203061;Note=LOG family protein YJL055W	
+##sequence-region P47004 1 100
+P47004	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000203030;Note=Putative uncharacterized protein YJL150W	
+##sequence-region P36127 1 104
+P36127	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000203206;Note=Uncharacterized protein YKR032W	
+##sequence-region P0C5P5 1 77
+P0C5P5	UniProtKB	Chain	1	77	.	.	.	ID=PRO_0000309043;Note=Putative uncharacterized YKL165C-A	
+P0C5P5	UniProtKB	Transmembrane	36	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36158 1 585
+P36158	UniProtKB	Chain	1	585	.	.	.	ID=PRO_0000203224;Note=Uncharacterized protein YKR078W	
+##sequence-region P36103 1 277
+P36103	UniProtKB	Chain	1	277	.	.	.	ID=PRO_0000203189;Note=Uncharacterized protein YKL023W	
+P36103	UniProtKB	Sequence conflict	25	26	.	.	.	Note=QQ->HE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35733 1 124
+P35733	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000203178;Note=Putative uncharacterized protein YKL053W	
+##sequence-region P36089 1 147
+P36089	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000203173;Note=Putative uncharacterized protein YKL066W	
+##sequence-region P36081 1 392
+P36081	UniProtKB	Chain	1	392	.	.	.	ID=PRO_0000203168;Note=Uncharacterized protein YKL077W	
+##sequence-region P34245 1 136
+P34245	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000203162;Note=Uncharacterized protein YKL097C	
+##sequence-region P36067 1 173
+P36067	UniProtKB	Chain	1	173	.	.	.	ID=PRO_0000203150;Note=Putative uncharacterized protein YKL131W	
+##sequence-region P36015 1 200
+P36015	UniProtKB	Chain	1	197	.	.	.	ID=PRO_0000206781;Note=Synaptobrevin homolog YKT6	
+P36015	UniProtKB	Propeptide	198	200	.	.	.	ID=PRO_0000396675;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36015	UniProtKB	Domain	7	129	.	.	.	Note=Longin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00231	
+P36015	UniProtKB	Domain	140	200	.	.	.	Note=v-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00290	
+P36015	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36015	UniProtKB	Modified residue	197	197	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36015	UniProtKB	Lipidation	196	196	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36015	UniProtKB	Lipidation	197	197	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36015	UniProtKB	Beta strand	3	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Beta strand	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Beta strand	17	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Beta strand	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H8M	
+P36015	UniProtKB	Turn	30	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Helix	35	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Beta strand	55	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Beta strand	64	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Beta strand	74	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Helix	87	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Helix	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Turn	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Helix	124	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6	
+P36015	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IOU	
+##sequence-region P36111 1 568
+P36111	UniProtKB	Chain	1	568	.	.	.	ID=PRO_0000203196;Note=Uncharacterized protein YKR015C	
+##sequence-region P0CF00 1 54
+P0CF00	UniProtKB	Chain	1	54	.	.	.	ID=PRO_0000393298;Note=Putative uncharacterized protein YLR157W-E	
+##sequence-region P0CY01 1 160
+P0CY01	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000410457;Note=UPF0479 membrane protein YLL067W-A	
+P0CY01	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CY01	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CY01	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region P0C5Q2 1 26
+P0C5Q2	UniProtKB	Chain	1	26	.	.	.	ID=PRO_0000309050;Note=Putative uncharacterized protein YMR013W-A	
+##sequence-region Q6Q572 1 108
+Q6Q572	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000299666;Note=Putative uncharacterized protein YMR031W-A	
+##sequence-region A0A023PZG9 1 121
+A0A023PZG9	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000431059;Note=Putative uncharacterized membrane protein YML047W-A	
+A0A023PZG9	UniProtKB	Transmembrane	2	22	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZG9	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZG9	UniProtKB	Transmembrane	89	109	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q6B0Y6 1 121
+Q6B0Y6	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000299667;Note=Putative uncharacterized protein YMR052C-A	
+Q6B0Y6	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6B0Y6	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6B0Y6	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6B0Y6	UniProtKB	Compositional bias	38	41	.	.	.	Note=Poly-Phe	
+##sequence-region Q12744 1 133
+Q12744	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000299663;Note=Putative uncharacterized protein YML094C-A	
+##sequence-region Q3E7B5 1 62
+Q3E7B5	UniProtKB	Chain	1	62	.	.	.	ID=PRO_0000247791;Note=Uncharacterized protein YMR230W-A	
+##sequence-region Q04909 1 80
+Q04909	UniProtKB	Chain	1	80	.	.	.	ID=PRO_0000203361;Note=Putative UPF0377 protein YMR324C	
+Q04909	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04526 1 418
+Q04526	UniProtKB	Chain	1	418	.	.	.	ID=PRO_0000203247;Note=Putative uncharacterized protein YML083C	
+##sequence-region P0CL35 1 160
+P0CL35	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000406010;Note=Putative UPF0479 protein YML133W-B	
+P0CL35	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL35	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL35	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region P03881 1 472
+P03881	UniProtKB	Chain	1	472	.	.	.	ID=PRO_0000196879;Note=Uncharacterized mitochondrial protein RF1	
+P03881	UniProtKB	Compositional bias	20	84	.	.	.	Note=Asn-rich	
+P03881	UniProtKB	Compositional bias	361	427	.	.	.	Note=Asn-rich	
+##sequence-region Q04674 1 123
+Q04674	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000203278;Note=Putative uncharacterized protein YMR057C	
+##sequence-region Q8TGL7 1 32
+Q8TGL7	UniProtKB	Chain	1	32	.	.	.	ID=PRO_0000299677;Note=Putative uncharacterized protein YNR003W-A	
+Q8TGL7	UniProtKB	Compositional bias	4	8	.	.	.	Note=Poly-Ser	
+##sequence-region Q3E7Z2 1 85
+Q3E7Z2	UniProtKB	Chain	1	85	.	.	.	ID=PRO_0000247802;Note=Uncharacterized protein YNL042W-B	
+##sequence-region Q8TGQ9 1 29
+Q8TGQ9	UniProtKB	Chain	1	29	.	.	.	ID=PRO_0000299675;Note=Putative uncharacterized protein YNL103W-A	
+##sequence-region Q8TGL9 1 27
+Q8TGL9	UniProtKB	Chain	1	27	.	.	.	ID=PRO_0000299674;Note=Putative uncharacterized protein YNL144W-A	
+##sequence-region P53737 1 142
+P53737	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000203479;Note=Putative uncharacterized protein YNR042W	
+P53737	UniProtKB	Compositional bias	96	105	.	.	.	Note=Poly-Glu	
+##sequence-region P53748 1 327
+P53748	UniProtKB	Chain	1	327	.	.	.	ID=PRO_0000203482;Note=Uncharacterized membrane protein YNR062C	
+P53748	UniProtKB	Topological domain	1	19	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Topological domain	41	51	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Topological domain	73	104	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Topological domain	126	141	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Topological domain	163	199	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Topological domain	221	235	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Transmembrane	236	256	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Topological domain	257	275	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Transmembrane	276	296	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Topological domain	297	300	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Transmembrane	301	321	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53748	UniProtKB	Topological domain	322	327	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53976 1 612
+P53976	UniProtKB	Chain	1	612	.	.	.	ID=PRO_0000203462;Note=Uncharacterized protein YNL018C	
+##sequence-region P53963 1 612
+P53963	UniProtKB	Chain	1	612	.	.	.	ID=PRO_0000203458;Note=Uncharacterized protein YNL034W	
+##sequence-region P53952 1 270
+P53952	UniProtKB	Chain	1	270	.	.	.	ID=PRO_0000203452;Note=Uncharacterized protein YNL050C	
+##sequence-region P0CL36 1 160
+P0CL36	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000406011;Note=Putative UPF0479 protein YNL339W-B	
+P0CL36	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL36	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL36	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region P53925 1 644
+P53925	UniProtKB	Chain	1	644	.	.	.	ID=PRO_0000203433;Note=Uncharacterized vacuolar membrane protein YNL115C	
+P53925	UniProtKB	Topological domain	1	90	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Topological domain	112	122	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Topological domain	144	147	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Transmembrane	148	168	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Topological domain	169	174	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Topological domain	196	271	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Transmembrane	272	292	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Topological domain	293	644	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Domain	348	619	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53925	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53925	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53925	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53925	UniProtKB	Modified residue	244	244	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53925	UniProtKB	Sequence conflict	644	644	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53908 1 130
+P53908	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000203424;Note=Uncharacterized membrane protein YNL143C	
+P53908	UniProtKB	Topological domain	1	58	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53908	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53908	UniProtKB	Topological domain	80	94	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53908	UniProtKB	Transmembrane	95	115	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53908	UniProtKB	Topological domain	116	130	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53880 1 145
+P53880	UniProtKB	Chain	1	145	.	.	.	ID=PRO_0000203406;Note=Putative uncharacterized protein YNL179C	
+P53880	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53856 1 143
+P53856	UniProtKB	Chain	1	143	.	.	.	ID=PRO_0000203385;Note=Putative uncharacterized protein YNL235C	
+P53856	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E807 1 68
+Q3E807	UniProtKB	Chain	1	68	.	.	.	ID=PRO_0000235936;Note=Uncharacterized protein YOR011W-A	
+##sequence-region Q08205 1 117
+Q08205	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000299689;Note=Putative uncharacterized protein YOL037C	
+Q08205	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08205	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08205	UniProtKB	Transmembrane	87	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36025 1 268
+P36025	UniProtKB	Chain	1	268	.	.	.	ID=PRO_0000203490;Note=Uncharacterized protein YOR062C	
+P36025	UniProtKB	Sequence conflict	154	154	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36025	UniProtKB	Sequence conflict	236	236	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08234 1 1294
+Q08234	UniProtKB	Chain	1	1294	.	.	.	ID=PRO_0000093467;Note=Uncharacterized ABC transporter ATP-binding protein/permease YOL075C	
+Q08234	UniProtKB	Topological domain	1	375	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Transmembrane	376	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Topological domain	397	495	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Transmembrane	496	516	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Topological domain	517	530	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Transmembrane	531	551	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Topological domain	552	604	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Transmembrane	605	625	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Topological domain	626	1038	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Transmembrane	1039	1059	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Topological domain	1060	1120	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Transmembrane	1121	1141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Topological domain	1142	1266	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Transmembrane	1267	1287	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Topological domain	1288	1294	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Domain	28	287	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q08234	UniProtKB	Domain	679	941	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q08234	UniProtKB	Nucleotide binding	62	69	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q08234	UniProtKB	Nucleotide binding	727	734	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q08234	UniProtKB	Glycosylation	41	41	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Glycosylation	86	86	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Glycosylation	101	101	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Glycosylation	151	151	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Glycosylation	341	341	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Glycosylation	349	349	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Glycosylation	371	371	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Glycosylation	528	528	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Glycosylation	983	983	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08234	UniProtKB	Sequence conflict	1164	1164	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08234	UniProtKB	Sequence conflict	1164	1164	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q3E7B9 1 74
+Q3E7B9	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E7B9	UniProtKB	Chain	19	74	.	.	.	ID=PRO_0000235935;Note=Uncharacterized protein YOR008C-A	
+Q3E7B9	UniProtKB	Topological domain	19	21	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E7B9	UniProtKB	Transmembrane	22	44	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E7B9	UniProtKB	Topological domain	45	74	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12275 1 1648
+Q12275	UniProtKB	Chain	1	1648	.	.	.	ID=PRO_0000237653;Note=Uncharacterized protein YOR093C	
+Q12275	UniProtKB	Transmembrane	228	248	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Transmembrane	1061	1081	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Transmembrane	1224	1244	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Domain	6	120	.	.	.	Note=DMAP-interaction	
+Q12275	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12275	UniProtKB	Modified residue	751	751	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12275	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	71	71	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	98	98	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	128	128	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	151	151	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	209	209	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	288	288	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	328	328	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	575	575	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	644	644	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	730	730	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	881	881	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	917	917	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	995	995	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	1009	1009	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	1198	1198	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	1301	1301	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	1302	1302	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	1447	1447	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	1472	1472	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	1488	1488	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	1565	1565	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	1597	1597	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12275	UniProtKB	Glycosylation	1634	1634	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C272 1 63
+P0C272	UniProtKB	Chain	1	63	.	.	.	ID=PRO_0000268631;Note=Uncharacterized protein YOL013W-A	
+##sequence-region Q3E7Y8 1 44
+Q3E7Y8	UniProtKB	Chain	1	44	.	.	.	ID=PRO_0000235934;Note=Uncharacterized protein YOL155W-A	
+##sequence-region P0CF19 1 215
+P0CF19	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000269759;Note=Putative uncharacterized transporter YOL162W	
+P0CF19	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CF19	UniProtKB	Transmembrane	30	50	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CF19	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CF19	UniProtKB	Transmembrane	87	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CF19	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CF19	UniProtKB	Transmembrane	156	176	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGS2 1 50
+Q8TGS2	UniProtKB	Chain	1	50	.	.	.	ID=PRO_0000245273;Note=Uncharacterized protein YOL019W-A	
+##sequence-region Q12282 1 236
+Q12282	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12282	UniProtKB	Chain	21	212	.	.	.	ID=PRO_0000237664;Note=Cell wall protein YOR214C	
+Q12282	UniProtKB	Propeptide	213	236	.	.	.	ID=PRO_0000237665;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12282	UniProtKB	Lipidation	212	212	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12282	UniProtKB	Glycosylation	155	155	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12282	UniProtKB	Glycosylation	160	160	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12282	UniProtKB	Glycosylation	203	203	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12282	UniProtKB	Glycosylation	212	212	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12225 1 109
+Q12225	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299726;Note=Putative uncharacterized protein YOR225W	
+Q12225	UniProtKB	Transmembrane	26	48	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08681 1 100
+Q08681	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299729;Note=Putative uncharacterized protein YOR248W	
+##sequence-region Q08736 1 102
+Q08736	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000299731;Note=Putative uncharacterized protein YOR277C	
+Q08736	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08736	UniProtKB	Compositional bias	5	12	.	.	.	Note=Poly-Ser	
+Q08736	UniProtKB	Compositional bias	65	72	.	.	.	Note=Poly-Ser	
+##sequence-region Q12040 1 230
+Q12040	UniProtKB	Chain	1	230	.	.	.	ID=PRO_0000245254;Note=Broad-specificity phosphatase YOR283W	
+Q12040	UniProtKB	Region	36	37	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12040	UniProtKB	Region	102	105	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12040	UniProtKB	Active site	24	24	.	.	.	Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707	
+Q12040	UniProtKB	Active site	102	102	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707	
+Q12040	UniProtKB	Site	166	166	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707	
+##sequence-region Q12261 1 157
+Q12261	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000299737;Note=Putative uncharacterized protein YOR325W	
+##sequence-region Q99326 1 363
+Q99326	UniProtKB	Chain	1	363	.	.	.	ID=PRO_0000245288;Note=SWIRM domain-containing protein YOR338W	
+Q99326	UniProtKB	Domain	266	363	.	.	.	Note=SWIRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00247	
+##sequence-region Q08872 1 117
+Q08872	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000299743;Note=Putative uncharacterized protein YOR366W	
+##sequence-region Q08903 1 112
+Q08903	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000299744;Note=Putative uncharacterized protein YOR379C	
+##sequence-region Q06328 1 317
+Q06328	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000253843;Note=Probable vacuolar amino acid transporter YPQ2	
+Q06328	UniProtKB	Topological domain	1	13	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Topological domain	35	39	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Transmembrane	40	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Topological domain	63	71	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Transmembrane	72	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Topological domain	95	143	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Transmembrane	144	164	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Topological domain	165	184	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Topological domain	206	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Topological domain	237	249	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Transmembrane	250	270	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Topological domain	271	317	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06328	UniProtKB	Domain	8	71	.	.	.	Note=PQ-loop 1	
+Q06328	UniProtKB	Domain	185	247	.	.	.	Note=PQ-loop 2	
+Q06328	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40583 1 537
+P40583	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Propeptide	25	52	.	.	.	ID=PRO_0000025844;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Chain	53	515	.	.	.	ID=PRO_0000025845;Note=Aspartic proteinase yapsin-6	
+P40583	UniProtKB	Propeptide	516	537	.	.	.	ID=PRO_0000025846;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Domain	67	426	.	.	.	Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
+P40583	UniProtKB	Active site	85	85	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
+P40583	UniProtKB	Active site	324	324	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
+P40583	UniProtKB	Lipidation	515	515	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Glycosylation	57	57	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Glycosylation	149	149	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Glycosylation	156	156	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Glycosylation	161	161	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Glycosylation	183	183	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Glycosylation	195	195	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Glycosylation	311	311	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Glycosylation	363	363	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Glycosylation	375	375	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Glycosylation	379	379	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40583	UniProtKB	Glycosylation	472	472	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P48559 1 417
+P48559	UniProtKB	Chain	1	417	.	.	.	ID=PRO_0000121322;Note=GTP-binding protein YPT11	
+P48559	UniProtKB	Nucleotide binding	97	104	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48559	UniProtKB	Nucleotide binding	228	232	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48559	UniProtKB	Nucleotide binding	292	295	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48559	UniProtKB	Lipidation	415	415	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48559	UniProtKB	Lipidation	416	416	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48559	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Impairs interaction with MYO2. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144	
+P48559	UniProtKB	Mutagenesis	206	206	.	.	.	Note=Abolishes interaction with MYO2. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144	
+##sequence-region P51996 1 222
+P51996	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38555	
+P51996	UniProtKB	Chain	2	222	.	.	.	ID=PRO_0000121324;Note=GTP-binding protein YPT32/YPT11	
+P51996	UniProtKB	Nucleotide binding	20	27	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P51996	UniProtKB	Nucleotide binding	68	72	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P51996	UniProtKB	Nucleotide binding	126	129	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P51996	UniProtKB	Motif	42	50	.	.	.	Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P51996	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38555	
+P51996	UniProtKB	Lipidation	221	221	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P51996	UniProtKB	Lipidation	222	222	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P51996	UniProtKB	Mutagenesis	27	27	.	.	.	Note=Binds preferentially GDP. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12045183;Dbxref=PMID:12045183	
+P51996	UniProtKB	Mutagenesis	49	49	.	.	.	Note=Cold sensitive. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12045183;Dbxref=PMID:12045183	
+P51996	UniProtKB	Mutagenesis	72	72	.	.	.	Note=Reduces GTPase activity. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12045183;Dbxref=PMID:12045183	
+P51996	UniProtKB	Mutagenesis	126	126	.	.	.	Note=Blocks nucleotide binding. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12045183;Dbxref=PMID:12045183	
+P51996	UniProtKB	Mutagenesis	141	141	.	.	.	Note=Loss of function at 37 degrees Celsius. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151665;Dbxref=PMID:9151665	
+P51996	UniProtKB	Beta strand	11	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Helix	26	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Beta strand	47	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Beta strand	60	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Helix	76	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Beta strand	88	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Helix	98	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Helix	104	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Beta strand	120	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Helix	128	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Helix	138	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Beta strand	151	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Turn	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+P51996	UniProtKB	Helix	163	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO	
+##sequence-region P40517 1 327
+P40517	UniProtKB	Chain	1	327	.	.	.	ID=PRO_0000213671;Note=Ran-specific GTPase-activating protein 2	
+P40517	UniProtKB	Domain	191	327	.	.	.	Note=RanBD1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00164	
+P40517	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40517	UniProtKB	Modified residue	179	179	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40517	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Turn	142	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Helix	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Helix	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Beta strand	212	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Beta strand	232	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Beta strand	252	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Turn	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Beta strand	264	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Beta strand	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Beta strand	281	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Helix	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Beta strand	289	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Beta strand	303	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+P40517	UniProtKB	Helix	311	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF	
+##sequence-region P38374 1 65
+P38374	UniProtKB	Chain	1	65	.	.	.	ID=PRO_0000066513;Note=Protein YSY6	
+P38374	UniProtKB	Topological domain	1	44	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38374	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P50111 1 915
+P50111	UniProtKB	Chain	1	915	.	.	.	ID=PRO_0000066569;Note=Protein ZDS1	
+P50111	UniProtKB	Compositional bias	716	719	.	.	.	Note=Poly-Glu	
+P50111	UniProtKB	Compositional bias	907	914	.	.	.	Note=Poly-Gln	
+P50111	UniProtKB	Modified residue	229	229	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P50111	UniProtKB	Sequence conflict	84	84	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50111	UniProtKB	Sequence conflict	393	393	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50111	UniProtKB	Sequence conflict	413	413	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25620 1 114
+P25620	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000202564;Note=Uncharacterized protein YCR022C	
+##sequence-region P25352 1 136
+P25352	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000202565;Note=Uncharacterized protein YCR025C	
+##sequence-region P25640 1 136
+P25640	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000202573;Note=Putative uncharacterized protein YCR064C	
+##sequence-region Q12264 1 106
+Q12264	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000299845;Note=Putative uncharacterized protein YDL023C	
+##sequence-region Q07355 1 123
+Q07355	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000299851;Note=Putative uncharacterized protein YDL050C	
+Q07355	UniProtKB	Transmembrane	34	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12298 1 539
+Q12298	UniProtKB	Chain	1	539	.	.	.	ID=PRO_0000244440;Note=Uncharacterized ABC transporter ATP-binding protein YDR061W	
+Q12298	UniProtKB	Domain	8	265	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q12298	UniProtKB	Domain	307	537	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q12298	UniProtKB	Nucleotide binding	339	346	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+##sequence-region Q8TGP8 1 144
+Q8TGP8	UniProtKB	Chain	1	144	.	.	.	ID=PRO_0000299855;Note=Putative uncharacterized protein YDL086C-A	
+##sequence-region Q03864 1 110
+Q03864	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000299873;Note=Uncharacterized protein YDR102C	
+##sequence-region Q07535 1 126
+Q07535	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000277621;Note=Putative uncharacterized protein YDL118W	
+##sequence-region Q07555 1 291
+Q07555	UniProtKB	Chain	1	291	.	.	.	ID=PRO_0000240872;Note=Uncharacterized protein YDL129W	
+Q07555	UniProtKB	Modified residue	267	267	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q03900 1 495
+Q03900	UniProtKB	Chain	1	495	.	.	.	ID=PRO_0000253831;Note=Uncharacterized protein YDR132C	
+##sequence-region P0CX65 1 440
+P0CX65	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000203500;Note=Transposon Ty1-DR5 Gag polyprotein	
+P0CX65	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279030;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX65	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279031;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX65	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX65	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX65	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX65	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q3E774 1 43
+Q3E774	UniProtKB	Chain	1	43	.	.	.	ID=PRO_0000240876;Note=Uncharacterized protein YDL159W-A	
+##sequence-region Q12135 1 159
+Q12135	UniProtKB	Chain	1	159	.	.	.	ID=PRO_0000299862;Note=Putative uncharacterized protein YDL172C	
+Q12135	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12135	UniProtKB	Transmembrane	44	64	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12135	UniProtKB	Transmembrane	67	87	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12301 1 547
+Q12301	UniProtKB	Chain	1	547	.	.	.	ID=PRO_0000241453;Note=Uncharacterized membrane protein YDL180W	
+Q12301	UniProtKB	Topological domain	1	19	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Topological domain	41	64	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Topological domain	86	89	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Topological domain	111	139	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Topological domain	161	340	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Transmembrane	341	361	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Topological domain	362	394	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Transmembrane	395	415	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Topological domain	416	523	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Transmembrane	524	544	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Topological domain	545	547	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12301	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q8TGR6 1 39
+Q8TGR6	UniProtKB	Chain	1	39	.	.	.	ID=PRO_0000299751;Note=Putative uncharacterized protein YDR524C-A	
+##sequence-region Q6Q5X2 1 51
+Q6Q5X2	UniProtKB	Chain	1	51	.	.	.	ID=PRO_0000242623;Note=Cysteine-rich and transmembrane domain-containing protein YDR034W-B	
+Q6Q5X2	UniProtKB	Transmembrane	28	44	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6Q5X2	UniProtKB	Compositional bias	30	48	.	.	.	Note=Cys-rich	
+##sequence-region Q04170 1 232
+Q04170	UniProtKB	Chain	1	232	.	.	.	ID=PRO_0000253851;Note=Uncharacterized protein YDR391C	
+##sequence-region P87269 1 146
+P87269	UniProtKB	Chain	1	146	.	.	.	ID=PRO_0000299893;Note=Putative uncharacterized protein YDR433W	
+P87269	UniProtKB	Compositional bias	39	117	.	.	.	Note=Val-rich	
+##sequence-region Q04100 1 135
+Q04100	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04100	UniProtKB	Chain	26	135	.	.	.	ID=PRO_0000299895;Note=Putative uncharacterized protein YDR445C	
+Q04100	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04434 1 166
+Q04434	UniProtKB	Chain	1	166	.	.	.	ID=PRO_0000299904;Note=Putative uncharacterized protein YDR535C	
+##sequence-region Q03051 1 99
+Q03051	UniProtKB	Chain	1	99	.	.	.	ID=PRO_0000211369;Note=Putative UPF0320 protein YDR543C	
+##sequence-region Q04585 1 715
+Q04585	UniProtKB	Chain	1	715	.	.	.	ID=PRO_0000244445;Note=Uncharacterized sugar kinase YDR109C	
+##sequence-region Q3E7X8 1 1277
+Q3E7X8	UniProtKB	Chain	1	1277	.	.	.	ID=PRO_0000268166;Note=Y' element ATP-dependent helicase YEL077C	
+Q3E7X8	UniProtKB	Domain	222	399	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q3E7X8	UniProtKB	Domain	454	605	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q3E7X8	UniProtKB	Nucleotide binding	235	242	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q3E7X8	UniProtKB	Motif	345	348	.	.	.	Note=DEAH box	
+Q3E7X8	UniProtKB	Compositional bias	683	875	.	.	.	Note=Thr-rich	
+##sequence-region P0C5M8 1 29
+P0C5M8	UniProtKB	Chain	1	29	.	.	.	ID=PRO_0000309026;Note=Uncharacterized protein YER090C-A	
+##sequence-region A0A023PZG5 1 101
+A0A023PZG5	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZG5	UniProtKB	Chain	26	101	.	.	.	ID=PRO_0000431000;Note=Putative uncharacterized protein YER137W-A	
+##sequence-region A0A023PXK2 1 192
+A0A023PXK2	UniProtKB	Chain	1	192	.	.	.	ID=PRO_0000431003;Note=Putative uncharacterized membrane protein YER148W-A	
+A0A023PXK2	UniProtKB	Transmembrane	7	29	.	.	.	Note=Helical%3B Signal-anchor;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXK2	UniProtKB	Transmembrane	51	67	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXK2	UniProtKB	Compositional bias	10	192	.	.	.	Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016	
+##sequence-region P39992 1 682
+P39992	UniProtKB	Chain	1	682	.	.	.	ID=PRO_0000202610;Note=Uncharacterized protein YEL023C	
+P39992	UniProtKB	Sequence conflict	281	281	.	.	.	Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32616 1 141
+P32616	UniProtKB	Chain	1	141	.	.	.	ID=PRO_0000202606;Note=Uncharacterized protein YEL045C	
+P32616	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32616	UniProtKB	Transmembrane	67	87	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32616	UniProtKB	Nucleotide binding	15	22	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07804 1 573
+Q07804	UniProtKB	Chain	1	573	.	.	.	ID=PRO_0000248404;Note=Sterol esterase 1	
+Q07804	UniProtKB	Topological domain	1	12	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07804	UniProtKB	Intramembrane	13	33	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07804	UniProtKB	Topological domain	34	573	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07804	UniProtKB	Active site	315	315	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07804	UniProtKB	Active site	489	489	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07804	UniProtKB	Active site	520	520	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P0CX61 1 438
+P0CX61	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000279313;Note=Transposon Ty2-F Gag polyprotein	
+P0CX61	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279314;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX61	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000279315;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX61	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX61	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q45U48 1 73
+Q45U48	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000245382;Note=Uncharacterized protein YGR035W-A	
+##sequence-region Q2V2P6 1 80
+Q2V2P6	UniProtKB	Chain	1	80	.	.	.	ID=PRO_0000245377;Note=Uncharacterized protein YGL194C-A	
+Q2V2P6	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53225 1 103
+P53225	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000202793;Note=Uncharacterized protein YGR039W	
+P53225	UniProtKB	Natural variant	26	26	.	.	.	Note=In strain: SK1. E->G	
+P53225	UniProtKB	Natural variant	39	39	.	.	.	Note=In strain: SK1. S->R	
+P53225	UniProtKB	Natural variant	79	79	.	.	.	Note=In strain: SK1. N->D	
+##sequence-region P0C2J2 1 438
+P0C2J2	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000279321;Note=Transposon Ty2-GR1 Gag polyprotein	
+P0C2J2	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279322;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J2	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000279323;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J2	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J2	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q3E786 1 66
+Q3E786	UniProtKB	Chain	1	66	.	.	.	ID=PRO_0000245389;Note=Uncharacterized protein YGR240C-A	
+##sequence-region P53242 1 292
+P53242	UniProtKB	Chain	1	292	.	.	.	ID=PRO_0000202803;Note=Uncharacterized protein YGR066C	
+P53242	UniProtKB	Natural variant	231	231	.	.	.	Note=In strain: SK1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P53242	UniProtKB	Sequence conflict	229	229	.	.	.	Note=L->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53268 1 129
+P53268	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000202815;Note=Putative uncharacterized protein YGR114C	
+P53268	UniProtKB	Transmembrane	15	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53268	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53268	UniProtKB	Transmembrane	107	127	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q99315 1 1547
+Q99315	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15956549;Dbxref=PMID:15956549	
+Q99315	UniProtKB	Chain	2	1547	.	.	.	ID=PRO_0000279356;Note=Transposon Ty3-G Gag-Pol polyprotein	
+Q99315	UniProtKB	Chain	2	207	.	.	.	ID=PRO_0000279357;Note=Capsid protein	
+Q99315	UniProtKB	Peptide	208	233	.	.	.	ID=PRO_0000279358;Note=Spacer peptide p3	
+Q99315	UniProtKB	Chain	234	309	.	.	.	ID=PRO_0000279359;Note=Nucleocapsid protein p11	
+Q99315	UniProtKB	Chain	310	442	.	.	.	ID=PRO_0000279360;Note=Ty3 protease	
+Q99315	UniProtKB	Peptide	443	535	.	.	.	ID=PRO_0000279361;Note=Spacer peptide J;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99315	UniProtKB	Chain	536	1011	.	.	.	ID=PRO_0000279362;Note=Reverse transcriptase/ribonuclease H	
+Q99315	UniProtKB	Chain	1012	1547	.	.	.	ID=PRO_0000279363;Note=Integrase p61	
+Q99315	UniProtKB	Chain	1038	1547	.	.	.	ID=PRO_0000279364;Note=Integrase p58	
+Q99315	UniProtKB	Domain	620	797	.	.	.	Note=Reverse transcriptase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405	
+Q99315	UniProtKB	Domain	893	1011	.	.	.	Note=RNase H Ty3/gyspy-type	
+Q99315	UniProtKB	Domain	1159	1324	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99315	UniProtKB	Zinc finger	265	282	.	.	.	Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+Q99315	UniProtKB	Region	1106	1145	.	.	.	Note=Integrase-type zinc finger-like	
+Q99315	UniProtKB	Active site	336	336	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99315	UniProtKB	Metal binding	686	686	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99315	UniProtKB	Metal binding	748	748	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99315	UniProtKB	Metal binding	749	749	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99315	UniProtKB	Metal binding	893	893	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99315	UniProtKB	Metal binding	936	936	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99315	UniProtKB	Metal binding	961	961	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99315	UniProtKB	Metal binding	1175	1175	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99315	UniProtKB	Metal binding	1236	1236	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99315	UniProtKB	Site	207	208	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q99315	UniProtKB	Site	233	234	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q99315	UniProtKB	Site	309	310	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q99315	UniProtKB	Site	442	443	.	.	.	Note=Cleavage%3B by Ty3 protease;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99315	UniProtKB	Site	535	536	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q99315	UniProtKB	Site	1011	1012	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q99315	UniProtKB	Site	1037	1038	.	.	.	Note=Cleavage%3B by Ty3 protease%3B partial	
+Q99315	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15956549;Dbxref=PMID:15956549	
+Q99315	UniProtKB	Mutagenesis	267	267	.	.	.	Note=Reduces level of VLP formation and maturation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7515969;Dbxref=PMID:7515969	
+Q99315	UniProtKB	Mutagenesis	275	275	.	.	.	Note=Reduces level of VLP formation and maturation. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7515969;Dbxref=PMID:7515969	
+Q99315	UniProtKB	Turn	552	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	558	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Turn	565	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	608	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	636	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	646	650	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	653	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	669	673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	681	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	690	693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	694	696	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	698	704	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	712	717	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	725	737	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	743	746	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	749	756	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	757	773	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	780	782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	795	797	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	802	804	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	806	809	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Turn	810	814	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	821	832	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Turn	833	837	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	841	844	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	849	853	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	863	871	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Turn	876	878	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	884	891	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	899	906	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	908	911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	913	921	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	932	944	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	948	951	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	957	959	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	965	969	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	970	972	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	976	986	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Beta strand	997	1000	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+Q99315	UniProtKB	Helix	1001	1008	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8	
+##sequence-region P53278 1 816
+P53278	UniProtKB	Chain	1	816	.	.	.	ID=PRO_0000202822;Note=Uncharacterized protein YGR130C	
+P53278	UniProtKB	Compositional bias	164	185	.	.	.	Note=Poly-Ser	
+P53278	UniProtKB	Compositional bias	205	218	.	.	.	Note=Poly-Thr	
+P53278	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53278	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53278	UniProtKB	Modified residue	347	347	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53278	UniProtKB	Modified residue	809	809	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P0C5N3 1 154
+P0C5N3	UniProtKB	Transit peptide	1	42	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C5N3	UniProtKB	Chain	43	154	.	.	.	ID=PRO_0000309031;Note=Uncharacterized protein YGL041W-A%2C mitochondrial	
+##sequence-region P42936 1 225
+P42936	UniProtKB	Chain	1	225	.	.	.	ID=PRO_0000186046;Note=Putative elongation factor 1 gamma homolog	
+P42936	UniProtKB	Domain	94	225	.	.	.	Note=GST C-terminal	
+##sequence-region P53310 1 102
+P53310	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000202857;Note=Putative uncharacterized protein YGR242W	
+P53310	UniProtKB	Transmembrane	29	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40326 1 108
+P40326	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000202866;Note=Uncharacterized protein YGR269W	
+P40326	UniProtKB	Sequence conflict	53	53	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53156 1 320
+P53156	UniProtKB	Chain	1	320	.	.	.	ID=PRO_0000202758;Note=Uncharacterized protein YGL081W	
+P53156	UniProtKB	Domain	22	86	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+P53156	UniProtKB	Compositional bias	235	269	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P53156	UniProtKB	Compositional bias	248	258	.	.	.	Note=Poly-Glu	
+##sequence-region P53143 1 142
+P53143	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000202753;Note=Putative uncharacterized protein YGL102C	
+##sequence-region P53071 1 178
+P53071	UniProtKB	Chain	1	178	.	.	.	ID=PRO_0000202710;Note=Uncharacterized protein YGL235W	
+##sequence-region A0A023PXE5 1 117
+A0A023PXE5	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000431015;Note=Putative uncharacterized protein YHL006W-A	
+##sequence-region O13535 1 1793
+O13535	UniProtKB	Chain	1	1793	.	.	.	ID=PRO_0000279074;Note=Transposon Ty1-H Gag-Pol polyprotein	
+O13535	UniProtKB	Chain	1	439	.	.	.	ID=PRO_0000279075;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O13535	UniProtKB	Chain	440	620	.	.	.	ID=PRO_0000279076;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O13535	UniProtKB	Chain	621	1255	.	.	.	ID=PRO_0000279077;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O13535	UniProtKB	Chain	1256	1793	.	.	.	ID=PRO_0000279078;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O13535	UniProtKB	Domain	698	873	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13535	UniProtKB	Domain	1376	1514	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+O13535	UniProtKB	Domain	1648	1790	.	.	.	Note=RNase H Ty1/copia-type	
+O13535	UniProtKB	Region	337	439	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O13535	UniProtKB	Region	621	678	.	.	.	Note=Integrase-type zinc finger-like	
+O13535	UniProtKB	Motif	1216	1250	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O13535	UniProtKB	Compositional bias	72	146	.	.	.	Note=Pro-rich	
+O13535	UniProtKB	Active site	499	499	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+O13535	UniProtKB	Metal binding	709	709	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13535	UniProtKB	Metal binding	774	774	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13535	UniProtKB	Metal binding	1384	1384	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13535	UniProtKB	Metal binding	1465	1465	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13535	UniProtKB	Metal binding	1466	1466	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13535	UniProtKB	Metal binding	1648	1648	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13535	UniProtKB	Metal binding	1690	1690	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13535	UniProtKB	Metal binding	1723	1723	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13535	UniProtKB	Site	439	440	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O13535	UniProtKB	Site	620	621	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O13535	UniProtKB	Site	1255	1256	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q05451 1 56
+Q05451	UniProtKB	Chain	1	56	.	.	.	ID=PRO_0000202894;Note=Putative uncharacterized protein YHR050W-A	
+##sequence-region P38809 1 366
+P38809	UniProtKB	Chain	1	366	.	.	.	ID=PRO_0000202907;Note=Uncharacterized protein YHR097C	
+P38809	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38809	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38809	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38809	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38809	UniProtKB	Modified residue	294	294	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38809	UniProtKB	Modified residue	359	359	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38809	UniProtKB	Cross-link	78	78	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P38809	UniProtKB	Cross-link	187	187	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P38809	UniProtKB	Cross-link	242	242	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region P38834 1 111
+P38834	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000202916;Note=Uncharacterized protein YHR130C	
+P38834	UniProtKB	Transmembrane	18	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38841 1 114
+P38841	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38841	UniProtKB	Chain	20	114	.	.	.	ID=PRO_0000026706;Note=Uncharacterized protein YHR138C	
+P38841	UniProtKB	Modified residue	41	41	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P0CI67 1 198
+P0CI67	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000402771;Note=Uncharacterized protein YHR213W	
+P0CI67	UniProtKB	Domain	1	110	.	.	.	Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164	
+P0CI67	UniProtKB	Compositional bias	133	198	.	.	.	Note=Ser/Thr-rich	
+##sequence-region Q3E7Z3 1 45
+Q3E7Z3	UniProtKB	Chain	1	45	.	.	.	ID=PRO_0000245406;Note=Uncharacterized protein YIR018C-A	
+##sequence-region Q3E739 1 70
+Q3E739	UniProtKB	Chain	1	70	.	.	.	ID=PRO_0000245407;Note=Uncharacterized protein YIR021W-A	
+Q3E739	UniProtKB	Transmembrane	15	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03884 1 112
+Q03884	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000299757;Note=Putative uncharacterized protein YIL100C-A	
+Q03884	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03884	UniProtKB	Transmembrane	58	78	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03884	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CL42 1 160
+P0CL42	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000406015;Note=Putative UPF0479 protein YJL225W-A	
+P0CL42	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL42	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL42	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region P0CL25 1 75
+P0CL25	UniProtKB	Chain	1	75	.	.	.	ID=PRO_0000202950;Note=Putative UPF0377 protein YIL174W	
+##sequence-region P40566 1 764
+P40566	UniProtKB	Chain	1	764	.	.	.	ID=PRO_0000184056;Note=Uncharacterized glycosyl hydrolase YIR007W	
+P40566	UniProtKB	Active site	265	265	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40566	UniProtKB	Modified residue	594	594	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40572 1 265
+P40572	UniProtKB	Chain	1	265	.	.	.	ID=PRO_0000203005;Note=Uncharacterized protein YIR016W	
+P40572	UniProtKB	Nucleotide binding	137	144	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40586 1 236
+P40586	UniProtKB	Chain	1	236	.	.	.	ID=PRO_0000203009;Note=Uncharacterized protein YIR042C	
+P40586	UniProtKB	Domain	47	191	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+##sequence-region P47100 1 1755
+P47100	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000199564;Note=Transposon Ty1-JR2 Gag-Pol polyprotein	
+P47100	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279088;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47100	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279089;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47100	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279090;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47100	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279091;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47100	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47100	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P47100	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+P47100	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47100	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+P47100	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47100	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P47100	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47100	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47100	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47100	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47100	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47100	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47100	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47100	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47100	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47100	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47100	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47100	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region P0CL41 1 160
+P0CL41	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000299787;Note=Putative UPF0479 protein YIL177W-A	
+P0CL41	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL41	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL41	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region P47139 1 656
+P47139	UniProtKB	Chain	1	656	.	.	.	ID=PRO_0000203108;Note=Uncharacterized protein YJR098C	
+P47139	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47139	UniProtKB	Sequence conflict	410	415	.	.	.	Note=TIFTKE->LFSLR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47145 1 328
+P47145	UniProtKB	Chain	1	328	.	.	.	ID=PRO_0000090374;Note=Putative lipase YJR107W	
+P47145	UniProtKB	Active site	181	181	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59952	
+P47145	UniProtKB	Active site	253	253	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59952	
+P47145	UniProtKB	Active site	315	315	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59952	
+P47145	UniProtKB	Sequence conflict	14	14	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47145	UniProtKB	Sequence conflict	66	66	.	.	.	Note=G->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47148 1 283
+P47148	UniProtKB	Chain	1	283	.	.	.	ID=PRO_0000203112;Note=Uncharacterized protein YJR111C	
+##sequence-region P47172 1 347
+P47172	UniProtKB	Chain	1	347	.	.	.	ID=PRO_0000203125;Note=Uncharacterized protein YJR141W	
+##sequence-region P47184 1 120
+P47184	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000203129;Note=Putative uncharacterized protein YJR157W	
+##sequence-region P47022 1 219
+P47022	UniProtKB	Chain	1	219	.	.	.	ID=PRO_0000203044;Note=Uncharacterized protein YJL118W	
+P47022	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47022	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47022	UniProtKB	Compositional bias	149	155	.	.	.	Note=Poly-Arg	
+P47022	UniProtKB	Compositional bias	191	196	.	.	.	Note=Poly-Gln	
+##sequence-region P47020 1 107
+P47020	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000203042;Note=Putative uncharacterized protein YJL120W	
+P47020	UniProtKB	Transmembrane	15	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47020	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47020	UniProtKB	Transmembrane	87	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47014 1 750
+P47014	UniProtKB	Chain	1	750	.	.	.	ID=PRO_0000203038;Note=Uncharacterized protein YJL132W	
+P47014	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47014	UniProtKB	Transmembrane	465	485	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47014	UniProtKB	Transmembrane	586	606	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47085 1 338
+P47085	UniProtKB	Chain	1	338	.	.	.	ID=PRO_0000134398;Note=MEMO1 family protein YJR008W	
+##sequence-region P47090 1 510
+P47090	UniProtKB	Chain	1	510	.	.	.	ID=PRO_0000203085;Note=Uncharacterized endoplasmic reticulum membrane protein YJR015W	
+P47090	UniProtKB	Topological domain	1	89	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Topological domain	111	123	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Transmembrane	124	144	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Topological domain	145	312	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Transmembrane	313	333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Topological domain	334	349	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Transmembrane	350	370	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Topological domain	371	381	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Transmembrane	382	402	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Topological domain	403	416	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Transmembrane	417	437	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Topological domain	438	474	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Transmembrane	475	495	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Topological domain	496	510	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47090	UniProtKB	Sequence conflict	324	324	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q3E826 1 78
+Q3E826	UniProtKB	Chain	1	78	.	.	.	ID=PRO_0000245421;Note=Uncharacterized protein YKL068W-A	
+##sequence-region P36140 1 101
+P36140	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000203214;Note=Putative uncharacterized protein YKR047W	
+##sequence-region P36153 1 106
+P36153	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000203220;Note=Uncharacterized protein YKR073C	
+##sequence-region P36099 1 201
+P36099	UniProtKB	Chain	1	201	.	.	.	ID=PRO_0000203188;Note=Putative uncharacterized protein YKL030W	
+##sequence-region P36087 1 169
+P36087	UniProtKB	Chain	1	169	.	.	.	ID=PRO_0000203172;Note=Uncharacterized protein YKL070W	
+##sequence-region P36079 1 204
+P36079	UniProtKB	Chain	1	204	.	.	.	ID=PRO_0000203166;Note=Putative uncharacterized protein YKL083W	
+##sequence-region P36030 1 115
+P36030	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000211374;Note=Putative UPF0320 protein YKL225W	
+##sequence-region P36109 1 125
+P36109	UniProtKB	Chain	1	125	.	.	.	ID=PRO_0000203195;Note=Putative uncharacterized protein YKR012C	
+##sequence-region Q07895 1 862
+Q07895	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Chain	24	862	.	.	.	ID=PRO_0000247181;Note=FAS1 domain-containing protein YLR001C	
+Q07895	UniProtKB	Topological domain	24	762	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Transmembrane	763	783	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Topological domain	784	862	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Domain	34	162	.	.	.	Note=FAS1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00082	
+Q07895	UniProtKB	Domain	463	604	.	.	.	Note=FAS1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00082	
+Q07895	UniProtKB	Domain	606	744	.	.	.	Note=FAS1 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00082	
+Q07895	UniProtKB	Glycosylation	68	68	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	112	112	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	152	152	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	200	200	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	291	291	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	333	333	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	450	450	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	521	521	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	542	542	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	569	569	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	663	663	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	679	679	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07895	UniProtKB	Glycosylation	688	688	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07927 1 99
+Q07927	UniProtKB	Chain	1	99	.	.	.	ID=PRO_0000247155;Note=Uncharacterized protein YLR012C	
+##sequence-region P0CF33 1 103
+P0CF33	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000393435;Note=Putative truncated guanine nucleotide exchange factor YLL017W	
+P0CF33	UniProtKB	Domain	26	97	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+##sequence-region Q07967 1 263
+Q07967	UniProtKB	Chain	1	263	.	.	.	ID=PRO_0000247203;Note=Putative uncharacterized protein YLR030W	
+##sequence-region Q07834 1 825
+Q07834	UniProtKB	Chain	1	825	.	.	.	ID=PRO_0000247115;Note=KH domain-containing protein YLL032C	
+Q07834	UniProtKB	Domain	482	556	.	.	.	Note=KH	
+Q07834	UniProtKB	Compositional bias	783	806	.	.	.	Note=Tyr-rich	
+Q07834	UniProtKB	Modified residue	762	762	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+##sequence-region Q12110 1 428
+Q12110	UniProtKB	Chain	1	428	.	.	.	ID=PRO_0000247204;Note=Uncharacterized protein YLR049C	
+Q12110	UniProtKB	Compositional bias	89	97	.	.	.	Note=Poly-Ser	
+Q12110	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+##sequence-region Q12244 1 843
+Q12244	UniProtKB	Chain	1	843	.	.	.	ID=PRO_0000247135;Note=Uncharacterized transcriptional regulatory protein YLL054C	
+Q12244	UniProtKB	DNA binding	15	42	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region Q99208 1 1374
+Q99208	UniProtKB	Chain	1	1374	.	.	.	ID=PRO_0000268167;Note=Y' element ATP-dependent helicase YLL066C	
+Q99208	UniProtKB	Domain	375	552	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q99208	UniProtKB	Domain	609	758	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q99208	UniProtKB	Nucleotide binding	388	395	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q99208	UniProtKB	Motif	498	501	.	.	.	Note=DEAH box	
+Q99208	UniProtKB	Compositional bias	836	972	.	.	.	Note=Thr-rich	
+##sequence-region P0CX68 1 440
+P0CX68	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000409785;Note=Transposon Ty1-LR1 Gag polyprotein	
+P0CX68	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000409786;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX68	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000409787;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX68	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX68	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX68	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX68	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q12138 1 136
+Q12138	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000247351;Note=Putative uncharacterized protein YLR125W	
+##sequence-region P0CE96 1 114
+P0CE96	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000203233;Note=Putative uncharacterized protein YLR156W	
+##sequence-region O13531 1 108
+O13531	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000299622;Note=Putative uncharacterized protein YLR202C	
+##sequence-region Q05948 1 407
+Q05948	UniProtKB	Chain	1	407	.	.	.	ID=PRO_0000247175;Note=Uncharacterized SVF1-like protein YLR225C	
+Q05948	UniProtKB	Cross-link	22	22	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region A0A023PXG7 1 101
+A0A023PXG7	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000431044;Note=Putative uncharacterized membrane protein YLR230W	
+A0A023PXG7	UniProtKB	Transmembrane	68	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXP4 1 132
+A0A023PXP4	UniProtKB	Chain	1	132	.	.	.	ID=PRO_0000431045;Note=Putative uncharacterized protein YLR235C	
+##sequence-region O13574 1 117
+O13574	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000299626;Note=Uncharacterized protein YLR255C	
+##sequence-region Q06146 1 321
+Q06146	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q06146	UniProtKB	Chain	2	321	.	.	.	ID=PRO_0000247208;Note=Uncharacterized protein YLR257W	
+Q06146	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylvaline;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q06146	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q06146	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06146	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06146	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q06146	UniProtKB	Modified residue	126	126	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06146	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q06146	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06146	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06146	UniProtKB	Modified residue	159	159	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06146	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q06146	UniProtKB	Modified residue	240	240	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q06146	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q06146	UniProtKB	Modified residue	270	270	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q06152 1 274
+Q06152	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000247779;Note=Uncharacterized protein YLR271W	
+Q06152	UniProtKB	Domain	41	87	.	.	.	Note=G-patch;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00092	
+##sequence-region O13540 1 129
+O13540	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000299628;Note=Putative uncharacterized protein YLR279W	
+O13540	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E810 1 57
+Q3E810	UniProtKB	Chain	1	57	.	.	.	ID=PRO_0000247211;Note=Uncharacterized protein YLR342W-A	
+Q3E810	UniProtKB	Transmembrane	4	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06137 1 509
+Q06137	UniProtKB	Chain	1	509	.	.	.	ID=PRO_0000268185;Note=Putative 6-phosphofructo-2-kinase/fructose-2%2C6-bisphosphatase YLR345W	
+Q06137	UniProtKB	Nucleotide binding	90	98	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+Q06137	UniProtKB	Nucleotide binding	212	217	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+Q06137	UniProtKB	Nucleotide binding	415	418	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953	
+Q06137	UniProtKB	Nucleotide binding	460	464	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953	
+Q06137	UniProtKB	Region	6	291	.	.	.	Note=6-phosphofructo-2-kinase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06137	UniProtKB	Region	292	466	.	.	.	Note=Fructose-2%2C6-bisphosphatase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06137	UniProtKB	Active site	173	173	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+Q06137	UniProtKB	Binding site	237	237	.	.	.	Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+Q06137	UniProtKB	Binding site	298	298	.	.	.	Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+Q06137	UniProtKB	Binding site	433	433	.	.	.	Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+Q06137	UniProtKB	Binding site	464	464	.	.	.	Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953	
+Q06137	UniProtKB	Site	298	298	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+Q06137	UniProtKB	Site	459	459	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+Q06137	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q7LIF2 1 110
+Q7LIF2	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000299642;Note=Uncharacterized protein YLR365W	
+##sequence-region O13545 1 129
+O13545	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000299644;Note=Putative uncharacterized protein YLR374C	
+O13545	UniProtKB	Transmembrane	33	50	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGT1 1 49
+Q8TGT1	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q8TGT1	UniProtKB	Chain	23	49	.	.	.	ID=PRO_0000247217;Note=Uncharacterized protein YLR406C-A	
+##sequence-region Q06204 1 433
+Q06204	UniProtKB	Chain	1	433	.	.	.	ID=PRO_0000268190;Note=Putative hexokinase YLR446W	
+Q06204	UniProtKB	Domain	1	424	.	.	.	Note=Hexokinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+Q06204	UniProtKB	Region	51	194	.	.	.	Note=Hexokinase small subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+Q06204	UniProtKB	Region	132	154	.	.	.	Note=Glucose-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06204	UniProtKB	Region	195	413	.	.	.	Note=Hexokinase large subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+Q06204	UniProtKB	Sequence conflict	52	52	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region O13557 1 183
+O13557	UniProtKB	Chain	1	183	.	.	.	ID=PRO_0000299653;Note=Putative uncharacterized protein YLR463C	
+##sequence-region P0CY00 1 160
+P0CY00	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000410456;Note=UPF0479 membrane protein YLL066W-A	
+P0CY00	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CY00	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CY00	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region P0CL39 1 160
+P0CL39	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000406013;Note=Putative UPF0479 protein YLR467C-A	
+P0CL39	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL39	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL39	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region Q8TGS9 1 76
+Q8TGS9	UniProtKB	Chain	1	76	.	.	.	ID=PRO_0000247784;Note=Uncharacterized protein YMR001C-A	
+##sequence-region Q6B0Y1 1 158
+Q6B0Y1	UniProtKB	Chain	1	158	.	.	.	ID=PRO_0000299665;Note=Putative uncharacterized protein YML009W-B	
+Q6B0Y1	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXP7 1 132
+A0A023PXP7	UniProtKB	Chain	1	132	.	.	.	ID=PRO_0000431060;Note=Putative uncharacterized protein YML034C-A	
+##sequence-region Q6B0Y7 1 121
+Q6B0Y7	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000299668;Note=Putative uncharacterized protein YMR075C-A	
+Q6B0Y7	UniProtKB	Compositional bias	70	75	.	.	.	Note=Poly-Leu	
+Q6B0Y7	UniProtKB	Compositional bias	79	88	.	.	.	Note=Poly-Leu	
+##sequence-region Q8TGT0 1 57
+Q8TGT0	UniProtKB	Chain	1	57	.	.	.	ID=PRO_0000247781;Note=Uncharacterized protein YML100W-A	
+##sequence-region Q04214 1 1755
+Q04214	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000199567;Note=Transposon Ty1-MR1 Gag-Pol polyprotein	
+Q04214	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279127;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04214	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279128;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04214	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279129;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04214	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279130;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04214	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04214	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q04214	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q04214	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04214	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q04214	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04214	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q04214	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04214	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04214	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04214	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04214	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04214	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04214	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04214	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04214	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04214	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04214	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q6B0R2 1 128
+Q6B0R2	UniProtKB	Chain	1	128	.	.	.	ID=PRO_0000299672;Note=Putative uncharacterized protein YMR193C-A	
+Q6B0R2	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6B0R2	UniProtKB	Transmembrane	95	115	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04304 1 227
+Q04304	UniProtKB	Chain	1	227	.	.	.	ID=PRO_0000203286;Note=UPF0659 protein YMR090W	
+##sequence-region Q3E841 1 98
+Q3E841	UniProtKB	Chain	1	98	.	.	.	ID=PRO_0000247803;Note=Uncharacterized protein YNR034W-A	
+Q3E841	UniProtKB	Helix	7	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG	
+Q3E841	UniProtKB	Beta strand	15	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG	
+Q3E841	UniProtKB	Beta strand	26	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG	
+Q3E841	UniProtKB	Helix	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG	
+Q3E841	UniProtKB	Helix	41	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG	
+Q3E841	UniProtKB	Beta strand	53	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG	
+Q3E841	UniProtKB	Beta strand	66	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG	
+Q3E841	UniProtKB	Beta strand	75	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG	
+##sequence-region P53837 1 131
+P53837	UniProtKB	Chain	1	131	.	.	.	ID=PRO_0000203379;Note=Putative uncharacterized protein YNL276C	
+##sequence-region P53729 1 429
+P53729	UniProtKB	Chain	1	429	.	.	.	ID=PRO_0000203476;Note=Uncharacterized protein YNR029C	
+P53729	UniProtKB	Domain	362	428	.	.	.	Note=CobW C-terminal	
+P53729	UniProtKB	Nucleotide binding	78	85	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53729	UniProtKB	Nucleotide binding	139	143	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53729	UniProtKB	Nucleotide binding	244	247	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53751 1 1116
+P53751	UniProtKB	Chain	1	1116	.	.	.	ID=PRO_0000203483;Note=Uncharacterized membrane glycoprotein YNR065C	
+P53751	UniProtKB	Transmembrane	934	957	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53751	UniProtKB	Repeat	21	32	.	.	.	Note=BNR 1	
+P53751	UniProtKB	Repeat	67	78	.	.	.	Note=BNR 2	
+P53751	UniProtKB	Repeat	307	318	.	.	.	Note=BNR 3	
+P53751	UniProtKB	Repeat	404	415	.	.	.	Note=BNR 4	
+P53751	UniProtKB	Repeat	607	618	.	.	.	Note=BNR 5	
+P53751	UniProtKB	Repeat	686	697	.	.	.	Note=BNR 6	
+P53751	UniProtKB	Repeat	727	738	.	.	.	Note=BNR 7	
+P53751	UniProtKB	Glycosylation	35	35	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53751	UniProtKB	Glycosylation	336	336	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53751	UniProtKB	Glycosylation	553	553	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53751	UniProtKB	Glycosylation	846	846	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53751	UniProtKB	Glycosylation	985	985	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53754 1 272
+P53754	UniProtKB	Chain	1	272	.	.	.	ID=PRO_0000203485;Note=Uncharacterized protein YNR068C	
+##sequence-region P53757 1 342
+P53757	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000197449;Note=Uncharacterized isomerase YNR071C	
+P53757	UniProtKB	Active site	176	176	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10126	
+P53757	UniProtKB	Binding site	69	69	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53757	UniProtKB	Binding site	240	240	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53757	UniProtKB	Beta strand	13	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Turn	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	21	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	31	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Helix	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Helix	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	80	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Helix	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	111	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	117	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	128	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	136	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Turn	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	154	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Turn	181	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	193	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	201	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Turn	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	212	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	240	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Turn	246	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Turn	257	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	263	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Turn	271	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	276	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	304	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Helix	314	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Helix	318	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Helix	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+P53757	UniProtKB	Beta strand	332	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA	
+##sequence-region P53977 1 112
+P53977	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000203463;Note=Putative uncharacterized protein YNL017C	
+##sequence-region P53962 1 389
+P53962	UniProtKB	Chain	1	389	.	.	.	ID=PRO_0000051485;Note=Uncharacterized WD repeat-containing protein YNL035C	
+P53962	UniProtKB	Repeat	11	53	.	.	.	Note=WD 1	
+P53962	UniProtKB	Repeat	146	186	.	.	.	Note=WD 2	
+P53962	UniProtKB	Repeat	289	330	.	.	.	Note=WD 3	
+P53962	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P0CL30 1 191
+P0CL30	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL30	UniProtKB	Chain	18	191	.	.	.	ID=PRO_0000406007;Note=Putative uncharacterized protein YNL339W-A	
+P0CL30	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL30	UniProtKB	Compositional bias	13	159	.	.	.	Note=Gly/Ser-rich	
+##sequence-region P53921 1 115
+P53921	UniProtKB	Natural variant	11	11	.	.	.	Note=In strain: V1-09 and YJM339. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53921	UniProtKB	Natural variant	31	31	.	.	.	Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+##sequence-region Q08207 1 100
+Q08207	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299688;Note=Putative uncharacterized protein YOL035C	
+Q08207	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08207	UniProtKB	Transmembrane	41	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08207	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08439 1 144
+Q08439	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08439	UniProtKB	Chain	23	144	.	.	.	ID=PRO_0000299708;Note=Putative uncharacterized protein YOR055W	
+##sequence-region Q08240 1 163
+Q08240	UniProtKB	Chain	1	163	.	.	.	ID=PRO_0000262743;Note=Putative uncharacterized membrane protein YOL099C	
+Q08240	UniProtKB	Topological domain	1	33	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q08240	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08240	UniProtKB	Topological domain	55	117	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q08240	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08240	UniProtKB	Topological domain	139	163	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+##sequence-region Q12322 1 202
+Q12322	UniProtKB	Chain	1	202	.	.	.	ID=PRO_0000203489;Note=Putative uncharacterized protein YOL114C	
+##sequence-region P0CX59 1 440
+P0CX59	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279166;Note=Transposon Ty1-OR Gag polyprotein	
+P0CX59	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279167;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX59	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279168;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX59	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX59	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX59	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX59	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q08272 1 129
+Q08272	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08272	UniProtKB	Chain	25	129	.	.	.	ID=PRO_0000299696;Note=Putative uncharacterized protein YOL134C	
+Q08272	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08272	UniProtKB	Transmembrane	95	115	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08272	UniProtKB	Compositional bias	61	66	.	.	.	Note=Poly-Ser	
+##sequence-region Q03080 1 316
+Q03080	UniProtKB	Chain	1	316	.	.	.	ID=PRO_0000238637;Note=Uncharacterized protein YPL039W	
+##sequence-region P0C5E1 1 128
+P0C5E1	UniProtKB	Chain	1	128	.	.	.	ID=PRO_0000302032;Note=Putative uncharacterized protein YPR059C	
+##sequence-region Q02749 1 293
+Q02749	UniProtKB	Chain	1	293	.	.	.	ID=PRO_0000238642;Note=Uncharacterized protein YPL068C	
+##sequence-region Q06813 1 372
+Q06813	UniProtKB	Chain	1	372	.	.	.	ID=PRO_0000255980;Note=Uncharacterized protein YPR078C	
+##sequence-region Q06839 1 1073
+Q06839	UniProtKB	Chain	1	1073	.	.	.	ID=PRO_0000257826;Note=PX domain-containing protein YPR097W	
+Q06839	UniProtKB	Domain	273	506	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
+Q06839	UniProtKB	Modified residue	310	310	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06839	UniProtKB	Modified residue	451	451	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06839	UniProtKB	Sequence conflict	848	848	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0C2I9 1 1755
+P0C2I9	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279174;Note=Transposon Ty1-PR1 Gag-Pol polyprotein	
+P0C2I9	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279175;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I9	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279176;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I9	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279177;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I9	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279178;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I9	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I9	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0C2I9	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+P0C2I9	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I9	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+P0C2I9	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I9	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P0C2I9	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I9	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I9	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I9	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I9	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I9	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I9	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I9	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I9	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I9	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I9	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I9	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region P0C2J1 1 1755
+P0C2J1	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279184;Note=Transposon Ty1-PR3 Gag-Pol polyprotein	
+P0C2J1	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279185;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J1	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279186;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J1	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279187;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J1	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279188;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J1	UniProtKB	Domain	660	829	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J1	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0C2J1	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+P0C2J1	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J1	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+P0C2J1	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J1	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0C2J1	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P0C2J1	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J1	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J1	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J1	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J1	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J1	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J1	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J1	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J1	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J1	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J1	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J1	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region Q08922 1 127
+Q08922	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000299806;Note=Putative uncharacterized protein YPL182C	
+Q08922	UniProtKB	Transmembrane	47	67	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08922	UniProtKB	Transmembrane	84	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08922	UniProtKB	Compositional bias	6	42	.	.	.	Note=Ser-rich	
+##sequence-region Q08954 1 240
+Q08954	UniProtKB	Chain	1	240	.	.	.	ID=PRO_0000238659;Note=Smr domain-containing protein YPL199C	
+Q08954	UniProtKB	Domain	97	173	.	.	.	Note=Smr;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00321	
+##sequence-region Q99401 1 129
+Q99401	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000299811;Note=Putative uncharacterized protein YPL238C	
+Q99401	UniProtKB	Transmembrane	22	42	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99401	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99401	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99401	UniProtKB	Compositional bias	35	42	.	.	.	Note=Poly-Phe	
+Q99401	UniProtKB	Compositional bias	70	75	.	.	.	Note=Poly-Phe	
+Q99401	UniProtKB	Compositional bias	104	108	.	.	.	Note=Poly-Phe	
+##sequence-region Q12523 1 523
+Q12523	UniProtKB	Chain	1	523	.	.	.	ID=PRO_0000242490;Note=WD repeat-containing protein YPL247C	
+Q12523	UniProtKB	Repeat	173	213	.	.	.	Note=WD 1	
+Q12523	UniProtKB	Repeat	241	281	.	.	.	Note=WD 2	
+Q12523	UniProtKB	Repeat	285	325	.	.	.	Note=WD 3	
+Q12523	UniProtKB	Repeat	392	432	.	.	.	Note=WD 4	
+Q12523	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12523	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q08980 1 353
+Q08980	UniProtKB	Chain	1	353	.	.	.	ID=PRO_0000252279;Note=Probable transport protein YPL264C	
+Q08980	UniProtKB	Topological domain	1	16	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Topological domain	38	51	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Transmembrane	52	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Topological domain	70	94	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Transmembrane	95	115	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Topological domain	116	116	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Topological domain	138	144	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Topological domain	166	188	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Topological domain	210	218	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Transmembrane	219	239	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Topological domain	240	254	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Topological domain	276	282	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Transmembrane	283	303	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Topological domain	304	304	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Transmembrane	305	325	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Topological domain	326	353	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08980	UniProtKB	Domain	24	160	.	.	.	Note=EamA 1	
+Q08980	UniProtKB	Domain	200	326	.	.	.	Note=EamA 2	
+##sequence-region Q08990 1 100
+Q08990	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000269761;Note=Putative uncharacterized protein YPL278C	
+##sequence-region A0A023PXI5 1 187
+A0A023PXI5	UniProtKB	Chain	1	187	.	.	.	ID=PRO_0000431064;Note=Putative uncharacterized protein YPR197C	
+##sequence-region P43587 1 155
+P43587	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P43587	UniProtKB	Chain	2	155	.	.	.	ID=PRO_0000202681;Note=Type 1 phosphatases regulator YPI1	
+P43587	UniProtKB	Motif	51	53	.	.	.	Note=GLC7-binding	
+P43587	UniProtKB	Compositional bias	93	103	.	.	.	Note=Poly-Ser	
+P43587	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P43587	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P43587	UniProtKB	Modified residue	133	133	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P43587	UniProtKB	Mutagenesis	51	51	.	.	.	Note=Prevents interaction with GLC7. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18172024;Dbxref=PMID:18172024	
+P43587	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Prevents interaction with GLC7 and reduces nuclear levels of GLC7 and SDS22. W->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14506263,ECO:0000269|PubMed:18172024;Dbxref=PMID:14506263,PMID:18172024	
+##sequence-region P46951 1 817
+P46951	UniProtKB	Chain	1	817	.	.	.	ID=PRO_0000202843;Note=Cargo-transport protein YPP1	
+P46951	UniProtKB	Helix	17	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	39	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	63	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Turn	85	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	90	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	114	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	137	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	161	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	185	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	203	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	217	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	239	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	264	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	291	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	306	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	326	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	361	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Turn	382	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	387	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	418	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	429	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	446	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	450	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	457	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	485	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	507	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Turn	517	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	526	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Beta strand	538	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	543	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	569	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	590	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	598	607	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	614	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Beta strand	619	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	626	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Beta strand	644	646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	649	659	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Beta strand	663	665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	668	679	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	686	697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	702	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	747	767	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	769	772	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	775	784	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	791	804	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+P46951	UniProtKB	Helix	812	815	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C	
+##sequence-region P36019 1 220
+P36019	UniProtKB	Chain	1	220	.	.	.	ID=PRO_0000121327;Note=GTP-binding protein YPT53	
+P36019	UniProtKB	Nucleotide binding	19	26	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36019	UniProtKB	Nucleotide binding	67	71	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36019	UniProtKB	Nucleotide binding	125	128	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36019	UniProtKB	Modified residue	220	220	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36019	UniProtKB	Lipidation	218	218	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36019	UniProtKB	Lipidation	220	220	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P0CX57 1 440
+P0CX57	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000278982;Note=Transposon Ty1-A Gag polyprotein	
+P0CX57	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000278983;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX57	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000278984;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX57	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX57	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX57	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region P39557 1 106
+P39557	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000202428;Note=Putative uncharacterized membrane protein YAR047C	
+P39557	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39557	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39557	UniProtKB	Topological domain	28	32	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39557	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39557	UniProtKB	Topological domain	54	73	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39557	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39557	UniProtKB	Topological domain	95	106	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38749 1 330
+P38749	UniProtKB	Chain	1	330	.	.	.	ID=PRO_0000076523;Note=AP-1-like transcription factor YAP3	
+P38749	UniProtKB	Domain	144	207	.	.	.	Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P38749	UniProtKB	Region	147	168	.	.	.	Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P38749	UniProtKB	Region	172	207	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P38749	UniProtKB	Compositional bias	107	112	.	.	.	Note=Poly-Asn	
+P38749	UniProtKB	Modified residue	135	135	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q03935 1 383
+Q03935	UniProtKB	Chain	1	383	.	.	.	ID=PRO_0000076526;Note=AP-1-like transcription factor YAP6	
+Q03935	UniProtKB	Domain	221	284	.	.	.	Note=bZIP	
+Q03935	UniProtKB	Region	223	247	.	.	.	Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03935	UniProtKB	Region	249	277	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03935	UniProtKB	Compositional bias	263	333	.	.	.	Note=Asn-rich	
+##sequence-region Q8TGQ6 1 49
+Q8TGQ6	UniProtKB	Chain	1	49	.	.	.	ID=PRO_0000299792;Note=Putative uncharacterized protein YBL006W-A	
+##sequence-region O43137 1 85
+O43137	UniProtKB	Chain	1	85	.	.	.	ID=PRO_0000248436;Note=Uncharacterized protein YBR085C-A	
+O43137	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P89495 1 111
+P89495	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000299790;Note=Putative uncharacterized protein YBL109W	
+P89495	UniProtKB	Compositional bias	63	99	.	.	.	Note=His-rich	
+##sequence-region Q12217 1 440
+Q12217	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000278998;Note=Transposon Ty1-BR Gag polyprotein	
+Q12217	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000278999;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12217	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279000;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12217	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12217	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q12217	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12217	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q12193 1 1756
+Q12193	UniProtKB	Chain	1	1756	.	.	.	ID=PRO_0000278993;Note=Transposon Ty1-BR Gag-Pol polyprotein	
+Q12193	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000278994;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12193	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000278995;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12193	UniProtKB	Chain	583	1218	.	.	.	ID=PRO_0000278996;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12193	UniProtKB	Chain	1219	1756	.	.	.	ID=PRO_0000278997;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12193	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12193	UniProtKB	Domain	1339	1477	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12193	UniProtKB	Domain	1611	1753	.	.	.	Note=RNase H Ty1/copia-type	
+Q12193	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12193	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q12193	UniProtKB	Motif	1179	1213	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12193	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q12193	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q12193	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12193	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12193	UniProtKB	Metal binding	1347	1347	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12193	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12193	UniProtKB	Metal binding	1429	1429	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12193	UniProtKB	Metal binding	1611	1611	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12193	UniProtKB	Metal binding	1653	1653	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12193	UniProtKB	Metal binding	1686	1686	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12193	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12193	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12193	UniProtKB	Site	1218	1219	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12193	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region Q3E762 1 66
+Q3E762	UniProtKB	Chain	1	66	.	.	.	ID=PRO_0000248443;Note=Putative uncharacterized protein YBR230W-A	
+##sequence-region P0C5K9 1 27
+P0C5K9	UniProtKB	Chain	1	27	.	.	.	ID=PRO_0000309007;Note=Uncharacterized protein YBL039C-A	
+##sequence-region P38309 1 107
+P38309	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000202510;Note=Putative uncharacterized protein YBR206W	
+##sequence-region P38318 1 560
+P38318	UniProtKB	Chain	1	560	.	.	.	ID=PRO_0000202514;Note=Uncharacterized membrane protein YBR220C	
+P38318	UniProtKB	Topological domain	1	17	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Transmembrane	18	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Topological domain	39	54	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Topological domain	76	88	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Transmembrane	89	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Topological domain	110	139	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Topological domain	161	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Topological domain	194	214	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Transmembrane	215	235	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Topological domain	236	329	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Transmembrane	330	350	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Topological domain	351	374	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Transmembrane	375	395	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Topological domain	396	421	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Transmembrane	422	442	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Topological domain	443	521	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Transmembrane	522	542	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38318	UniProtKB	Topological domain	543	560	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38355 1 427
+P38355	UniProtKB	Chain	1	427	.	.	.	ID=PRO_0000123805;Note=Uncharacterized transporter YBR287W	
+P38355	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38355	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38355	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38355	UniProtKB	Transmembrane	253	273	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38355	UniProtKB	Transmembrane	288	308	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38355	UniProtKB	Transmembrane	327	347	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38355	UniProtKB	Transmembrane	358	378	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38355	UniProtKB	Transmembrane	397	417	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38355	UniProtKB	Modified residue	199	199	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38355	UniProtKB	Modified residue	234	234	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38355	UniProtKB	Sequence conflict	425	425	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38142 1 488
+P38142	UniProtKB	Chain	1	488	.	.	.	ID=PRO_0000050463;Note=Probable metabolite transport protein YBR241C	
+P38142	UniProtKB	Topological domain	1	18	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	19	39	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	40	87	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	109	121	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	143	146	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	168	178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	179	198	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	199	204	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	205	225	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	226	299	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	300	320	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	321	322	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	323	337	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	338	344	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	345	364	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	365	390	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	391	411	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	412	419	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	420	442	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	443	446	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Transmembrane	447	463	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Topological domain	464	488	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Glycosylation	63	63	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38142	UniProtKB	Sequence conflict	438	438	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38338 1 688
+P38338	UniProtKB	Chain	1	688	.	.	.	ID=PRO_0000202526;Note=Uncharacterized protein YBR259W	
+##sequence-region P38083 1 404
+P38083	UniProtKB	Chain	1	404	.	.	.	ID=PRO_0000202476;Note=Uncharacterized protein YBR063C	
+P38083	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38083	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38253 1 122
+P38253	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000202481;Note=Uncharacterized protein YBR090C	
+P38253	UniProtKB	Transmembrane	9	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38253	UniProtKB	Sequence conflict	101	101	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38253	UniProtKB	Sequence conflict	101	101	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P87012 1 153
+P87012	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000248411;Note=Putative pelota-like protein YCL001W-A	
+##sequence-region Q8TGQ0 1 78
+Q8TGQ0	UniProtKB	Chain	1	78	.	.	.	ID=PRO_0000299839;Note=Putative uncharacterized protein YCR081C-A	
+Q8TGQ0	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q8TGQ0	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q96VG5 1 65
+Q96VG5	UniProtKB	Chain	1	65	.	.	.	ID=PRO_0000299841;Note=Putative uncharacterized protein YCR102W-A	
+##sequence-region Q8J0M4 1 134
+Q8J0M4	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q8J0M4	UniProtKB	Chain	24	134	.	.	.	ID=PRO_0000045281;Note=UPF0357 protein YCL012C	
+Q8J0M4	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q8J0M4	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q8J0M4	UniProtKB	Cross-link	86	86	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P25562 1 171
+P25562	UniProtKB	Chain	1	171	.	.	.	ID=PRO_0000202541;Note=Putative uncharacterized protein YCL022C	
+##sequence-region P25593 1 260
+P25593	UniProtKB	Chain	1	260	.	.	.	ID=PRO_0000202556;Note=Putative uncharacterized protein YCL068C	
+P25593	UniProtKB	Sequence conflict	76	76	.	.	.	Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25614 1 215
+P25614	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000202561;Note=Putative uncharacterized protein YCR013C	
+##sequence-region Q12235 1 531
+Q12235	UniProtKB	Chain	1	531	.	.	.	ID=PRO_0000247151;Note=High affinity cysteine transporter	
+Q12235	UniProtKB	Topological domain	1	54	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	76	97	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	119	120	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	142	154	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	155	175	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	176	186	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	208	218	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	219	239	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	240	285	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	286	306	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	307	324	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	325	345	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	346	352	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	353	373	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	374	378	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	379	399	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	400	413	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	414	436	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	437	447	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Transmembrane	448	468	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Topological domain	469	531	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Coiled coil	469	498	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12235	UniProtKB	Modified residue	500	500	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12235	UniProtKB	Modified residue	501	501	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12235	UniProtKB	Glycosylation	146	146	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25631 1 222
+P25631	UniProtKB	Chain	1	222	.	.	.	ID=PRO_0000067244;Note=Ankyrin repeat-containing protein YCR051W	
+P25631	UniProtKB	Repeat	1	29	.	.	.	Note=ANK 1	
+P25631	UniProtKB	Repeat	36	66	.	.	.	Note=ANK 2	
+P25631	UniProtKB	Repeat	70	99	.	.	.	Note=ANK 3	
+##sequence-region P25607 1 182
+P25607	UniProtKB	Chain	1	182	.	.	.	ID=PRO_0000202584;Note=Uncharacterized protein YCR101C	
+P25607	UniProtKB	Repeat	58	69	.	.	.	Note=BNR 1	
+P25607	UniProtKB	Repeat	102	113	.	.	.	Note=BNR 2	
+##sequence-region Q12023 1 107
+Q12023	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000299843;Note=Putative uncharacterized protein YDL011C	
+Q12023	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12023	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12023	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGP7 1 34
+Q8TGP7	UniProtKB	Chain	1	34	.	.	.	ID=PRO_0000299846;Note=Putative uncharacterized protein YDL025W-A	
+##sequence-region Q07790 1 131
+Q07790	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07790	UniProtKB	Chain	20	131	.	.	.	ID=PRO_0000299871;Note=Putative uncharacterized protein YDR053W	
+Q07790	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07790	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07410 1 141
+Q07410	UniProtKB	Chain	1	141	.	.	.	ID=PRO_0000299852;Note=Putative uncharacterized protein YDL062W	
+##sequence-region Q07454 1 984
+Q07454	UniProtKB	Chain	1	984	.	.	.	ID=PRO_0000248460;Note=UPF0592 protein YDL073W	
+##sequence-region Q12103 1 647
+Q12103	UniProtKB	Chain	1	647	.	.	.	ID=PRO_0000240859;Note=Putative lipase YDL109C	
+Q12103	UniProtKB	Active site	274	274	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037	
+##sequence-region Q03855 1 1755
+Q03855	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279001;Note=Transposon Ty1-DR1 Gag-Pol polyprotein	
+Q03855	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279002;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03855	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279003;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03855	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279004;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03855	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279005;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03855	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03855	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q03855	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q03855	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03855	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q03855	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03855	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q03855	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q03855	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03855	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03855	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03855	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03855	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03855	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03855	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03855	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03855	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03855	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03855	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03855	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region P0C5L7 1 38
+P0C5L7	UniProtKB	Chain	1	38	.	.	.	ID=PRO_0000309015;Note=Uncharacterized protein YDR118W-A	
+##sequence-region Q12407 1 687
+Q12407	UniProtKB	Chain	1	687	.	.	.	ID=PRO_0000242140;Note=Putative metabolite transport protein YDL199C	
+Q12407	UniProtKB	Topological domain	1	122	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Topological domain	144	164	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Transmembrane	165	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Topological domain	186	192	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Transmembrane	193	213	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Topological domain	214	216	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Topological domain	238	251	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Transmembrane	252	272	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Topological domain	273	283	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Transmembrane	284	304	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Topological domain	305	410	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Transmembrane	411	431	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Topological domain	432	439	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Transmembrane	440	460	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Topological domain	461	469	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Transmembrane	470	490	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Topological domain	491	500	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Transmembrane	501	521	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Topological domain	522	533	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Transmembrane	534	554	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Topological domain	555	687	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12407	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q12240 1 137
+Q12240	UniProtKB	Chain	1	137	.	.	.	ID=PRO_0000299876;Note=Uncharacterized protein YDR215C	
+Q12240	UniProtKB	Transmembrane	75	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07649 1 183
+Q07649	UniProtKB	Chain	1	183	.	.	.	ID=PRO_0000299865;Note=Putative uncharacterized protein YDL221W	
+##sequence-region Q03494 1 1770
+Q03494	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000279292;Note=Transposon Ty2-DR2 Gag-Pol polyprotein	
+Q03494	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279293;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03494	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000279294;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03494	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000279295;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03494	UniProtKB	Chain	1233	1770	.	.	.	ID=PRO_0000279296;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03494	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03494	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q03494	UniProtKB	Domain	1625	1767	.	.	.	Note=RNase H Ty1/copia-type	
+Q03494	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03494	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+Q03494	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03494	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03494	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03494	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03494	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03494	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03494	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03494	UniProtKB	Metal binding	1625	1625	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03494	UniProtKB	Metal binding	1667	1667	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03494	UniProtKB	Metal binding	1700	1700	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03494	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03494	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03494	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q07746 1 117
+Q07746	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000299867;Note=Uncharacterized protein YDL242W	
+##sequence-region P87281 1 107
+P87281	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000299879;Note=Putative uncharacterized protein YDR269C	
+P87281	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87281	UniProtKB	Transmembrane	47	67	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87281	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P87280 1 109
+P87280	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299882;Note=Putative uncharacterized protein YDR290W	
+P87280	UniProtKB	Transmembrane	63	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05503 1 100
+Q05503	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299884;Note=Putative uncharacterized protein YDR340W	
+Q05503	UniProtKB	Transmembrane	28	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03418 1 163
+Q03418	UniProtKB	Chain	1	163	.	.	.	ID=PRO_0000299899;Note=Putative uncharacterized protein YDR491C	
+Q03418	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXB9 1 121
+A0A023PXB9	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000430988;Note=Putative uncharacterized membrane protein YDR199W	
+A0A023PXB9	UniProtKB	Transmembrane	26	46	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXB9	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXB9	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5M6 1 65
+P0C5M6	UniProtKB	Signal peptide	1	16	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C5M6	UniProtKB	Chain	17	65	.	.	.	ID=PRO_0000309024;Note=Putative uncharacterized protein YEL020C-B	
+##sequence-region Q8TGP4 1 53
+Q8TGP4	UniProtKB	Chain	1	53	.	.	.	ID=PRO_0000299908;Note=Putative uncharacterized protein YEL032C-A	
+##sequence-region A0A023PYE4 1 107
+A0A023PYE4	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000430993;Note=Putative uncharacterized membrane protein YER067C-A	
+A0A023PYE4	UniProtKB	Transmembrane	37	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P89888 1 203
+P89888	UniProtKB	Chain	1	203	.	.	.	ID=PRO_0000299657;Note=Putative uncharacterized protein YEL075W-A	
+##sequence-region Q3E7A2 1 54
+Q3E7A2	UniProtKB	Chain	1	54	.	.	.	ID=PRO_0000245371;Note=Uncharacterized protein YER078W-A	
+##sequence-region A0A023PZG0 1 170
+A0A023PZG0	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZG0	UniProtKB	Chain	22	170	.	.	.	ID=PRO_0000430996;Note=Putative uncharacterized membrane protein YER084W-A;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZG0	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX66 1 440
+P0CX66	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000409779;Note=Transposon Ty1-ER2 Gag polyprotein	
+P0CX66	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000409780;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX66	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000409781;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX66	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX66	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX66	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX66	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region A0A023PYF7 1 126
+A0A023PYF7	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000431006;Note=Putative uncharacterized protein YER172C-A	
+##sequence-region P0CX94 1 160
+P0CX94	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000277622;Note=UPF0479 membrane protein YER190C-B	
+P0CX94	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX94	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX94	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region A0A023PXD3 1 107
+A0A023PXD3	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000431009;Note=Putative uncharacterized protein YER088C-A	
+##sequence-region P40004 1 342
+P40004	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000213361;Note=UDP-N-acetylglucosamine transporter YEA4	
+P40004	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Topological domain	28	35	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Topological domain	57	61	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Topological domain	83	96	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Transmembrane	97	117	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Topological domain	118	123	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Transmembrane	124	144	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Topological domain	145	168	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Transmembrane	169	189	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Topological domain	190	253	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Transmembrane	254	274	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Topological domain	275	307	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Transmembrane	308	328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40004	UniProtKB	Topological domain	329	342	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39999 1 101
+P39999	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000202614;Note=Uncharacterized protein YEL014C	
+##sequence-region P39991 1 1188
+P39991	UniProtKB	Chain	1	1188	.	.	.	ID=PRO_0000202609;Note=Uncharacterized protein YEL025C	
+P39991	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39991	UniProtKB	Transmembrane	878	898	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39991	UniProtKB	Transmembrane	1089	1109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39989 1 153
+P39989	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39989	UniProtKB	Chain	22	153	.	.	.	ID=PRO_0000014314;Note=Uncharacterized protein YEL028W	
+##sequence-region P39977 1 110
+P39977	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000202601;Note=Uncharacterized protein YEL068C	
+##sequence-region P39971 1 216
+P39971	UniProtKB	Chain	1	216	.	.	.	ID=PRO_0000202597;Note=Uncharacterized protein YEL076C	
+##sequence-region P40028 1 759
+P40028	UniProtKB	Chain	1	759	.	.	.	ID=PRO_0000202629;Note=Holliday junction resolvase YEN1	
+P40028	UniProtKB	Modified residue	730	730	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40028	UniProtKB	Modified residue	731	731	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40028	UniProtKB	Sequence conflict	59	59	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40028	UniProtKB	Sequence conflict	164	165	.	.	.	Note=LL->FV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40028	UniProtKB	Sequence conflict	346	346	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40076 1 114
+P40076	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000202646;Note=Uncharacterized protein YER121W	
+##sequence-region P0C5M9 1 85
+P0C5M9	UniProtKB	Chain	1	85	.	.	.	ID=PRO_0000309027;Note=Uncharacterized protein YFR009W-A	
+##sequence-region Q3E817 1 63
+Q3E817	UniProtKB	Chain	1	63	.	.	.	ID=PRO_0000245373;Note=Uncharacterized protein YFL041W-A	
+##sequence-region Q06676 1 274
+Q06676	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000252273;Note=FIT family protein YFT2	
+Q06676	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Topological domain	33	60	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Transmembrane	61	81	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Topological domain	82	124	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Transmembrane	125	145	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Topological domain	146	170	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Topological domain	192	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Topological domain	237	247	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Transmembrane	248	268	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06676	UniProtKB	Topological domain	269	274	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12141 1 1755
+Q12141	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279053;Note=Transposon Ty1-GR1 Gag-Pol polyprotein	
+Q12141	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279054;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12141	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279055;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12141	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279056;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12141	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279057;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12141	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12141	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12141	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q12141	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12141	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q12141	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12141	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q12141	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12141	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12141	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12141	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12141	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12141	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12141	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12141	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12141	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12141	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12141	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12141	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region Q3E772 1 92
+Q3E772	UniProtKB	Chain	1	92	.	.	.	ID=PRO_0000245386;Note=Uncharacterized protein YGR169C-A	
+Q3E772	UniProtKB	Coiled coil	17	80	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53216 1 100
+P53216	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000202789;Note=Uncharacterized protein YGR025W	
+##sequence-region P53229 1 120
+P53229	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000202795;Note=Uncharacterized protein YGR045C	
+P53229	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E740 1 77
+Q3E740	UniProtKB	Chain	1	77	.	.	.	ID=PRO_0000245376;Note=Uncharacterized protein YGL258W-A	
+Q3E740	UniProtKB	Domain	1	77	.	.	.	Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
+##sequence-region P53263 1 149
+P53263	UniProtKB	Chain	1	149	.	.	.	ID=PRO_0000202812;Note=Putative uncharacterized protein YGR107W	
+##sequence-region P53272 1 402
+P53272	UniProtKB	Chain	1	402	.	.	.	ID=PRO_0000202818;Note=Uncharacterized protein YGR122W	
+##sequence-region P53274 1 230
+P53274	UniProtKB	Chain	1	230	.	.	.	ID=PRO_0000202820;Note=Uncharacterized protein YGR126W	
+P53274	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P53287 1 111
+P53287	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000202831;Note=Uncharacterized protein YGR151C	
+##sequence-region P32475 1 115
+P32475	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000202839;Note=Putative uncharacterized protein YGR176W	
+P32475	UniProtKB	Sequence conflict	56	59	.	.	.	Note=IRHD->NSPR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53308 1 114
+P53308	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000202850;Note=Putative uncharacterized protein YGR228W	
+P53308	UniProtKB	Transmembrane	21	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53308	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53308	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53316 1 781
+P53316	UniProtKB	Chain	1	781	.	.	.	ID=PRO_0000082030;Note=Uncharacterized RNA-binding protein YGR250C	
+P53316	UniProtKB	Domain	195	273	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P53316	UniProtKB	Domain	295	418	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P53316	UniProtKB	Domain	540	638	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P53316	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53316	UniProtKB	Modified residue	433	433	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53316	UniProtKB	Modified residue	435	435	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53316	UniProtKB	Modified residue	482	482	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53316	UniProtKB	Modified residue	485	485	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53316	UniProtKB	Modified residue	486	486	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53316	UniProtKB	Modified residue	501	501	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P53336 1 341
+P53336	UniProtKB	Chain	1	341	.	.	.	ID=PRO_0000202872;Note=Putative methyltransferase YGR283C	
+##sequence-region P53190 1 111
+P53190	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000202774;Note=Putative uncharacterized protein YGL024W	
+P53190	UniProtKB	Transmembrane	22	42	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53190	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53190	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53175 1 101
+P53175	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000202768;Note=Putative uncharacterized protein YGL052W	
+##sequence-region P53160 1 108
+P53160	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000202761;Note=Putative uncharacterized protein YGL074C	
+P53160	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53160	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53122 1 345
+P53122	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000202739;Note=Uncharacterized protein YGL138C	
+##sequence-region P53110 1 370
+P53110	UniProtKB	Chain	1	370	.	.	.	ID=PRO_0000202732;Note=Uncharacterized protein YGL159W	
+P53110	UniProtKB	Compositional bias	81	86	.	.	.	Note=Poly-Asn	
+P53110	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P53097 1 103
+P53097	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000202723;Note=Uncharacterized protein YGL193C	
+##sequence-region P53074 1 147
+P53074	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000202712;Note=Uncharacterized protein YGL230C	
+P53074	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07074 1 71
+Q07074	UniProtKB	Chain	1	71	.	.	.	ID=PRO_0000245393;Note=Uncharacterized protein YHR007C-A	
+Q07074	UniProtKB	Transmembrane	21	43	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07074	UniProtKB	Sequence conflict	24	26	.	.	.	Note=LFL->FFF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region A0A023PXL1 1 197
+A0A023PXL1	UniProtKB	Chain	1	197	.	.	.	ID=PRO_0000431016;Note=Putative uncharacterized membrane protein YHL019W-A	
+A0A023PXL1	UniProtKB	Transmembrane	150	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PYG5 1 108
+A0A023PYG5	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000431020;Note=Putative uncharacterized protein YHL046W-A	
+##sequence-region P0C5B8 1 160
+P0C5B8	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000299785;Note=Putative UPF0479 protein YHL050W-A	
+P0C5B8	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C5B8	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C5B8	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region A0A023PXF2 1 106
+A0A023PXF2	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000431025;Note=Putative uncharacterized protein YHR071C-A	
+##sequence-region P0C2I4 1 478
+P0C2I4	UniProtKB	Chain	1	478	.	.	.	ID=PRO_0000279079;Note=Transposon Ty1-H Gag polyprotein	
+P0C2I4	UniProtKB	Chain	1	439	.	.	.	ID=PRO_0000279080;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I4	UniProtKB	Peptide	440	478	.	.	.	ID=PRO_0000279081;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I4	UniProtKB	Region	337	439	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I4	UniProtKB	Compositional bias	72	146	.	.	.	Note=Pro-rich	
+P0C2I4	UniProtKB	Site	439	440	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region A0A023PXM2 1 81
+A0A023PXM2	UniProtKB	Chain	1	81	.	.	.	ID=PRO_0000431026;Note=Putative uncharacterized protein YHR131W-A	
+##sequence-region P32792 1 385
+P32792	UniProtKB	Chain	1	385	.	.	.	ID=PRO_0000202888;Note=UPF0744 protein YSC83	
+##sequence-region P38799 1 552
+P38799	UniProtKB	Chain	1	552	.	.	.	ID=PRO_0000202900;Note=Uncharacterized protein YHR078W	
+P38799	UniProtKB	Transmembrane	127	147	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38799	UniProtKB	Transmembrane	160	180	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38799	UniProtKB	Transmembrane	393	413	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38799	UniProtKB	Transmembrane	517	537	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38831 1 101
+P38831	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000202914;Note=Uncharacterized protein YHR125W	
+##sequence-region P38833 1 243
+P38833	UniProtKB	Chain	1	243	.	.	.	ID=PRO_0000202915;Note=Uncharacterized protein YHR127W	
+P38833	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P38867 1 453
+P38867	UniProtKB	Chain	1	453	.	.	.	ID=PRO_0000202932;Note=Uncharacterized protein YHR177W	
+P38867	UniProtKB	Compositional bias	256	259	.	.	.	Note=Poly-Gln	
+P38867	UniProtKB	Beta strand	7	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Helix	15	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Helix	39	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Beta strand	50	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Helix	56	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Beta strand	79	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Beta strand	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Beta strand	112	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Beta strand	136	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Helix	147	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Helix	158	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Helix	162	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+P38867	UniProtKB	Helix	171	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B	
+##sequence-region P38870 1 785
+P38870	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38870	UniProtKB	Chain	2	785	.	.	.	ID=PRO_0000202935;Note=Uncharacterized protein YHR182W	
+P38870	UniProtKB	Domain	520	702	.	.	.	Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172	
+P38870	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region A0A023PZF9 1 107
+A0A023PZF9	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000431030;Note=Putative uncharacterized membrane protein YIR023C-A	
+A0A023PZF9	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZE9 1 123
+A0A023PZE9	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000431031;Note=Putative uncharacterized protein YIL029W-A	
+##sequence-region A0A023PYI5 1 133
+A0A023PYI5	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000431033;Note=Putative uncharacterized membrane protein YIR036W-A	
+A0A023PYI5	UniProtKB	Transmembrane	91	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXN3 1 127
+A0A023PXN3	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000431036;Note=Putative uncharacterized protein YIL068W-A	
+##sequence-region Q45U18 1 67
+Q45U18	UniProtKB	Chain	1	67	.	.	.	ID=PRO_0000245401;Note=Uncharacterized protein YIL134C-A	
+Q45U18	UniProtKB	Transmembrane	13	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q45U18	UniProtKB	Transmembrane	45	64	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40538 1 142
+P40538	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000202996;Note=Uncharacterized protein YIL029C	
+P40538	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40538	UniProtKB	Transmembrane	30	50	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40538	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40434 1 1758
+P40434	UniProtKB	Chain	1	1758	.	.	.	ID=PRO_0000102207;Note=Y' element ATP-dependent helicase YIL177C	
+P40434	UniProtKB	Domain	668	845	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P40434	UniProtKB	Domain	900	1051	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P40434	UniProtKB	Nucleotide binding	681	688	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region P0C5P1 1 38
+P0C5P1	UniProtKB	Chain	1	38	.	.	.	ID=PRO_0000309039;Note=Putative uncharacterized protein YJL127W-A	
+##sequence-region P47126 1 109
+P47126	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000203102;Note=Uncharacterized protein YJR079W	
+P47126	UniProtKB	Compositional bias	16	20	.	.	.	Note=Poly-Phe	
+##sequence-region P47028 1 122
+P47028	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000203048;Note=Putative uncharacterized protein YJL086C	
+P47028	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P42947 1 387
+P42947	UniProtKB	Chain	1	387	.	.	.	ID=PRO_0000203046;Note=Uncharacterized UPF0442 protein YJL107C	
+##sequence-region P47003 1 119
+P47003	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000203029;Note=Putative uncharacterized protein YJL152W	
+P47003	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46994 1 122
+P46994	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000203026;Note=Putative uncharacterized protein YJL169W	
+##sequence-region P39542 1 402
+P39542	UniProtKB	Chain	1	402	.	.	.	ID=PRO_0000206786;Note=Uncharacterized transporter YJL193W	
+P39542	UniProtKB	Topological domain	1	12	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Topological domain	34	50	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Topological domain	72	103	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Topological domain	125	134	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Transmembrane	135	155	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Topological domain	156	165	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Transmembrane	166	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Topological domain	187	206	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Transmembrane	207	227	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Topological domain	228	271	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Transmembrane	272	292	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Topological domain	293	353	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Transmembrane	354	374	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39542	UniProtKB	Topological domain	375	402	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40898 1 147
+P40898	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000203014;Note=Putative uncharacterized protein YJL211C	
+##sequence-region P47092 1 110
+P47092	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000203087;Note=Putative uncharacterized protein YJR020W	
+##sequence-region Q3E7A7 1 99
+Q3E7A7	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E7A7	UniProtKB	Chain	20	99	.	.	.	ID=PRO_0000245424;Note=Uncharacterized protein YKL018C-A	
+##sequence-region P36133 1 167
+P36133	UniProtKB	Chain	1	167	.	.	.	ID=PRO_0000203209;Note=Putative uncharacterized protein YKR040C	
+P36133	UniProtKB	Compositional bias	144	167	.	.	.	Note=Lys-rich (highly basic)	
+##sequence-region P36134 1 250
+P36134	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000203210;Note=Uncharacterized protein YKR041W	
+P36134	UniProtKB	Cross-link	17	17	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region Q86ZR7 1 236
+Q86ZR7	UniProtKB	Chain	1	236	.	.	.	ID=PRO_0000203186;Note=Putative uncharacterized hydrolase YKL033W-A	
+##sequence-region P35736 1 922
+P35736	UniProtKB	Chain	1	922	.	.	.	ID=PRO_0000203180;Note=Uncharacterized protein YKL050C	
+##sequence-region P36083 1 450
+P36083	UniProtKB	Chain	1	450	.	.	.	ID=PRO_0000203170;Note=Uncharacterized protein YKL075C	
+##sequence-region P0CX72 1 440
+P0CX72	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000409794;Note=Transposon Ty1-LR2 Gag polyprotein	
+P0CX72	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000409795;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX72	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000409796;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX72	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX72	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX72	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX72	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region P0CY04 1 43
+P0CY04	UniProtKB	Chain	1	43	.	.	.	ID=PRO_0000410460;Note=Uncharacterized protein YLR157C-C	
+##sequence-region P0C5P6 1 37
+P0C5P6	UniProtKB	Chain	1	37	.	.	.	ID=PRO_0000309044;Note=Uncharacterized protein YLR163W-A	
+##sequence-region O13546 1 115
+O13546	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000299624;Note=Putative uncharacterized protein YLR232W	
+##sequence-region O13542 1 113
+O13542	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000299630;Note=Putative uncharacterized protein YLR282C	
+##sequence-region Q3E771 1 56
+Q3E771	UniProtKB	Chain	1	56	.	.	.	ID=PRO_0000247137;Note=Uncharacterized protein YLR285C-A	
+##sequence-region Q8TGM3 1 30
+Q8TGM3	UniProtKB	Chain	1	30	.	.	.	ID=PRO_0000299634;Note=Putative uncharacterized protein YLR299C-A	
+##sequence-region Q3E825 1 87
+Q3E825	UniProtKB	Chain	1	87	.	.	.	ID=PRO_0000247162;Note=Uncharacterized protein YLR307C-A	
+##sequence-region Q06409 1 1932
+Q06409	UniProtKB	Chain	1	1932	.	.	.	ID=PRO_0000247776;Note=DOCK-like protein YLR422W	
+Q06409	UniProtKB	Domain	1410	1824	.	.	.	Note=DHR-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00984	
+##sequence-region O13560 1 100
+O13560	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299652;Note=Putative uncharacterized protein YLR444C	
+O13560	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13560	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06199 1 204
+Q06199	UniProtKB	Chain	1	204	.	.	.	ID=PRO_0000268191;Note=Pyridoxamine 5'-phosphate oxidase YLR456W homolog	
+Q06199	UniProtKB	Nucleotide binding	65	66	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06199	UniProtKB	Binding site	127	127	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q3E760 1 96
+Q3E760	UniProtKB	Chain	1	96	.	.	.	ID=PRO_0000247785;Note=Uncharacterized protein YMR030W-A	
+Q3E760	UniProtKB	Transmembrane	59	81	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E760	UniProtKB	Glycosylation	4	4	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E809 1 52
+Q3E809	UniProtKB	Chain	1	52	.	.	.	ID=PRO_0000247782;Note=Uncharacterized protein YML054C-A	
+##sequence-region P0CF18 1 432
+P0CF18	UniProtKB	Chain	1	432	.	.	.	ID=PRO_0000393382;Note=Uncharacterized protein YMR085W	
+P0CF18	UniProtKB	Domain	105	244	.	.	.	Note=SIS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00797	
+P0CF18	UniProtKB	Domain	277	422	.	.	.	Note=SIS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00797	
+##sequence-region Q6B0Z2 1 105
+Q6B0Z2	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000299661;Note=Putative uncharacterized protein YML101C-A	
+Q6B0Z2	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6B0Z2	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6B0Z2	UniProtKB	Sequence conflict	11	11	.	.	.	Note=K->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0C5Q4 1 74
+P0C5Q4	UniProtKB	Chain	1	74	.	.	.	ID=PRO_0000309052;Note=Putative uncharacterized protein YMR141W-A	
+P0C5Q4	UniProtKB	Transmembrane	54	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXH6 1 127
+A0A023PXH6	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000431055;Note=Putative uncharacterized membrane protein YMR172C-A	
+A0A023PXH6	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXH6	UniProtKB	Transmembrane	83	103	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E766 1 64
+Q3E766	UniProtKB	Chain	1	64	.	.	.	ID=PRO_0000247788;Note=Uncharacterized protein YMR175W-A	
+##sequence-region Q03703 1 340
+Q03703	UniProtKB	Chain	1	340	.	.	.	ID=PRO_0000203258;Note=Uncharacterized protein YML037C	
+##sequence-region Q04502 1 122
+Q04502	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000203246;Note=Putative uncharacterized protein YML089C	
+##sequence-region P0CL29 1 191
+P0CL29	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL29	UniProtKB	Chain	18	191	.	.	.	ID=PRO_0000406006;Note=Putative uncharacterized protein YML133W-A	
+P0CL29	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL29	UniProtKB	Compositional bias	13	159	.	.	.	Note=Gly/Ser-rich	
+##sequence-region Q03207 1 126
+Q03207	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000203239;Note=Uncharacterized protein YML122C	
+##sequence-region Q03099 1 1374
+Q03099	UniProtKB	Chain	1	1374	.	.	.	ID=PRO_0000102209;Note=Y' element ATP-dependent helicase YML133C	
+Q03099	UniProtKB	Domain	375	552	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q03099	UniProtKB	Domain	609	758	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q03099	UniProtKB	Nucleotide binding	388	395	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region Q04364 1 514
+Q04364	UniProtKB	Chain	1	514	.	.	.	ID=PRO_0000106320;Note=TPR repeat-containing protein YMR018W	
+Q04364	UniProtKB	Repeat	174	207	.	.	.	Note=TPR 1	
+Q04364	UniProtKB	Repeat	218	252	.	.	.	Note=TPR 2	
+Q04364	UniProtKB	Repeat	254	286	.	.	.	Note=TPR 3	
+Q04364	UniProtKB	Repeat	288	320	.	.	.	Note=TPR 4	
+Q04364	UniProtKB	Repeat	326	359	.	.	.	Note=TPR 5	
+Q04364	UniProtKB	Repeat	360	393	.	.	.	Note=TPR 6	
+Q04364	UniProtKB	Repeat	394	427	.	.	.	Note=TPR 7	
+Q04364	UniProtKB	Repeat	429	461	.	.	.	Note=TPR 8	
+Q04364	UniProtKB	Sequence conflict	9	9	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99337 1 1749
+Q99337	UniProtKB	Chain	1	1749	.	.	.	ID=PRO_0000279145;Note=Transposon Ty1-NL2 Gag-Pol polyprotein	
+Q99337	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279146;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99337	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279147;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99337	UniProtKB	Chain	583	1211	.	.	.	ID=PRO_0000279148;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99337	UniProtKB	Chain	1212	1749	.	.	.	ID=PRO_0000279149;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99337	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99337	UniProtKB	Domain	1332	1470	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q99337	UniProtKB	Domain	1604	1746	.	.	.	Note=RNase H Ty1/copia-type	
+Q99337	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99337	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q99337	UniProtKB	Motif	1172	1206	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99337	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q99337	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99337	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99337	UniProtKB	Metal binding	1340	1340	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99337	UniProtKB	Metal binding	1421	1421	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99337	UniProtKB	Metal binding	1422	1422	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99337	UniProtKB	Metal binding	1604	1604	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99337	UniProtKB	Metal binding	1646	1646	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99337	UniProtKB	Metal binding	1679	1679	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99337	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99337	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99337	UniProtKB	Site	1211	1212	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53740 1 393
+P53740	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000207672;Note=Probable phospholipid translocase non-catalytic subunit CRF1	
+P53740	UniProtKB	Topological domain	1	46	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P53740	UniProtKB	Transmembrane	47	67	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53740	UniProtKB	Topological domain	68	334	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P53740	UniProtKB	Transmembrane	335	355	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53740	UniProtKB	Topological domain	356	393	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P53740	UniProtKB	Glycosylation	78	78	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53740	UniProtKB	Glycosylation	123	123	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53740	UniProtKB	Glycosylation	187	187	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53740	UniProtKB	Glycosylation	202	202	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53740	UniProtKB	Glycosylation	213	213	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53740	UniProtKB	Glycosylation	240	240	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53740	UniProtKB	Glycosylation	291	291	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53967 1 105
+P53967	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000203459;Note=Putative uncharacterized protein YNL028W	
+##sequence-region P53932 1 642
+P53932	UniProtKB	Chain	1	642	.	.	.	ID=PRO_0000123807;Note=Uncharacterized transporter YNL095C	
+P53932	UniProtKB	Topological domain	1	15	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Topological domain	37	42	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Topological domain	64	73	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Topological domain	95	104	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Topological domain	126	142	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Transmembrane	143	163	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Topological domain	164	460	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Transmembrane	461	481	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Topological domain	482	499	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Transmembrane	500	520	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Topological domain	521	538	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Transmembrane	539	559	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Topological domain	560	574	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Transmembrane	575	595	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Topological domain	596	614	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Transmembrane	615	635	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53932	UniProtKB	Topological domain	636	642	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53929 1 270
+P53929	UniProtKB	Chain	1	270	.	.	.	ID=PRO_0000203436;Note=Uncharacterized protein YNL108C	
+P53929	UniProtKB	Beta strand	5	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Helix	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Beta strand	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Helix	38	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Beta strand	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Helix	67	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Helix	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Helix	107	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Turn	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Helix	135	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Beta strand	162	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Helix	169	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Beta strand	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Beta strand	189	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Beta strand	203	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Helix	218	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Beta strand	224	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Beta strand	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+P53929	UniProtKB	Helix	253	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2	
+##sequence-region P53907 1 740
+P53907	UniProtKB	Chain	1	740	.	.	.	ID=PRO_0000203423;Note=Uncharacterized protein YNL144C	
+##sequence-region P53878 1 407
+P53878	UniProtKB	Chain	1	407	.	.	.	ID=PRO_0000203405;Note=Uncharacterized oxidoreductase YNL181W	
+P53878	UniProtKB	Topological domain	1	290	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53878	UniProtKB	Transmembrane	291	311	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53878	UniProtKB	Topological domain	312	407	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53878	UniProtKB	Nucleotide binding	57	79	.	.	.	Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53878	UniProtKB	Coiled coil	361	390	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53878	UniProtKB	Sequence conflict	262	262	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40163 1 203
+P40163	UniProtKB	Chain	1	203	.	.	.	ID=PRO_0000203394;Note=Putative uncharacterized protein YNL203C	
+P40163	UniProtKB	Transmembrane	89	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40163	UniProtKB	Sequence conflict	160	160	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40163	UniProtKB	Sequence conflict	178	178	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40163	UniProtKB	Sequence conflict	183	183	.	.	.	Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40163	UniProtKB	Sequence conflict	186	186	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53857 1 426
+P53857	UniProtKB	Chain	1	426	.	.	.	ID=PRO_0000053402;Note=Uncharacterized globin-like protein YNL234W	
+##sequence-region Q12169 1 119
+Q12169	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000299701;Note=Uncharacterized protein YOR015W	
+Q12169	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12169	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q870I1 1 96
+Q870I1	UniProtKB	Chain	1	96	.	.	.	ID=PRO_0000299687;Note=Putative uncharacterized protein YOL013W-B	
+Q870I1	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q870I1	UniProtKB	Natural variant	48	48	.	.	.	Note=In strain: CEN.PK 113-7D. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430	
+Q870I1	UniProtKB	Natural variant	59	59	.	.	.	Note=In strain: CEN.PK 113-7D. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430	
+Q870I1	UniProtKB	Natural variant	69	69	.	.	.	Note=In strain: CEN.PK 113-7D. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430	
+##sequence-region Q08540 1 154
+Q08540	UniProtKB	Chain	1	154	.	.	.	ID=PRO_0000299719;Note=Putative uncharacterized protein YOR169C	
+##sequence-region Q08560 1 144
+Q08560	UniProtKB	Chain	1	144	.	.	.	ID=PRO_0000237662;Note=Putative uncharacterized protein YOR186W	
+Q08560	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08560	UniProtKB	Glycosylation	14	14	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08560	UniProtKB	Glycosylation	15	15	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12501 1 1770
+Q12501	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000279348;Note=Transposon Ty2-OR2 Gag-Pol polyprotein	
+Q12501	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279349;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12501	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000279350;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12501	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000279351;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12501	UniProtKB	Chain	1233	1770	.	.	.	ID=PRO_0000279352;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12501	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12501	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12501	UniProtKB	Domain	1625	1767	.	.	.	Note=RNase H Ty1/copia-type	
+Q12501	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12501	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+Q12501	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12501	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12501	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12501	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12501	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12501	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12501	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12501	UniProtKB	Metal binding	1625	1625	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12501	UniProtKB	Metal binding	1667	1667	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12501	UniProtKB	Metal binding	1700	1700	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12501	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12501	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12501	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q3E7Y7 1 49
+Q3E7Y7	UniProtKB	Chain	1	49	.	.	.	ID=PRO_0000245283;Note=Uncharacterized protein YOR293C-A	
+##sequence-region Q12506 1 109
+Q12506	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299735;Note=Uncharacterized protein YOR314W	
+##sequence-region Q08842 1 122
+Q08842	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000299742;Note=Putative uncharacterized protein YOR364W	
+Q08842	UniProtKB	Sequence conflict	96	96	.	.	.	Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08902 1 515
+Q08902	UniProtKB	Chain	1	515	.	.	.	ID=PRO_0000244476;Note=Drug resistance protein YOR378W	
+Q08902	UniProtKB	Topological domain	1	78	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	79	99	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	100	111	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	133	140	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	162	171	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	172	192	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	193	202	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	203	223	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	224	241	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	263	270	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	271	291	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	292	310	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	311	331	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	332	346	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	347	367	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	368	374	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	375	395	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	396	403	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	404	424	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	425	435	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	436	456	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	457	479	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Transmembrane	480	500	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08902	UniProtKB	Topological domain	501	515	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08915 1 147
+Q08915	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000299745;Note=Putative uncharacterized protein YOR392W	
+Q08915	UniProtKB	Transmembrane	69	89	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E769 1 90
+Q3E769	UniProtKB	Chain	1	90	.	.	.	ID=PRO_0000245277;Note=Uncharacterized protein YOL159C-A	
+##sequence-region P0C5R3 1 77
+P0C5R3	UniProtKB	Chain	1	77	.	.	.	ID=PRO_0000309061;Note=Putative uncharacterized protein YOR073W-A	
+##sequence-region A0A023PZ99 1 116
+A0A023PZ99	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000430979;Note=Putative uncharacterized protein YDR008C	
+A0A023PZ99	UniProtKB	Transmembrane	20	42	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZE6 1 104
+A0A023PZE6	UniProtKB	Signal peptide	1	16	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZE6	UniProtKB	Chain	17	104	.	.	.	ID=PRO_0000430980;Note=Putative uncharacterized membrane protein YDR048C	
+A0A023PZE6	UniProtKB	Transmembrane	74	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07379 1 328
+Q07379	UniProtKB	Chain	1	328	.	.	.	ID=PRO_0000248458;Note=Putative uncharacterized protein YDL057W	
+##sequence-region Q07509 1 169
+Q07509	UniProtKB	Chain	1	169	.	.	.	ID=PRO_0000299856;Note=Putative uncharacterized protein YDL094C	
+Q07509	UniProtKB	Transmembrane	55	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12441 1 440
+Q12441	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279014;Note=Transposon Ty1-DR3 Gag polyprotein	
+Q12441	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279015;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12441	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279016;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12441	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12441	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q12441	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12441	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q99231 1 1755
+Q99231	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279009;Note=Transposon Ty1-DR3 Gag-Pol polyprotein	
+Q99231	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279010;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99231	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279011;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99231	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279012;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99231	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279013;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99231	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99231	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q99231	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q99231	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99231	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q99231	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99231	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q99231	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q99231	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99231	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99231	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99231	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99231	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99231	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99231	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99231	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q99231	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99231	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99231	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99231	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q12047 1 102
+Q12047	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000299858;Note=Putative uncharacterized protein YDL158C	
+##sequence-region Q3E789 1 49
+Q3E789	UniProtKB	Chain	1	49	.	.	.	ID=PRO_0000253832;Note=Uncharacterized protein YDR169C-A	
+##sequence-region Q3E796 1 67
+Q3E796	UniProtKB	Chain	1	67	.	.	.	ID=PRO_0000253833;Note=Uncharacterized protein YDR182W-A	
+Q3E796	UniProtKB	Transmembrane	12	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5E0 1 132
+P0C5E0	UniProtKB	Chain	1	132	.	.	.	ID=PRO_0000302031;Note=Putative uncharacterized protein YDR193W	
+P0C5E0	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5L9 1 24
+P0C5L9	UniProtKB	Chain	1	24	.	.	.	ID=PRO_0000309017;Note=Putative uncharacterized protein YDL247W-A	
+##sequence-region P87282 1 123
+P87282	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000299880;Note=Putative uncharacterized protein YDR271C	
+##sequence-region P0C5M0 1 45
+P0C5M0	UniProtKB	Chain	1	45	.	.	.	ID=PRO_0000309018;Note=Uncharacterized protein YDR320W-B	
+P0C5M0	UniProtKB	Compositional bias	40	44	.	.	.	Note=Poly-Lys	
+##sequence-region P87285 1 100
+P87285	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299887;Note=Putative uncharacterized protein YDR355C	
+P87285	UniProtKB	Transmembrane	20	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87285	UniProtKB	Transmembrane	44	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13522 1 166
+O13522	UniProtKB	Chain	1	166	.	.	.	ID=PRO_0000299888;Note=Putative uncharacterized protein YDR396W	
+O13522	UniProtKB	Transmembrane	4	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13522	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13522	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04033 1 374
+Q04033	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04033	UniProtKB	Chain	19	374	.	.	.	ID=PRO_0000253823;Note=Probable aminopeptidase YDR415C	
+Q04033	UniProtKB	Metal binding	177	177	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04033	UniProtKB	Metal binding	196	196	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04033	UniProtKB	Metal binding	196	196	.	.	.	Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04033	UniProtKB	Metal binding	235	235	.	.	.	Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04033	UniProtKB	Metal binding	262	262	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04033	UniProtKB	Metal binding	340	340	.	.	.	Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P87270 1 130
+P87270	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000299894;Note=Putative uncharacterized protein YDR442W	
+P87270	UniProtKB	Transmembrane	21	43	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P87271 1 102
+P87271	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000299896;Note=Putative uncharacterized protein YDR455C	
+##sequence-region Q03362 1 224
+Q03362	UniProtKB	Chain	1	224	.	.	.	ID=PRO_0000253853;Note=Uncharacterized protein YDR476C	
+Q03362	UniProtKB	Glycosylation	10	10	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03362	UniProtKB	Glycosylation	70	70	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03362	UniProtKB	Glycosylation	74	74	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03057 1 142
+Q03057	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000299906;Note=Putative uncharacterized protein YDR544C	
+Q03057	UniProtKB	Compositional bias	20	47	.	.	.	Note=His-rich	
+##sequence-region Q8TGP9 1 58
+Q8TGP9	UniProtKB	Chain	1	58	.	.	.	ID=PRO_0000299859;Note=Putative uncharacterized protein YDL159C-B	
+Q8TGP9	UniProtKB	Transmembrane	18	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5M3 1 85
+P0C5M3	UniProtKB	Chain	1	85	.	.	.	ID=PRO_0000309021;Note=Putative uncharacterized protein YDR183C-A	
+P0C5M3	UniProtKB	Transmembrane	20	42	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C5M3	UniProtKB	Transmembrane	52	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PYD3 1 111
+A0A023PYD3	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000430987;Note=Putative uncharacterized protein YDR094W	
+##sequence-region P0C5M5 1 37
+P0C5M5	UniProtKB	Chain	1	37	.	.	.	ID=PRO_0000309023;Note=Putative uncharacterized protein YDL114W-A	
+##sequence-region Q04925 1 415
+Q04925	UniProtKB	Chain	1	415	.	.	.	ID=PRO_0000253838;Note=SVF1-like protein YDR222W	
+##sequence-region Q8TGR5 1 104
+Q8TGR5	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000299909;Note=Putative uncharacterized protein YEL030C-A	
+##sequence-region P0CX95 1 160
+P0CX95	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000410452;Note=UPF0479 membrane protein YEL077W-A	
+P0CX95	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX95	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX95	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region Q02590 1 73
+Q02590	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000299913;Note=Putative uncharacterized protein YER091C-A	
+##sequence-region P0CX71 1 440
+P0CX71	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000409791;Note=Transposon Ty1-ER1 Gag polyprotein	
+P0CX71	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000409792;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX71	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000409793;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX71	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX71	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX71	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX71	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region P40097 1 107
+P40097	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000202659;Note=Uncharacterized protein YER181C%2C mitochondrial	
+P40097	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40097	UniProtKB	Transmembrane	58	78	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZC3 1 113
+A0A023PZC3	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000430999;Note=Putative uncharacterized protein YER133W-A	
+##sequence-region Q03619 1 1755
+Q03619	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279048;Note=Transposon Ty1-ER2 Gag-Pol polyprotein	
+Q03619	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279049;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03619	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279050;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03619	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279051;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03619	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279052;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03619	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03619	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q03619	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q03619	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03619	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q03619	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03619	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q03619	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q03619	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03619	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03619	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03619	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03619	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03619	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03619	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03619	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03619	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03619	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03619	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P40000 1 116
+P40000	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000202615;Note=Putative uncharacterized protein YEL010W	
+##sequence-region P40083 1 148
+P40083	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000202652;Note=Uncharacterized protein YEL137C	
+##sequence-region A0A023PXK7 1 284
+A0A023PXK7	UniProtKB	Chain	1	284	.	.	.	ID=PRO_0000431011;Note=Putative uncharacterized membrane protein YFL021C-A	
+A0A023PXK7	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXK7	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXK7	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXK7	UniProtKB	Compositional bias	44	96	.	.	.	Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016	
+##sequence-region A0A023PZH4 1 101
+A0A023PZH4	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000431013;Note=Putative uncharacterized protein YFR052C-A	
+A0A023PZH4	UniProtKB	Transmembrane	58	80	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43562 1 540
+P43562	UniProtKB	Chain	1	540	.	.	.	ID=PRO_0000050464;Note=Probable metabolite transport protein YFL040W	
+P43562	UniProtKB	Topological domain	1	29	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	30	50	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	51	67	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	89	101	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	102	122	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	123	126	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	127	147	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	148	158	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	159	179	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	180	187	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	209	275	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	276	296	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	297	313	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	314	334	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	335	341	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	342	362	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	363	385	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	386	406	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	407	428	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	429	449	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	450	455	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Transmembrane	456	476	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Topological domain	477	540	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Glycosylation	52	52	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43562	UniProtKB	Glycosylation	374	374	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43552 1 160
+P43552	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43552	UniProtKB	Chain	24	160	.	.	.	ID=PRO_0000014318;Note=Uncharacterized membrane protein YFL051C	
+P43552	UniProtKB	Topological domain	24	132	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43552	UniProtKB	Transmembrane	133	155	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43552	UniProtKB	Topological domain	156	160	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43549 1 646
+P43549	UniProtKB	Chain	1	646	.	.	.	ID=PRO_0000064099;Note=Uncharacterized membrane protein YFL054C	
+P43549	UniProtKB	Topological domain	1	350	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Transmembrane	351	371	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Topological domain	372	383	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Transmembrane	384	404	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Topological domain	405	427	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Transmembrane	428	448	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Topological domain	449	481	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Transmembrane	482	502	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Topological domain	503	509	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Transmembrane	510	530	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Topological domain	531	569	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Transmembrane	570	590	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Topological domain	591	646	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43549	UniProtKB	Motif	408	410	.	.	.	Note=NPA 1	
+P43549	UniProtKB	Motif	538	540	.	.	.	Note=NPA 2	
+##sequence-region P0CX99 1 160
+P0CX99	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000202666;Note=UPF0479 membrane protein YFL068W	
+P0CX99	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX99	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX99	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+P0CX99	UniProtKB	Sequence conflict	47	47	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43625 1 151
+P43625	UniProtKB	Chain	1	151	.	.	.	ID=PRO_0000202701;Note=Uncharacterized protein YFR057W	
+##sequence-region Q8TGT8 1 28
+Q8TGT8	UniProtKB	Chain	1	28	.	.	.	ID=PRO_0000245387;Note=Uncharacterized protein YGR174W-A	
+##sequence-region P53217 1 278
+P53217	UniProtKB	Chain	1	278	.	.	.	ID=PRO_0000202790;Note=Uncharacterized membrane protein YGR026W	
+P53217	UniProtKB	Topological domain	1	34	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53217	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53217	UniProtKB	Topological domain	56	129	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53217	UniProtKB	Transmembrane	130	150	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53217	UniProtKB	Topological domain	151	180	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53217	UniProtKB	Transmembrane	181	201	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53217	UniProtKB	Topological domain	202	205	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53217	UniProtKB	Transmembrane	206	222	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53217	UniProtKB	Topological domain	223	278	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53232 1 107
+P53232	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000202798;Note=Putative uncharacterized protein YGR051C	
+##sequence-region Q12337 1 1770
+Q12337	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000279316;Note=Transposon Ty2-GR1 Gag-Pol polyprotein	
+Q12337	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279317;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12337	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000279318;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12337	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000279319;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12337	UniProtKB	Chain	1233	1770	.	.	.	ID=PRO_0000279320;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12337	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12337	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12337	UniProtKB	Domain	1625	1767	.	.	.	Note=RNase H Ty1/copia-type	
+Q12337	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12337	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+Q12337	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12337	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12337	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12337	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12337	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12337	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12337	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12337	UniProtKB	Metal binding	1625	1625	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12337	UniProtKB	Metal binding	1667	1667	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12337	UniProtKB	Metal binding	1700	1700	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12337	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12337	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12337	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53249 1 370
+P53249	UniProtKB	Signal peptide	1	27	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53249	UniProtKB	Chain	28	370	.	.	.	ID=PRO_0000014322;Note=Putative uncharacterized protein YGR079W	
+P53249	UniProtKB	Compositional bias	140	146	.	.	.	Note=Poly-Asp	
+P53249	UniProtKB	Glycosylation	59	59	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53249	UniProtKB	Glycosylation	98	98	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53249	UniProtKB	Glycosylation	126	126	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53249	UniProtKB	Glycosylation	171	171	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53249	UniProtKB	Glycosylation	221	221	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53249	UniProtKB	Glycosylation	230	230	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53249	UniProtKB	Glycosylation	262	262	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53275 1 312
+P53275	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000202821;Note=Uncharacterized protein YGR127W	
+##sequence-region P53291 1 111
+P53291	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000202836;Note=Uncharacterized protein YGR164W	
+##sequence-region P53339 1 147
+P53339	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000014323;Note=Putative uncharacterized membrane protein YGR290W	
+P53339	UniProtKB	Topological domain	1	16	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53339	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53339	UniProtKB	Topological domain	38	105	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53339	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53339	UniProtKB	Topological domain	127	147	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53144 1 215
+P53144	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000202754;Note=HD domain-containing protein YGL101W	
+P53144	UniProtKB	Domain	58	164	.	.	.	Note=HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01175	
+##sequence-region P53134 1 725
+P53134	UniProtKB	Chain	1	725	.	.	.	ID=PRO_0000213789;Note=Putative oligopeptide transporter YGL114W	
+P53134	UniProtKB	Transmembrane	28	48	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53134	UniProtKB	Transmembrane	134	154	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53134	UniProtKB	Transmembrane	254	274	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53134	UniProtKB	Transmembrane	353	373	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53134	UniProtKB	Transmembrane	449	469	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53134	UniProtKB	Transmembrane	472	492	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53134	UniProtKB	Transmembrane	564	584	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53134	UniProtKB	Transmembrane	644	664	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53134	UniProtKB	Transmembrane	697	717	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38887 1 602
+P38887	UniProtKB	Chain	1	602	.	.	.	ID=PRO_0000202941;Note=Uncharacterized protein YHR202W	
+P38887	UniProtKB	Glycosylation	305	305	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38887	UniProtKB	Glycosylation	497	497	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38887	UniProtKB	Glycosylation	577	577	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXL7 1 144
+A0A023PXL7	UniProtKB	Chain	1	144	.	.	.	ID=PRO_0000431021;Note=Putative uncharacterized membrane protein YHR056W-A	
+A0A023PXL7	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXL7	UniProtKB	Transmembrane	60	80	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZI4 1 120
+A0A023PZI4	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000431023;Note=Putative uncharacterized membrane protein YHR069C-A	
+A0A023PZI4	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZI4	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13537 1 118
+O13537	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000299930;Note=Putative uncharacterized protein YHR145C	
+O13537	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZI9 1 157
+A0A023PZI9	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000431028;Note=Putative uncharacterized protein YHR182C-A	
+##sequence-region Q8TGK0 1 99
+Q8TGK0	UniProtKB	Chain	1	99	.	.	.	ID=PRO_0000202437;Note=Putative uncharacterized protein YHR214C-E	
+##sequence-region Q8TGK1 1 99
+Q8TGK1	UniProtKB	Chain	1	99	.	.	.	ID=PRO_0000245399;Note=Uncharacterized protein YHR213W-B	
+##sequence-region P0C5N6 1 59
+P0C5N6	UniProtKB	Chain	1	59	.	.	.	ID=PRO_0000309034;Note=Uncharacterized protein YHR032W-A	
+##sequence-region P0C2J7 1 1802
+P0C2J7	UniProtKB	Chain	1	1802	.	.	.	ID=PRO_0000279380;Note=Transposon Ty4-H Gag-Pol polyprotein	
+P0C2J7	UniProtKB	Domain	619	786	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J7	UniProtKB	Domain	1375	1510	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0C2J7	UniProtKB	Domain	1644	1790	.	.	.	Note=RNase H Ty1/copia-type	
+P0C2J7	UniProtKB	Region	381	501	.	.	.	Note=Ty4 protease	
+P0C2J7	UniProtKB	Region	539	599	.	.	.	Note=Integrase-type zinc finger-like	
+P0C2J7	UniProtKB	Coiled coil	39	115	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C2J7	UniProtKB	Active site	414	414	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J7	UniProtKB	Metal binding	630	630	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J7	UniProtKB	Metal binding	695	695	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J7	UniProtKB	Metal binding	1383	1383	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J7	UniProtKB	Metal binding	1462	1462	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J7	UniProtKB	Metal binding	1463	1463	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J7	UniProtKB	Metal binding	1644	1644	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J7	UniProtKB	Metal binding	1686	1686	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J7	UniProtKB	Metal binding	1720	1720	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+##sequence-region P0C5N7 1 58
+P0C5N7	UniProtKB	Chain	1	58	.	.	.	ID=PRO_0000309035;Note=Uncharacterized protein YHR073W-A	
+##sequence-region Q03888 1 244
+Q03888	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000299761;Note=Putative uncharacterized protein YIR020C-B	
+Q03888	UniProtKB	Sequence conflict	38	38	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region A0A023PZF3 1 158
+A0A023PZF3	UniProtKB	Chain	1	158	.	.	.	ID=PRO_0000431037;Note=Putative uncharacterized protein YIL071W-A	
+A0A023PZF3	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZF3	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZJ9 1 123
+A0A023PZJ9	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000431038;Note=Putative uncharacterized protein YIL115W-A	
+##sequence-region P0CF21 1 127
+P0CF21	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000393393;Note=Putative truncated L-serine dehydratase YIL168W	
+P0CF21	UniProtKB	Modified residue	39	39	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q7LHG5 1 1498
+Q7LHG5	UniProtKB	Chain	1	1498	.	.	.	ID=PRO_0000279367;Note=Transposon Ty3-I Gag-Pol polyprotein	
+Q7LHG5	UniProtKB	Chain	1	207	.	.	.	ID=PRO_0000279368;Note=Capsid protein	
+Q7LHG5	UniProtKB	Peptide	208	233	.	.	.	ID=PRO_0000279369;Note=Spacer peptide p3	
+Q7LHG5	UniProtKB	Chain	234	309	.	.	.	ID=PRO_0000279370;Note=Nucleocapsid protein p11	
+Q7LHG5	UniProtKB	Chain	310	442	.	.	.	ID=PRO_0000279371;Note=Ty3 protease	
+Q7LHG5	UniProtKB	Peptide	443	561	.	.	.	ID=PRO_0000279372;Note=Spacer peptide J;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q7LHG5	UniProtKB	Chain	562	1037	.	.	.	ID=PRO_0000279373;Note=Reverse transcriptase/ribonuclease H	
+Q7LHG5	UniProtKB	Chain	1038	1498	.	.	.	ID=PRO_0000279374;Note=Integrase p52	
+Q7LHG5	UniProtKB	Chain	1064	1498	.	.	.	ID=PRO_0000279375;Note=Integrase p49	
+Q7LHG5	UniProtKB	Domain	646	823	.	.	.	Note=Reverse transcriptase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405	
+Q7LHG5	UniProtKB	Domain	919	1037	.	.	.	Note=RNase H Ty3/gyspy-type	
+Q7LHG5	UniProtKB	Domain	1185	1350	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q7LHG5	UniProtKB	Zinc finger	265	282	.	.	.	Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+Q7LHG5	UniProtKB	Region	1132	1171	.	.	.	Note=Integrase-type zinc finger-like	
+Q7LHG5	UniProtKB	Active site	336	336	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q7LHG5	UniProtKB	Metal binding	712	712	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q7LHG5	UniProtKB	Metal binding	774	774	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q7LHG5	UniProtKB	Metal binding	775	775	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q7LHG5	UniProtKB	Metal binding	1201	1201	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q7LHG5	UniProtKB	Metal binding	1262	1262	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q7LHG5	UniProtKB	Site	207	208	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q7LHG5	UniProtKB	Site	233	234	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q7LHG5	UniProtKB	Site	309	310	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q7LHG5	UniProtKB	Site	442	443	.	.	.	Note=Cleavage%3B by Ty3 protease;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q7LHG5	UniProtKB	Site	561	562	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q7LHG5	UniProtKB	Site	1037	1038	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q7LHG5	UniProtKB	Site	1063	1064	.	.	.	Note=Cleavage%3B by Ty3 protease%3B partial	
+Q7LHG5	UniProtKB	Sequence conflict	502	502	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40520 1 121
+P40520	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40520	UniProtKB	Chain	24	121	.	.	.	ID=PRO_0000202985;Note=Uncharacterized protein YIL059C	
+P40520	UniProtKB	Glycosylation	68	68	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40520	UniProtKB	Glycosylation	84	84	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53039 1 248
+P53039	UniProtKB	Chain	1	248	.	.	.	ID=PRO_0000066269;Note=Protein transport protein YIP1	
+P53039	UniProtKB	Topological domain	1	110	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53039	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53039	UniProtKB	Topological domain	132	132	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53039	UniProtKB	Transmembrane	133	153	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53039	UniProtKB	Topological domain	154	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53039	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53039	UniProtKB	Topological domain	194	196	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53039	UniProtKB	Transmembrane	197	217	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53039	UniProtKB	Topological domain	218	227	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53039	UniProtKB	Transmembrane	228	248	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53039	UniProtKB	Mutagenesis	70	70	.	.	.	Note=In YIP1-41%3B lethal%3B abolishes binding to YIF1%2C YPT1 and YPT31. In YIP1-40%3B temperature sensitive%3B reduces binding to YPT31%2C and inhibits ER vesicle budding%3B when associated with A-130. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160	
+P53039	UniProtKB	Mutagenesis	70	70	.	.	.	Note=In YIP1-4%3B temperature sensitive%3B reduces binding to YIF1%2C YPT1 and YPT31. In YIP1-44%3B lethal%3B when associated with E-130. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160	
+P53039	UniProtKB	Mutagenesis	70	70	.	.	.	Note=In YIP1-42%3B temperature sensitive%3B abolishes binding to YPT1 and YPT31%2C and inhibits ER vesicle budding. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160	
+P53039	UniProtKB	Mutagenesis	76	76	.	.	.	Note=In YIP1-6%3B lethal%3B reduces binding to YIF1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160	
+P53039	UniProtKB	Mutagenesis	81	81	.	.	.	Note=In YIP1-9%3B lethal. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160	
+P53039	UniProtKB	Mutagenesis	114	114	.	.	.	Note=In YIP1-1%3B blocks ER-Golgi protein transport%2C and causes a severe growth defect at 36 degrees Celsius%3B when associated with E-129. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9724632;Dbxref=PMID:9724632	
+P53039	UniProtKB	Mutagenesis	129	129	.	.	.	Note=In YIP1-1%3B blocks ER-Golgi protein transport%2C and causes a severe growth defect at 36 degrees Celsius%3B when associated with L-114. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9724632;Dbxref=PMID:9724632	
+P53039	UniProtKB	Mutagenesis	130	130	.	.	.	Note=In YIP1-40%3B temperature sensitive%3B reduces binding to YPT31%2C and inhibits ER vesicle budding%3B when associated with G-70. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160	
+P53039	UniProtKB	Mutagenesis	130	130	.	.	.	Note=In YIP1-44%3B lethal%3B when associated with K-70. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160	
+P53039	UniProtKB	Mutagenesis	153	155	.	.	.	Note=In YIP1-12%3B abolishes binding to YPT1 and YPT31. LMS->GGG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160	
+P53039	UniProtKB	Mutagenesis	175	175	.	.	.	Note=In YIP1-2%3B abolishes binding to YPT1 and YPT31%2C reduces binding to YIF1%2C blocks ER-Golgi protein transport%2C and causes a severe growth defect at 36 degrees Celsius. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9724632;Dbxref=PMID:9724632	
+P53039	UniProtKB	Mutagenesis	177	177	.	.	.	Note=In YIP1-18%3B abolishes binding to YIF1%2C YPT1 and YPT31. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160	
+P53039	UniProtKB	Mutagenesis	180	180	.	.	.	Note=In YIP1-19%3B lethal%3B abolishes binding to YPT1 and YPT31%2C and reduces binding to YIF1. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160	
+##sequence-region P40446 1 119
+P40446	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000204050;Note=Putative nitrilase-like protein YIL165C	
+P40446	UniProtKB	Domain	1	82	.	.	.	Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P40446	UniProtKB	Active site	21	21	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q8TGN3 1 28
+Q8TGN3	UniProtKB	Chain	1	28	.	.	.	ID=PRO_0000299762;Note=Uncharacterized protein YJL077W-A	
+##sequence-region P47151 1 130
+P47151	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000203113;Note=Putative uncharacterized protein YJR114W	
+##sequence-region P47174 1 117
+P47174	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000203127;Note=Uncharacterized protein YJR146W	
+##sequence-region P47063 1 138
+P47063	UniProtKB	Chain	1	138	.	.	.	ID=PRO_0000203072;Note=Uncharacterized protein YJL027C	
+##sequence-region P40365 1 116
+P40365	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000203055;Note=Putative uncharacterized protein YJL067W	
+P40365	UniProtKB	Transmembrane	40	60	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40365	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5P2 1 29
+P0C5P2	UniProtKB	Chain	1	29	.	.	.	ID=PRO_0000309040;Note=Uncharacterized protein YKL100W-A	
+##sequence-region P36155 1 307
+P36155	UniProtKB	Chain	1	307	.	.	.	ID=PRO_0000203222;Note=Uncharacterized protein YKR075C	
+P36155	UniProtKB	Compositional bias	254	270	.	.	.	Note=His-rich	
+##sequence-region P36092 1 106
+P36092	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000203182;Note=Uncharacterized protein YKL044W	
+P36092	UniProtKB	Transmembrane	85	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P35725 1 167
+P35725	UniProtKB	Chain	1	167	.	.	.	ID=PRO_0000203175;Note=Uncharacterized protein YKL063C	
+##sequence-region P36031 1 110
+P36031	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000203130;Note=Putative UPF0377 protein YKL223W	
+##sequence-region Q2V2P1 1 62
+Q2V2P1	UniProtKB	Chain	1	62	.	.	.	ID=PRO_0000262874;Note=Coiled-coil domain-containing protein YLR146W-A	
+Q2V2P1	UniProtKB	Coiled coil	14	49	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C2I7 1 1755
+P0C2I7	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279109;Note=Transposon Ty1-LR4 Gag-Pol polyprotein	
+P0C2I7	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279110;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I7	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279111;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I7	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279112;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I7	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279113;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I7	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I7	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0C2I7	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+P0C2I7	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I7	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+P0C2I7	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I7	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0C2I7	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P0C2I7	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I7	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I7	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I7	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I7	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I7	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I7	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I7	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I7	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I7	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I7	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I7	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region Q06479 1 807
+Q06479	UniProtKB	Chain	1	807	.	.	.	ID=PRO_0000268189;Note=F-box protein YLR352W	
+Q06479	UniProtKB	Domain	220	266	.	.	.	Note=F-box	
+##sequence-region O13579 1 124
+O13579	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000299645;Note=Putative uncharacterized protein YLR379W	
+O13579	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06051 1 157
+Q06051	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000299646;Note=Putative uncharacterized protein YLR400W	
+Q06051	UniProtKB	Transmembrane	42	64	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGJ4 1 38
+Q8TGJ4	UniProtKB	Chain	1	38	.	.	.	ID=PRO_0000247780;Note=Putative uncharacterized protein YLR466C-B	
+##sequence-region P0C5Q0 1 46
+P0C5Q0	UniProtKB	Chain	1	46	.	.	.	ID=PRO_0000309048;Note=Putative uncharacterized protein YLR154W-F	
+##sequence-region P0CE97 1 114
+P0CE97	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000393295;Note=Putative uncharacterized protein YLR159W	
+##sequence-region P0C5Q1 1 40
+P0C5Q1	UniProtKB	Chain	1	40	.	.	.	ID=PRO_0000309049;Note=Uncharacterized protein YLR364C-A	
+##sequence-region Q8TGJ7 1 56
+Q8TGJ7	UniProtKB	Chain	1	56	.	.	.	ID=PRO_0000247154;Note=Uncharacterized protein YLL066W-B	
+Q8TGJ7	UniProtKB	Compositional bias	20	51	.	.	.	Note=His/Thr-rich	
+##sequence-region P53956 1 172
+P53956	UniProtKB	Chain	1	172	.	.	.	ID=PRO_0000203454;Note=Uncharacterized endoplasmic reticulum membrane protein YNL046W	
+P53956	UniProtKB	Topological domain	1	101	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53956	UniProtKB	Transmembrane	102	122	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53956	UniProtKB	Topological domain	123	145	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53956	UniProtKB	Transmembrane	146	164	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53956	UniProtKB	Topological domain	165	172	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53948 1 110
+P53948	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000203450;Note=Putative uncharacterized protein YNL057W	
+##sequence-region Q08465 1 219
+Q08465	UniProtKB	Chain	1	219	.	.	.	ID=PRO_0000240248;Note=Protein YNG1	
+Q08465	UniProtKB	Zinc finger	155	204	.	.	.	Note=PHD-type%3B degenerate	
+Q08465	UniProtKB	Metal binding	158	158	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Metal binding	160	160	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Metal binding	171	171	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Metal binding	176	176	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Metal binding	182	182	.	.	.	Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Metal binding	185	185	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Metal binding	198	198	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Metal binding	202	202	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Binding site	157	157	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Binding site	168	168	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Binding site	172	172	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Binding site	180	180	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+Q08465	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JMI	
+Q08465	UniProtKB	Beta strand	165	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JMI	
+Q08465	UniProtKB	Beta strand	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JMI	
+Q08465	UniProtKB	Turn	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JMI	
+Q08465	UniProtKB	Helix	200	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JMI	
+##sequence-region P53926 1 123
+P53926	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000203434;Note=Putative uncharacterized protein YNL114C	
+P53926	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53926	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53922 1 161
+P53922	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000203431;Note=Putative uncharacterized protein YNL120C	
+##sequence-region P40162 1 140
+P40162	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000203393;Note=Putative uncharacterized protein YNL205C	
+##sequence-region Q99248 1 730
+Q99248	UniProtKB	Chain	1	730	.	.	.	ID=PRO_0000235938;Note=Uncharacterized protein YOR019W	
+##sequence-region Q3E735 1 80
+Q3E735	UniProtKB	Chain	1	80	.	.	.	ID=PRO_0000237646;Note=Uncharacterized membrane protein YOR034C-A	
+Q3E735	UniProtKB	Transmembrane	10	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08504 1 108
+Q08504	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000299712;Note=Uncharacterized protein YOR105W	
+Q08504	UniProtKB	Compositional bias	46	97	.	.	.	Note=Ile-rich	
+##sequence-region Q08532 1 130
+Q08532	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08532	UniProtKB	Chain	21	130	.	.	.	ID=PRO_0000299716;Note=Putative uncharacterized protein YOR139C	
+##sequence-region P0C5R0 1 36
+P0C5R0	UniProtKB	Chain	1	36	.	.	.	ID=PRO_0000309058;Note=Putative uncharacterized protein YOR314W-A	
+##sequence-region Q08321 1 113
+Q08321	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000299698;Note=Uncharacterized protein YOL160W	
+##sequence-region Q8TGJ1 1 51
+Q8TGJ1	UniProtKB	Chain	1	51	.	.	.	ID=PRO_0000211379;Note=UPF0320 protein YOL166W-A	
+##sequence-region Q08620 1 132
+Q08620	UniProtKB	Chain	1	132	.	.	.	ID=PRO_0000299723;Note=Putative uncharacterized protein YOR200W	
+##sequence-region Q12439 1 438
+Q12439	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000279345;Note=Transposon Ty2-OR1 Gag polyprotein	
+Q12439	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279346;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12439	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000279347;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12439	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12439	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12293 1 438
+Q12293	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000279353;Note=Transposon Ty2-OR2 Gag polyprotein	
+Q12293	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279354;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12293	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000279355;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12293	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12293	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q8TGL2 1 66
+Q8TGL2	UniProtKB	Chain	1	66	.	.	.	ID=PRO_0000299727;Note=Putative uncharacterized protein YOR231C-A	
+##sequence-region Q08728 1 135
+Q08728	UniProtKB	Chain	1	135	.	.	.	ID=PRO_0000299730;Note=Putative uncharacterized protein YOR263C	
+Q08728	UniProtKB	Compositional bias	57	63	.	.	.	Note=Poly-Ser	
+##sequence-region Q08373 1 112
+Q08373	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000299699;Note=Putative uncharacterized protein YOL166C	
+Q08373	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08373	UniProtKB	Transmembrane	69	89	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12402 1 180
+Q12402	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378	
+Q12402	UniProtKB	Chain	2	180	.	.	.	ID=PRO_0000101859;Note=Protein YOP1	
+Q12402	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12402	UniProtKB	Transmembrane	61	81	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12402	UniProtKB	Transmembrane	89	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12402	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12402	UniProtKB	Region	2	17	.	.	.	Note=Interaction with YIP1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278413;Dbxref=PMID:11278413	
+Q12402	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378	
+##sequence-region Q02659 1 185
+Q02659	UniProtKB	Chain	1	185	.	.	.	ID=PRO_0000299797;Note=Putative uncharacterized protein YPL025C	
+Q02659	UniProtKB	Compositional bias	110	117	.	.	.	Note=Poly-Phe	
+##sequence-region Q3E7B4 1 63
+Q3E7B4	UniProtKB	Chain	1	63	.	.	.	ID=PRO_0000238636;Note=Uncharacterized protein YPL038W-A	
+##sequence-region Q02781 1 134
+Q02781	UniProtKB	Chain	1	134	.	.	.	ID=PRO_0000299800;Note=Uncharacterized protein YPL062W	
+##sequence-region Q02754 1 198
+Q02754	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000238641;Note=Uncharacterized protein YPL067C	
+Q02754	UniProtKB	Sequence conflict	78	78	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02754	UniProtKB	Helix	18	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Helix	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Helix	37	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Helix	55	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Helix	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Beta strand	86	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Beta strand	101	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Helix	119	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Helix	140	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Beta strand	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Turn	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Beta strand	163	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Turn	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+Q02754	UniProtKB	Helix	179	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI	
+##sequence-region Q02831 1 240
+Q02831	UniProtKB	Chain	1	240	.	.	.	ID=PRO_0000238644;Note=Uncharacterized protein YPL077C	
+Q02831	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02831	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region O13586 1 101
+O13586	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000299822;Note=Putative uncharacterized protein YPR092W	
+##sequence-region O13548 1 118
+O13548	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000299824;Note=Putative uncharacterized protein YPR099C	
+##sequence-region O13519 1 122
+O13519	UniProtKB	Signal peptide	1	33	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13519	UniProtKB	Chain	34	122	.	.	.	ID=PRO_0000299805;Note=Putative uncharacterized protein YPL136W	
+##sequence-region Q2V2P0 1 78
+Q2V2P0	UniProtKB	Chain	1	78	.	.	.	ID=PRO_0000242692;Note=Uncharacterized protein YPR145C-A	
+##sequence-region Q6Q5H1 1 440
+Q6Q5H1	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279189;Note=Transposon Ty1-PR3 Gag polyprotein	
+Q6Q5H1	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279190;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q6Q5H1	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279191;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q6Q5H1	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q6Q5H1	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q6Q5H1	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q6Q5H1	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+Q6Q5H1	UniProtKB	Sequence conflict	199	199	.	.	.	Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12042 1 273
+Q12042	UniProtKB	Chain	1	273	.	.	.	ID=PRO_0000238655;Note=Vacuolar membrane protein YPL162C	
+Q12042	UniProtKB	Topological domain	1	13	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12042	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12042	UniProtKB	Topological domain	35	51	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12042	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12042	UniProtKB	Topological domain	73	97	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12042	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12042	UniProtKB	Topological domain	119	156	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12042	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12042	UniProtKB	Topological domain	178	198	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12042	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12042	UniProtKB	Topological domain	220	273	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08930 1 360
+Q08930	UniProtKB	Chain	1	360	.	.	.	ID=PRO_0000238658;Note=Ubiquitin carboxyl-terminal hydrolase MIY1	
+Q08930	UniProtKB	Active site	28	28	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N5J2	
+Q08930	UniProtKB	Active site	216	216	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N5J2	
+Q08930	UniProtKB	Site	296	296	.	.	.	Note=Ubiquitin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N5J2	
+Q08930	UniProtKB	Site	299	300	.	.	.	Note=Ubiquitin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N5J2	
+Q08930	UniProtKB	Site	303	303	.	.	.	Note=Ubiquitin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N5J2	
+##sequence-region Q08958 1 114
+Q08958	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000299809;Note=Putative uncharacterized protein YPL205C	
+Q08958	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q99395 1 206
+Q99395	UniProtKB	Chain	1	206	.	.	.	ID=PRO_0000242135;Note=Uncharacterized protein YPL229W	
+Q99395	UniProtKB	Compositional bias	40	65	.	.	.	Note=Gln-rich	
+Q99395	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q12179 1 454
+Q12179	UniProtKB	Chain	1	454	.	.	.	ID=PRO_0000242145;Note=Uncharacterized protein YPL245W	
+##sequence-region Q08977 1 551
+Q08977	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000255978;Note=UPF0662 protein YPL260W	
+Q08977	UniProtKB	Coiled coil	174	213	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08977	UniProtKB	Coiled coil	249	300	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08977	UniProtKB	Sequence conflict	90	90	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08977	UniProtKB	Sequence conflict	128	128	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38298 1 316
+P38298	UniProtKB	Chain	1	316	.	.	.	ID=PRO_0000212466;Note=Alkaline ceramidase YPC1	
+P38298	UniProtKB	Topological domain	1	68	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Transmembrane	69	89	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Topological domain	90	93	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Topological domain	115	135	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Topological domain	157	160	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Topological domain	182	195	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Transmembrane	196	216	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Topological domain	217	228	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Transmembrane	229	249	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38298	UniProtKB	Topological domain	250	316	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07688 1 167
+Q07688	UniProtKB	Chain	1	167	.	.	.	ID=PRO_0000262758;Note=Phosphorelay intermediate protein YPD1	
+Q07688	UniProtKB	Domain	24	129	.	.	.	Note=HPt;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00110	
+Q07688	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphohistidine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00110,ECO:0000269|PubMed:8808622;Dbxref=PMID:8808622	
+Q07688	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Loss of function. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8808622;Dbxref=PMID:8808622	
+Q07688	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Reduces binding of the 4-aspartylphosphate of SLN1. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15628880;Dbxref=PMID:15628880	
+Q07688	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Reduces phosphoryl transfer rate. G->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15628880;Dbxref=PMID:15628880	
+Q07688	UniProtKB	Mutagenesis	74	74	.	.	.	Note=In NH1%3B causes resistance to the antifungal antibiotic pradimicin. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15015733;Dbxref=PMID:15015733	
+Q07688	UniProtKB	Mutagenesis	86	86	.	.	.	Note=Reduces phosphoryl transfer rate. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15628880;Dbxref=PMID:15628880	
+Q07688	UniProtKB	Mutagenesis	90	90	.	.	.	Note=Reduces phosphoryl transfer rate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15628880;Dbxref=PMID:15628880	
+Q07688	UniProtKB	Helix	11	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+Q07688	UniProtKB	Turn	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+Q07688	UniProtKB	Helix	26	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+Q07688	UniProtKB	Helix	56	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+Q07688	UniProtKB	Helix	76	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+Q07688	UniProtKB	Helix	99	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+Q07688	UniProtKB	Helix	109	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+Q07688	UniProtKB	Beta strand	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+Q07688	UniProtKB	Turn	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+Q07688	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+Q07688	UniProtKB	Helix	135	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+##sequence-region P53819 1 1859
+P53819	UniProtKB	Chain	1	1859	.	.	.	ID=PRO_0000102205;Note=Y' element ATP-dependent helicase protein 1 copy 6	
+P53819	UniProtKB	Domain	861	1038	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53819	UniProtKB	Domain	1095	1244	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P53819	UniProtKB	Nucleotide binding	874	881	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region P53584 1 459
+P53584	UniProtKB	Chain	1	459	.	.	.	ID=PRO_0000066529;Note=Protein YTP1	
+P53584	UniProtKB	Topological domain	1	6	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Topological domain	28	59	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Transmembrane	60	80	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Topological domain	81	82	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Transmembrane	83	103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Topological domain	104	122	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Topological domain	144	170	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Topological domain	192	205	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Transmembrane	206	226	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Topological domain	227	266	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Topological domain	288	295	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Transmembrane	296	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Topological domain	317	322	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Transmembrane	323	343	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Topological domain	344	351	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Transmembrane	352	372	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Topological domain	373	389	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Transmembrane	390	410	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53584	UniProtKB	Topological domain	411	459	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E741 1 30
+Q3E741	UniProtKB	Chain	1	30	.	.	.	ID=PRO_0000248427;Note=Putative uncharacterized protein YAL037C-A	
+##sequence-region Q3E791 1 96
+Q3E791	UniProtKB	Chain	1	96	.	.	.	ID=PRO_0000248428;Note=Uncharacterized protein YAL063C-A	
+##sequence-region O13588 1 104
+O13588	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000299789;Note=Putative uncharacterized protein YAL069W	
+##sequence-region A0A023PXA5 1 189
+A0A023PXA5	UniProtKB	Chain	1	189	.	.	.	ID=PRO_0000430976;Note=Putative uncharacterized protein YAL019W-A	
+##sequence-region P39559 1 98
+P39559	UniProtKB	Chain	1	98	.	.	.	ID=PRO_0000202429;Note=Putative uncharacterized protein YA5053W	
+P39559	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39559	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39563 1 99
+P39563	UniProtKB	Chain	1	99	.	.	.	ID=PRO_0000202433;Note=Uncharacterized protein YAR064W	
+P39563	UniProtKB	Transmembrane	74	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39566 1 99
+P39566	UniProtKB	Chain	1	99	.	.	.	ID=PRO_0000202436;Note=Putative uncharacterized protein YAR070C	
+##sequence-region Q08182 1 245
+Q08182	UniProtKB	Chain	1	245	.	.	.	ID=PRO_0000076527;Note=AP-1-like transcription factor YAP7	
+Q08182	UniProtKB	Domain	125	188	.	.	.	Note=bZIP	
+Q08182	UniProtKB	Region	130	149	.	.	.	Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08182	UniProtKB	Region	153	181	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38294 1 104
+P38294	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000202503;Note=Putative uncharacterized protein YBR174C	
+##sequence-region Q8TGK4 1 73
+Q8TGK4	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000248446;Note=Uncharacterized protein YBR298C-A	
+Q8TGK4	UniProtKB	Sequence conflict	48	48	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q8TGK4	UniProtKB	Sequence conflict	48	48	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q8TGK4	UniProtKB	Sequence conflict	48	48	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q8TGK4	UniProtKB	Sequence conflict	48	48	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38299 1 523
+P38299	UniProtKB	Chain	1	523	.	.	.	ID=PRO_0000202505;Note=Uncharacterized protein YBR184W	
+##sequence-region P38306 1 217
+P38306	UniProtKB	Chain	1	217	.	.	.	ID=PRO_0000202508;Note=Uncharacterized protein YBR197C	
+##sequence-region I2HB52 1 66
+I2HB52	UniProtKB	Chain	1	66	.	.	.	ID=PRO_0000419187;Note=Uncharacterized protein YBR056W-A	
+I2HB52	UniProtKB	Compositional bias	26	29	.	.	.	Note=Poly-Pro	
+I2HB52	UniProtKB	Compositional bias	33	62	.	.	.	Note=Cys-rich	
+##sequence-region P38161 1 101
+P38161	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000202438;Note=Putative UPF0377 protein YBL108W	
+##sequence-region P38233 1 116
+P38233	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000202475;Note=Putative uncharacterized protein YBR051W	
+P38233	UniProtKB	Transmembrane	24	44	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38233	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38235 1 358
+P38235	UniProtKB	Chain	1	358	.	.	.	ID=PRO_0000173052;Note=Uncharacterized protein YBR053C	
+P38235	UniProtKB	Sequence conflict	178	178	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38268 1 175
+P38268	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000202488;Note=Putative uncharacterized protein YBR116C	
+P38268	UniProtKB	Transmembrane	143	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38269 1 119
+P38269	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000202489;Note=Putative uncharacterized protein YBR124W	
+P38269	UniProtKB	Transmembrane	80	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGQ2 1 116
+Q8TGQ2	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q8TGQ2	UniProtKB	Chain	22	116	.	.	.	ID=PRO_0000299837;Note=Putative uncharacterized protein YCR045W-A	
+##sequence-region Q3E830 1 75
+Q3E830	UniProtKB	Chain	1	75	.	.	.	ID=PRO_0000248451;Note=Uncharacterized protein YCR075W-A	
+Q3E830	UniProtKB	Beta strand	11	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM	
+Q3E830	UniProtKB	Beta strand	21	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM	
+Q3E830	UniProtKB	Helix	27	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM	
+Q3E830	UniProtKB	Helix	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM	
+Q3E830	UniProtKB	Helix	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM	
+Q3E830	UniProtKB	Beta strand	47	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM	
+Q3E830	UniProtKB	Beta strand	66	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM	
+##sequence-region Q3E7Z8 1 88
+Q3E7Z8	UniProtKB	Chain	1	88	.	.	.	ID=PRO_0000248452;Note=Uncharacterized protein YCR024C-B	
+Q3E7Z8	UniProtKB	Transmembrane	5	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E7Z8	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25384 1 1770
+P25384	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000199562;Note=Transposon Ty2-C Gag-Pol polyprotein	
+P25384	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279278;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25384	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000279279;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25384	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000279280;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25384	UniProtKB	Chain	1233	1770	.	.	.	ID=PRO_0000279281;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25384	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P25384	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P25384	UniProtKB	Domain	1625	1767	.	.	.	Note=RNase H Ty1/copia-type	
+P25384	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25384	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+P25384	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25384	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25384	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P25384	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P25384	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P25384	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P25384	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P25384	UniProtKB	Metal binding	1625	1625	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P25384	UniProtKB	Metal binding	1667	1667	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P25384	UniProtKB	Metal binding	1700	1700	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P25384	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25384	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25384	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25384	UniProtKB	Sequence conflict	460	460	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25384	UniProtKB	Sequence conflict	460	460	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25384	UniProtKB	Sequence conflict	629	629	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25384	UniProtKB	Sequence conflict	629	629	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25384	UniProtKB	Sequence conflict	814	814	.	.	.	Note=S->SA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25384	UniProtKB	Sequence conflict	814	814	.	.	.	Note=S->SA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25384	UniProtKB	Sequence conflict	1577	1578	.	.	.	Note=AQ->LN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25384	UniProtKB	Sequence conflict	1577	1578	.	.	.	Note=AQ->LN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25563 1 115
+P25563	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000202542;Note=Putative uncharacterized protein YCL023C	
+##sequence-region P25600 1 308
+P25600	UniProtKB	Chain	1	308	.	.	.	ID=PRO_0000203503;Note=Putative transposon Ty5-1 protein YCL074W	
+##sequence-region P39978 1 195
+P39978	UniProtKB	Chain	1	195	.	.	.	ID=PRO_0000202602;Note=Uncharacterized protein YEL067C	
+##sequence-region P39972 1 122
+P39972	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000202598;Note=Uncharacterized protein YEL075C	
+##sequence-region P40049 1 302
+P40049	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40049	UniProtKB	Chain	24	302	.	.	.	ID=PRO_0000014316;Note=Putative uncharacterized protein YER076C	
+P40049	UniProtKB	Glycosylation	65	65	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40049	UniProtKB	Glycosylation	86	86	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40049	UniProtKB	Glycosylation	93	93	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40049	UniProtKB	Glycosylation	220	220	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40049	UniProtKB	Glycosylation	231	231	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CL27 1 191
+P0CL27	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL27	UniProtKB	Chain	18	191	.	.	.	ID=PRO_0000299916;Note=Putative uncharacterized protein YER190C-A	
+P0CL27	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL27	UniProtKB	Compositional bias	13	159	.	.	.	Note=Gly/Ser-rich	
+##sequence-region Q07451 1 203
+Q07451	UniProtKB	Chain	1	203	.	.	.	ID=PRO_0000248402;Note=Endoplasmic reticulum transmembrane protein 3	
+Q07451	UniProtKB	Topological domain	1	6	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07451	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07451	UniProtKB	Topological domain	28	45	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07451	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07451	UniProtKB	Topological domain	67	110	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07451	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07451	UniProtKB	Topological domain	132	203	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGU2 1 87
+Q8TGU2	UniProtKB	Chain	1	87	.	.	.	ID=PRO_0000245375;Note=Uncharacterized protein YFR032C-B	
+Q8TGU2	UniProtKB	Transmembrane	20	42	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43580 1 148
+P43580	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000202679;Note=Uncharacterized protein YFL012W	
+##sequence-region P43564 1 1073
+P43564	UniProtKB	Chain	1	1073	.	.	.	ID=PRO_0000202674;Note=Uncharacterized membrane protein YFL034W	
+P43564	UniProtKB	Topological domain	1	552	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43564	UniProtKB	Transmembrane	553	573	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43564	UniProtKB	Topological domain	574	576	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43564	UniProtKB	Transmembrane	577	597	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43564	UniProtKB	Topological domain	598	694	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43564	UniProtKB	Transmembrane	695	715	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43564	UniProtKB	Topological domain	716	752	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43564	UniProtKB	Transmembrane	753	773	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43564	UniProtKB	Topological domain	774	1073	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43564	UniProtKB	Modified residue	435	435	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43564	UniProtKB	Modified residue	1037	1037	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43564	UniProtKB	Sequence conflict	323	323	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43546 1 152
+P43546	UniProtKB	Chain	1	152	.	.	.	ID=PRO_0000070371;Note=Putative aryl-alcohol dehydrogenase YFL057C	
+##sequence-region P43622 1 192
+P43622	UniProtKB	Chain	1	192	.	.	.	ID=PRO_0000202699;Note=Uncharacterized protein YFR054C	
+##sequence-region P53151 1 121
+P53151	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000202756;Note=Uncharacterized protein YGL088W	
+P53151	UniProtKB	Transmembrane	26	46	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53151	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53084 1 216
+P53084	UniProtKB	Chain	1	216	.	.	.	ID=PRO_0000202716;Note=Putative uncharacterized protein YGL218W	
+##sequence-region P53066 1 181
+P53066	UniProtKB	Chain	1	181	.	.	.	ID=PRO_0000067245;Note=Ankyrin repeat-containing protein YGL242C	
+P53066	UniProtKB	Repeat	49	78	.	.	.	Note=ANK 1	
+P53066	UniProtKB	Repeat	85	120	.	.	.	Note=ANK 2	
+P53066	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53066	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region O13533 1 98
+O13533	UniProtKB	Chain	1	98	.	.	.	ID=PRO_0000299926;Note=Putative uncharacterized protein YHR049C-A	
+O13533	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13533	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CL33 1 64
+P0CL33	UniProtKB	Chain	1	64	.	.	.	ID=PRO_0000406009;Note=Putative uncharacterized protein YHR054W-A	
+P0CL33	UniProtKB	Transmembrane	33	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZE1 1 111
+A0A023PZE1	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000431022;Note=Putative uncharacterized membrane protein YHR063W-A	
+A0A023PZE1	UniProtKB	Transmembrane	7	29	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZE1	UniProtKB	Transmembrane	49	71	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZE1	UniProtKB	Compositional bias	77	110	.	.	.	Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016	
+##sequence-region A0A023PZE4 1 103
+A0A023PZE4	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000431027;Note=Putative uncharacterized protein YHR165W-A	
+A0A023PZE4	UniProtKB	Compositional bias	24	97	.	.	.	Note=Gly-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00008	
+##sequence-region P0C5N5 1 34
+P0C5N5	UniProtKB	Chain	1	34	.	.	.	ID=PRO_0000309033;Note=Putative uncharacterized protein YHR180C-B	
+##sequence-region O13534 1 161
+O13534	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000202944;Note=Putative uncharacterized protein YHR214W-A	
+##sequence-region P0CX19 1 203
+P0CX19	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX19	UniProtKB	Chain	24	184	.	.	.	ID=PRO_0000409754;Note=Putative GPI-anchored protein YHR214W	
+P0CX19	UniProtKB	Propeptide	185	203	.	.	.	ID=PRO_0000409755;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX19	UniProtKB	Compositional bias	25	57	.	.	.	Note=Ser-rich	
+P0CX19	UniProtKB	Lipidation	184	184	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX19	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX19	UniProtKB	Glycosylation	138	138	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX93 1 97
+P0CX93	UniProtKB	Chain	1	97	.	.	.	ID=PRO_0000410451;Note=Uncharacterized protein YHR214C-D	
+P0CX93	UniProtKB	Transmembrane	5	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX93	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX93	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q6Q5P6 1 413
+Q6Q5P6	UniProtKB	Chain	1	413	.	.	.	ID=PRO_0000279381;Note=Transposon Ty4-H Gag polyprotein	
+Q6Q5P6	UniProtKB	Coiled coil	39	115	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38745 1 532
+P38745	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Chain	21	532	.	.	.	ID=PRO_0000014326;Note=Uncharacterized membrane protein YHL071W	
+P38745	UniProtKB	Topological domain	21	193	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Transmembrane	194	214	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Topological domain	215	226	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Transmembrane	227	247	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Topological domain	248	262	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Transmembrane	263	283	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Topological domain	284	301	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Transmembrane	302	322	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Topological domain	323	330	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Transmembrane	331	351	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Topological domain	352	375	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Transmembrane	376	396	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Topological domain	397	414	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Transmembrane	415	435	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Topological domain	436	532	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Modified residue	497	497	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38745	UniProtKB	Glycosylation	152	152	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38745	UniProtKB	Glycosylation	253	253	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38740 1 315
+P38740	UniProtKB	Chain	1	315	.	.	.	ID=PRO_0000014325;Note=Uncharacterized protein YHL026C	
+P38740	UniProtKB	Transmembrane	18	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38740	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38740	UniProtKB	Transmembrane	244	264	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38775 1 560
+P38775	UniProtKB	Chain	1	560	.	.	.	ID=PRO_0000202893;Note=Putative uncharacterized protein YHR045W	
+P38775	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38775	UniProtKB	Transmembrane	61	81	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38775	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38775	UniProtKB	Transmembrane	305	325	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38775	UniProtKB	Transmembrane	442	462	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04013 1 314
+Q04013	UniProtKB	Chain	1	314	.	.	.	ID=PRO_0000090688;Note=Citrate/oxoglutarate carrier protein	
+Q04013	UniProtKB	Transmembrane	23	44	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04013	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04013	UniProtKB	Transmembrane	111	127	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04013	UniProtKB	Transmembrane	178	198	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04013	UniProtKB	Transmembrane	218	238	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04013	UniProtKB	Transmembrane	273	294	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04013	UniProtKB	Repeat	18	100	.	.	.	Note=Solcar 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00282	
+Q04013	UniProtKB	Repeat	107	199	.	.	.	Note=Solcar 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00282	
+Q04013	UniProtKB	Repeat	217	301	.	.	.	Note=Solcar 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00282	
+Q04013	UniProtKB	DNA binding	246	259	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9742088;Dbxref=PMID:9742088	
+Q04013	UniProtKB	Mutagenesis	249	253	.	.	.	Note=Fails to bind DNA in vitro. PNRPK->GGGGG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9742088;Dbxref=PMID:9742088	
+##sequence-region Q04116 1 353
+Q04116	UniProtKB	Chain	1	353	.	.	.	ID=PRO_0000049386;Note=Homeobox protein YHP1	
+Q04116	UniProtKB	DNA binding	173	232	.	.	.	Note=Homeobox;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108	
+Q04116	UniProtKB	Modified residue	315	315	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q03885 1 199
+Q03885	UniProtKB	Chain	1	199	.	.	.	ID=PRO_0000299759;Note=Putative uncharacterized protein YIR017W-A	
+Q03885	UniProtKB	Transmembrane	40	60	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03885	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03885	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03885	UniProtKB	Transmembrane	166	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03885	UniProtKB	Sequence conflict	185	185	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03885	UniProtKB	Sequence conflict	198	199	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region A0A023PZJ3 1 112
+A0A023PZJ3	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000431032;Note=Putative uncharacterized membrane protein YIL030W-A	
+A0A023PZJ3	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXF8 1 147
+A0A023PXF8	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000431035;Note=Putative uncharacterized membrane protein YIL066W-A	
+A0A023PXF8	UniProtKB	Transmembrane	13	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q2V2P5 1 75
+Q2V2P5	UniProtKB	Chain	1	75	.	.	.	ID=PRO_0000245402;Note=Uncharacterized protein YIL102C-A	
+Q2V2P5	UniProtKB	Transmembrane	5	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q2V2P5	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q2V2P4 1 73
+Q2V2P4	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q2V2P4	UniProtKB	Chain	23	73	.	.	.	ID=PRO_0000245400;Note=Uncharacterized protein YIL156W-B	
+##sequence-region Q03886 1 80
+Q03886	UniProtKB	Chain	1	80	.	.	.	ID=PRO_0000299760;Note=Putative uncharacterized protein YIR020W-A	
+##sequence-region P40543 1 189
+P40543	UniProtKB	Chain	1	189	.	.	.	ID=PRO_0000203000;Note=Uncharacterized protein YIL024C	
+P40543	UniProtKB	Modified residue	107	107	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40543	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40508 1 320
+P40508	UniProtKB	Chain	1	320	.	.	.	ID=PRO_0000202980;Note=Uncharacterized protein YIL077C	
+P40508	UniProtKB	Modified residue	230	230	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q06596 1 294
+Q06596	UniProtKB	Chain	1	294	.	.	.	ID=PRO_0000076528;Note=AP-1-like transcription factor YAP8	
+Q06596	UniProtKB	Domain	22	72	.	.	.	Note=bZIP	
+Q06596	UniProtKB	Region	22	45	.	.	.	Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06596	UniProtKB	Region	44	72	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P40017 1 923
+P40017	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40017	UniProtKB	Chain	2	923	.	.	.	ID=PRO_0000210176;Note=Carnitine O-acetyltransferase YAT2	
+P40017	UniProtKB	Region	530	541	.	.	.	Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40017	UniProtKB	Binding site	576	576	.	.	.	Note=Carnitine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40017	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40017	UniProtKB	Modified residue	783	783	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P0C269 1 39
+P0C269	UniProtKB	Chain	1	39	.	.	.	ID=PRO_0000268623;Note=Uncharacterized protein YBL100W-C	
+##sequence-region P0C5L2 1 88
+P0C5L2	UniProtKB	Chain	1	88	.	.	.	ID=PRO_0000309010;Note=Putative uncharacterized protein YBR076C-A	
+P0C5L2	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C5L2	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E7Y4 1 105
+Q3E7Y4	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000248407;Note=Putative uncharacterized helicase-like protein YBL112C	
+Q3E7Y4	UniProtKB	Domain	2	44	.	.	.	Note=Helicase C-terminal	
+##sequence-region Q12266 1 440
+Q12266	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000278990;Note=Transposon Ty1-BL Gag polyprotein	
+Q12266	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000278991;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12266	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000278992;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12266	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12266	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12490 1 1755
+Q12490	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000278985;Note=Transposon Ty1-BL Gag-Pol polyprotein	
+Q12490	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000278986;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12490	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000278987;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12490	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000278988;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12490	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000278989;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12490	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12490	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12490	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q12490	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12490	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q12490	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12490	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q12490	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12490	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12490	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12490	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12490	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12490	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12490	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12490	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12490	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12490	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12490	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q3E776 1 120
+Q3E776	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000248444;Note=Uncharacterized protein YBR255C-A	
+Q3E776	UniProtKB	Transmembrane	22	44	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E776	UniProtKB	Glycosylation	114	114	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38201 1 376
+P38201	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000202461;Note=Uncharacterized protein YBL029W	
+##sequence-region P38194 1 122
+P38194	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000202459;Note=Uncharacterized protein YBL044W	
+##sequence-region P34224 1 193
+P34224	UniProtKB	Chain	1	193	.	.	.	ID=PRO_0000202454;Note=Uncharacterized protein YBL059W	
+P34224	UniProtKB	Transmembrane	119	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38180 1 368
+P38180	UniProtKB	Chain	1	368	.	.	.	ID=PRO_0000202447;Note=Uncharacterized protein YBL081W	
+##sequence-region P38220 1 110
+P38220	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000202471;Note=Uncharacterized protein YBR027C	
+P38220	UniProtKB	Transmembrane	6	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38220	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q96VH1 1 84
+Q96VH1	UniProtKB	Chain	1	84	.	.	.	ID=PRO_0000299835;Note=Putative uncharacterized protein YCR018C-A	
+Q96VH1	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q96VH1	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E787 1 52
+Q3E787	UniProtKB	Chain	1	52	.	.	.	ID=PRO_0000248453;Note=Putative uncharacterized protein YCR095W-A	
+##sequence-region Q3E819 1 63
+Q3E819	UniProtKB	Chain	1	63	.	.	.	ID=PRO_0000248454;Note=Uncharacterized protein YCR108C	
+##sequence-region P37263 1 153
+P37263	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000202578;Note=UPF0743 protein YCR087C-A	
+P37263	UniProtKB	Zinc finger	1	26	.	.	.	Note=C2HC LYAR-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01145	
+P37263	UniProtKB	Zinc finger	27	52	.	.	.	Note=C2HC LYAR-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01145	
+##sequence-region P42937 1 148
+P42937	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000202844;Note=CDC25-like phosphatase YCH1	
+P42937	UniProtKB	Domain	29	137	.	.	.	Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+P42937	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P42937	UniProtKB	Beta strand	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FS5	
+P42937	UniProtKB	Beta strand	8	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Helix	14	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Turn	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Beta strand	33	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FS5	
+P42937	UniProtKB	Helix	56	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Helix	63	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Beta strand	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Beta strand	84	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Beta strand	91	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Helix	96	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Helix	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Beta strand	116	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Helix	124	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Turn	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Beta strand	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+P42937	UniProtKB	Helix	144	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A	
+##sequence-region P25347 1 104
+P25347	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000202559;Note=Uncharacterized protein YCR001W	
+##sequence-region P25354 1 239
+P25354	UniProtKB	Chain	1	239	.	.	.	ID=PRO_0000207531;Note=DUP240 protein YCR007C	
+P25354	UniProtKB	Topological domain	1	54	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25354	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25354	UniProtKB	Topological domain	76	79	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25354	UniProtKB	Transmembrane	80	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25354	UniProtKB	Topological domain	105	239	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25354	UniProtKB	Natural variant	2	2	.	.	.	Note=In strain: CLIB 219. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P25354	UniProtKB	Natural variant	42	42	.	.	.	Note=In strain: CLIB 219%2C CLIB 410%2C CLIB 413%2C CLIB 630 haplotype Ha1%2C K1%2C YIIc12 haplotype Ha2 and CLIB 382. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P25354	UniProtKB	Natural variant	215	215	.	.	.	Note=In strain: CLIB 630. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+##sequence-region P25654 1 182
+P25654	UniProtKB	Chain	1	182	.	.	.	ID=PRO_0000202580;Note=UPF0587 protein YCR090C	
+##sequence-region Q12195 1 79
+Q12195	UniProtKB	Chain	1	79	.	.	.	ID=PRO_0000299869;Note=Putative uncharacterized protein YDR015C	
+##sequence-region P0C1Z1 1 29
+P0C1Z1	UniProtKB	Chain	1	29	.	.	.	ID=PRO_0000253882;Note=Uncharacterized protein YDR524W-C	
+##sequence-region Q04408 1 483
+Q04408	UniProtKB	Chain	1	483	.	.	.	ID=PRO_0000253854;Note=Uncharacterized protein YDR514C	
+##sequence-region Q03049 1 344
+Q03049	UniProtKB	Chain	1	344	.	.	.	ID=PRO_0000253887;Note=Putative uncharacterized oxidoreductase YDR541C	
+Q03049	UniProtKB	Sequence conflict	341	341	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03049	UniProtKB	Sequence conflict	341	341	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q3E7B7 1 68
+Q3E7B7	UniProtKB	Chain	1	68	.	.	.	ID=PRO_0000268193;Note=SERF-like protein YDL085C-A	
+Q3E7B7	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q12331 1 272
+Q12331	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12331	UniProtKB	Chain	27	272	.	.	.	ID=PRO_0000008801;Note=FAS1 domain-containing protein YDR262W	
+Q12331	UniProtKB	Domain	100	269	.	.	.	Note=FAS1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00082	
+##sequence-region P43551 1 465
+P43551	UniProtKB	Chain	1	465	.	.	.	ID=PRO_0000114996;Note=Uncharacterized transcriptional regulatory protein YFL052W	
+P43551	UniProtKB	DNA binding	8	34	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P43624 1 122
+P43624	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000202700;Note=Putative uncharacterized protein YFR056C	
+P43624	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43624	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGU0 1 28
+Q8TGU0	UniProtKB	Chain	1	28	.	.	.	ID=PRO_0000245380;Note=Uncharacterized protein YGL007C-A	
+##sequence-region Q8TGP1 1 76
+Q8TGP1	UniProtKB	Chain	1	76	.	.	.	ID=PRO_0000299920;Note=Putative uncharacterized protein YGL123C-A	
+##sequence-region P0CX67 1 440
+P0CX67	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000409782;Note=Transposon Ty1-GR3 Gag polyprotein	
+P0CX67	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000409783;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX67	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000409784;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX67	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX67	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX67	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX67	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q8TGU1 1 46
+Q8TGU1	UniProtKB	Chain	1	46	.	.	.	ID=PRO_0000245378;Note=Uncharacterized protein YGL188C-A	
+##sequence-region P53212 1 290
+P53212	UniProtKB	Chain	1	290	.	.	.	ID=PRO_0000175945;Note=Probable transcriptional regulatory protein HAH1	
+##sequence-region Q8TGN7 1 72
+Q8TGN7	UniProtKB	Chain	1	72	.	.	.	ID=PRO_0000299924;Note=Putative uncharacterized protein YGR270C-A	
+Q8TGN7	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53243 1 804
+P53243	UniProtKB	Chain	1	804	.	.	.	ID=PRO_0000046863;Note=Zinc finger protein YGR067C	
+P53243	UniProtKB	Zinc finger	8	30	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P53243	UniProtKB	Zinc finger	36	59	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+##sequence-region P53182 1 67
+P53182	UniProtKB	Chain	1	67	.	.	.	ID=PRO_0000202771;Note=Putative uncharacterized protein YGL041C	
+P53182	UniProtKB	Transmembrane	13	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53182	UniProtKB	Transmembrane	42	64	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53139 1 140
+P53139	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53139	UniProtKB	Chain	2	140	.	.	.	ID=PRO_0000202751;Note=Uncharacterized protein YGL108C	
+P53139	UniProtKB	Compositional bias	41	49	.	.	.	Note=Poly-Lys	
+P53139	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53139	UniProtKB	Lipidation	4	4	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53116 1 101
+P53116	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53116	UniProtKB	Chain	19	101	.	.	.	ID=PRO_0000014321;Note=Uncharacterized protein YGL149W	
+P53116	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53116	UniProtKB	Compositional bias	24	28	.	.	.	Note=Poly-Leu	
+##sequence-region P53105 1 115
+P53105	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000202726;Note=Putative uncharacterized protein YGL177W	
+##sequence-region P53100 1 379
+P53100	UniProtKB	Chain	1	379	.	.	.	ID=PRO_0000076037;Note=Putative 2-hydroxyacid dehydrogenase YGL185C	
+P53100	UniProtKB	Nucleotide binding	207	208	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53100	UniProtKB	Nucleotide binding	291	293	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53100	UniProtKB	Nucleotide binding	341	344	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53100	UniProtKB	Active site	293	293	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53100	UniProtKB	Active site	322	322	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53100	UniProtKB	Active site	341	341	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53100	UniProtKB	Binding site	317	317	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53089 1 101
+P53089	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000202719;Note=Uncharacterized protein YGL204C	
+P53089	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53089	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PYG1 1 162
+A0A023PYG1	UniProtKB	Chain	1	162	.	.	.	ID=PRO_0000431014;Note=Putative uncharacterized membrane protein YHL002C-A	
+A0A023PYG1	UniProtKB	Transmembrane	132	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXE8 1 106
+A0A023PXE8	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000431017;Note=Putative uncharacterized protein YHR028W-A	
+##sequence-region Q8TGT5 1 39
+Q8TGT5	UniProtKB	Chain	1	39	.	.	.	ID=PRO_0000299925;Note=Putative uncharacterized protein YHR032C-A	
+##sequence-region P38899 1 603
+P38899	UniProtKB	Chain	1	603	.	.	.	ID=PRO_0000202947;Note=Putative uncharacterized protein YHR218W	
+##sequence-region P38730 1 149
+P38730	UniProtKB	Chain	1	149	.	.	.	ID=PRO_0000202878;Note=Uncharacterized protein YHL041W	
+P38730	UniProtKB	Sequence conflict	124	124	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38727 1 235
+P38727	UniProtKB	Chain	1	235	.	.	.	ID=PRO_0000207533;Note=DUP240 protein YHL044W	
+P38727	UniProtKB	Topological domain	1	44	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38727	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38727	UniProtKB	Topological domain	66	72	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38727	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38727	UniProtKB	Topological domain	94	235	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38727	UniProtKB	Natural variant	9	9	.	.	.	Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	47	47	.	.	.	Note=In strain: CLIB 219%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C YIIc12 haplotype Ha2 and YIIc17 haplotype Ha2. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	75	75	.	.	.	Note=In strain: CLIB 95%2C CLIB 382%2C CLIB 556 haplotype Ha1%2C K1%2C R12%2C R13%2C YIIc12 haplotype Ha1 and YIIc17 haplotype Ha1. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	77	77	.	.	.	Note=In strain: CLIB 388. L->F	
+P38727	UniProtKB	Natural variant	86	86	.	.	.	Note=In strain: CLIB 388. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	96	96	.	.	.	Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	103	103	.	.	.	Note=In strain: CLIB 388%2C CLIB 410%2C CLIB 556 haplotype Ha2%2C CLIB 630%2C YIIc12 haplotype Ha2 and YIIc17 haplotype Ha2. R->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	124	124	.	.	.	Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	145	145	.	.	.	Note=In strain: R12 haplotype Ha2. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	157	157	.	.	.	Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	160	160	.	.	.	Note=In strain: CLIB 556 haplotype Ha1. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	180	180	.	.	.	Note=In strain: CLIB 95%2C CLIB 382%2C K1%2C R12%2C R13%2C YIIc12 haplotype Ha1 and YIIc17 haplotype Ha1. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	189	189	.	.	.	Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	225	235	.	.	.	Note=In strain: CLIB 630. EDKYPEMGVTV->RISIQRWGTQF	
+P38727	UniProtKB	Natural variant	233	233	.	.	.	Note=In strain: CLIB 219%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C YIIc12 haplotype Ha2 and YIIc17 haplotype Ha2. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38727	UniProtKB	Natural variant	234	234	.	.	.	Note=In strain: CLIB 413 haplotype Ha1. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+##sequence-region P38765 1 294
+P38765	UniProtKB	Chain	1	294	.	.	.	ID=PRO_0000162387;Note=Uncharacterized isomerase YHI9	
+P38765	UniProtKB	Active site	52	52	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38765	UniProtKB	Beta strand	3	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	19	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Helix	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Helix	38	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	53	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	65	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Helix	81	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	101	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	110	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	120	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Helix	135	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	154	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Helix	170	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Helix	180	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	194	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	209	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Helix	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	221	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Helix	228	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	248	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Helix	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	262	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	276	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+P38765	UniProtKB	Beta strand	284	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5	
+##sequence-region P38690 1 423
+P38690	UniProtKB	Chain	1	423	.	.	.	ID=PRO_0000109779;Note=Uncharacterized protein YHR033W	
+P38690	UniProtKB	Domain	315	406	.	.	.	Note=PUA	
+P38690	UniProtKB	Nucleotide binding	170	171	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38690	UniProtKB	Nucleotide binding	214	220	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38690	UniProtKB	Binding site	51	51	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38690	UniProtKB	Binding site	138	138	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38690	UniProtKB	Binding site	150	150	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38690	UniProtKB	Sequence conflict	117	117	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38769 1 630
+P38769	UniProtKB	Chain	1	630	.	.	.	ID=PRO_0000202891;Note=Uncharacterized protein YHR035W	
+##sequence-region P38842 1 239
+P38842	UniProtKB	Chain	1	239	.	.	.	ID=PRO_0000202921;Note=UPF0641 membrane protein YHR140W	
+P38842	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Transmembrane	12	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Topological domain	32	45	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Topological domain	67	99	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Topological domain	121	125	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Transmembrane	126	146	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Topological domain	147	162	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Transmembrane	163	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Topological domain	184	204	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Transmembrane	205	225	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38842	UniProtKB	Topological domain	226	239	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q02598 1 104
+Q02598	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000245404;Note=Uncharacterized protein YIL014C-A	
+##sequence-region A0A023PXN9 1 150
+A0A023PXN9	UniProtKB	Chain	1	150	.	.	.	ID=PRO_0000431040;Note=Putative uncharacterized membrane protein YIL171W-A	
+A0A023PXN9	UniProtKB	Transmembrane	15	35	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXN9	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXN9	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXN9	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40521 1 94
+P40521	UniProtKB	Chain	1	94	.	.	.	ID=PRO_0000202986;Note=Putative uncharacterized protein YIL058W	
+P40521	UniProtKB	Natural variant	7	7	.	.	.	Note=In strain: CEN.PK 113-7D. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430	
+P40521	UniProtKB	Natural variant	40	40	.	.	.	Note=In strain: CEN.PK 113-7D. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430	
+P40521	UniProtKB	Natural variant	49	49	.	.	.	Note=In strain: CEN.PK 113-7D. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430	
+P40521	UniProtKB	Natural variant	70	71	.	.	.	Note=In strain: CEN.PK 113-7D. IL->VF	
+##sequence-region P40519 1 144
+P40519	UniProtKB	Chain	1	144	.	.	.	ID=PRO_0000202984;Note=Uncharacterized protein YIL060W	
+P40519	UniProtKB	Transmembrane	72	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40455 1 235
+P40455	UniProtKB	Chain	1	235	.	.	.	ID=PRO_0000202956;Note=Uncharacterized protein YIL152W	
+##sequence-region P53093 1 235
+P53093	UniProtKB	Chain	1	235	.	.	.	ID=PRO_0000202721;Note=Protein YIP4	
+P53093	UniProtKB	Transmembrane	89	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53093	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53093	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53093	UniProtKB	Transmembrane	186	206	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53093	UniProtKB	Transmembrane	215	235	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX74 1 440
+P0CX74	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000203496;Note=Transposon Ty1-JR1 Gag polyprotein	
+P0CX74	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279086;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX74	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279087;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX74	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX74	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX74	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX74	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q3E828 1 52
+Q3E828	UniProtKB	Chain	1	52	.	.	.	ID=PRO_0000245410;Note=UPF0618 protein YJL127C-B	
+Q3E828	UniProtKB	Transmembrane	28	46	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E801 1 27
+Q3E801	UniProtKB	Chain	1	27	.	.	.	ID=PRO_0000245408;Note=Uncharacterized protein YJL136W-A	
+##sequence-region P0C5N9 1 73
+P0C5N9	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000309037;Note=Putative uncharacterized protein YJL156W-A	
+P0C5N9	UniProtKB	Transmembrane	54	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47023 1 414
+P47023	UniProtKB	Chain	1	414	.	.	.	ID=PRO_0000203501;Note=Transposon Ty4-J Gag polyprotein	
+P47023	UniProtKB	Coiled coil	39	115	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47121 1 122
+P47121	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47121	UniProtKB	Chain	19	122	.	.	.	ID=PRO_0000014334;Note=Putative uncharacterized protein YJR071W	
+P47121	UniProtKB	Glycosylation	15	15	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47024 1 1803
+P47024	UniProtKB	Chain	1	1803	.	.	.	ID=PRO_0000203502;Note=Transposon Ty4-J Gag-Pol polyprotein	
+P47024	UniProtKB	Domain	620	787	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47024	UniProtKB	Domain	1376	1511	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P47024	UniProtKB	Domain	1645	1791	.	.	.	Note=RNase H Ty1/copia-type	
+P47024	UniProtKB	Region	382	502	.	.	.	Note=Ty4 protease	
+P47024	UniProtKB	Region	540	600	.	.	.	Note=Integrase-type zinc finger-like	
+P47024	UniProtKB	Coiled coil	39	115	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47024	UniProtKB	Active site	415	415	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47024	UniProtKB	Metal binding	631	631	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47024	UniProtKB	Metal binding	696	696	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47024	UniProtKB	Metal binding	1384	1384	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47024	UniProtKB	Metal binding	1463	1463	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47024	UniProtKB	Metal binding	1464	1464	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47024	UniProtKB	Metal binding	1645	1645	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47024	UniProtKB	Metal binding	1687	1687	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47024	UniProtKB	Metal binding	1721	1721	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P47024	UniProtKB	Sequence conflict	452	452	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47024	UniProtKB	Sequence conflict	684	684	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47024	UniProtKB	Sequence conflict	920	920	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47024	UniProtKB	Sequence conflict	1020	1020	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47024	UniProtKB	Sequence conflict	1803	1803	.	.	.	Note=Y->YLINEVLNTQISVEVQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47152 1 169
+P47152	UniProtKB	Chain	1	169	.	.	.	ID=PRO_0000203114;Note=Uncharacterized protein YJR115W	
+##sequence-region P47157 1 116
+P47157	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47157	UniProtKB	Chain	20	116	.	.	.	ID=PRO_0000014335;Note=Putative uncharacterized protein YJR120W	
+P47157	UniProtKB	Sequence conflict	111	111	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47162 1 119
+P47162	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000203119;Note=Uncharacterized protein YJR128W	
+##sequence-region P40361 1 888
+P40361	UniProtKB	Chain	1	888	.	.	.	ID=PRO_0000194416;Note=Inactive deaminase YJL070C	
+P40361	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40361	UniProtKB	Modified residue	41	41	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40361	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40361	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P47009 1 104
+P47009	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000203034;Note=Uncharacterized protein YJL144W	
+P47009	UniProtKB	Compositional bias	72	78	.	.	.	Note=Poly-Asn	
+##sequence-region P46996 1 555
+P46996	UniProtKB	Chain	1	555	.	.	.	ID=PRO_0000203027;Note=Uncharacterized membrane protein YJL163C	
+P46996	UniProtKB	Topological domain	1	83	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Transmembrane	84	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Topological domain	105	125	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Transmembrane	126	146	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Topological domain	147	188	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Topological domain	210	229	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Transmembrane	230	250	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Topological domain	251	257	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Transmembrane	258	278	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Topological domain	279	356	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Transmembrane	357	377	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Topological domain	378	386	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Transmembrane	387	407	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Topological domain	408	428	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Transmembrane	429	449	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Topological domain	450	459	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Transmembrane	460	480	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Topological domain	481	491	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Transmembrane	492	512	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Topological domain	513	523	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Transmembrane	524	544	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46996	UniProtKB	Topological domain	545	555	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46986 1 105
+P46986	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000203022;Note=Putative uncharacterized protein YJL182C	
+P46986	UniProtKB	Transmembrane	41	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39532 1 115
+P39532	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000203016;Note=Putative uncharacterized protein YJL202C	
+P39532	UniProtKB	Transmembrane	69	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40889 1 1758
+P40889	UniProtKB	Chain	1	1758	.	.	.	ID=PRO_0000102208;Note=Y' element ATP-dependent helicase YJL225C	
+P40889	UniProtKB	Domain	668	845	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P40889	UniProtKB	Domain	900	1051	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P40889	UniProtKB	Nucleotide binding	681	688	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region P47094 1 133
+P47094	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000203089;Note=Putative uncharacterized protein YJR023C	
+P47094	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47094	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47094	UniProtKB	Compositional bias	10	30	.	.	.	Note=Poly-Leu	
+P47094	UniProtKB	Sequence conflict	28	28	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q8TGM9 1 89
+Q8TGM9	UniProtKB	Chain	1	89	.	.	.	ID=PRO_0000299767;Note=Putative uncharacterized protein YKR075W-A	
+Q8TGM9	UniProtKB	Transmembrane	39	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGN0 1 38
+Q8TGN0	UniProtKB	Chain	1	38	.	.	.	ID=PRO_0000299766;Note=Putative uncharacterized protein YKL156C-A	
+##sequence-region P36138 1 183
+P36138	UniProtKB	Chain	1	183	.	.	.	ID=PRO_0000203213;Note=Uncharacterized protein YKR045C	
+P36138	UniProtKB	Compositional bias	25	29	.	.	.	Note=Poly-Thr	
+P36138	UniProtKB	Compositional bias	99	108	.	.	.	Note=Gln-rich	
+P36138	UniProtKB	Cross-link	21	21	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P36151 1 352
+P36151	UniProtKB	Chain	1	352	.	.	.	ID=PRO_0000203218;Note=Uncharacterized protein YKR070W	
+P36151	UniProtKB	Beta strand	14	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Turn	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	34	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	59	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	84	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Turn	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	94	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	104	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	114	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	119	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	137	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Turn	148	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	157	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	167	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	200	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	212	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	220	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	249	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	268	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RF6	
+P36151	UniProtKB	Turn	285	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	290	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Turn	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	303	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	313	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	318	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Beta strand	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+P36151	UniProtKB	Helix	340	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2	
+##sequence-region P40544 1 346
+P40544	UniProtKB	Chain	1	346	.	.	.	ID=PRO_0000213698;Note=Zinc transporter YKE4	
+P40544	UniProtKB	Topological domain	1	2	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Topological domain	24	69	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Topological domain	91	99	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Topological domain	121	126	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Transmembrane	127	147	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Topological domain	148	202	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Transmembrane	203	223	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Topological domain	224	252	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Transmembrane	253	273	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Topological domain	274	290	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Transmembrane	291	311	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Topological domain	312	322	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Transmembrane	323	343	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Topological domain	344	346	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Glycosylation	184	184	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Glycosylation	274	274	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40544	UniProtKB	Glycosylation	285	285	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P34251 1 309
+P34251	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000203158;Note=Uncharacterized oxidoreductase YKL107W	
+P34251	UniProtKB	Transmembrane	23	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36073 1 130
+P36073	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000203156;Note=Putative uncharacterized protein YKL115C	
+##sequence-region P36065 1 132
+P36065	UniProtKB	Chain	1	132	.	.	.	ID=PRO_0000203148;Note=Putative uncharacterized protein YKL136W	
+##sequence-region P36042 1 193
+P36042	UniProtKB	Chain	1	193	.	.	.	ID=PRO_0000203134;Note=Putative uncharacterized protein YKL202W	
+P36042	UniProtKB	Compositional bias	100	181	.	.	.	Note=Leu/Phe/Pro/Ser-rich	
+##sequence-region Q02203 1 525
+Q02203	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02203	UniProtKB	Chain	22	525	.	.	.	ID=PRO_0000203192;Note=Uncharacterized protein YKR005C	
+Q02203	UniProtKB	Topological domain	22	448	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02203	UniProtKB	Transmembrane	449	469	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02203	UniProtKB	Topological domain	470	525	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02203	UniProtKB	Compositional bias	304	361	.	.	.	Note=Thr-rich	
+##sequence-region Q8TGM8 1 30
+Q8TGM8	UniProtKB	Chain	1	30	.	.	.	ID=PRO_0000299601;Note=Putative uncharacterized protein YLL019W-A	
+##sequence-region Q07865 1 126
+Q07865	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000299604;Note=Putative uncharacterized protein YLL037W	
+Q07865	UniProtKB	Transmembrane	5	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07989 1 106
+Q07989	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000299608;Note=Putative uncharacterized protein YLR041W	
+##sequence-region Q12253 1 270
+Q12253	UniProtKB	Chain	1	270	.	.	.	ID=PRO_0000247195;Note=Uncharacterized membrane protein YLR046C	
+Q12253	UniProtKB	Topological domain	1	37	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Topological domain	59	65	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Topological domain	87	93	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Topological domain	115	140	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Topological domain	162	181	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Topological domain	203	220	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Transmembrane	221	241	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12253	UniProtKB	Topological domain	242	270	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12026 1 108
+Q12026	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000247206;Note=Putative uncharacterized protein YLR053C	
+##sequence-region Q12177 1 298
+Q12177	UniProtKB	Chain	1	298	.	.	.	ID=PRO_0000247152;Note=Uncharacterized protein YLL056C	
+##sequence-region P25575 1 107
+P25575	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000202548;Note=Putative uncharacterized protein YCL046W	
+##sequence-region P25602 1 247
+P25602	UniProtKB	Chain	1	247	.	.	.	ID=PRO_0000202558;Note=Putative uncharacterized protein YCL076W	
+##sequence-region P37265 1 110
+P37265	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000202567;Note=Uncharacterized protein YCR041W	
+P37265	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37265	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37265	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25652 1 171
+P25652	UniProtKB	Chain	1	171	.	.	.	ID=PRO_0000202579;Note=Putative uncharacterized protein YCR087W	
+##sequence-region Q12115 1 100
+Q12115	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299844;Note=Putative uncharacterized protein YDL016C	
+Q12115	UniProtKB	Compositional bias	41	95	.	.	.	Note=Ser-rich	
+##sequence-region P0C5L6 1 82
+P0C5L6	UniProtKB	Chain	1	82	.	.	.	ID=PRO_0000309014;Note=Uncharacterized protein YDL022C-A	
+##sequence-region A0A023PXH9 1 235
+A0A023PXH9	UniProtKB	Chain	1	235	.	.	.	ID=PRO_0000430981;Note=Putative uncharacterized membrane protein YDR149C	
+A0A023PXH9	UniProtKB	Transmembrane	167	187	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXH9	UniProtKB	Transmembrane	190	210	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12394 1 121
+Q12394	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000299857;Note=Putative uncharacterized protein YDL152W	
+Q12394	UniProtKB	Transmembrane	65	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12394	UniProtKB	Compositional bias	5	54	.	.	.	Note=Ser-rich	
+##sequence-region P0C2I3 1 1755
+P0C2I3	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279032;Note=Transposon Ty1-DR6 Gag-Pol polyprotein	
+P0C2I3	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279033;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I3	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279034;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I3	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279035;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I3	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279036;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I3	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I3	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0C2I3	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+P0C2I3	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I3	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+P0C2I3	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I3	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0C2I3	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P0C2I3	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I3	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I3	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I3	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I3	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I3	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I3	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I3	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I3	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I3	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I3	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I3	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region A0A023PXI4 1 105
+A0A023PXI4	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXI4	UniProtKB	Chain	25	105	.	.	.	ID=PRO_0000430983;Note=Putative uncharacterized protein YDR203W	
+##sequence-region Q03480 1 137
+Q03480	UniProtKB	Chain	1	137	.	.	.	ID=PRO_0000299875;Note=Uncharacterized protein YDR209C	
+Q03480	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q00590 1 100
+Q00590	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299748;Note=Putative uncharacterized protein YDL213W-A	
+Q00590	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12392 1 438
+Q12392	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000279289;Note=Transposon Ty2-DR1 Gag polyprotein	
+Q12392	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279290;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12392	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000279291;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12392	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12392	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03483 1 438
+Q03483	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000279297;Note=Transposon Ty2-DR2 Gag polyprotein	
+Q03483	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279298;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03483	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000279299;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03483	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03483	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q07738 1 123
+Q07738	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000242485;Note=Uncharacterized protein YDL241W	
+##sequence-region Q06640 1 478
+Q06640	UniProtKB	Chain	1	478	.	.	.	ID=PRO_0000253805;Note=F-box protein YDR306C	
+Q06640	UniProtKB	Domain	112	173	.	.	.	Note=F-box	
+Q06640	UniProtKB	Compositional bias	81	90	.	.	.	Note=Poly-Ser	
+##sequence-region P87287 1 132
+P87287	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87287	UniProtKB	Chain	25	132	.	.	.	ID=PRO_0000253845;Note=Uncharacterized protein YDR366C	
+P87287	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87287	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5M2 1 81
+P0C5M2	UniProtKB	Chain	1	81	.	.	.	ID=PRO_0000309020;Note=Putative uncharacterized protein YDR406W-A	
+P0C5M2	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C5M2	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q2V2P7 1 80
+Q2V2P7	UniProtKB	Chain	1	80	.	.	.	ID=PRO_0000253852;Note=Uncharacterized protein YDR461C-A	
+##sequence-region P87272 1 115
+P87272	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000299900;Note=Putative uncharacterized protein YDR509W	
+P87272	UniProtKB	Transmembrane	5	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87272	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5M4 1 75
+P0C5M4	UniProtKB	Chain	1	75	.	.	.	ID=PRO_0000309022;Note=Putative uncharacterized protein YDL185C-A	
+##sequence-region Q12147 1 103
+Q12147	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000299847;Note=Putative uncharacterized protein YDL026W	
+Q12147	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12147	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12426 1 110
+Q12426	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000299868;Note=Uncharacterized protein YDR010C	
+##sequence-region A0A023PXI8 1 105
+A0A023PXI8	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000430989;Note=Putative uncharacterized protein YER006C-A	
+##sequence-region Q8TGP2 1 70
+Q8TGP2	UniProtKB	Chain	1	70	.	.	.	ID=PRO_0000299911;Note=Putative uncharacterized protein YER023C-A	
+##sequence-region A0A023PZF5 1 109
+A0A023PZF5	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000430992;Note=Putative uncharacterized protein YER046W-A	
+##sequence-region A0A023PXC7 1 143
+A0A023PXC7	UniProtKB	Chain	1	143	.	.	.	ID=PRO_0000430994;Note=Putative uncharacterized membrane protein YER068C-A	
+A0A023PXC7	UniProtKB	Transmembrane	20	39	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXC7	UniProtKB	Transmembrane	113	135	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX16 1 216
+P0CX16	UniProtKB	Chain	1	216	.	.	.	ID=PRO_0000268170;Note=Putative uncharacterized protein YEL076C-A	
+##sequence-region A0A023PZB8 1 112
+A0A023PZB8	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000430995;Note=Putative uncharacterized membrane protein YER079C-A	
+A0A023PZB8	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZB8	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P87191 1 123
+P87191	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000299914;Note=Putative uncharacterized protein YER119C-A	
+##sequence-region A0A023PYF4 1 145
+A0A023PYF4	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PYF4	UniProtKB	Chain	27	145	.	.	.	ID=PRO_0000431001;Note=Uncharacterized protein YER145C-A	
+##sequence-region Q8TGR3 1 71
+Q8TGR3	UniProtKB	Chain	1	71	.	.	.	ID=PRO_0000299915;Note=Putative uncharacterized protein YER158W-A	
+Q8TGR3	UniProtKB	Transmembrane	44	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39961 1 794
+P39961	UniProtKB	Chain	1	794	.	.	.	ID=PRO_0000114995;Note=Uncharacterized transcriptional regulatory protein YER184C	
+P39961	UniProtKB	DNA binding	18	44	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P39961	UniProtKB	Metal binding	18	18	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39961	UniProtKB	Metal binding	18	18	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39961	UniProtKB	Metal binding	21	21	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39961	UniProtKB	Metal binding	28	28	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39961	UniProtKB	Metal binding	34	34	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39961	UniProtKB	Metal binding	34	34	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39961	UniProtKB	Metal binding	37	37	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39961	UniProtKB	Metal binding	44	44	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P39953 1 335
+P39953	UniProtKB	Chain	1	335	.	.	.	ID=PRO_0000090694;Note=Mitochondrial nicotinamide adenine dinucleotide transporter 2	
+P39953	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39953	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39953	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39953	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39953	UniProtKB	Transmembrane	247	267	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39953	UniProtKB	Transmembrane	298	318	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39953	UniProtKB	Repeat	36	128	.	.	.	Note=Solcar 1	
+P39953	UniProtKB	Repeat	136	225	.	.	.	Note=Solcar 2	
+P39953	UniProtKB	Repeat	241	329	.	.	.	Note=Solcar 3	
+##sequence-region P40095 1 573
+P40095	UniProtKB	Chain	1	573	.	.	.	ID=PRO_0000202656;Note=Uncharacterized protein YER158C	
+P40095	UniProtKB	Repeat	102	103	.	.	.	Note=1	
+P40095	UniProtKB	Repeat	104	105	.	.	.	Note=2	
+P40095	UniProtKB	Repeat	106	107	.	.	.	Note=3	
+P40095	UniProtKB	Repeat	108	109	.	.	.	Note=4	
+P40095	UniProtKB	Repeat	110	111	.	.	.	Note=5	
+P40095	UniProtKB	Repeat	112	113	.	.	.	Note=6	
+P40095	UniProtKB	Repeat	114	115	.	.	.	Note=7	
+P40095	UniProtKB	Repeat	116	117	.	.	.	Note=8	
+P40095	UniProtKB	Repeat	118	119	.	.	.	Note=9	
+P40095	UniProtKB	Repeat	120	121	.	.	.	Note=10	
+P40095	UniProtKB	Region	102	121	.	.	.	Note=10 X 2 AA tandem repeats of N-M	
+P40095	UniProtKB	Glycosylation	63	63	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40095	UniProtKB	Glycosylation	123	123	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40095	UniProtKB	Glycosylation	236	236	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40095	UniProtKB	Glycosylation	437	437	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40095	UniProtKB	Glycosylation	442	442	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40095	UniProtKB	Glycosylation	498	498	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40095	UniProtKB	Glycosylation	535	535	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40095	UniProtKB	Glycosylation	541	541	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5N0 1 62
+P0C5N0	UniProtKB	Chain	1	62	.	.	.	ID=PRO_0000309028;Note=Uncharacterized protein YFR010W-A	
+P0C5N0	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C5N0	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXD9 1 105
+A0A023PXD9	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000431010;Note=Putative uncharacterized membrane protein YFL015W-A	
+A0A023PXD9	UniProtKB	Transmembrane	25	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGU3 1 33
+Q8TGU3	UniProtKB	Chain	1	33	.	.	.	ID=PRO_0000299659;Note=Putative uncharacterized protein YFL031C-A	
+##sequence-region Q12085 1 440
+Q12085	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279058;Note=Transposon Ty1-GR1 Gag polyprotein	
+Q12085	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279059;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12085	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279060;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12085	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12085	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12085	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q12485 1 440
+Q12485	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279066;Note=Transposon Ty1-GR2 Gag polyprotein	
+Q12485	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279067;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12485	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279068;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12485	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12485	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q12485	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12485	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q12269 1 1755
+Q12269	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279061;Note=Transposon Ty1-GR2 Gag-Pol polyprotein	
+Q12269	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279062;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12269	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279063;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12269	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279064;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12269	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279065;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12269	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12269	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12269	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q12269	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12269	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q12269	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12269	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q12269	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q12269	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12269	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12269	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12269	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12269	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12269	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12269	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12269	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12269	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12269	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12269	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12269	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region P53209 1 190
+P53209	UniProtKB	Chain	1	190	.	.	.	ID=PRO_0000202783;Note=Uncharacterized membrane protein YGR016W	
+P53209	UniProtKB	Topological domain	1	55	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53209	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53209	UniProtKB	Topological domain	77	80	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53209	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53209	UniProtKB	Topological domain	102	123	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53209	UniProtKB	Transmembrane	124	144	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53209	UniProtKB	Topological domain	145	149	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53209	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53209	UniProtKB	Topological domain	171	190	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53211 1 109
+P53211	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000202785;Note=Uncharacterized protein YGR018C	
+##sequence-region P53231 1 118
+P53231	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000202797;Note=Uncharacterized protein YGR050C	
+##sequence-region P0CX62 1 438
+P0CX62	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000409814;Note=Transposon Ty2-GR2 Gag polyprotein	
+P0CX62	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000409815;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX62	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000409816;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX62	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX62	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38722 1 271
+P38722	UniProtKB	Chain	1	271	.	.	.	ID=PRO_0000202876;Note=Uncharacterized protein YHL049C	
+##sequence-region A0A023PXG3 1 133
+A0A023PXG3	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000431042;Note=Putative uncharacterized membrane protein YIL156W-A	
+A0A023PXG3	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXG3	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40539 1 132
+P40539	UniProtKB	Chain	1	132	.	.	.	ID=PRO_0000202997;Note=Putative uncharacterized protein YIL028W	
+##sequence-region P40448 1 117
+P40448	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000202951;Note=Uncharacterized protein YIL163C	
+##sequence-region P40442 1 995
+P40442	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40442	UniProtKB	Chain	24	995	.	.	.	ID=PRO_0000014330;Note=Putative uncharacterized protein YIL169C	
+P40442	UniProtKB	Domain	26	253	.	.	.	Note=Methyl-accepting transducer;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00284	
+P40442	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40442	UniProtKB	Glycosylation	35	35	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40442	UniProtKB	Glycosylation	468	468	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40442	UniProtKB	Glycosylation	664	664	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGT2 1 49
+Q8TGT2	UniProtKB	Chain	1	49	.	.	.	ID=PRO_0000245420;Note=Uncharacterized protein YKL096C-B	
+Q8TGT2	UniProtKB	Transmembrane	31	48	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36128 1 141
+P36128	UniProtKB	Chain	1	141	.	.	.	ID=PRO_0000203207;Note=Putative uncharacterized protein YKR033C	
+##sequence-region P36086 1 256
+P36086	UniProtKB	Chain	1	256	.	.	.	ID=PRO_0000203171;Note=Uncharacterized oxidoreductase YKL071W	
+P36086	UniProtKB	Nucleotide binding	13	19	.	.	.	Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36086	UniProtKB	Active site	164	164	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36086	UniProtKB	Binding site	148	148	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P34248 1 587
+P34248	UniProtKB	Chain	1	587	.	.	.	ID=PRO_0000073915;Note=Probable intramembrane protease YKL100C	
+P34248	UniProtKB	Topological domain	1	85	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Topological domain	107	156	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Topological domain	178	192	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Transmembrane	193	213	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Topological domain	214	303	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Transmembrane	304	324	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Topological domain	325	328	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Transmembrane	329	349	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Topological domain	350	351	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Transmembrane	352	372	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Topological domain	373	401	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Transmembrane	402	422	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Topological domain	423	450	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Transmembrane	451	471	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Topological domain	472	475	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Transmembrane	476	496	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Topological domain	497	587	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34248	UniProtKB	Motif	477	479	.	.	.	Note=PAL	
+P34248	UniProtKB	Compositional bias	550	587	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P34248	UniProtKB	Active site	366	366	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34248	UniProtKB	Active site	411	411	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P36072 1 103
+P36072	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000203155;Note=Putative uncharacterized protein YKL118W	
+##sequence-region P36058 1 169
+P36058	UniProtKB	Chain	1	169	.	.	.	ID=PRO_0000203145;Note=Putative uncharacterized protein YKL153W	
+##sequence-region P36114 1 725
+P36114	UniProtKB	Chain	1	725	.	.	.	ID=PRO_0000203198;Note=Mitochondrial outer membrane protein YKR018C	
+P36114	UniProtKB	Transmembrane	296	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36114	UniProtKB	Transmembrane	341	361	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36114	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36114	UniProtKB	Modified residue	246	246	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36114	UniProtKB	Modified residue	377	377	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36114	UniProtKB	Modified residue	380	380	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P36114	UniProtKB	Beta strand	55	57	.	.	.	.	
+##sequence-region P35995 1 705
+P35995	UniProtKB	Chain	1	705	.	.	.	ID=PRO_0000115000;Note=Uncharacterized transcriptional regulatory protein YKL222C	
+P35995	UniProtKB	DNA binding	24	52	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region Q02209 1 353
+Q02209	UniProtKB	Chain	1	353	.	.	.	ID=PRO_0000203194;Note=Uncharacterized protein YKR011C	
+##sequence-region Q3E814 1 58
+Q3E814	UniProtKB	Chain	1	58	.	.	.	ID=PRO_0000247097;Note=Uncharacterized protein YLL006W-A	
+Q3E814	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C2I6 1 1755
+P0C2I6	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279104;Note=Transposon Ty1-LR3 Gag-Pol polyprotein	
+P0C2I6	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279105;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I6	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279106;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I6	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279107;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I6	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279108;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I6	UniProtKB	Domain	660	829	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I6	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0C2I6	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+P0C2I6	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I6	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+P0C2I6	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I6	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0C2I6	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P0C2I6	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I6	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I6	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I6	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I6	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I6	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I6	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I6	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I6	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I6	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I6	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I6	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region P0CY02 1 43
+P0CY02	UniProtKB	Chain	1	43	.	.	.	ID=PRO_0000410458;Note=Uncharacterized protein YLR154C-H	
+##sequence-region Q06235 1 118
+Q06235	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000262878;Note=Protein YLR162W	
+Q06235	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06251 1 628
+Q06251	UniProtKB	Chain	1	628	.	.	.	ID=PRO_0000247127;Note=Uncharacterized protein YLR177W	
+Q06251	UniProtKB	Domain	472	565	.	.	.	Note=PSP1 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00744	
+Q06251	UniProtKB	Compositional bias	154	169	.	.	.	Note=Poly-Gln	
+Q06251	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06251	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06251	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06251	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06251	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q06267 1 115
+Q06267	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000299620;Note=Putative uncharacterized protein YLR184W	
+##sequence-region Q05777 1 254
+Q05777	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05777	UniProtKB	Chain	18	232	.	.	.	ID=PRO_0000247130;Note=Cell wall protein YLR194C	
+Q05777	UniProtKB	Propeptide	233	254	.	.	.	ID=PRO_0000247131;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05777	UniProtKB	Compositional bias	104	206	.	.	.	Note=Ser-rich	
+Q05777	UniProtKB	Lipidation	232	232	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05777	UniProtKB	Glycosylation	229	229	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C2J4 1 438
+P0C2J4	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000279329;Note=Transposon Ty2-LR1 Gag polyprotein	
+P0C2J4	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279330;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J4	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000279331;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J4	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J4	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P0C2J3 1 1770
+P0C2J3	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000279324;Note=Transposon Ty2-LR1 Gag-Pol polyprotein	
+P0C2J3	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279325;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J3	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000279326;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J3	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000279327;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J3	UniProtKB	Chain	1233	1770	.	.	.	ID=PRO_0000279328;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J3	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J3	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0C2J3	UniProtKB	Domain	1625	1767	.	.	.	Note=RNase H Ty1/copia-type	
+P0C2J3	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J3	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+P0C2J3	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J3	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J3	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J3	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J3	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J3	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J3	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J3	UniProtKB	Metal binding	1625	1625	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J3	UniProtKB	Metal binding	1667	1667	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J3	UniProtKB	Metal binding	1700	1700	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J3	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J3	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J3	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q8TGR0 1 75
+Q8TGR0	UniProtKB	Chain	1	75	.	.	.	ID=PRO_0000299651;Note=Putative uncharacterized protein YLR437C-A	
+##sequence-region Q8TGM1 1 34
+Q8TGM1	UniProtKB	Chain	1	34	.	.	.	ID=PRO_0000299752;Note=Putative uncharacterized protein YLR399W-A	
+##sequence-region Q06057 1 63
+Q06057	UniProtKB	Chain	1	63	.	.	.	ID=PRO_0000299647;Note=Putative uncharacterized protein YLR402W	
+Q06057	UniProtKB	Transmembrane	15	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E742 1 68
+Q3E742	UniProtKB	Chain	1	68	.	.	.	ID=PRO_0000247219;Note=Uncharacterized protein YLR412C-A	
+Q3E742	UniProtKB	Compositional bias	19	59	.	.	.	Note=Lys-rich	
+##sequence-region Q06695 1 132
+Q06695	UniProtKB	Chain	1	132	.	.	.	ID=PRO_0000299648;Note=Putative uncharacterized protein YLR416C	
+##sequence-region P0CX17 1 216
+P0CX17	UniProtKB	Chain	1	216	.	.	.	ID=PRO_0000409752;Note=Putative uncharacterized protein YLR464W	
+##sequence-region P0C5P8 1 28
+P0C5P8	UniProtKB	Chain	1	28	.	.	.	ID=PRO_0000309046;Note=Putative uncharacterized protein YLR149C-A	
+##sequence-region P0C5P9 1 54
+P0C5P9	UniProtKB	Chain	1	54	.	.	.	ID=PRO_0000309047;Note=Putative uncharacterized protein YLR154W-B	
+##sequence-region P38746 1 405
+P38746	UniProtKB	Chain	1	405	.	.	.	ID=PRO_0000122455;Note=Obg-like ATPase homolog	
+P38746	UniProtKB	Domain	17	283	.	.	.	Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P38746	UniProtKB	Nucleotide binding	26	31	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P38746	UniProtKB	Binding site	231	231	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38746	UniProtKB	Sequence conflict	63	63	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38746	UniProtKB	Sequence conflict	149	149	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38746	UniProtKB	Sequence conflict	323	323	.	.	.	Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q6B0Y8 1 125
+Q6B0Y8	UniProtKB	Chain	1	125	.	.	.	ID=PRO_0000299664;Note=Putative uncharacterized protein YML012C-A	
+Q6B0Y8	UniProtKB	Compositional bias	7	21	.	.	.	Note=Poly-Ser	
+##sequence-region P0C261 1 129
+P0C261	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000262741;Note=Putative uncharacterized membrane protein YML057C-A	
+P0C261	UniProtKB	Topological domain	1	28	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C261	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C261	UniProtKB	Topological domain	50	54	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C261	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C261	UniProtKB	Topological domain	76	129	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q6B2I9 1 109
+Q6B2I9	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299662;Note=Putative uncharacterized protein YML099W-A	
+Q6B2I9	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGS8 1 64
+Q8TGS8	UniProtKB	Chain	1	64	.	.	.	ID=PRO_0000247786;Note=Uncharacterized protein YMR105W-A	
+##sequence-region P0CX76 1 440
+P0CX76	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000409803;Note=Transposon Ty1-ML2 Gag polyprotein	
+P0CX76	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000409804;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX76	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000409805;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX76	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX76	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX76	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX76	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q6B0X1 1 177
+Q6B0X1	UniProtKB	Chain	1	177	.	.	.	ID=PRO_0000299670;Note=Putative uncharacterized protein YMR135W-A	
+##sequence-region P0C5Q3 1 49
+P0C5Q3	UniProtKB	Chain	1	49	.	.	.	ID=PRO_0000309051;Note=Uncharacterized protein YMR013C-A	
+P0C5Q3	UniProtKB	Transmembrane	5	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04223 1 302
+Q04223	UniProtKB	Chain	1	302	.	.	.	ID=PRO_0000203300;Note=Uncharacterized protein YMR130W	
+##sequence-region P40207 1 237
+P40207	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000203302;Note=Uncharacterized protein YMR134W	
+P40207	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E782 1 47
+Q3E782	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E782	UniProtKB	Chain	26	47	.	.	.	ID=PRO_0000247794;Note=Uncharacterized protein YMR247W-A	
+##sequence-region A0A023PXH2 1 111
+A0A023PXH2	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000431048;Note=Putative uncharacterized membrane protein YML031C-A	
+##sequence-region Q03236 1 431
+Q03236	UniProtKB	Chain	1	431	.	.	.	ID=PRO_0000203323;Note=Uncharacterized protein YMR187C	
+Q03236	UniProtKB	Transmembrane	228	248	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03236	UniProtKB	Transmembrane	279	299	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03236	UniProtKB	Transmembrane	349	369	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03236	UniProtKB	Transmembrane	388	408	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03695 1 313
+Q03695	UniProtKB	Chain	1	313	.	.	.	ID=PRO_0000203329;Note=Uncharacterized protein YMR206W	
+Q03695	UniProtKB	Compositional bias	3	6	.	.	.	Note=Poly-Ser	
+Q03695	UniProtKB	Compositional bias	146	149	.	.	.	Note=Poly-Gln	
+Q03695	UniProtKB	Compositional bias	246	252	.	.	.	Note=Poly-Ser	
+##sequence-region Q04018 1 355
+Q04018	UniProtKB	Chain	1	355	.	.	.	ID=PRO_0000203336;Note=Uncharacterized protein YMR244W	
+Q04018	UniProtKB	Transmembrane	6	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04835 1 414
+Q04835	UniProtKB	Chain	1	414	.	.	.	ID=PRO_0000203340;Note=Uncharacterized membrane protein YMR253C	
+Q04835	UniProtKB	Topological domain	1	66	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Transmembrane	67	87	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Topological domain	88	106	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Transmembrane	107	127	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Topological domain	128	144	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Transmembrane	145	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Topological domain	168	171	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Transmembrane	172	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Topological domain	192	199	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Topological domain	221	241	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Topological domain	263	269	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Transmembrane	270	290	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Topological domain	291	307	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Transmembrane	308	328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Topological domain	329	357	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Transmembrane	358	378	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Topological domain	379	414	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04835	UniProtKB	Domain	78	215	.	.	.	Note=EamA 1	
+Q04835	UniProtKB	Domain	253	379	.	.	.	Note=EamA 2	
+Q04835	UniProtKB	Cross-link	40	40	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q04835	UniProtKB	Sequence conflict	278	278	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03263 1 540
+Q03263	UniProtKB	Chain	1	540	.	.	.	ID=PRO_0000173429;Note=Uncharacterized transporter YMR279C	
+Q03263	UniProtKB	Topological domain	1	61	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	83	108	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	130	131	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	153	169	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	170	190	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	191	203	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	225	232	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	254	272	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	273	293	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	294	295	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	296	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	317	334	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	335	355	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	356	372	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	394	398	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	399	419	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	420	429	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	430	450	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	451	461	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	462	482	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	483	502	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Transmembrane	503	523	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03263	UniProtKB	Topological domain	524	540	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5Q6 1 74
+P0C5Q6	UniProtKB	Chain	1	74	.	.	.	ID=PRO_0000309054;Note=Putative uncharacterized protein YMR194C-A	
+##sequence-region Q04898 1 105
+Q04898	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000114626;Note=Putative uncharacterized protein YMR321C	
+Q04898	UniProtKB	Domain	1	101	.	.	.	Note=Hcy-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333	
+##sequence-region Q03730 1 393
+Q03730	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000203261;Note=Uncharacterized vacuolar membrane protein YML018C	
+Q03730	UniProtKB	Topological domain	1	17	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Transmembrane	18	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Topological domain	39	46	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Transmembrane	47	67	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Topological domain	68	132	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Transmembrane	133	153	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Topological domain	154	156	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Transmembrane	157	176	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Topological domain	177	182	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Transmembrane	183	200	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Topological domain	201	219	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Transmembrane	220	240	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Topological domain	241	257	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Transmembrane	258	278	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Topological domain	279	292	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Transmembrane	293	313	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Topological domain	314	321	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Transmembrane	322	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Topological domain	343	345	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Transmembrane	346	366	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Topological domain	367	393	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03730	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q03730	UniProtKB	Sequence conflict	257	257	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03161 1 297
+Q03161	UniProtKB	Chain	1	297	.	.	.	ID=PRO_0000213035;Note=Glucose-6-phosphate 1-epimerase	
+Q03161	UniProtKB	Active site	159	159	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670	
+Q03161	UniProtKB	Active site	264	264	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670	
+Q03161	UniProtKB	Binding site	57	57	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670	
+Q03161	UniProtKB	Binding site	81	81	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670	
+Q03161	UniProtKB	Binding site	86	86	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670	
+Q03161	UniProtKB	Binding site	203	203	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670	
+Q03161	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03161	UniProtKB	Beta strand	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	7	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	17	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	30	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Helix	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Helix	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	91	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Turn	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	102	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Helix	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Helix	114	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	125	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	134	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	152	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Helix	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	170	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	179	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Turn	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	187	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	193	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	202	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	215	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	222	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	234	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Helix	241	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Helix	256	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	260	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+Q03161	UniProtKB	Beta strand	279	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR	
+##sequence-region Q8TGL8 1 51
+Q8TGL8	UniProtKB	Chain	1	51	.	.	.	ID=PRO_0000299676;Note=Putative uncharacterized protein YNL097W-A	
+Q8TGL8	UniProtKB	Compositional bias	43	47	.	.	.	Note=Poly-Cys	
+##sequence-region Q3E7Z1 1 64
+Q3E7Z1	UniProtKB	Chain	1	64	.	.	.	ID=PRO_0000247799;Note=Uncharacterized protein YNL146C-A	
+##sequence-region P53828 1 104
+P53828	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000203373;Note=Putative uncharacterized protein YNL296W	
+##sequence-region P53826 1 146
+P53826	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53826	UniProtKB	Chain	25	146	.	.	.	ID=PRO_0000014338;Note=Putative uncharacterized protein YNL319W	
+P53826	UniProtKB	Glycosylation	99	99	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53826	UniProtKB	Glycosylation	106	106	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53736 1 256
+P53736	UniProtKB	Chain	1	256	.	.	.	ID=PRO_0000203478;Note=Uncharacterized protein YNR040W	
+##sequence-region P53749 1 607
+P53749	UniProtKB	Chain	1	607	.	.	.	ID=PRO_0000115005;Note=Uncharacterized transcriptional regulatory protein YNR063W	
+P53749	UniProtKB	DNA binding	16	44	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P0C271 1 40
+P0C271	UniProtKB	Chain	1	40	.	.	.	ID=PRO_0000268630;Note=Uncharacterized protein YNL097C-B	
+##sequence-region P53758 1 84
+P53758	UniProtKB	Chain	1	84	.	.	.	ID=PRO_0000211378;Note=UPF0320 protein YNR077C	
+##sequence-region P53979 1 125
+P53979	UniProtKB	Chain	1	125	.	.	.	ID=PRO_0000203464;Note=Putative uncharacterized protein YNL013C	
+P53979	UniProtKB	Transmembrane	28	48	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53979	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53960 1 456
+P53960	UniProtKB	Chain	1	456	.	.	.	ID=PRO_0000203457;Note=Putative alanyl-tRNA editing protein alaX	
+P53960	UniProtKB	Metal binding	125	125	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53960	UniProtKB	Metal binding	129	129	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53960	UniProtKB	Metal binding	240	240	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53960	UniProtKB	Metal binding	244	244	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53947 1 316
+P53947	UniProtKB	Chain	1	316	.	.	.	ID=PRO_0000203449;Note=Vacuolar membrane protein YNL058C	
+P53947	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53947	UniProtKB	Compositional bias	26	65	.	.	.	Note=Ser-rich	
+P53947	UniProtKB	Compositional bias	235	243	.	.	.	Note=Poly-Glu	
+P53947	UniProtKB	Modified residue	148	148	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53947	UniProtKB	Modified residue	256	256	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53947	UniProtKB	Modified residue	276	276	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38806 1 282
+P38806	UniProtKB	Chain	1	282	.	.	.	ID=PRO_0000212679;Note=Chromatin modification-related protein YNG2	
+P38806	UniProtKB	Zinc finger	222	271	.	.	.	Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+P38806	UniProtKB	Coiled coil	35	86	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38806	UniProtKB	Metal binding	225	225	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Metal binding	227	227	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Metal binding	238	238	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Metal binding	243	243	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Metal binding	249	249	.	.	.	Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Metal binding	252	252	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Metal binding	265	265	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Metal binding	268	268	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Binding site	224	224	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Binding site	235	235	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Binding site	239	239	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Binding site	247	247	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P38806	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38806	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38806	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38806	UniProtKB	Helix	3	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P38806	UniProtKB	Turn	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P38806	UniProtKB	Helix	17	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P38806	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P38806	UniProtKB	Helix	65	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P38806	UniProtKB	Beta strand	225	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MUM	
+P38806	UniProtKB	Turn	250	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MUM	
+P38806	UniProtKB	Helix	266	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MUM	
+##sequence-region P53936 1 158
+P53936	UniProtKB	Chain	1	158	.	.	.	ID=PRO_0000203443;Note=Putative uncharacterized protein YNL089C	
+##sequence-region P53906 1 100
+P53906	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000203422;Note=Uncharacterized protein YNL146W	
+P53906	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53906	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53906	UniProtKB	Sequence conflict	15	15	.	.	.	Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53906	UniProtKB	Sequence conflict	21	21	.	.	.	Note=T->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53888 1 131
+P53888	UniProtKB	Chain	1	131	.	.	.	ID=PRO_0000203410;Note=Putative uncharacterized protein YNL170W	
+##sequence-region P53862 1 258
+P53862	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53862	UniProtKB	Chain	24	258	.	.	.	ID=PRO_0000014339;Note=putative uncharacterized membrane protein YNL228W	
+P53862	UniProtKB	Topological domain	24	64	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53862	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53862	UniProtKB	Topological domain	86	123	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53862	UniProtKB	Transmembrane	124	144	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53862	UniProtKB	Topological domain	145	230	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53862	UniProtKB	Transmembrane	231	251	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53862	UniProtKB	Topological domain	252	258	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53862	UniProtKB	Compositional bias	79	82	.	.	.	Note=Poly-Phe	
+P53862	UniProtKB	Compositional bias	88	92	.	.	.	Note=Poly-Ser	
+P53862	UniProtKB	Compositional bias	129	141	.	.	.	Note=Poly-Phe	
+P53862	UniProtKB	Glycosylation	118	118	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08187 1 201
+Q08187	UniProtKB	Chain	1	201	.	.	.	ID=PRO_0000245275;Note=Uncharacterized protein YOL029C	
+Q08187	UniProtKB	Compositional bias	85	93	.	.	.	Note=Poly-Ser	
+##sequence-region Q08206 1 761
+Q08206	UniProtKB	Chain	1	761	.	.	.	ID=PRO_0000235921;Note=Uncharacterized protein YOL036W	
+Q08206	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q08498 1 113
+Q08498	UniProtKB	Signal peptide	1	29	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08498	UniProtKB	Chain	30	113	.	.	.	ID=PRO_0000299710;Note=Putative uncharacterized protein YOR082C	
+Q08498	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08498	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E7Y9 1 61
+Q3E7Y9	UniProtKB	Chain	1	61	.	.	.	ID=PRO_0000235930;Note=Uncharacterized protein YOL097W-A	
+##sequence-region Q08241 1 117
+Q08241	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000299694;Note=Putative uncharacterized protein YOL106W	
+##sequence-region Q08270 1 108
+Q08270	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000235933;Note=Uncharacterized protein YOL131W	
+##sequence-region Q12243 1 111
+Q12243	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000299704;Note=Uncharacterized protein YOR029W	
+##sequence-region O13521 1 115
+O13521	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000299798;Note=Putative uncharacterized protein YPL035C	
+##sequence-region A0A023PZM3 1 137
+A0A023PZM3	UniProtKB	Chain	1	137	.	.	.	ID=PRO_0000431062;Note=Putative uncharacterized membrane protein YPR050C	
+A0A023PZM3	UniProtKB	Transmembrane	26	42	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZM3	UniProtKB	Transmembrane	52	69	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13582 1 124
+O13582	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000299820;Note=Putative uncharacterized protein YPR076W	
+O13582	UniProtKB	Compositional bias	33	40	.	.	.	Note=Poly-Glu	
+##sequence-region O13517 1 100
+O13517	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299802;Note=Putative uncharacterized protein YPL102C	
+##sequence-region Q02961 1 396
+Q02961	UniProtKB	Chain	1	396	.	.	.	ID=PRO_0000234369;Note=Putative 2-hydroxyacid dehydrogenase YPL113C	
+Q02961	UniProtKB	Nucleotide binding	227	228	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02961	UniProtKB	Nucleotide binding	311	313	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02961	UniProtKB	Nucleotide binding	361	364	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02961	UniProtKB	Active site	313	313	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02961	UniProtKB	Active site	342	342	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02961	UniProtKB	Active site	361	361	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02961	UniProtKB	Binding site	337	337	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P0CX73 1 440
+P0CX73	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000409797;Note=Transposon Ty1-PL Gag polyprotein	
+P0CX73	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000409798;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX73	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000409799;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX73	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX73	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX73	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX73	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region P0CX58 1 440
+P0CX58	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000409776;Note=Transposon Ty1-PR1 Gag polyprotein	
+P0CX58	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000409777;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX58	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000409778;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX58	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX58	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX58	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q06522 1 304
+Q06522	UniProtKB	Chain	1	304	.	.	.	ID=PRO_0000257828;Note=Uncharacterized protein YPR147C	
+Q06522	UniProtKB	Transmembrane	156	176	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06522	UniProtKB	Glycosylation	95	95	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12152 1 901
+Q12152	UniProtKB	Chain	1	901	.	.	.	ID=PRO_0000234368;Note=Putative serine/threonine-protein kinase YPL150W	
+Q12152	UniProtKB	Domain	41	287	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12152	UniProtKB	Nucleotide binding	47	55	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12152	UniProtKB	Compositional bias	398	517	.	.	.	Note=Ser-rich	
+Q12152	UniProtKB	Compositional bias	588	712	.	.	.	Note=Ser-rich	
+Q12152	UniProtKB	Active site	157	157	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q12152	UniProtKB	Binding site	70	70	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12152	UniProtKB	Modified residue	456	456	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+Q12152	UniProtKB	Modified residue	533	533	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region A0A023PYK2 1 111
+A0A023PYK2	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000431063;Note=Putative uncharacterized membrane protein YPR170C	
+A0A023PYK2	UniProtKB	Transmembrane	20	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06594 1 109
+Q06594	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299834;Note=Uncharacterized protein YPR195C	
+##sequence-region Q08993 1 238
+Q08993	UniProtKB	Chain	1	238	.	.	.	ID=PRO_0000268172;Note=Putative uncharacterized protein YPR202W	
+##sequence-region P0CX98 1 160
+P0CX98	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000410455;Note=UPF0479 membrane protein YPR204C-A	
+P0CX98	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX98	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX98	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region Q8TGL0 1 81
+Q8TGL0	UniProtKB	Chain	1	81	.	.	.	ID=PRO_0000299810;Note=Putative uncharacterized protein YPL222C-A	
+##sequence-region P0C5S0 1 95
+P0C5S0	UniProtKB	Chain	1	95	.	.	.	ID=PRO_0000309068;Note=Putative uncharacterized protein YPL250W-A	
+##sequence-region Q08976 1 102
+Q08976	UniProtKB	Signal peptide	1	41	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08976	UniProtKB	Chain	42	102	.	.	.	ID=PRO_0000299813;Note=Uncharacterized protein YPL261C	
+Q08976	UniProtKB	Sequence conflict	99	99	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CF36 1 145
+P0CF36	UniProtKB	Chain	1	145	.	.	.	ID=PRO_0000393443;Note=Putative uncharacterized protein YPL276W	
+P0CF36	UniProtKB	Binding site	97	97	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160	
+P0CF36	UniProtKB	Binding site	121	121	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160	
+##sequence-region A0A0B7P3V8 1 1104
+A0A0B7P3V8	UniProtKB	Chain	1	1104	.	.	.	ID=PRO_0000434006;Note=Transposon Ty4-P Gag-Pol polyprotein	
+A0A0B7P3V8	UniProtKB	Domain	619	786	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+A0A0B7P3V8	UniProtKB	Region	381	501	.	.	.	Note=Ty4 protease	
+A0A0B7P3V8	UniProtKB	Region	539	599	.	.	.	Note=Integrase-type zinc finger-like	
+A0A0B7P3V8	UniProtKB	Coiled coil	48	112	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A0B7P3V8	UniProtKB	Active site	414	414	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+A0A0B7P3V8	UniProtKB	Metal binding	630	630	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+A0A0B7P3V8	UniProtKB	Metal binding	695	695	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+##sequence-region P0C5S1 1 26
+P0C5S1	UniProtKB	Chain	1	26	.	.	.	ID=PRO_0000309069;Note=Uncharacterized protein YPR160W-A	
+##sequence-region P0C1V3 1 61
+P0C1V3	UniProtKB	Chain	1	61	.	.	.	ID=PRO_0000248425;Note=Putative uncharacterized protein YAL016C-B	
+##sequence-region A0A023PXH4 1 145
+A0A023PXH4	UniProtKB	Chain	1	145	.	.	.	ID=PRO_0000430971;Note=Putative uncharacterized membrane protein YAL026C-A	
+A0A023PXH4	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGK6 1 75
+Q8TGK6	UniProtKB	Chain	1	75	.	.	.	ID=PRO_0000248403;Note=Putative UPF0377 protein YAL067W-A	
+##sequence-region Q8TGK7 1 84
+Q8TGK7	UniProtKB	Chain	1	84	.	.	.	ID=PRO_0000211368;Note=Putative UPF0320 protein YAL068W-A	
+##sequence-region D6VPM8 1 179
+D6VPM8	UniProtKB	Chain	1	179	.	.	.	ID=PRO_0000402276;Note=Putative DUP240 protein YAR023C	
+D6VPM8	UniProtKB	Transmembrane	4	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6VPM8	UniProtKB	Transmembrane	26	46	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6VPM8	UniProtKB	Sequence conflict	20	20	.	.	.	Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+D6VPM8	UniProtKB	Sequence conflict	20	20	.	.	.	Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+D6VPM8	UniProtKB	Sequence conflict	20	20	.	.	.	Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+D6VPM8	UniProtKB	Sequence conflict	46	46	.	.	.	Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+D6VPM8	UniProtKB	Sequence conflict	46	46	.	.	.	Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+D6VPM8	UniProtKB	Sequence conflict	46	46	.	.	.	Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39549 1 74
+P39549	UniProtKB	Chain	1	74	.	.	.	ID=PRO_0000207530;Note=DUP240 protein YAR029W	
+##sequence-region P39550 1 113
+P39550	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000202427;Note=Putative uncharacterized protein YAR030C	
+##sequence-region Q8TGU8 1 32
+Q8TGU8	UniProtKB	Chain	1	32	.	.	.	ID=PRO_0000248432;Note=Uncharacterized protein YBL071C-B	
+##sequence-region P0C5L3 1 47
+P0C5L3	UniProtKB	Chain	1	47	.	.	.	ID=PRO_0000309011;Note=Putative uncharacterized protein YBR103C-A	
+##sequence-region Q8TGQ4 1 31
+Q8TGQ4	UniProtKB	Chain	1	31	.	.	.	ID=PRO_0000299795;Note=Putative uncharacterized protein YBR141W-A	
+##sequence-region Q2V2Q3 1 67
+Q2V2Q3	UniProtKB	Chain	1	67	.	.	.	ID=PRO_0000248441;Note=Putative uncharacterized protein YBR201C-A	
+##sequence-region Q3E781 1 34
+Q3E781	UniProtKB	Chain	1	34	.	.	.	ID=PRO_0000248442;Note=Uncharacterized protein YBR221W-A	
+##sequence-region A0A023PXH5 1 47
+A0A023PXH5	UniProtKB	Chain	1	47	.	.	.	ID=PRO_0000430977;Note=Putative uncharacterized protein YBR126W-B	
+##sequence-region P38303 1 103
+P38303	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000202506;Note=Putative uncharacterized protein YBR190W	
+##sequence-region P38320 1 171
+P38320	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38320	UniProtKB	Chain	25	171	.	.	.	ID=PRO_0000014311;Note=Putative uncharacterized membrane protein YBR224W	
+P38320	UniProtKB	Topological domain	25	70	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38320	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38320	UniProtKB	Topological domain	92	140	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38320	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38320	UniProtKB	Topological domain	162	171	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38150 1 797
+P38150	UniProtKB	Chain	1	797	.	.	.	ID=PRO_0000194415;Note=Inactive deaminase YBR284W	
+P38150	UniProtKB	Transmembrane	627	647	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38209 1 133
+P38209	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000202463;Note=Putative uncharacterized protein YBL012C	
+##sequence-region P38202 1 106
+P38202	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000202462;Note=UPF0642 protein YBL028C	
+##sequence-region Q03904 1 111
+Q03904	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000299874;Note=Putative uncharacterized protein YDR133C	
+Q03904	UniProtKB	Transmembrane	64	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGP3 1 30
+Q8TGP3	UniProtKB	Chain	1	30	.	.	.	ID=PRO_0000299910;Note=Putative uncharacterized protein YEL008C-A	
+##sequence-region A0A023PYD9 1 177
+A0A023PYD9	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PYD9	UniProtKB	Chain	23	177	.	.	.	ID=PRO_0000430991;Note=Putative uncharacterized membrane protein YEL018C-A	
+A0A023PYD9	UniProtKB	Transmembrane	31	51	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PYD9	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PYD9	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5M7 1 63
+P0C5M7	UniProtKB	Chain	1	63	.	.	.	ID=PRO_0000309025;Note=Putative uncharacterized protein YEL050W-A	
+P0C5M7	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGU4 1 54
+Q8TGU4	UniProtKB	Chain	1	54	.	.	.	ID=PRO_0000245372;Note=Uncharacterized protein YER175W-A	
+##sequence-region P32618 1 956
+P32618	UniProtKB	Chain	1	956	.	.	.	ID=PRO_0000202607;Note=Uncharacterized protein YEL043W	
+P32618	UniProtKB	Domain	40	141	.	.	.	Note=Fibronectin type-III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316	
+P32618	UniProtKB	Modified residue	154	154	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P32618	UniProtKB	Modified residue	501	501	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32618	UniProtKB	Modified residue	520	520	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32618	UniProtKB	Modified residue	802	802	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32618	UniProtKB	Modified residue	842	842	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32618	UniProtKB	Modified residue	895	895	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32618	UniProtKB	Sequence conflict	467	467	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07950 1 538
+Q07950	UniProtKB	Chain	1	538	.	.	.	ID=PRO_0000248405;Note=Sterol esterase 2	
+Q07950	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07950	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07950	UniProtKB	Topological domain	33	538	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07950	UniProtKB	Active site	287	287	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07950	UniProtKB	Active site	480	480	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07950	UniProtKB	Active site	511	511	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07950	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q07950	UniProtKB	Modified residue	107	107	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P39974 1 107
+P39974	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000202599;Note=Uncharacterized protein YEL073C	
+##sequence-region P40058 1 173
+P40058	UniProtKB	Chain	1	173	.	.	.	ID=PRO_0000202639;Note=Uncharacterized protein YER085C	
+##sequence-region P40082 1 130
+P40082	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000202651;Note=Uncharacterized protein YER135C	
+##sequence-region P43540 1 174
+P43540	UniProtKB	Chain	1	174	.	.	.	ID=PRO_0000202669;Note=Uncharacterized protein YFL064C	
+P43540	UniProtKB	Sequence conflict	104	104	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43538 1 392
+P43538	UniProtKB	Chain	1	392	.	.	.	ID=PRO_0000102206;Note=Y' element ATP-dependent helicase YFL066C	
+P43538	UniProtKB	Domain	1	175	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P43538	UniProtKB	Domain	232	381	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P43538	UniProtKB	Nucleotide binding	11	18	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region P43597 1 1233
+P43597	UniProtKB	Chain	1	1233	.	.	.	ID=PRO_0000202686;Note=Uncharacterized protein YFR016C	
+P43597	UniProtKB	Domain	1132	1233	.	.	.	Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686	
+P43597	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P43597	UniProtKB	Modified residue	462	462	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43597	UniProtKB	Modified residue	523	523	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43597	UniProtKB	Modified residue	861	861	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P43597	UniProtKB	Modified residue	975	975	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P43597	UniProtKB	Modified residue	1037	1037	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43597	UniProtKB	Modified residue	1046	1046	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P43608 1 114
+P43608	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000202693;Note=Uncharacterized protein YFR035C	
+P43608	UniProtKB	Transmembrane	58	78	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43608	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43617 1 309
+P43617	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000090695;Note=Uncharacterized mitochondrial carrier YFR045W	
+P43617	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43617	UniProtKB	Transmembrane	47	67	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43617	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43617	UniProtKB	Transmembrane	184	204	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43617	UniProtKB	Transmembrane	222	242	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43617	UniProtKB	Transmembrane	285	305	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43617	UniProtKB	Repeat	6	83	.	.	.	Note=Solcar 1	
+P43617	UniProtKB	Repeat	97	211	.	.	.	Note=Solcar 2	
+P43617	UniProtKB	Repeat	216	302	.	.	.	Note=Solcar 3	
+##sequence-region Q8TGN8 1 31
+Q8TGN8	UniProtKB	Chain	1	31	.	.	.	ID=PRO_0000299923;Note=Putative uncharacterized protein YGR068W-A	
+##sequence-region P53205 1 108
+P53205	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000202780;Note=Putative uncharacterized protein YGR011W	
+##sequence-region P53213 1 109
+P53213	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000202786;Note=Putative uncharacterized protein YGR022C	
+##sequence-region P53240 1 122
+P53240	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000202802;Note=Putative uncharacterized protein YGR064W	
+##sequence-region P53245 1 111
+P53245	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000202805;Note=Putative uncharacterized protein YGR069W	
+P53245	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53245	UniProtKB	Compositional bias	36	47	.	.	.	Note=Poly-Phe	
+##sequence-region P53282 1 124
+P53282	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000202826;Note=Putative uncharacterized protein YGR137W	
+P53282	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53288 1 203
+P53288	UniProtKB	Chain	1	203	.	.	.	ID=PRO_0000202834;Note=Putative uncharacterized protein YGR160W	
+P53288	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53288	UniProtKB	Compositional bias	43	52	.	.	.	Note=Poly-Ser	
+P53288	UniProtKB	Compositional bias	89	98	.	.	.	Note=Poly-Ser	
+P53288	UniProtKB	Compositional bias	99	108	.	.	.	Note=Poly-Glu	
+P53288	UniProtKB	Compositional bias	163	167	.	.	.	Note=Poly-Glu	
+##sequence-region P53307 1 113
+P53307	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000202848;Note=Uncharacterized protein YGR219W	
+##sequence-region P53329 1 174
+P53329	UniProtKB	Chain	1	174	.	.	.	ID=PRO_0000202868;Note=Uncharacterized protein YGR273C	
+##sequence-region P25338 1 174
+P25338	UniProtKB	Chain	1	174	.	.	.	ID=PRO_0000202776;Note=Uncharacterized endoplasmic reticulum membrane protein YGL010W	
+P25338	UniProtKB	Topological domain	1	23	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25338	UniProtKB	Transmembrane	24	44	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25338	UniProtKB	Topological domain	45	63	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25338	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25338	UniProtKB	Topological domain	85	98	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25338	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25338	UniProtKB	Topological domain	120	131	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25338	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25338	UniProtKB	Topological domain	153	174	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25338	UniProtKB	Sequence conflict	105	105	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25338	UniProtKB	Sequence conflict	105	105	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25338	UniProtKB	Sequence conflict	122	174	.	.	.	Note=RPALIDNLVQSLVLAPYFIMFEFLFKLGFMPRLKATLEHDLEIKQRNLRMQRQ->TSQR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25338	UniProtKB	Sequence conflict	122	174	.	.	.	Note=RPALIDNLVQSLVLAPYFIMFEFLFKLGFMPRLKATLEHDLEIKQRNLRMQRQ->TSQR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53186 1 121
+P53186	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000202772;Note=Uncharacterized protein YGL034C	
+P53186	UniProtKB	Nucleotide binding	77	84	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53181 1 101
+P53181	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000202770;Note=Putative uncharacterized protein YGL042C	
+P53181	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53181	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53138 1 107
+P53138	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000202750;Note=Putative uncharacterized protein YGL109W	
+##sequence-region P53132 1 145
+P53132	UniProtKB	Chain	1	145	.	.	.	ID=PRO_0000202746;Note=Uncharacterized protein YGL118C	
+##sequence-region P53126 1 111
+P53126	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000202741;Note=Putative uncharacterized protein YGL132W	
+##sequence-region P53120 1 1219
+P53120	UniProtKB	Chain	1	1219	.	.	.	ID=PRO_0000202737;Note=Uncharacterized membrane protein YGL140C	
+P53120	UniProtKB	Topological domain	1	36	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	37	57	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	58	74	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	96	123	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	124	144	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	145	146	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	168	183	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	184	204	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	205	629	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	630	650	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	651	663	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	664	684	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	685	687	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	688	705	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	706	709	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	710	730	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	731	732	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	733	753	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	754	766	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	767	787	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	788	796	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Transmembrane	797	817	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Topological domain	818	1219	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53120	UniProtKB	Modified residue	1167	1167	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+P53120	UniProtKB	Modified residue	1191	1191	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53120	UniProtKB	Modified residue	1198	1198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53120	UniProtKB	Modified residue	1199	1199	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P0CL28 1 191
+P0CL28	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL28	UniProtKB	Chain	18	191	.	.	.	ID=PRO_0000406005;Note=Putative uncharacterized protein YGR296C-A	
+P0CL28	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL28	UniProtKB	Compositional bias	13	159	.	.	.	Note=Gly/Ser-rich	
+##sequence-region P53085 1 113
+P53085	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000202717;Note=Putative uncharacterized protein YGL217C	
+##sequence-region Q3E7Z6 1 27
+Q3E7Z6	UniProtKB	Chain	1	27	.	.	.	ID=PRO_0000245392;Note=Uncharacterized protein YHL015W-A	
+##sequence-region A0A023PZD5 1 153
+A0A023PZD5	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000431018;Note=Putative uncharacterized protein YHL030W-A	
+##sequence-region Q3E758 1 44
+Q3E758	UniProtKB	Chain	1	44	.	.	.	ID=PRO_0000245391;Note=Uncharacterized protein YHL048C-A	
+##sequence-region P0CL32 1 64
+P0CL32	UniProtKB	Chain	1	64	.	.	.	ID=PRO_0000299927;Note=Putative uncharacterized protein YHR052W-A	
+P0CL32	UniProtKB	Transmembrane	33	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PYH0 1 136
+A0A023PYH0	UniProtKB	Signal peptide	1	35	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PYH0	UniProtKB	Chain	36	136	.	.	.	ID=PRO_0000431024;Note=Putative uncharacterized protein YHR070C-A	
+##sequence-region O13536 1 103
+O13536	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000299929;Note=Uncharacterized protein YHR139C-A	
+##sequence-region Q3E815 1 49
+Q3E815	UniProtKB	Chain	1	49	.	.	.	ID=PRO_0000245396;Note=Uncharacterized membrane protein YHR175W-A	
+Q3E815	UniProtKB	Transmembrane	17	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38868 1 163
+P38868	UniProtKB	Chain	1	163	.	.	.	ID=PRO_0000202933;Note=Uncharacterized protein YHR180W	
+P38868	UniProtKB	Transmembrane	7	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E7Z5 1 69
+Q3E7Z5	UniProtKB	Chain	1	69	.	.	.	ID=PRO_0000245405;Note=Uncharacterized protein YIL002W-A	
+Q3E7Z5	UniProtKB	Coiled coil	21	64	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E7Z4 1 54
+Q3E7Z4	UniProtKB	Chain	1	54	.	.	.	ID=PRO_0000245403;Note=Uncharacterized protein YIL046W-A	
+Q3E7Z4	UniProtKB	Transmembrane	21	43	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGN5 1 46
+Q8TGN5	UniProtKB	Chain	1	46	.	.	.	ID=PRO_0000299756;Note=Uncharacterized protein YIL105W-A	
+##sequence-region A0A023PYI2 1 110
+A0A023PYI2	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000431039;Note=Putative uncharacterized protein YIL142C-A	
+##sequence-region P0CF22 1 210
+P0CF22	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000393394;Note=Putative truncated L-serine dehydratase SDL1	
+##sequence-region P40551 1 113
+P40551	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000203001;Note=Uncharacterized protein YIL012W	
+##sequence-region P40542 1 124
+P40542	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000202999;Note=Putative uncharacterized protein YIL025C	
+##sequence-region Q08956 1 461
+Q08956	UniProtKB	Chain	1	461	.	.	.	ID=PRO_0000238632;Note=Protein YIG1	
+##sequence-region P25637 1 258
+P25637	UniProtKB	Chain	1	258	.	.	.	ID=PRO_0000207657;Note=Protein IMPACT homolog	
+P25637	UniProtKB	Domain	10	114	.	.	.	Note=RWD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00179	
+P25637	UniProtKB	Cross-link	187	187	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25637	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Slightly increases interaction with GCN1 and ACT1 and does not prevent inhibition of GCN2 activity in amino acid-starved cells%3B when associated with A-90. E->A	
+P25637	UniProtKB	Mutagenesis	90	90	.	.	.	Note=Slightly increases interaction with GCN1 and ACT1 and does not prevent inhibition of GCN2 activity in amino acid-starved cells%3B when associated with A-87. D->A	
+P25637	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Decreases interaction with GCN1%2C but not with ACT1%2C and prevents inhibition of GCN2 activity in amino acid-starved cells%3B when associated with A-106. D->A	
+P25637	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Decreases interaction with GCN1%2C but not with ACT1%2C and prevents inhibition of GCN2 activity in amino acid-starved cells%3B when associated with A-102. E->A	
+##sequence-region P40497 1 633
+P40497	UniProtKB	Chain	1	633	.	.	.	ID=PRO_0000202973;Note=Uncharacterized protein YIL092W	
+P40497	UniProtKB	Transmembrane	99	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40497	UniProtKB	Transmembrane	217	233	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40488 1 101
+P40488	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000202967;Note=Uncharacterized protein YIL102C	
+##sequence-region P40483 1 696
+P40483	UniProtKB	Chain	1	696	.	.	.	ID=PRO_0000078181;Note=Putative zinc metalloproteinase YIL108W	
+P40483	UniProtKB	Domain	522	695	.	.	.	Note=Jacalin-type lectin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01088	
+P40483	UniProtKB	Active site	319	319	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P40483	UniProtKB	Metal binding	318	318	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P40483	UniProtKB	Metal binding	322	322	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P40483	UniProtKB	Metal binding	328	328	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P40483	UniProtKB	Modified residue	361	361	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40483	UniProtKB	Cross-link	245	245	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40483	UniProtKB	Cross-link	478	478	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40483	UniProtKB	Cross-link	518	518	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40483	UniProtKB	Cross-link	579	579	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40483	UniProtKB	Cross-link	590	590	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40483	UniProtKB	Cross-link	596	596	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40483	UniProtKB	Sequence conflict	696	696	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region A0A023PXM7 1 112
+A0A023PXM7	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000431043;Note=Putative uncharacterized protein YIL020C-A	
+A0A023PXM7	UniProtKB	Transmembrane	7	26	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXM7	UniProtKB	Transmembrane	36	58	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P28626 1 145
+P28626	UniProtKB	Chain	1	145	.	.	.	ID=PRO_0000203309;Note=Putative uncharacterized protein YIM2	
+P28626	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28626	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28626	UniProtKB	Sequence conflict	39	39	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28626	UniProtKB	Sequence conflict	83	83	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28626	UniProtKB	Sequence conflict	115	115	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28626	UniProtKB	Sequence conflict	132	132	.	.	.	Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28626	UniProtKB	Sequence conflict	143	143	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53108 1 310
+P53108	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000202730;Note=Protein YIP5	
+P53108	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53108	UniProtKB	Transmembrane	181	201	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53108	UniProtKB	Transmembrane	220	240	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53108	UniProtKB	Transmembrane	249	269	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53108	UniProtKB	Transmembrane	290	310	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53108	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P0CL23 1 45
+P0CL23	UniProtKB	Chain	1	45	.	.	.	ID=PRO_0000202949;Note=Putative UPF0377 protein YIL175W	
+##sequence-region Q8TGN1 1 49
+Q8TGN1	UniProtKB	Chain	1	49	.	.	.	ID=PRO_0000299765;Note=Putative uncharacterized protein YJR140W-A	
+##sequence-region P47159 1 448
+P47159	UniProtKB	Chain	1	448	.	.	.	ID=PRO_0000203118;Note=Uncharacterized membrane protein YJR124C	
+P47159	UniProtKB	Topological domain	1	50	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Topological domain	72	93	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Topological domain	115	146	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Topological domain	168	184	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Topological domain	206	260	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Transmembrane	261	281	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Topological domain	282	287	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Transmembrane	288	308	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Topological domain	309	333	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Transmembrane	334	354	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Topological domain	355	386	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Transmembrane	387	407	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Topological domain	408	416	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Transmembrane	417	437	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Topological domain	438	448	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Nucleotide binding	386	393	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47159	UniProtKB	Sequence conflict	448	448	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47188 1 116
+P47188	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000211373;Note=Putative UPF0320 protein YJR162C	
+##sequence-region P47078 1 108
+P47078	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000203078;Note=Uncharacterized protein YJL009W	
+P47078	UniProtKB	Glycosylation	33	33	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47021 1 107
+P47021	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000203043;Note=Putative uncharacterized protein YJL119C	
+##sequence-region P47012 1 105
+P47012	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000203036;Note=Putative uncharacterized protein YJL135W	
+##sequence-region P40895 1 119
+P40895	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000203012;Note=Putative uncharacterized protein YJL215C	
+##sequence-region P40892 1 196
+P40892	UniProtKB	Chain	1	196	.	.	.	ID=PRO_0000068743;Note=Putative acetyltransferase YJL218W	
+##sequence-region P47086 1 261
+P47086	UniProtKB	Chain	1	261	.	.	.	ID=PRO_0000203082;Note=Uncharacterized protein YJR011C	
+P47086	UniProtKB	Sequence conflict	142	142	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36119 1 530
+P36119	UniProtKB	Chain	1	530	.	.	.	ID=PRO_0000203202;Note=Uncharacterized protein YKR023W	
+P36119	UniProtKB	Modified residue	426	426	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36119	UniProtKB	Modified residue	431	431	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36119	UniProtKB	Modified residue	434	434	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P36119	UniProtKB	Modified residue	457	457	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36119	UniProtKB	Cross-link	509	509	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P0CE69 1 306
+P0CE69	UniProtKB	Chain	1	306	.	.	.	ID=PRO_0000392613;Note=Putative uncharacterized protein YKR104W	
+P0CE69	UniProtKB	Domain	33	286	.	.	.	Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P0CE69	UniProtKB	Nucleotide binding	67	74	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+##sequence-region P0C5P3 1 30
+P0C5P3	UniProtKB	Chain	1	30	.	.	.	ID=PRO_0000309041;Note=Uncharacterized protein YKL145W-A	
+P0C5P3	UniProtKB	Transmembrane	7	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E765 1 70
+Q3E765	UniProtKB	Chain	1	70	.	.	.	ID=PRO_0000245418;Note=Uncharacterized protein YKL183C-A	
+Q3E765	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36098 1 137
+P36098	UniProtKB	Chain	1	137	.	.	.	ID=PRO_0000203187;Note=Putative uncharacterized protein YKL031W	
+P36098	UniProtKB	Transmembrane	36	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36098	UniProtKB	Transmembrane	113	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P34249 1 101
+P34249	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000203160;Note=Uncharacterized protein YKL102C	
+##sequence-region P36071 1 126
+P36071	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000203154;Note=Putative uncharacterized protein YKL123W	
+##sequence-region Q08018 1 140
+Q08018	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000299609;Note=Putative uncharacterized protein YLR076C	
+##sequence-region Q12528 1 110
+Q12528	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000299611;Note=Uncharacterized protein YLR111W	
+Q12528	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12174 1 109
+Q12174	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299615;Note=Putative uncharacterized protein YLR123C	
+Q12174	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12288 1 251
+Q12288	UniProtKB	Chain	1	251	.	.	.	ID=PRO_0000247340;Note=Putative glutamine amidotransferase YLR126C	
+Q12288	UniProtKB	Domain	48	232	.	.	.	Note=Glutamine amidotransferase type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+Q12288	UniProtKB	Active site	112	112	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+Q12288	UniProtKB	Active site	198	198	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+Q12288	UniProtKB	Active site	200	200	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+##sequence-region P0CY05 1 43
+P0CY05	UniProtKB	Chain	1	43	.	.	.	ID=PRO_0000410461;Note=Uncharacterized protein YLR159C-A	
+##sequence-region Q06070 1 228
+Q06070	UniProtKB	Chain	1	228	.	.	.	ID=PRO_0000268628;Note=Uncharacterized protein YLR407W	
+Q06070	UniProtKB	Sequence conflict	226	228	.	.	.	Note=GMP->ACHD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region O13578 1 112
+O13578	UniProtKB	Transit peptide	1	21	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13578	UniProtKB	Chain	22	112	.	.	.	ID=PRO_0000247258;Note=Putative uncharacterized protein YLR415C%2C mitochondrial	
+##sequence-region Q06698 1 1435
+Q06698	UniProtKB	Chain	1	1435	.	.	.	ID=PRO_0000247257;Note=Putative ATP-dependent RNA helicase YLR419W	
+Q06698	UniProtKB	Domain	365	406	.	.	.	Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
+Q06698	UniProtKB	Domain	430	531	.	.	.	Note=RWD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00179	
+Q06698	UniProtKB	Domain	614	782	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q06698	UniProtKB	Domain	845	1020	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q06698	UniProtKB	Nucleotide binding	627	634	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q06698	UniProtKB	Motif	729	732	.	.	.	Note=DEAH box	
+Q06698	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06698	UniProtKB	Modified residue	816	816	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q06188 1 304
+Q06188	UniProtKB	Chain	1	304	.	.	.	ID=PRO_0000247356;Note=PWWP domain-containing protein YLR455W	
+Q06188	UniProtKB	Domain	7	68	.	.	.	Note=PWWP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00162	
+##sequence-region Q6B0Y5 1 42
+Q6B0Y5	UniProtKB	Chain	1	42	.	.	.	ID=PRO_0000270976;Note=Putative uncharacterized membrane protein YMR046W-A	
+Q6B0Y5	UniProtKB	Transmembrane	5	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZL2 1 124
+A0A023PZL2	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZL2	UniProtKB	Chain	20	124	.	.	.	ID=PRO_0000431057;Note=Putative uncharacterized membrane protein YMR119W-A	
+A0A023PZL2	UniProtKB	Transmembrane	37	57	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZL2	UniProtKB	Transmembrane	86	108	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04711 1 1755
+Q04711	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000199566;Note=Transposon Ty1-ML1 Gag-Pol polyprotein	
+Q04711	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279117;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04711	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279118;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04711	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279119;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04711	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279120;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04711	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04711	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q04711	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q04711	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04711	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q04711	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04711	UniProtKB	Compositional bias	72	146	.	.	.	Note=Pro-rich	
+Q04711	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q04711	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04711	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04711	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04711	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04711	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04711	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04711	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04711	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04711	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04711	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04711	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03434 1 1755
+Q03434	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000199565;Note=Transposon Ty1-ML2 Gag-Pol polyprotein	
+Q03434	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279123;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03434	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279124;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03434	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279125;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03434	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279126;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03434	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03434	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q03434	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q03434	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03434	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q03434	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03434	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q03434	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q03434	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03434	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03434	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03434	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03434	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03434	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03434	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03434	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03434	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03434	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03434	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03434	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region A0A023PYJ4 1 111
+A0A023PYJ4	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000431056;Note=Putative uncharacterized protein YMR153C-A	
+##sequence-region P40218 1 223
+P40218	UniProtKB	Chain	1	223	.	.	.	ID=PRO_0000203307;Note=Uncharacterized protein YMR147W	
+##sequence-region Q04336 1 1088
+Q04336	UniProtKB	Chain	1	1088	.	.	.	ID=PRO_0000203326;Note=Uncharacterized protein YMR196W	
+Q04336	UniProtKB	Modified residue	299	299	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04336	UniProtKB	Modified residue	984	984	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04336	UniProtKB	Modified residue	1013	1013	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04336	UniProtKB	Modified residue	1081	1081	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q04019 1 206
+Q04019	UniProtKB	Chain	1	206	.	.	.	ID=PRO_0000203337;Note=Putative uncharacterized protein YMR245W	
+##sequence-region Q04838 1 102
+Q04838	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000203341;Note=Uncharacterized protein YMR254C	
+Q04838	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04838	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04838	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03508 1 461
+Q03508	UniProtKB	Chain	1	461	.	.	.	ID=PRO_0000203347;Note=Uncharacterized protein YMR265C	
+##sequence-region Q03559 1 197
+Q03559	UniProtKB	Chain	1	197	.	.	.	ID=PRO_0000203351;Note=Uncharacterized protein YMR295C	
+Q03559	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q03559	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q03559	UniProtKB	Cross-link	26	26	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q03559	UniProtKB	Cross-link	32	32	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q04869 1 349
+Q04869	UniProtKB	Chain	1	349	.	.	.	ID=PRO_0000203357;Note=Uncharacterized protein YMR315W	
+Q04869	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q6Q571 1 112
+Q6Q571	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000299669;Note=Putative uncharacterized protein YMR086C-A	
+##sequence-region A0A023PYJ0 1 108
+A0A023PYJ0	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000431058;Note=Putative uncharacterized membrane protein YML009C-A	
+A0A023PYJ0	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39523 1 943
+P39523	UniProtKB	Chain	1	943	.	.	.	ID=PRO_0000203298;Note=Uncharacterized protein YMR124W	
+P39523	UniProtKB	Compositional bias	59	66	.	.	.	Note=Poly-Gln	
+P39523	UniProtKB	Compositional bias	93	100	.	.	.	Note=Poly-Gln	
+P39523	UniProtKB	Compositional bias	164	169	.	.	.	Note=Poly-Gly	
+P39523	UniProtKB	Compositional bias	170	175	.	.	.	Note=Poly-Asp	
+P39523	UniProtKB	Compositional bias	371	381	.	.	.	Note=Poly-Gln	
+P39523	UniProtKB	Compositional bias	536	539	.	.	.	Note=Poly-Glu	
+P39523	UniProtKB	Compositional bias	715	718	.	.	.	Note=Poly-Ser	
+P39523	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39523	UniProtKB	Modified residue	553	553	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39523	UniProtKB	Modified residue	586	586	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39523	UniProtKB	Modified residue	619	619	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39523	UniProtKB	Modified residue	649	649	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39523	UniProtKB	Modified residue	681	681	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39523	UniProtKB	Modified residue	766	766	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39523	UniProtKB	Modified residue	771	771	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q04215 1 440
+Q04215	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000203499;Note=Transposon Ty1-MR1 Gag polyprotein	
+Q04215	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279131;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04215	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279132;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04215	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04215	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region I2HB70 1 103
+I2HB70	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+I2HB70	UniProtKB	Chain	22	103	.	.	.	ID=PRO_0000419188;Note=Uncharacterized protein YMR316C-A	
+##sequence-region A0A023PXQ4 1 394
+A0A023PXQ4	UniProtKB	Chain	1	394	.	.	.	ID=PRO_0000431054;Note=Putative uncharacterized membrane protein YMR173W-A	
+A0A023PXQ4	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Transmembrane	73	95	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Transmembrane	152	172	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Transmembrane	179	198	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Transmembrane	293	313	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Transmembrane	340	360	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ4	UniProtKB	Compositional bias	2	361	.	.	.	Note=Thr-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00017	
+A0A023PXQ4	UniProtKB	Compositional bias	19	167	.	.	.	Note=Met-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00013	
+A0A023PXQ4	UniProtKB	Compositional bias	243	344	.	.	.	Note=Met-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00013	
+##sequence-region Q8TGS7 1 28
+Q8TGS7	UniProtKB	Chain	1	28	.	.	.	ID=PRO_0000247789;Note=Uncharacterized protein YMR182W-A	
+Q8TGS7	UniProtKB	Transmembrane	5	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40214 1 342
+P40214	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000203305;Note=Uncharacterized protein YMR144W	
+##sequence-region Q8TGS5 1 35
+Q8TGS5	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q8TGS5	UniProtKB	Chain	19	35	.	.	.	ID=PRO_0000247795;Note=Uncharacterized protein YMR272W-B	
+##sequence-region A0A023PXI0 1 129
+A0A023PXI0	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000431050;Note=Putative uncharacterized membrane protein YMR306C-A	
+A0A023PXI0	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXI0	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03795 1 547
+Q03795	UniProtKB	Chain	1	547	.	.	.	ID=PRO_0000203311;Note=Uncharacterized membrane protein YMR155W	
+Q03795	UniProtKB	Topological domain	1	21	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Transmembrane	22	42	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Topological domain	43	58	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Topological domain	80	83	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Transmembrane	84	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Topological domain	105	110	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Topological domain	132	144	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Topological domain	166	175	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Transmembrane	176	196	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Topological domain	197	323	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Transmembrane	324	344	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Topological domain	345	398	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Transmembrane	399	419	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Topological domain	420	437	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Transmembrane	438	458	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Topological domain	459	469	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Transmembrane	470	490	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Topological domain	491	514	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Transmembrane	515	535	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Topological domain	536	547	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03795	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q03648 1 457
+Q03648	UniProtKB	Chain	1	457	.	.	.	ID=PRO_0000203330;Note=Uncharacterized protein YMR209C	
+Q03648	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03648	UniProtKB	Transmembrane	250	270	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05016 1 267
+Q05016	UniProtKB	Chain	1	267	.	.	.	ID=PRO_0000054873;Note=NADP-dependent 3-hydroxy acid dehydrogenase	
+Q05016	UniProtKB	Nucleotide binding	20	25	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+Q05016	UniProtKB	Nucleotide binding	48	49	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+Q05016	UniProtKB	Nucleotide binding	75	76	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+Q05016	UniProtKB	Nucleotide binding	198	205	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+Q05016	UniProtKB	Active site	168	168	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001	
+Q05016	UniProtKB	Binding site	102	102	.	.	.	Note=NADP%3B via carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+Q05016	UniProtKB	Binding site	155	155	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05016	UniProtKB	Binding site	168	168	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+Q05016	UniProtKB	Binding site	172	172	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+Q05016	UniProtKB	Modified residue	260	260	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05016	UniProtKB	Helix	5	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Beta strand	15	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	24	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Turn	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Beta strand	41	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	50	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	82	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Beta strand	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	117	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	129	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Beta strand	149	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	166	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Turn	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Beta strand	192	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Beta strand	201	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	205	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Turn	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	214	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Helix	229	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Beta strand	246	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+Q05016	UniProtKB	Beta strand	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU	
+##sequence-region P38430 1 313
+P38430	UniProtKB	Chain	1	313	.	.	.	ID=PRO_0000203344;Note=Uncharacterized deoxyribonuclease YMR262W	
+P38430	UniProtKB	Metal binding	8	8	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38430	UniProtKB	Metal binding	10	10	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38430	UniProtKB	Metal binding	126	126	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38430	UniProtKB	Metal binding	126	126	.	.	.	Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38430	UniProtKB	Metal binding	180	180	.	.	.	Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38430	UniProtKB	Metal binding	207	207	.	.	.	Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38430	UniProtKB	Metal binding	262	262	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38430	UniProtKB	Sequence conflict	24	24	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38430	UniProtKB	Sequence conflict	167	167	.	.	.	Note=C->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04893 1 1140
+Q04893	UniProtKB	Chain	1	1140	.	.	.	ID=PRO_0000203359;Note=Uncharacterized protein YMR317W	
+Q04893	UniProtKB	Sequence conflict	271	272	.	.	.	Note=VI->SV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q04893	UniProtKB	Sequence conflict	278	279	.	.	.	Note=WA->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q6B0R7 1 102
+Q6B0R7	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000211375;Note=Putative UPF0320 protein YMR326C	
+Q6B0R7	UniProtKB	Sequence conflict	99	99	.	.	.	Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32331 1 307
+P32331	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32331	UniProtKB	Transmembrane	83	103	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32331	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32331	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32331	UniProtKB	Transmembrane	223	243	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32331	UniProtKB	Transmembrane	277	298	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32331	UniProtKB	Repeat	26	106	.	.	.	Note=Solcar 1	
+P32331	UniProtKB	Repeat	121	204	.	.	.	Note=Solcar 2	
+P32331	UniProtKB	Repeat	218	305	.	.	.	Note=Solcar 3	
+P32331	UniProtKB	Sequence conflict	101	101	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04521 1 102
+Q04521	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04521	UniProtKB	Chain	20	102	.	.	.	ID=PRO_0000014337;Note=Putative uncharacterized protein YML084W	
+##sequence-region Q03759 1 105
+Q03759	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03759	UniProtKB	Chain	2	105	.	.	.	ID=PRO_0000203242;Note=Uncharacterized protein YML108W	
+Q03759	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03759	UniProtKB	Beta strand	7	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z	
+Q03759	UniProtKB	Turn	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z	
+Q03759	UniProtKB	Beta strand	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z	
+Q03759	UniProtKB	Beta strand	37	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z	
+Q03759	UniProtKB	Helix	50	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z	
+Q03759	UniProtKB	Beta strand	72	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z	
+Q03759	UniProtKB	Turn	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z	
+Q03759	UniProtKB	Beta strand	81	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z	
+Q03759	UniProtKB	Helix	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z	
+Q03759	UniProtKB	Helix	91	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z	
+##sequence-region P47147 1 688
+P47147	UniProtKB	Chain	1	688	.	.	.	ID=PRO_0000094948;Note=Phosphoinositide 3-phosphatase	
+P47147	UniProtKB	Domain	155	637	.	.	.	Note=Myotubularin phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00669	
+P47147	UniProtKB	Active site	397	397	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10044	
+P47147	UniProtKB	Sequence conflict	85	85	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47147	UniProtKB	Sequence conflict	85	85	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CX09 1 502
+P0CX09	UniProtKB	Chain	1	502	.	.	.	ID=PRO_0000409748;Note=Mannitol dehydrogenase YNR073C	
+##sequence-region Q12112 1 1755
+Q12112	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279137;Note=Transposon Ty1-NL1 Gag-Pol polyprotein	
+Q12112	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279138;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12112	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279139;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12112	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279140;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12112	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279141;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12112	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12112	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12112	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q12112	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12112	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q12112	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12112	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q12112	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12112	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12112	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12112	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12112	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12112	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12112	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12112	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12112	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12112	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12112	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q3E7Z0 1 62
+Q3E7Z0	UniProtKB	Chain	1	62	.	.	.	ID=PRO_0000247797;Note=Uncharacterized protein YNL277W-A	
+##sequence-region P53827 1 115
+P53827	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000203370;Note=Putative uncharacterized protein YNL303W	
+##sequence-region Q3E767 1 46
+Q3E767	UniProtKB	Chain	1	46	.	.	.	ID=PRO_0000247801;Note=Uncharacterized protein YNL067W-B	
+##sequence-region P53820 1 52
+P53820	UniProtKB	Chain	1	52	.	.	.	ID=PRO_0000203362;Note=Putative uncharacterized protein YNL338W	
+##sequence-region P53723 1 404
+P53723	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378	
+P53723	UniProtKB	Chain	2	404	.	.	.	ID=PRO_0000203473;Note=UPF0674 endoplasmic reticulum membrane protein YNR021W	
+P53723	UniProtKB	Transmembrane	49	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53723	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378	
+P53723	UniProtKB	Glycosylation	44	44	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53723	UniProtKB	Glycosylation	98	98	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08300 1 171
+Q08300	UniProtKB	Chain	1	171	.	.	.	ID=PRO_0000245276;Note=Uncharacterized protein YOL159C	
+##sequence-region P0CF20 1 169
+P0CF20	UniProtKB	Chain	1	169	.	.	.	ID=PRO_0000393392;Note=Putative uncharacterized transporter YOL163W	
+P0CF20	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CF20	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CF20	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E736 1 78
+Q3E736	UniProtKB	Chain	1	78	.	.	.	ID=PRO_0000237663;Note=Uncharacterized protein YOR192C-C	
+##sequence-region Q08756 1 102
+Q08756	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000299733;Note=Putative uncharacterized protein YOR300W	
+##sequence-region Q3E806 1 69
+Q3E806	UniProtKB	Chain	1	69	.	.	.	ID=PRO_0000245287;Note=Uncharacterized protein YOR316C-A	
+##sequence-region Q08786 1 185
+Q08786	UniProtKB	Chain	1	185	.	.	.	ID=PRO_0000262744;Note=Putative uncharacterized membrane protein YOR331C	
+Q08786	UniProtKB	Topological domain	1	69	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08786	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08786	UniProtKB	Topological domain	91	91	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08786	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08786	UniProtKB	Topological domain	113	118	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08786	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08786	UniProtKB	Topological domain	140	185	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12484 1 108
+Q12484	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000299740;Note=Uncharacterized protein YOR343C	
+##sequence-region Q08910 1 206
+Q08910	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08910	UniProtKB	Chain	20	206	.	.	.	ID=PRO_0000243950;Note=VEL1-related protein YOR387C	
+Q08910	UniProtKB	Glycosylation	26	26	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08910	UniProtKB	Glycosylation	48	48	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08910	UniProtKB	Glycosylation	91	91	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08910	UniProtKB	Glycosylation	139	139	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08910	UniProtKB	Glycosylation	152	152	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08910	UniProtKB	Glycosylation	183	183	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E832 1 53
+Q3E832	UniProtKB	Chain	1	53	.	.	.	ID=PRO_0000237652;Note=Uncharacterized protein YOR072W-B	
+##sequence-region Q08157 1 551
+Q08157	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000245272;Note=Uncharacterized membrane protein YOL019W	
+Q08157	UniProtKB	Topological domain	1	7	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08157	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08157	UniProtKB	Topological domain	29	88	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08157	UniProtKB	Transmembrane	89	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08157	UniProtKB	Topological domain	110	135	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08157	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08157	UniProtKB	Topological domain	157	160	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08157	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08157	UniProtKB	Topological domain	182	551	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08157	UniProtKB	Compositional bias	449	470	.	.	.	Note=Gln-rich	
+Q08157	UniProtKB	Modified residue	224	224	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08157	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08157	UniProtKB	Modified residue	363	363	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38070 1 525
+P38070	UniProtKB	Chain	1	525	.	.	.	ID=PRO_0000086073;Note=Serine/threonine-protein kinase YPK3	
+P38070	UniProtKB	Domain	128	424	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38070	UniProtKB	Domain	445	524	.	.	.	Note=AGC-kinase C-terminal	
+P38070	UniProtKB	Nucleotide binding	134	142	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38070	UniProtKB	Active site	277	277	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P38070	UniProtKB	Binding site	157	157	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38070	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950	
+P38070	UniProtKB	Modified residue	105	105	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38070	UniProtKB	Modified residue	107	107	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38070	UniProtKB	Modified residue	321	321	.	.	.	Note=Phosphoserine%3B by PKH1 or PKH2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12706	
+P38070	UniProtKB	Modified residue	490	490	.	.	.	Note=Phosphothreonine%3B by TORC1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12706	
+P38070	UniProtKB	Modified residue	513	513	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12706	
+##sequence-region Q3E7B3 1 70
+Q3E7B3	UniProtKB	Chain	1	70	.	.	.	ID=PRO_0000242624;Note=Uncharacterized protein YPR108W-A	
+##sequence-region Q6B0W0 1 111
+Q6B0W0	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000299817;Note=Putative uncharacterized protein YPR039W	
+Q6B0W0	UniProtKB	Transmembrane	48	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13572 1 173
+O13572	UniProtKB	Chain	1	173	.	.	.	ID=PRO_0000299831;Note=Putative uncharacterized protein YPR150W	
+O13572	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13572	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13572	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13572	UniProtKB	Transmembrane	127	147	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13572	UniProtKB	Sequence conflict	129	129	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53057 1 165
+P53057	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53057	UniProtKB	Chain	25	165	.	.	.	ID=PRO_0000014320;Note=Yapsin-5	
+P53057	UniProtKB	Domain	67	165	.	.	.	Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
+P53057	UniProtKB	Glycosylation	57	57	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38815 1 214
+P38815	UniProtKB	Chain	1	214	.	.	.	ID=PRO_0000202910;Note=PX domain-containing protein YPT35	
+P38815	UniProtKB	Domain	73	213	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
+P38815	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38815	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38815	UniProtKB	Mutagenesis	123	123	.	.	.	Note=Abolishes partially PtdIns(3)P-binding. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15263065;Dbxref=PMID:15263065	
+##sequence-region Q99260 1 215
+Q99260	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000121319;Note=GTP-binding protein YPT6	
+Q99260	UniProtKB	Nucleotide binding	17	24	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99260	UniProtKB	Nucleotide binding	65	69	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99260	UniProtKB	Nucleotide binding	124	127	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99260	UniProtKB	Motif	39	47	.	.	.	Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q99260	UniProtKB	Modified residue	215	215	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99260	UniProtKB	Lipidation	213	213	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99260	UniProtKB	Lipidation	215	215	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P31111 1 875
+P31111	UniProtKB	Chain	1	875	.	.	.	ID=PRO_0000066584;Note=Synaptonemal complex protein ZIP1	
+P31111	UniProtKB	Coiled coil	177	333	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31111	UniProtKB	Coiled coil	397	438	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31111	UniProtKB	Coiled coil	456	752	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31111	UniProtKB	Modified residue	481	481	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P31111	UniProtKB	Sequence conflict	55	55	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40021 1 1076
+P40021	UniProtKB	Chain	1	1076	.	.	.	ID=PRO_0000202624;Note=Zinc-regulated protein 8	
+P40021	UniProtKB	Compositional bias	119	126	.	.	.	Note=Poly-Pro	
+P40021	UniProtKB	Compositional bias	428	448	.	.	.	Note=Poly-Asp	
+P40021	UniProtKB	Modified residue	275	275	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40021	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P40021	UniProtKB	Modified residue	403	403	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40021	UniProtKB	Modified residue	407	407	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40021	UniProtKB	Modified residue	632	632	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40021	UniProtKB	Modified residue	676	676	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q12512 1 249
+Q12512	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12512	UniProtKB	Chain	21	249	.	.	.	ID=PRO_0000041751;Note=Protein ZPS1	
+Q12512	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12512	UniProtKB	Glycosylation	57	57	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12512	UniProtKB	Glycosylation	98	98	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12512	UniProtKB	Glycosylation	217	217	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13518 1 139
+O13518	UniProtKB	Chain	1	139	.	.	.	ID=PRO_0000299803;Note=Putative uncharacterized protein YPL114W	
+O13518	UniProtKB	Transmembrane	22	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13518	UniProtKB	Sequence conflict	9	9	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region O13571 1 109
+O13571	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299830;Note=Putative uncharacterized protein YPR146C	
+##sequence-region O13583 1 123
+O13583	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000299821;Note=Putative uncharacterized protein YPR077C	
+O13583	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06325 1 596
+Q06325	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Chain	26	596	.	.	.	ID=PRO_0000270564;Note=Aspartic proteinase yapsin-7	
+Q06325	UniProtKB	Topological domain	26	575	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Transmembrane	576	596	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Domain	56	440	.	.	.	Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
+Q06325	UniProtKB	Active site	74	74	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06325	UniProtKB	Active site	321	321	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06325	UniProtKB	Glycosylation	26	26	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	59	59	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	106	106	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	131	131	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	140	140	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	143	143	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	148	148	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	175	175	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	308	308	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	391	391	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	455	455	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	478	478	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	484	484	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	549	549	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Glycosylation	552	552	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06325	UniProtKB	Sequence conflict	299	299	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38146 1 199
+P38146	UniProtKB	Chain	1	199	.	.	.	ID=PRO_0000121321;Note=GTP-binding protein YPT10	
+P38146	UniProtKB	Nucleotide binding	11	18	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38146	UniProtKB	Nucleotide binding	65	69	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38146	UniProtKB	Nucleotide binding	122	125	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38146	UniProtKB	Modified residue	199	199	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36586	
+P38146	UniProtKB	Lipidation	197	197	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36586	
+P38146	UniProtKB	Lipidation	199	199	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36586	
+##sequence-region P38555 1 223
+P38555	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5	
+P38555	UniProtKB	Chain	2	223	.	.	.	ID=PRO_0000121323;Note=GTP-binding protein YPT31/YPT8	
+P38555	UniProtKB	Nucleotide binding	20	27	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38555	UniProtKB	Nucleotide binding	68	72	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38555	UniProtKB	Nucleotide binding	126	129	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38555	UniProtKB	Motif	42	50	.	.	.	Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38555	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5	
+P38555	UniProtKB	Lipidation	222	222	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38555	UniProtKB	Lipidation	223	223	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38555	UniProtKB	Beta strand	12	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Helix	26	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Beta strand	49	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Beta strand	60	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Turn	70	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Helix	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Turn	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Beta strand	88	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Helix	98	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Beta strand	120	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Helix	128	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Helix	138	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Beta strand	151	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P38555	UniProtKB	Helix	163	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+##sequence-region P36018 1 234
+P36018	UniProtKB	Chain	1	234	.	.	.	ID=PRO_0000121326;Note=GTP-binding protein YPT52	
+P36018	UniProtKB	Nucleotide binding	10	17	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36018	UniProtKB	Nucleotide binding	66	70	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36018	UniProtKB	Nucleotide binding	111	114	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36018	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36018	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36018	UniProtKB	Lipidation	232	232	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36018	UniProtKB	Lipidation	233	233	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36018	UniProtKB	Cross-link	151	151	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P0CX22 1 1796
+P0CX22	UniProtKB	Chain	1	1796	.	.	.	ID=PRO_0000409757;Note=Y' element ATP-dependent helicase protein 1 copy 8	
+P0CX22	UniProtKB	Domain	797	974	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P0CX22	UniProtKB	Domain	1031	1180	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P0CX22	UniProtKB	Nucleotide binding	810	817	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P0CX22	UniProtKB	Sequence conflict	1293	1293	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38280 1 609
+P38280	UniProtKB	Chain	1	609	.	.	.	ID=PRO_0000066511;Note=Spore-specific protein YSW1	
+P38280	UniProtKB	Modified residue	159	159	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38280	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38280	UniProtKB	Sequence conflict	58	58	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38280	UniProtKB	Sequence conflict	117	118	.	.	.	Note=KE->NQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38280	UniProtKB	Sequence conflict	223	224	.	.	.	Note=TP->IHR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38280	UniProtKB	Sequence conflict	271	271	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38280	UniProtKB	Sequence conflict	365	365	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38280	UniProtKB	Sequence conflict	415	416	.	.	.	Note=QQ->HE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38280	UniProtKB	Sequence conflict	460	460	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38280	UniProtKB	Sequence conflict	481	482	.	.	.	Note=LS->SR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38280	UniProtKB	Sequence conflict	488	494	.	.	.	Note=HNVYGND->PMFMAMI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38280	UniProtKB	Sequence conflict	495	609	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12324 1 675
+Q12324	UniProtKB	Chain	1	675	.	.	.	ID=PRO_0000215376;Note=Calcium channel YVC1	
+Q12324	UniProtKB	Topological domain	1	236	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Transmembrane	237	257	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Topological domain	258	295	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Transmembrane	296	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Topological domain	317	335	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Transmembrane	336	355	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Topological domain	356	376	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Transmembrane	377	397	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Topological domain	398	405	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Transmembrane	406	426	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Topological domain	427	436	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Transmembrane	437	457	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Topological domain	458	675	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Compositional bias	573	576	.	.	.	Note=Poly-Asp;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12324	UniProtKB	Modified residue	636	636	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P53303 1 486
+P53303	UniProtKB	Chain	1	486	.	.	.	ID=PRO_0000119040;Note=Zinc finger protein ZPR1	
+P53303	UniProtKB	Zinc finger	54	86	.	.	.	Note=C4-type 1	
+P53303	UniProtKB	Zinc finger	295	327	.	.	.	Note=C4-type 2	
+P53303	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53303	UniProtKB	Modified residue	407	407	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P0CF34 1 1048
+P0CF34	UniProtKB	Chain	1	1048	.	.	.	ID=PRO_0000393436;Note=Putative truncated guanine nucleotide exchange factor SDC25	
+P0CF34	UniProtKB	Domain	578	710	.	.	.	Note=N-terminal Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00135	
+P0CF34	UniProtKB	Domain	748	995	.	.	.	Note=Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00168	
+##sequence-region Q07880 1 148
+Q07880	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07880	UniProtKB	Chain	23	148	.	.	.	ID=PRO_0000299605;Note=Putative uncharacterized protein YLL044W	
+##sequence-region Q07881 1 127
+Q07881	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000299606;Note=Putative uncharacterized protein YLL047W	
+Q07881	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E798 1 87
+Q3E798	UniProtKB	Chain	1	87	.	.	.	ID=PRO_0000247352;Note=Uncharacterized protein YLR099W-A	
+##sequence-region P0C2I5 1 1755
+P0C2I5	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279099;Note=Transposon Ty1-LR2 Gag-Pol polyprotein	
+P0C2I5	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279100;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I5	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279101;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I5	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279102;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I5	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279103;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I5	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I5	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0C2I5	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+P0C2I5	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I5	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+P0C2I5	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I5	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0C2I5	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P0C2I5	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I5	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I5	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I5	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I5	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I5	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I5	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I5	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2I5	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I5	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I5	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I5	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region Q12077 1 108
+Q12077	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000299617;Note=Putative uncharacterized protein YLR140W	
+Q12077	UniProtKB	Transmembrane	10	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12077	UniProtKB	Compositional bias	28	34	.	.	.	Note=Poly-Phe	
+##sequence-region Q3E813 1 49
+Q3E813	UniProtKB	Chain	1	49	.	.	.	ID=PRO_0000262876;Note=Uncharacterized protein YLR154C-G	
+##sequence-region P0CE98 1 114
+P0CE98	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000393296;Note=Putative uncharacterized protein YLR161W	
+##sequence-region A0A023PZG4 1 107
+A0A023PZG4	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000431046;Note=Uncharacterized protein YLR236C	
+##sequence-region O13573 1 101
+O13573	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000299625;Note=Putative uncharacterized protein YLR252W	
+##sequence-region O13541 1 116
+O13541	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000299629;Note=Putative uncharacterized protein YLR280C	
+##sequence-region Q05867 1 314
+Q05867	UniProtKB	Transit peptide	1	29	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05867	UniProtKB	Chain	30	314	.	.	.	ID=PRO_0000247160;Note=Uncharacterized protein YLR283W%2C mitochondrial	
+Q05867	UniProtKB	Transmembrane	262	279	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05867	UniProtKB	Coiled coil	177	207	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05898 1 108
+Q05898	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000299633;Note=Uncharacterized protein YLR296W	
+Q05898	UniProtKB	Transmembrane	72	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05898	UniProtKB	Compositional bias	61	68	.	.	.	Note=Poly-Lys	
+##sequence-region O94085 1 183
+O94085	UniProtKB	Chain	1	183	.	.	.	ID=PRO_0000299638;Note=Putative uncharacterized protein YLR339C	
+O94085	UniProtKB	Transmembrane	153	175	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06139 1 101
+Q06139	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000247212;Note=Uncharacterized protein YLR346C%2C mitochondrial	
+##sequence-region Q3E795 1 98
+Q3E795	UniProtKB	Chain	1	98	.	.	.	ID=PRO_0000247214;Note=Uncharacterized protein YLR361C-A	
+Q3E795	UniProtKB	Compositional bias	5	11	.	.	.	Note=Poly-Asn	
+##sequence-region Q06689 1 675
+Q06689	UniProtKB	Signal peptide	1	28	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Chain	29	675	.	.	.	ID=PRO_0000247220;Note=Cell membrane protein YLR413W	
+Q06689	UniProtKB	Topological domain	29	532	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Transmembrane	533	553	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Topological domain	554	568	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Transmembrane	569	589	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Topological domain	590	610	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Transmembrane	611	631	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Topological domain	632	675	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Compositional bias	122	235	.	.	.	Note=Thr-rich	
+Q06689	UniProtKB	Modified residue	654	654	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06689	UniProtKB	Modified residue	665	665	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06689	UniProtKB	Glycosylation	49	49	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	72	72	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	142	142	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	160	160	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	194	194	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	215	215	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	252	252	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	286	286	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	299	299	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	318	318	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	322	322	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	358	358	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	375	375	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	405	405	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	429	429	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Glycosylation	468	468	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06689	UniProtKB	Cross-link	671	671	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region O13564 1 114
+O13564	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000299649;Note=Putative uncharacterized protein YLR428C	
+##sequence-region A0A023PZK9 1 126
+A0A023PZK9	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000431047;Note=Putative uncharacterized membrane protein YLR458W	
+A0A023PZK9	UniProtKB	Transmembrane	21	43	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZK9	UniProtKB	Transmembrane	48	70	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CE99 1 70
+P0CE99	UniProtKB	Chain	1	70	.	.	.	ID=PRO_0000393297;Note=Putative uncharacterized protein YLR157W-D	
+##sequence-region Q04461 1 462
+Q04461	UniProtKB	Chain	1	462	.	.	.	ID=PRO_0000203291;Note=Uncharacterized protein YMR111C	
+Q04461	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04461	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04461	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04461	UniProtKB	Modified residue	249	249	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q04461	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q04471 1 368
+Q04471	UniProtKB	Chain	1	368	.	.	.	ID=PRO_0000203292;Note=Putative peptidase YMR114C	
+Q04471	UniProtKB	Modified residue	338	338	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region A2P2R3 1 262
+A2P2R3	UniProtKB	Chain	1	262	.	.	.	ID=PRO_0000269757;Note=Putative glutamine--fructose-6-phosphate aminotransferase [isomerizing]	
+A2P2R3	UniProtKB	Domain	2	262	.	.	.	Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609	
+A2P2R3	UniProtKB	Active site	2	2	.	.	.	Note=Nucleophile%3B for GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609	
+##sequence-region Q04670 1 1755
+Q04670	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000199568;Note=Transposon Ty1-MR2 Gag-Pol polyprotein	
+Q04670	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279133;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04670	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279134;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04670	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279135;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04670	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279136;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04670	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04670	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q04670	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q04670	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04670	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q04670	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04670	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q04670	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q04670	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04670	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04670	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04670	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04670	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04670	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04670	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04670	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q04670	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04670	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04670	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04670	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region Q8TGS6 1 29
+Q8TGS6	UniProtKB	Chain	1	29	.	.	.	ID=PRO_0000247792;Note=Uncharacterized protein YMR242W-A	
+##sequence-region A0A023PZL7 1 119
+A0A023PZL7	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000431052;Note=Putative uncharacterized protein YMR294W-A	
+##sequence-region P0C5Q5 1 64
+P0C5Q5	UniProtKB	Chain	1	64	.	.	.	ID=PRO_0000309053;Note=Putative uncharacterized protein YMR307C-A	
+##sequence-region Q8TGS4 1 35
+Q8TGS4	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q8TGS4	UniProtKB	Chain	26	35	.	.	.	ID=PRO_0000247796;Note=Uncharacterized protein YMR315W-A	
+##sequence-region Q03823 1 816
+Q03823	UniProtKB	Chain	1	816	.	.	.	ID=PRO_0000203313;Note=Uncharacterized protein YMR160W	
+Q03823	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03823	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q03231 1 154
+Q03231	UniProtKB	Chain	1	154	.	.	.	ID=PRO_0000203320;Note=Uncharacterized protein YMR181C	
+Q03231	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q04814 1 134
+Q04814	UniProtKB	Chain	1	134	.	.	.	ID=PRO_0000203339;Note=Uncharacterized protein YMR252C	
+##sequence-region Q04867 1 317
+Q04867	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000203354;Note=Putative methyltransferase YMR310C	
+Q04867	UniProtKB	Modified residue	190	190	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32843 1 850
+P32843	UniProtKB	Transit peptide	1	44	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32843	UniProtKB	Chain	45	850	.	.	.	ID=PRO_0000081806;Note=Mitochondrial escape protein 2	
+P32843	UniProtKB	Topological domain	45	287	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32843	UniProtKB	Transmembrane	288	308	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32843	UniProtKB	Topological domain	309	850	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32843	UniProtKB	Domain	198	272	.	.	.	Note=RRM	
+P32843	UniProtKB	Mutagenesis	502	502	.	.	.	Note=In YME2-4%3B prevents mtDNA escape%2C growth on nonfermentable carbon sources and growth at 37 degrees Celsius on glucose. N->Y;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1557037,ECO:0000269|PubMed:16850347,ECO:0000269|PubMed:8649384;Dbxref=PMID:1557037,PMID:16850347,PMID:8649384	
+##sequence-region Q03629 1 201
+Q03629	UniProtKB	Chain	1	201	.	.	.	ID=PRO_0000203248;Note=Uncharacterized protein YML079W	
+Q03629	UniProtKB	Helix	17	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Helix	28	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	45	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	74	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	80	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	92	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	102	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	111	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	122	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Helix	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	136	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	146	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Turn	155	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	161	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Helix	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Beta strand	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Helix	181	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Helix	191	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+Q03629	UniProtKB	Helix	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7	
+##sequence-region Q03208 1 357
+Q03208	UniProtKB	Chain	1	357	.	.	.	ID=PRO_0000203240;Note=Uncharacterized protein YML119W	
+Q03208	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+##sequence-region Q03102 1 365
+Q03102	UniProtKB	Chain	1	365	.	.	.	ID=PRO_0000203238;Note=Uncharacterized membrane protein YML131W	
+Q03102	UniProtKB	Topological domain	1	133	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03102	UniProtKB	Transmembrane	134	154	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03102	UniProtKB	Topological domain	155	169	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03102	UniProtKB	Transmembrane	170	190	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03102	UniProtKB	Topological domain	191	365	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03102	UniProtKB	Sequence conflict	239	239	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04773 1 145
+Q04773	UniProtKB	Chain	1	145	.	.	.	ID=PRO_0000121548;Note=Uncharacterized protein YMR074C	
+Q04773	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04773	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q04773	UniProtKB	Modified residue	126	126	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04773	UniProtKB	Helix	3	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JXN	
+Q04773	UniProtKB	Helix	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FH0	
+Q04773	UniProtKB	Helix	52	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FH0	
+Q04773	UniProtKB	Helix	66	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FH0	
+Q04773	UniProtKB	Helix	91	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FH0	
+##sequence-region Q04436 1 120
+Q04436	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000203289;Note=Uncharacterized protein YMR103C	
+##sequence-region P0C5Q7 1 72
+P0C5Q7	UniProtKB	Chain	1	72	.	.	.	ID=PRO_0000309055;Note=Putative uncharacterized protein YNR001W-A	
+##sequence-region Q8TGJ2 1 30
+Q8TGJ2	UniProtKB	Chain	1	30	.	.	.	ID=PRO_0000247804;Note=Putative UPF0377 protein YNR075C-A	
+##sequence-region Q12391 1 440
+Q12391	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279142;Note=Transposon Ty1-NL1 Gag polyprotein	
+Q12391	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279143;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12391	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279144;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12391	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12391	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12470 1 440
+Q12470	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279150;Note=Transposon Ty1-NL2 Gag polyprotein	
+Q12470	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279151;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12470	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279152;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12470	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12470	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12470	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region P42840 1 284
+P42840	UniProtKB	Chain	1	284	.	.	.	ID=PRO_0000203364;Note=Uncharacterized membrane protein YNL320W	
+P42840	UniProtKB	Topological domain	1	8	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42840	UniProtKB	Transmembrane	9	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42840	UniProtKB	Topological domain	26	80	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42840	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42840	UniProtKB	Topological domain	102	284	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53821 1 84
+P53821	UniProtKB	Chain	1	84	.	.	.	ID=PRO_0000211377;Note=Putative UPF0320 protein YNL337W	
+##sequence-region P53719 1 212
+P53719	UniProtKB	Chain	1	212	.	.	.	ID=PRO_0000203471;Note=Uncharacterized protein YNR014W	
+P53719	UniProtKB	Compositional bias	30	42	.	.	.	Note=Poly-Ser	
+P53719	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:18407956,PMID:19779198	
+##sequence-region P53726 1 119
+P53726	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000203475;Note=Putative uncharacterized protein YNR025C	
+P53726	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53726	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53747 1 219
+P53747	UniProtKB	Chain	1	219	.	.	.	ID=PRO_0000203481;Note=Uncharacterized vacuolar membrane protein YNR061C	
+P53747	UniProtKB	Topological domain	1	15	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53747	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53747	UniProtKB	Topological domain	37	41	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53747	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53747	UniProtKB	Topological domain	63	63	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53747	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53747	UniProtKB	Topological domain	85	116	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53747	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53747	UniProtKB	Topological domain	138	219	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53980 1 444
+P53980	UniProtKB	Chain	1	444	.	.	.	ID=PRO_0000203465;Note=Uncharacterized protein YNL011C	
+##sequence-region P53902 1 135
+P53902	UniProtKB	Chain	1	135	.	.	.	ID=PRO_0000203420;Note=Putative uncharacterized protein YNL150W	
+P53902	UniProtKB	Compositional bias	41	50	.	.	.	Note=Poly-Ser	
+##sequence-region P53887 1 122
+P53887	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000203409;Note=Putative uncharacterized protein YNL171C	
+##sequence-region P40169 1 301
+P40169	UniProtKB	Chain	1	301	.	.	.	ID=PRO_0000203399;Note=Uncharacterized plasma membrane protein YNL194C	
+P40169	UniProtKB	Topological domain	1	5	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40169	UniProtKB	Transmembrane	6	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40169	UniProtKB	Topological domain	27	112	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40169	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40169	UniProtKB	Topological domain	134	143	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40169	UniProtKB	Transmembrane	144	164	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40169	UniProtKB	Topological domain	165	191	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40169	UniProtKB	Transmembrane	192	212	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40169	UniProtKB	Topological domain	213	301	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40159 1 199
+P40159	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40159	UniProtKB	Chain	2	199	.	.	.	ID=PRO_0000203391;Note=Uncharacterized protein YNL208W	
+P40159	UniProtKB	Compositional bias	25	196	.	.	.	Note=Gly-rich	
+P40159	UniProtKB	Compositional bias	119	123	.	.	.	Note=Poly-Asn	
+P40159	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40159	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40159	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q08110 1 124
+Q08110	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000245271;Note=Putative uncharacterized protein YOL014W	
+##sequence-region Q8TGS1 1 66
+Q8TGS1	UniProtKB	Chain	1	66	.	.	.	ID=PRO_0000237645;Note=Uncharacterized protein YOR032W-A	
+Q8TGS1	UniProtKB	Transmembrane	4	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q8TGS1	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E7Z9 1 31
+Q3E7Z9	UniProtKB	Chain	1	31	.	.	.	ID=PRO_0000235922;Note=Uncharacterized protein YOL038C-A	
+##sequence-region Q8TGL6 1 69
+Q8TGL6	UniProtKB	Chain	1	69	.	.	.	ID=PRO_0000299713;Note=Putative uncharacterized protein YOR108C-A	
+##sequence-region Q92392 1 440
+Q92392	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279158;Note=Transposon Ty1-OL Gag polyprotein	
+Q92392	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279159;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92392	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279160;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92392	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92392	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q92392	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q92392	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q08521 1 101
+Q08521	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000299714;Note=Putative uncharacterized protein YOR121C	
+##sequence-region Q08293 1 103
+Q08293	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000299697;Note=Putative uncharacterized protein YOL150C	
+##sequence-region Q08621 1 117
+Q08621	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000299724;Note=Putative uncharacterized protein YOR203W	
+##sequence-region Q12015 1 292
+Q12015	UniProtKB	Chain	1	292	.	.	.	ID=PRO_0000237667;Note=Transmembrane protein YOR223W	
+Q12015	UniProtKB	Topological domain	1	243	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12015	UniProtKB	Transmembrane	244	264	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12015	UniProtKB	Topological domain	265	273	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12015	UniProtKB	Transmembrane	274	291	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12015	UniProtKB	Topological domain	292	292	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12015	UniProtKB	Glycosylation	11	11	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12015	UniProtKB	Glycosylation	41	41	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12015	UniProtKB	Glycosylation	77	77	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12015	UniProtKB	Glycosylation	99	99	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12015	UniProtKB	Glycosylation	145	145	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08741 1 106
+Q08741	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000299732;Note=Putative uncharacterized protein YOR282W	
+Q08741	UniProtKB	Transmembrane	39	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08741	UniProtKB	Transmembrane	74	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08743 1 309
+Q08743	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000245252;Note=Vacuolar membrane protein YOR292C	
+Q08743	UniProtKB	Topological domain	1	52	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Topological domain	74	81	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Topological domain	103	183	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Transmembrane	184	204	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Topological domain	205	225	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Transmembrane	226	246	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Topological domain	247	260	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Transmembrane	261	281	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Topological domain	282	309	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Glycosylation	19	19	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08743	UniProtKB	Glycosylation	121	121	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08789 1 138
+Q08789	UniProtKB	Chain	1	138	.	.	.	ID=PRO_0000299738;Note=Putative uncharacterized protein YOR333C	
+Q08789	UniProtKB	Compositional bias	114	119	.	.	.	Note=Poly-Arg	
+##sequence-region Q08811 1 116
+Q08811	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000299741;Note=Putative uncharacterized protein YOR345C	
+Q08811	UniProtKB	Transmembrane	22	42	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E805 1 51
+Q3E805	UniProtKB	Chain	1	51	.	.	.	ID=PRO_0000244634;Note=Uncharacterized protein YOR376W-A	
+##sequence-region Q3E804 1 55
+Q3E804	UniProtKB	Chain	1	55	.	.	.	ID=PRO_0000244635;Note=Uncharacterized protein YOR381W-A	
+##sequence-region Q08912 1 624
+Q08912	UniProtKB	Signal peptide	1	29	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08912	UniProtKB	Chain	30	624	.	.	.	ID=PRO_0000244637;Note=Uncharacterized protein YOR389W	
+Q08912	UniProtKB	Glycosylation	68	68	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08912	UniProtKB	Glycosylation	150	150	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08912	UniProtKB	Glycosylation	219	219	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08912	UniProtKB	Glycosylation	366	366	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08912	UniProtKB	Glycosylation	441	441	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08912	UniProtKB	Glycosylation	447	447	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08912	UniProtKB	Glycosylation	464	464	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08912	UniProtKB	Glycosylation	528	528	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGL5 1 26
+Q8TGL5	UniProtKB	Chain	1	26	.	.	.	ID=PRO_0000299717;Note=Putative uncharacterized protein YOR161W-A	
+##sequence-region Q8TGQ8 1 70
+Q8TGQ8	UniProtKB	Chain	1	70	.	.	.	ID=PRO_0000299693;Note=Putative uncharacterized protein YOL085W-A	
+##sequence-region P0CL40 1 160
+P0CL40	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000406014;Note=Putative UPF0479 protein YOR396C-A	
+P0CL40	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL40	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL40	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region Q12219 1 294
+Q12219	UniProtKB	Chain	1	294	.	.	.	ID=PRO_0000237656;Note=Uncharacterized protein YOR114W	
+##sequence-region P34161 1 385
+P34161	UniProtKB	Chain	1	385	.	.	.	ID=PRO_0000049387;Note=Homeobox protein YOX1	
+P34161	UniProtKB	DNA binding	176	235	.	.	.	Note=Homeobox;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108	
+P34161	UniProtKB	Sequence conflict	291	296	.	.	.	Note=PRPHHS->QGLIIP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03083 1 165
+Q03083	UniProtKB	Chain	1	165	.	.	.	ID=PRO_0000240704;Note=Uncharacterized protein YPL034W	
+##sequence-region O13520 1 182
+O13520	UniProtKB	Chain	1	182	.	.	.	ID=PRO_0000299799;Note=Putative uncharacterized protein YPL044C	
+O13520	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13520	UniProtKB	Transmembrane	114	130	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13520	UniProtKB	Compositional bias	40	49	.	.	.	Note=Poly-Ser	
+##sequence-region Q12160 1 140
+Q12160	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000257824;Note=Uncharacterized protein YPR063C	
+Q12160	UniProtKB	Transmembrane	91	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12160	UniProtKB	Glycosylation	36	36	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40323 1 161
+P40323	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000203493;Note=Uncharacterized protein YPL073C	
+##sequence-region Q06821 1 456
+Q06821	UniProtKB	Chain	1	456	.	.	.	ID=PRO_0000242638;Note=Uncharacterized protein YPR084W	
+##sequence-region O13587 1 100
+O13587	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299823;Note=Uncharacterized protein YPR096C	
+##sequence-region Q02873 1 248
+Q02873	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02873	UniProtKB	Chain	27	248	.	.	.	ID=PRO_0000238646;Note=UPF0651 protein YPL107W%2C mitochondrial	
+Q02873	UniProtKB	Domain	69	116	.	.	.	Note=Oxidoreductase-like	
+##sequence-region Q06116 1 2489
+Q06116	UniProtKB	Chain	1	2489	.	.	.	ID=PRO_0000257827;Note=Uncharacterized protein YPR117W	
+Q06116	UniProtKB	Transmembrane	19	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Coiled coil	1610	1676	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Modified residue	2254	2254	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06116	UniProtKB	Modified residue	2278	2278	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06116	UniProtKB	Glycosylation	191	191	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	210	210	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	311	311	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	452	452	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	468	468	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	605	605	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	638	638	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	663	663	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	698	698	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	789	789	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	835	835	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	981	981	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	1255	1255	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	1404	1404	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	1476	1476	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	1978	1978	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	2189	2189	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06116	UniProtKB	Glycosylation	2279	2279	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13567 1 102
+O13567	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000299826;Note=Putative uncharacterized protein YPR126C	
+O13567	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13567	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX60 1 440
+P0CX60	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000409806;Note=Transposon Ty1-PR2 Gag polyprotein	
+P0CX60	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000409807;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX60	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000409808;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX60	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX60	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX60	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX60	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q06523 1 435
+Q06523	UniProtKB	Chain	1	435	.	.	.	ID=PRO_0000257829;Note=Uncharacterized protein YPR148C	
+Q06523	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q8TGR9 1 32
+Q8TGR9	UniProtKB	Chain	1	32	.	.	.	ID=PRO_0000238654;Note=Uncharacterized protein YPL152W-A	
+##sequence-region Q8TGK8 1 94
+Q8TGK8	UniProtKB	Chain	1	94	.	.	.	ID=PRO_0000299832;Note=Putative uncharacterized protein YPR160C-A	
+Q8TGK8	UniProtKB	Sequence conflict	12	12	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q8TGK8	UniProtKB	Sequence conflict	79	80	.	.	.	Note=PT->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0C5R8 1 61
+P0C5R8	UniProtKB	Chain	1	61	.	.	.	ID=PRO_0000309066;Note=Putative uncharacterized protein YPR170W-A	
+P0C5R8	UniProtKB	Transmembrane	5	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C5R8	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08927 1 131
+Q08927	UniProtKB	Chain	1	131	.	.	.	ID=PRO_0000299807;Note=Putative uncharacterized protein YPL185W	
+Q08927	UniProtKB	Transmembrane	13	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08927	UniProtKB	Transmembrane	60	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08927	UniProtKB	Transmembrane	100	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08953 1 137
+Q08953	UniProtKB	Chain	1	137	.	.	.	ID=PRO_0000299808;Note=Putative uncharacterized protein YPL197C	
+##sequence-region Q08995 1 1032
+Q08995	UniProtKB	Chain	1	1032	.	.	.	ID=PRO_0000268169;Note=Y' element ATP-dependent helicase YPR204W	
+Q08995	UniProtKB	Domain	1	175	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q08995	UniProtKB	Domain	232	381	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q08995	UniProtKB	Nucleotide binding	11	18	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q08995	UniProtKB	Motif	121	124	.	.	.	Note=DEAH box	
+Q08995	UniProtKB	Compositional bias	459	631	.	.	.	Note=Thr-rich	
+##sequence-region Q08971 1 146
+Q08971	UniProtKB	Chain	1	146	.	.	.	ID=PRO_0000242144;Note=Protein PBDC1 homolog	
+Q08971	UniProtKB	Beta strand	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Helix	12	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Helix	48	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Turn	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Helix	65	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Turn	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Helix	79	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Turn	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Beta strand	103	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Beta strand	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Helix	123	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Turn	136	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+Q08971	UniProtKB	Helix	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN	
+##sequence-region Q12058 1 100
+Q12058	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299812;Note=Putative uncharacterized protein YPL251W	
+Q12058	UniProtKB	Compositional bias	51	57	.	.	.	Note=Poly-Val	
+##sequence-region Q08984 1 517
+Q08984	UniProtKB	Chain	1	517	.	.	.	ID=PRO_0000242637;Note=Uncharacterized protein YPL272C	
+##sequence-region P0CX97 1 160
+P0CX97	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000410454;Note=UPF0479 membrane protein YPL283W-B	
+P0CX97	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX97	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX97	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region Q12159 1 226
+Q12159	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q12159	UniProtKB	Chain	2	226	.	.	.	ID=PRO_0000082007;Note=RNA annealing protein YRA1	
+Q12159	UniProtKB	Domain	78	158	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q12159	UniProtKB	Compositional bias	201	210	.	.	.	Note=Arg/Lys-rich (basic)	
+Q12159	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q12159	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q12159	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12159	UniProtKB	Helix	212	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+##sequence-region P53107 1 440
+P53107	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000213672;Note=Ran-specific GTPase-activating protein 30	
+P53107	UniProtKB	Domain	1	314	.	.	.	Note=RanBD1	
+P53107	UniProtKB	Modified residue	272	272	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q12436 1 422
+Q12436	UniProtKB	Chain	1	422	.	.	.	ID=PRO_0000068769;Note=Zinc-regulated transporter 2	
+Q12436	UniProtKB	Topological domain	1	27	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Transmembrane	28	48	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Topological domain	49	60	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Transmembrane	61	81	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Topological domain	82	99	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Topological domain	121	262	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Transmembrane	263	283	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Topological domain	284	290	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Transmembrane	291	311	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Topological domain	312	326	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Transmembrane	327	347	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Topological domain	348	358	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Transmembrane	359	379	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Topological domain	380	400	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Transmembrane	401	421	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Topological domain	422	422	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12436	UniProtKB	Region	276	277	.	.	.	Note=Heavy metals binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12436	UniProtKB	Modified residue	148	148	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12436	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12436	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12436	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12436	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32527 1 433
+P32527	UniProtKB	Chain	1	433	.	.	.	ID=PRO_0000071122;Note=Zuotin	
+P32527	UniProtKB	Domain	98	170	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P32527	UniProtKB	Compositional bias	306	357	.	.	.	Note=Ala/Lys-rich	
+P32527	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P32527	UniProtKB	Mutagenesis	128	128	.	.	.	Note=Loss of function%2C but still forms a heterodimer with SSZ1 and associates with ribosomes. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11929994;Dbxref=PMID:11929994	
+P32527	UniProtKB	Helix	184	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE	
+P32527	UniProtKB	Beta strand	199	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE	
+P32527	UniProtKB	Helix	214	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE	
+P32527	UniProtKB	Helix	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE	
+P32527	UniProtKB	Helix	249	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE	
+P32527	UniProtKB	Helix	284	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE	
+P32527	UniProtKB	Helix	348	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX	
+P32527	UniProtKB	Helix	371	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX	
+P32527	UniProtKB	Helix	374	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX	
+P32527	UniProtKB	Helix	390	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX	
+P32527	UniProtKB	Helix	404	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX	
+P32527	UniProtKB	Helix	408	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX	
+P32527	UniProtKB	Helix	426	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX	
+P32527	UniProtKB	Turn	430	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX	
+##sequence-region P40523 1 627
+P40523	UniProtKB	Chain	1	627	.	.	.	ID=PRO_0000202989;Note=Uncharacterized protein YIL055C	
+P40523	UniProtKB	Modified residue	559	559	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P40445 1 542
+P40445	UniProtKB	Chain	1	542	.	.	.	ID=PRO_0000121373;Note=Uncharacterized transporter YIL166C	
+P40445	UniProtKB	Topological domain	1	78	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Transmembrane	79	99	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Topological domain	100	119	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Topological domain	141	147	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Transmembrane	148	168	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Topological domain	169	176	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Topological domain	198	208	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Topological domain	230	241	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Topological domain	263	326	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Transmembrane	327	347	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Topological domain	348	359	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Transmembrane	360	380	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Topological domain	381	387	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Transmembrane	388	408	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Topological domain	409	416	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Transmembrane	417	437	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Topological domain	438	482	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Transmembrane	483	503	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40445	UniProtKB	Topological domain	504	542	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E775 1 16
+Q3E775	UniProtKB	Chain	1	16	.	.	.	ID=PRO_0000245417;Note=Uncharacterized protein YJR151W-A	
+##sequence-region P0C5P0 1 93
+P0C5P0	UniProtKB	Chain	1	93	.	.	.	ID=PRO_0000309038;Note=Uncharacterized protein YJL197C-A	
+##sequence-region P47114 1 497
+P47114	UniProtKB	Chain	1	497	.	.	.	ID=PRO_0000203096;Note=Uncharacterized vacuolar membrane protein YJR054W	
+P47114	UniProtKB	Topological domain	1	29	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47114	UniProtKB	Transmembrane	30	50	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47114	UniProtKB	Topological domain	51	80	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47114	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47114	UniProtKB	Topological domain	102	216	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47114	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47114	UniProtKB	Topological domain	238	497	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47114	UniProtKB	Modified residue	291	291	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47114	UniProtKB	Modified residue	319	319	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P47062 1 111
+P47062	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000203071;Note=Uncharacterized protein YJL028W	
+P47062	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47062	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CL24 1 45
+P0CL24	UniProtKB	Chain	1	45	.	.	.	ID=PRO_0000406004;Note=Putative UPF0377 protein YJL222W-B	
+##sequence-region P46992 1 396
+P46992	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Chain	20	368	.	.	.	ID=PRO_0000042986;Note=Cell wall protein YJL171C	
+P46992	UniProtKB	Propeptide	369	396	.	.	.	ID=PRO_0000406124;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Lipidation	368	368	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Glycosylation	51	51	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Glycosylation	99	99	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Glycosylation	122	122	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Glycosylation	146	146	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Glycosylation	174	174	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Glycosylation	219	219	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Glycosylation	249	249	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Glycosylation	267	267	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Glycosylation	300	300	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Glycosylation	328	328	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Glycosylation	346	346	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46992	UniProtKB	Sequence conflict	366	366	.	.	.	Note=K->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46992	UniProtKB	Sequence conflict	371	371	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46992	UniProtKB	Sequence conflict	374	374	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40891 1 150
+P40891	UniProtKB	Chain	1	150	.	.	.	ID=PRO_0000203010;Note=Putative uncharacterized protein YJL220W	
+##sequence-region P47087 1 207
+P47087	UniProtKB	Chain	1	207	.	.	.	ID=PRO_0000203083;Note=Uncharacterized protein YJR012C	
+P47087	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47087	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q2V2P2 1 73
+Q2V2P2	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000245422;Note=Uncharacterized protein YKL065W-A	
+Q2V2P2	UniProtKB	Transmembrane	37	54	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E7A0 1 39
+Q3E7A0	UniProtKB	Chain	1	39	.	.	.	ID=PRO_0000245419;Note=Uncharacterized protein YKL106C-A	
+##sequence-region P0C5P4 1 50
+P0C5P4	UniProtKB	Chain	1	50	.	.	.	ID=PRO_0000309042;Note=Putative uncharacterized protein YKL162C-A	
+##sequence-region P32859 1 130
+P32859	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000203184;Note=Putative uncharacterized protein YKL036C	
+##sequence-region P33324 1 310
+P33324	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000210747;Note=CRAL-TRIO domain-containing protein YKL091C	
+P33324	UniProtKB	Domain	101	274	.	.	.	Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056	
+P33324	UniProtKB	Helix	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	27	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	51	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Turn	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	65	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	87	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	95	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Beta strand	111	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Beta strand	122	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	133	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	142	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	160	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Beta strand	175	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	186	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	193	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Beta strand	211	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	223	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Turn	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	231	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	236	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Beta strand	242	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	249	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	264	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Beta strand	282	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B74	
+P33324	UniProtKB	Helix	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Turn	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+P33324	UniProtKB	Helix	304	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G	
+##sequence-region P36061 1 205
+P36061	UniProtKB	Chain	1	205	.	.	.	ID=PRO_0000203146;Note=Putative uncharacterized protein YKL147C	
+##sequence-region Q07799 1 665
+Q07799	UniProtKB	Chain	1	665	.	.	.	ID=PRO_0000247098;Note=Uncharacterized protein YLL007C	
+##sequence-region Q07811 1 101
+Q07811	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000299602;Note=Putative uncharacterized protein YLL020C	
+Q07811	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07811	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07990 1 161
+Q07990	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07990	UniProtKB	Chain	25	139	.	.	.	ID=PRO_0000247444;Note=Cell wall protein YLR042C	
+Q07990	UniProtKB	Propeptide	140	161	.	.	.	ID=PRO_0000247445;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07990	UniProtKB	Compositional bias	62	136	.	.	.	Note=Ser-rich	
+Q07990	UniProtKB	Lipidation	139	139	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07990	UniProtKB	Glycosylation	77	77	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07990	UniProtKB	Glycosylation	104	104	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07990	UniProtKB	Glycosylation	120	120	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12155 1 161
+Q12155	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000247205;Note=Uncharacterized membrane protein YLR050C	
+Q12155	UniProtKB	Topological domain	1	10	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12155	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12155	UniProtKB	Topological domain	32	61	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12155	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12155	UniProtKB	Topological domain	83	101	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12155	UniProtKB	Transmembrane	102	122	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12155	UniProtKB	Topological domain	123	161	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12155	UniProtKB	Domain	7	159	.	.	.	Note=EXPERA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01087	
+##sequence-region Q07888 1 1374
+Q07888	UniProtKB	Chain	1	1374	.	.	.	ID=PRO_0000268168;Note=Y' element ATP-dependent helicase YLL067C	
+Q07888	UniProtKB	Domain	375	552	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q07888	UniProtKB	Domain	609	758	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q07888	UniProtKB	Nucleotide binding	388	395	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q07888	UniProtKB	Motif	498	501	.	.	.	Note=DEAH box	
+Q07888	UniProtKB	Compositional bias	836	1008	.	.	.	Note=Thr-rich	
+##sequence-region Q08027 1 131
+Q08027	UniProtKB	Chain	1	131	.	.	.	ID=PRO_0000299610;Note=Putative uncharacterized protein YLR101C	
+Q08027	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08027	UniProtKB	Transmembrane	41	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08027	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12130 1 139
+Q12130	UniProtKB	Chain	1	139	.	.	.	ID=PRO_0000299612;Note=Uncharacterized protein YLR112W	
+##sequence-region Q12312 1 125
+Q12312	UniProtKB	Chain	1	125	.	.	.	ID=PRO_0000299614;Note=Uncharacterized protein YLR122C	
+Q12312	UniProtKB	Transmembrane	7	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX75 1 440
+P0CX75	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000409800;Note=Transposon Ty1-LR3 Gag polyprotein	
+P0CX75	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000409801;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX75	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000409802;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX75	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX75	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX75	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX75	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+P0CX75	UniProtKB	Sequence conflict	255	255	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99296 1 730
+Q99296	UniProtKB	Chain	1	730	.	.	.	ID=PRO_0000262875;Note=Uncharacterized protein YLR149C	
+Q99296	UniProtKB	Compositional bias	455	460	.	.	.	Note=Poly-Asn	
+Q99296	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q99296	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q99296	UniProtKB	Modified residue	483	483	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q99296	UniProtKB	Modified residue	651	651	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P54072 1 576
+P54072	UniProtKB	Chain	1	576	.	.	.	ID=PRO_0000123806;Note=Uncharacterized transporter YLR152C	
+P54072	UniProtKB	Topological domain	1	8	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Topological domain	30	45	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Topological domain	67	71	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Topological domain	93	103	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Topological domain	125	141	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Topological domain	163	400	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Transmembrane	401	421	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Topological domain	422	437	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Transmembrane	438	458	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Topological domain	459	476	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Transmembrane	477	497	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Topological domain	498	512	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Transmembrane	513	533	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Topological domain	534	545	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Transmembrane	546	566	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54072	UniProtKB	Topological domain	567	576	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CY03 1 43
+P0CY03	UniProtKB	Chain	1	43	.	.	.	ID=PRO_0000410459;Note=Uncharacterized protein YLR156C-A	
+##sequence-region P0C2J5 1 1598
+P0C2J5	UniProtKB	Chain	1	1598	.	.	.	ID=PRO_0000279332;Note=Transposon Ty2-LR2 Gag-Pol polyprotein	
+P0C2J5	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279333;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J5	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000279334;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J5	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000279335;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J5	UniProtKB	Chain	1233	1598	.	.	.	ID=PRO_0000279336;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J5	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J5	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0C2J5	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J5	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+P0C2J5	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J5	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J5	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J5	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J5	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J5	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J5	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0C2J5	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J5	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J5	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q3E732 1 38
+Q3E732	UniProtKB	Chain	1	38	.	.	.	ID=PRO_0000247136;Note=Putative uncharacterized protein YLR264C-A	
+##sequence-region O13550 1 116
+O13550	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000299627;Note=Putative uncharacterized protein YLR269C	
+O13550	UniProtKB	Transmembrane	5	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05854 1 1341
+Q05854	UniProtKB	Chain	1	1341	.	.	.	ID=PRO_0000115003;Note=Uncharacterized transcriptional regulatory protein YLR278C	
+Q05854	UniProtKB	DNA binding	41	68	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+Q05854	UniProtKB	Compositional bias	255	261	.	.	.	Note=Poly-Asn	
+Q05854	UniProtKB	Compositional bias	873	885	.	.	.	Note=Poly-Ser	
+Q05854	UniProtKB	Compositional bias	918	943	.	.	.	Note=Poly-Asn	
+Q05854	UniProtKB	Compositional bias	1231	1238	.	.	.	Note=Poly-Gln	
+Q05854	UniProtKB	Modified residue	1143	1143	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q05863 1 155
+Q05863	UniProtKB	Transit peptide	1	17	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05863	UniProtKB	Chain	18	155	.	.	.	ID=PRO_0000247341;Note=Uncharacterized peptide chain release factor-like protein YLR281C%2C mitochondrial	
+##sequence-region Q8TGM4 1 44
+Q8TGM4	UniProtKB	Chain	1	44	.	.	.	ID=PRO_0000299631;Note=Putative uncharacterized protein YLR286W-A	
+##sequence-region O13544 1 120
+O13544	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000299635;Note=Uncharacterized protein YLR302C	
+O13544	UniProtKB	Transmembrane	40	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13553 1 144
+O13553	UniProtKB	Chain	1	144	.	.	.	ID=PRO_0000299636;Note=Putative uncharacterized protein YLR317W	
+##sequence-region Q8TGM2 1 46
+Q8TGM2	UniProtKB	Chain	1	46	.	.	.	ID=PRO_0000299639;Note=Putative uncharacterized protein YLR347W-A	
+##sequence-region Q3E747 1 85
+Q3E747	UniProtKB	Chain	1	85	.	.	.	ID=PRO_0000247215;Note=Uncharacterized protein YLR363W-A	
+Q3E747	UniProtKB	Compositional bias	4	48	.	.	.	Note=Lys-rich	
+##sequence-region O13576 1 127
+O13576	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000299650;Note=Putative uncharacterized protein YLR434C	
+##sequence-region P54007 1 376
+P54007	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000203236;Note=Uncharacterized protein YLR460C	
+##sequence-region Q06493 1 454
+Q06493	UniProtKB	Transit peptide	1	45	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06493	UniProtKB	Chain	46	454	.	.	.	ID=PRO_0000244478;Note=LETM1 domain-containing protein YLH47%2C mitochondrial	
+Q06493	UniProtKB	Topological domain	46	136	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06493	UniProtKB	Transmembrane	137	157	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06493	UniProtKB	Topological domain	158	454	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06493	UniProtKB	Domain	177	371	.	.	.	Note=Letm1 RBD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01094	
+Q06493	UniProtKB	Coiled coil	376	423	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06493	UniProtKB	Sequence conflict	265	265	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06493	UniProtKB	Sequence conflict	265	265	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06493	UniProtKB	Sequence conflict	439	439	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06493	UniProtKB	Sequence conflict	439	439	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06493	UniProtKB	Sequence conflict	442	442	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06493	UniProtKB	Sequence conflict	442	442	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CD98 1 152
+P0CD98	UniProtKB	Chain	1	152	.	.	.	ID=PRO_0000391656;Note=Putative uncharacterized protein YLL053C	
+P0CD98	UniProtKB	Topological domain	1	5	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD98	UniProtKB	Transmembrane	6	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD98	UniProtKB	Topological domain	27	38	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD98	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD98	UniProtKB	Topological domain	60	65	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD98	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD98	UniProtKB	Topological domain	87	110	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD98	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD98	UniProtKB	Topological domain	132	152	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD98	UniProtKB	Motif	92	94	.	.	.	Note=NPA	
+##sequence-region Q3E7A6 1 36
+Q3E7A6	UniProtKB	Chain	1	36	.	.	.	ID=PRO_0000247783;Note=Uncharacterized protein YML007C-A%2C mitochondrial	
+##sequence-region Q03879 1 124
+Q03879	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000203296;Note=Uncharacterized protein YMR122C	
+##sequence-region Q6B108 1 100
+Q6B108	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299660;Note=Putative uncharacterized protein YML116W-A	
+##sequence-region Q04706 1 440
+Q04706	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000203498;Note=Transposon Ty1-ML1 Gag polyprotein	
+Q04706	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279121;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04706	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279122;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04706	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04706	UniProtKB	Compositional bias	72	146	.	.	.	Note=Pro-rich	
+Q04706	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04706	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q3E842 1 84
+Q3E842	UniProtKB	Chain	1	84	.	.	.	ID=PRO_0000247787;Note=Uncharacterized endoplasmic reticulum membrane protein YMR122W-A	
+Q3E842	UniProtKB	Transmembrane	66	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E842	UniProtKB	Compositional bias	3	50	.	.	.	Note=Ser-rich	
+Q3E842	UniProtKB	Glycosylation	45	45	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX69 1 440
+P0CX69	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000409788;Note=Transposon Ty1-MR2 Gag polyprotein	
+P0CX69	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000409789;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX69	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000409790;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX69	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX69	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX69	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX69	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q6B0X2 1 106
+Q6B0X2	UniProtKB	Signal peptide	1	27	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6B0X2	UniProtKB	Chain	28	106	.	.	.	ID=PRO_0000299671;Note=Putative uncharacterized protein YMR158W-B	
+Q6B0X2	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6B0X2	UniProtKB	Sequence conflict	79	79	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40211 1 102
+P40211	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000203304;Note=Uncharacterized protein YMR141C	
+##sequence-region A0A023PZH5 1 115
+A0A023PZH5	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000431053;Note=Putative uncharacterized membrane protein YMR290W-A	
+A0A023PZH5	UniProtKB	Transmembrane	15	35	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZH5	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZH5	UniProtKB	Compositional bias	58	66	.	.	.	Note=Poly-Leu;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZH5	UniProtKB	Compositional bias	99	107	.	.	.	Note=Poly-Lys;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PYJ7 1 116
+A0A023PYJ7	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000431051;Note=Putative uncharacterized membrane protein YMR304C-A	
+A0A023PYJ7	UniProtKB	Transmembrane	55	77	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PYJ7	UniProtKB	Transmembrane	87	109	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXQ9 1 102
+A0A023PXQ9	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000431049;Note=Putative uncharacterized membrane protein YMR316C-B	
+A0A023PXQ9	UniProtKB	Transmembrane	33	55	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ9	UniProtKB	Transmembrane	57	79	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXQ9	UniProtKB	Compositional bias	44	81	.	.	.	Note=Val-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00020	
+##sequence-region Q03829 1 368
+Q03829	UniProtKB	Chain	1	368	.	.	.	ID=PRO_0000090699;Note=Uncharacterized mitochondrial carrier YMR166C	
+Q03829	UniProtKB	Transmembrane	56	77	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03829	UniProtKB	Transmembrane	115	135	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03829	UniProtKB	Transmembrane	149	165	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03829	UniProtKB	Transmembrane	219	239	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03829	UniProtKB	Transmembrane	260	280	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03829	UniProtKB	Transmembrane	332	353	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03829	UniProtKB	Repeat	51	138	.	.	.	Note=Solcar 1	
+Q03829	UniProtKB	Repeat	146	240	.	.	.	Note=Solcar 2	
+Q03829	UniProtKB	Repeat	254	360	.	.	.	Note=Solcar 3	
+##sequence-region Q03219 1 274
+Q03219	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000203319;Note=Uncharacterized protein YMR178W	
+Q03219	UniProtKB	Modified residue	263	263	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q3E843 1 45
+Q3E843	UniProtKB	Chain	1	45	.	.	.	ID=PRO_0000268629;Note=Uncharacterized protein YMR158C-A	
+##sequence-region Q03649 1 449
+Q03649	UniProtKB	Chain	1	449	.	.	.	ID=PRO_0000212455;Note=Putative esterase YMR210W	
+Q03649	UniProtKB	Domain	151	392	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03649	UniProtKB	Active site	232	232	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03649	UniProtKB	Active site	364	364	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03649	UniProtKB	Active site	392	392	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03649	UniProtKB	Cross-link	82	82	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q8TGM0 1 37
+Q8TGM0	UniProtKB	Chain	1	37	.	.	.	ID=PRO_0000299673;Note=Uncharacterized protein YMR272W-A	
+##sequence-region Q04897 1 101
+Q04897	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000203360;Note=Uncharacterized protein YMR320W	
+##sequence-region Q03722 1 664
+Q03722	UniProtKB	Chain	1	664	.	.	.	ID=PRO_0000203260;Note=Uncharacterized protein YML020W	
+Q03722	UniProtKB	Sequence conflict	34	34	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38087 1 329
+P38087	UniProtKB	Transit peptide	1	33	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38087	UniProtKB	Chain	34	329	.	.	.	ID=PRO_0000019266;Note=Carrier protein YMC2%2C mitochondrial	
+P38087	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38087	UniProtKB	Transmembrane	84	104	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38087	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38087	UniProtKB	Transmembrane	205	225	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38087	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38087	UniProtKB	Transmembrane	297	318	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38087	UniProtKB	Repeat	34	115	.	.	.	Note=Solcar 1	
+P38087	UniProtKB	Repeat	143	226	.	.	.	Note=Solcar 2	
+P38087	UniProtKB	Repeat	238	325	.	.	.	Note=Solcar 3	
+##sequence-region Q03697 1 442
+Q03697	UniProtKB	Chain	1	442	.	.	.	ID=PRO_0000213402;Note=Putative nucleotide-sugar transporter YMD8	
+Q03697	UniProtKB	Topological domain	1	3	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Transmembrane	4	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Topological domain	25	32	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Topological domain	54	76	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Topological domain	98	107	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Transmembrane	108	128	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Topological domain	129	132	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Transmembrane	133	153	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Topological domain	154	166	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Transmembrane	167	187	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Topological domain	188	254	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Topological domain	276	301	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Transmembrane	302	322	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Topological domain	323	329	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Transmembrane	330	350	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Topological domain	351	355	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Transmembrane	356	376	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Topological domain	377	442	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03697	UniProtKB	Modified residue	209	209	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03697	UniProtKB	Glycosylation	99	99	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53957 1 106
+P53957	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000203455;Note=Putative uncharacterized protein YNL043C	
+##sequence-region P53912 1 376
+P53912	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000203426;Note=Uncharacterized protein YNL134C	
+##sequence-region P40168 1 261
+P40168	UniProtKB	Chain	1	261	.	.	.	ID=PRO_0000203398;Note=Uncharacterized protein YNL195C	
+##sequence-region Q08411 1 143
+Q08411	UniProtKB	Chain	1	143	.	.	.	ID=PRO_0000299705;Note=Putative uncharacterized protein YOR041C	
+Q08411	UniProtKB	Compositional bias	9	121	.	.	.	Note=Ser-rich	
+##sequence-region Q99345 1 113
+Q99345	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000299692;Note=Uncharacterized protein YOL085C	
+Q99345	UniProtKB	Compositional bias	91	96	.	.	.	Note=Poly-Asp	
+##sequence-region P0C5Q9 1 33
+P0C5Q9	UniProtKB	Chain	1	33	.	.	.	ID=PRO_0000309057;Note=Putative uncharacterized protein YOR008W-B	
+##sequence-region Q08503 1 116
+Q08503	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000299711;Note=Putative uncharacterized protein YOR102W	
+##sequence-region Q99210 1 232
+Q99210	UniProtKB	Chain	1	232	.	.	.	ID=PRO_0000123091;Note=Maf-like protein YOR111W	
+Q99210	UniProtKB	Active site	52	52	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12273 1 1755
+Q12273	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279153;Note=Transposon Ty1-OL Gag-Pol polyprotein	
+Q12273	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279154;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12273	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279155;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12273	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279156;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12273	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279157;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12273	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12273	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12273	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q12273	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12273	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q12273	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12273	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q12273	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q12273	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12273	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12273	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12273	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12273	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12273	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12273	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12273	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12273	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12273	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12273	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12273	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region Q08533 1 101
+Q08533	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000299753;Note=Putative uncharacterized protein YOR146W	
+Q08533	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08533	UniProtKB	Compositional bias	41	69	.	.	.	Note=Ser-rich	
+##sequence-region Q12249 1 139
+Q12249	UniProtKB	Chain	1	139	.	.	.	ID=PRO_0000299725;Note=Putative uncharacterized protein YOR218C	
+Q12249	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12113 1 1770
+Q12113	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000279340;Note=Transposon Ty2-OR1 Gag-Pol polyprotein	
+Q12113	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279341;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12113	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000279342;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12113	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000279343;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12113	UniProtKB	Chain	1233	1770	.	.	.	ID=PRO_0000279344;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12113	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12113	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12113	UniProtKB	Domain	1625	1767	.	.	.	Note=RNase H Ty1/copia-type	
+Q12113	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12113	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+Q12113	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12113	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12113	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12113	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12113	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12113	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12113	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12113	UniProtKB	Metal binding	1625	1625	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12113	UniProtKB	Metal binding	1667	1667	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12113	UniProtKB	Metal binding	1700	1700	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12113	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12113	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12113	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q08734 1 132
+Q08734	UniProtKB	Chain	1	132	.	.	.	ID=PRO_0000245282;Note=Uncharacterized protein YOR268C	
+Q08734	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12012 1 251
+Q12012	UniProtKB	Chain	1	251	.	.	.	ID=PRO_0000142373;Note=Uncharacterized protein YOR289W	
+Q12012	UniProtKB	Domain	21	246	.	.	.	Note=AMMECR1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00467	
+##sequence-region Q99318 1 101
+Q99318	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000299736;Note=Putative uncharacterized protein YOR318C	
+##sequence-region Q8TGL1 1 26
+Q8TGL1	UniProtKB	Chain	1	26	.	.	.	ID=PRO_0000299739;Note=Putative uncharacterized protein YOR335W-A	
+##sequence-region P0C5R2 1 82
+P0C5R2	UniProtKB	Chain	1	82	.	.	.	ID=PRO_0000309060;Note=Putative uncharacterized protein YOR072W-A	
+##sequence-region Q08428 1 113
+Q08428	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000299707;Note=Putative uncharacterized protein YOR053W	
+Q08428	UniProtKB	Transmembrane	4	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08428	UniProtKB	Compositional bias	21	76	.	.	.	Note=Arg/His-rich	
+##sequence-region Q3E834 1 85
+Q3E834	UniProtKB	Chain	1	85	.	.	.	ID=PRO_0000232636;Note=Protein transport protein YOS1	
+Q3E834	UniProtKB	Transmembrane	2	22	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E834	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E834	UniProtKB	Mutagenesis	18	18	.	.	.	Note=In YOS1-1%3B impairs interaction with YIP1%2C blocks ER-Golgi protein transport%2C and causes a severe growth defect at 37 degrees Celsius. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15659647;Dbxref=PMID:15659647	
+Q3E834	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Lethal. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15659647;Dbxref=PMID:15659647	
+##sequence-region Q12145 1 317
+Q12145	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000255974;Note=Zinc finger protein YPR013C	
+Q12145	UniProtKB	Zinc finger	254	276	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q12145	UniProtKB	Zinc finger	282	306	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+##sequence-region P0C5R5 1 86
+P0C5R5	UniProtKB	Chain	1	86	.	.	.	ID=PRO_0000309063;Note=Putative uncharacterized protein YPR016W-A	
+##sequence-region Q12139 1 1133
+Q12139	UniProtKB	Chain	1	1133	.	.	.	ID=PRO_0000255976;Note=Zinc finger protein YPR022C	
+Q12139	UniProtKB	Zinc finger	31	55	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q12139	UniProtKB	Zinc finger	61	91	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q12139	UniProtKB	Compositional bias	159	320	.	.	.	Note=Gln-rich	
+##sequence-region Q3E752 1 67
+Q3E752	UniProtKB	Chain	1	67	.	.	.	ID=PRO_0000242699;Note=Uncharacterized protein YPR036W-A	
+Q3E752	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q3E752	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q02826 1 108
+Q02826	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000299801;Note=Uncharacterized protein YPL080C	
+##sequence-region Q06833 1 770
+Q06833	UniProtKB	Chain	1	770	.	.	.	ID=PRO_0000257815;Note=Uncharacterized PH domain-containing protein YPR091C	
+Q06833	UniProtKB	Topological domain	1	5	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Transmembrane	6	26	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Topological domain	27	770	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Domain	114	266	.	.	.	Note=PH	
+Q06833	UniProtKB	Modified residue	640	640	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+Q06833	UniProtKB	Modified residue	669	669	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+Q06833	UniProtKB	Modified residue	717	717	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06833	UniProtKB	Modified residue	720	720	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q06833	UniProtKB	Modified residue	723	723	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06833	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Glycosylation	263	263	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Glycosylation	279	279	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Glycosylation	300	300	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Glycosylation	391	391	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Glycosylation	528	528	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Glycosylation	529	529	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Glycosylation	595	595	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Glycosylation	620	620	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Glycosylation	700	700	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06833	UniProtKB	Glycosylation	718	718	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q02981 1 657
+Q02981	UniProtKB	Transit peptide	1	15	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02981	UniProtKB	Chain	16	657	.	.	.	ID=PRO_0000200738;Note=ABC1 family protein YPL109C%2C mitochondrial	
+##sequence-region Q8TGK9 1 57
+Q8TGK9	UniProtKB	Chain	1	57	.	.	.	ID=PRO_0000299804;Note=Putative uncharacterized protein YPL135C-A	
+##sequence-region Q8TGQ7 1 33
+Q8TGQ7	UniProtKB	Chain	1	33	.	.	.	ID=PRO_0000244639;Note=Uncharacterized protein YPR159C-A	
+Q8TGQ7	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06616 1 221
+Q06616	UniProtKB	Chain	1	221	.	.	.	ID=PRO_0000257831;Note=Nuclear envelope protein YPR174C	
+Q06616	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06616	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06616	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q12697 1 1472
+Q12697	UniProtKB	Chain	1	1472	.	.	.	ID=PRO_0000046351;Note=Vacuolar cation-transporting ATPase YPK9	
+Q12697	UniProtKB	Topological domain	1	293	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	294	315	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	316	321	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	322	344	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	345	488	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	489	511	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	512	514	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	515	533	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	534	693	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	694	713	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	714	726	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	727	748	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	749	1244	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	1245	1264	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	1265	1271	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	1272	1289	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	1290	1307	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	1308	1331	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	1332	1351	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	1352	1374	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	1375	1387	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	1388	1407	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	1408	1423	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Transmembrane	1424	1446	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Topological domain	1447	1472	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12697	UniProtKB	Active site	781	781	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12697	UniProtKB	Metal binding	1187	1187	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12697	UniProtKB	Metal binding	1191	1191	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12697	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12697	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12697	UniProtKB	Modified residue	108	108	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12697	UniProtKB	Modified residue	1117	1117	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12697	UniProtKB	Modified residue	1120	1120	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38279 1 296
+P38279	UniProtKB	Chain	1	296	.	.	.	ID=PRO_0000202496;Note=Probable vacuolar amino acid transporter YPQ3	
+P38279	UniProtKB	Topological domain	1	12	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Topological domain	34	44	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Topological domain	66	68	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Transmembrane	69	89	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Topological domain	90	163	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Topological domain	185	199	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Topological domain	221	238	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Transmembrane	239	259	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Topological domain	260	262	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Transmembrane	263	283	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Topological domain	284	296	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38279	UniProtKB	Domain	10	76	.	.	.	Note=PQ-loop 1	
+P38279	UniProtKB	Domain	208	270	.	.	.	Note=PQ-loop 2	
+##sequence-region Q6B0W2 1 109
+Q6B0W2	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299815;Note=Uncharacterized protein YPR014C	
+##sequence-region O13569 1 170
+O13569	UniProtKB	Chain	1	170	.	.	.	ID=PRO_0000299828;Note=Putative uncharacterized protein YPR136C	
+O13569	UniProtKB	Compositional bias	34	136	.	.	.	Note=Ser-rich	
+##sequence-region O13570 1 187
+O13570	UniProtKB	Chain	1	187	.	.	.	ID=PRO_0000299829;Note=Putative uncharacterized protein YPR142C	
+O13570	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13570	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13570	UniProtKB	Transmembrane	129	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13570	UniProtKB	Compositional bias	42	55	.	.	.	Note=Poly-Ser	
+O13570	UniProtKB	Compositional bias	73	81	.	.	.	Note=Poly-Ser	
+##sequence-region Q12346 1 211
+Q12346	UniProtKB	Chain	1	211	.	.	.	ID=PRO_0000252276;Note=Uncharacterized membrane protein YPR071W	
+Q12346	UniProtKB	Topological domain	1	33	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12346	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12346	UniProtKB	Topological domain	55	58	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12346	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12346	UniProtKB	Topological domain	80	116	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12346	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12346	UniProtKB	Topological domain	138	162	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12346	UniProtKB	Transmembrane	163	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12346	UniProtKB	Topological domain	184	211	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12303 1 508
+Q12303	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Propeptide	21	47	.	.	.	ID=PRO_0000025841;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10191273;Dbxref=PMID:10191273	
+Q12303	UniProtKB	Chain	48	483	.	.	.	ID=PRO_0000025842;Note=Aspartic proteinase yapsin-3	
+Q12303	UniProtKB	Propeptide	484	508	.	.	.	ID=PRO_0000025843;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Domain	63	394	.	.	.	Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
+Q12303	UniProtKB	Active site	81	81	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q12303	UniProtKB	Active site	288	288	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q12303	UniProtKB	Lipidation	483	483	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Glycosylation	75	75	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Glycosylation	120	120	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Glycosylation	160	160	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Glycosylation	163	163	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Glycosylation	275	275	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Glycosylation	309	309	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Glycosylation	328	328	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Glycosylation	367	367	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Glycosylation	422	422	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Glycosylation	445	445	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12303	UniProtKB	Glycosylation	462	462	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CD97 1 72
+P0CD97	UniProtKB	Chain	1	72	.	.	.	ID=PRO_0000391664;Note=Uncharacterized protein YER039C-A	
+P0CD97	UniProtKB	Topological domain	1	12	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD97	UniProtKB	Transmembrane	13	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD97	UniProtKB	Topological domain	33	46	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD97	UniProtKB	Transmembrane	47	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD97	UniProtKB	Topological domain	70	72	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P41920 1 201
+P41920	UniProtKB	Chain	1	201	.	.	.	ID=PRO_0000213670;Note=Ran-specific GTPase-activating protein 1	
+P41920	UniProtKB	Domain	64	200	.	.	.	Note=RanBD1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00164	
+P41920	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P41920	UniProtKB	Beta strand	83	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P41920	UniProtKB	Turn	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P41920	UniProtKB	Beta strand	102	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P41920	UniProtKB	Turn	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P41920	UniProtKB	Beta strand	122	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P41920	UniProtKB	Turn	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P41920	UniProtKB	Beta strand	134	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P41920	UniProtKB	Beta strand	153	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P41920	UniProtKB	Beta strand	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WVF	
+P41920	UniProtKB	Beta strand	170	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+P41920	UniProtKB	Helix	181	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT	
+##sequence-region Q12172 1 810
+Q12172	UniProtKB	Chain	1	810	.	.	.	ID=PRO_0000269651;Note=Zinc finger transcription factor YRR1	
+Q12172	UniProtKB	DNA binding	54	82	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P25036 1 478
+P25036	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25036	UniProtKB	Chain	18	478	.	.	.	ID=PRO_0000027206;Note=Subtilisin-like protease 3	
+P25036	UniProtKB	Domain	210	446	.	.	.	Note=Peptidase S8	
+P25036	UniProtKB	Active site	213	213	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25036	UniProtKB	Active site	245	245	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25036	UniProtKB	Active site	407	407	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25036	UniProtKB	Sequence conflict	22	22	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25036	UniProtKB	Sequence conflict	105	105	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25036	UniProtKB	Sequence conflict	189	205	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25036	UniProtKB	Sequence conflict	289	289	.	.	.	Note=Y->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12024 1 460
+Q12024	UniProtKB	Chain	1	460	.	.	.	ID=PRO_0000051466;Note=Ribosome biogenesis protein YTM1	
+Q12024	UniProtKB	Repeat	101	140	.	.	.	Note=WD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029	
+Q12024	UniProtKB	Repeat	142	180	.	.	.	Note=WD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029	
+Q12024	UniProtKB	Repeat	206	244	.	.	.	Note=WD 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029	
+Q12024	UniProtKB	Repeat	285	325	.	.	.	Note=WD 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029	
+Q12024	UniProtKB	Repeat	327	366	.	.	.	Note=WD 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029	
+Q12024	UniProtKB	Repeat	373	413	.	.	.	Note=WD 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029	
+Q12024	UniProtKB	Repeat	424	460	.	.	.	Note=WD 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029	
+Q12024	UniProtKB	Region	99	460	.	.	.	Note=Sufficient for interaction with ERB1 and association with 66S pre-ribosomes;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18448671,ECO:0000269|PubMed:26657628;Dbxref=PMID:18448671,PMID:26657628	
+Q12024	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Weakens the interaction with ERB1%2C leading to mostly ribosome-unbound YTM1 and defects in 60S maturation. Disrupts the interaction with YTM1 and cannot sustain growth%3B when associated with E-310. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26657628;Dbxref=PMID:26657628	
+Q12024	UniProtKB	Mutagenesis	123	123	.	.	.	Note=Disrupts the interaction with YTM1 and cannot sustain growth%3B when associated with E-310. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26657628;Dbxref=PMID:26657628	
+Q12024	UniProtKB	Mutagenesis	310	310	.	.	.	Note=Disrupts the interaction with YTM1 and cannot sustain growth%3B when associated with R-104 or A-123. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26657628;Dbxref=PMID:26657628	
+Q12024	UniProtKB	Mutagenesis	398	398	.	.	.	Note=In ytm1-1%3B abrogates binding to ERB1 and impairs 27S pre-rRNA processing and 66S pre-ribosome maturation%3B when associated with N-442. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16287855;Dbxref=PMID:16287855	
+Q12024	UniProtKB	Mutagenesis	442	442	.	.	.	Note=In ytm1-1%3B abrogates binding to ERB1 and impairs 27S pre-rRNA processing and 66S pre-ribosome maturation%3B when associated with D-398. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16287855;Dbxref=PMID:16287855	
+##sequence-region Q08245 1 113
+Q08245	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000269|Ref.4;Dbxref=PMID:15665377	
+Q08245	UniProtKB	Chain	2	113	.	.	.	ID=PRO_0000066571;Note=Protein ZEO1	
+Q08245	UniProtKB	Coiled coil	2	97	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08245	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000269|Ref.4;Dbxref=PMID:15665377	
+Q08245	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q08245	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198	
+Q08245	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198	
+Q08245	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198	
+Q08245	UniProtKB	Cross-link	18	18	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08245	UniProtKB	Cross-link	23	23	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08245	UniProtKB	Cross-link	29	29	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08245	UniProtKB	Cross-link	34	34	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08245	UniProtKB	Cross-link	45	45	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08245	UniProtKB	Cross-link	57	57	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08245	UniProtKB	Cross-link	82	82	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P53061 1 704
+P53061	UniProtKB	Chain	1	704	.	.	.	ID=PRO_0000202706;Note=Protein ZIP2	
+##sequence-region P53831 1 123
+P53831	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000203376;Note=Putative uncharacterized protein YNL285W	
+##sequence-region P0C5Q8 1 48
+P0C5Q8	UniProtKB	Chain	1	48	.	.	.	ID=PRO_0000309056;Note=Putative uncharacterized protein YNL067W-A	
+##sequence-region P53717 1 134
+P53717	UniProtKB	Chain	1	134	.	.	.	ID=PRO_0000203469;Note=Putative uncharacterized protein YNR005C	
+P53717	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53750 1 290
+P53750	UniProtKB	Chain	1	290	.	.	.	ID=PRO_0000207080;Note=Uncharacterized hydrolase YNR064C	
+P53750	UniProtKB	Domain	30	274	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53750	UniProtKB	Active site	269	269	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53752 1 436
+P53752	UniProtKB	Chain	1	436	.	.	.	ID=PRO_0000203484;Note=Uncharacterized membrane glycoprotein YNR066C	
+P53752	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53752	UniProtKB	Repeat	57	68	.	.	.	Note=BNR 1	
+P53752	UniProtKB	Repeat	101	112	.	.	.	Note=BNR 2	
+P53752	UniProtKB	Repeat	229	240	.	.	.	Note=BNR 3	
+P53752	UniProtKB	Repeat	394	405	.	.	.	Note=BNR 4	
+P53752	UniProtKB	Glycosylation	157	157	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53981 1 241
+P53981	UniProtKB	Chain	1	241	.	.	.	ID=PRO_0000203466;Note=Uncharacterized phosphatase YNL010W	
+##sequence-region P53975 1 284
+P53975	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53975	UniProtKB	Chain	25	284	.	.	.	ID=PRO_0000014341;Note=Uncharacterized membrane protein YNL019C	
+P53975	UniProtKB	Topological domain	25	84	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53975	UniProtKB	Transmembrane	85	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53975	UniProtKB	Topological domain	105	284	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53975	UniProtKB	Glycosylation	270	270	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53928 1 181
+P53928	UniProtKB	Chain	1	181	.	.	.	ID=PRO_0000203435;Note=Putative uncharacterized membrane protein YNL109W	
+P53928	UniProtKB	Topological domain	1	14	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53928	UniProtKB	Transmembrane	15	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53928	UniProtKB	Topological domain	36	58	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53928	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53928	UniProtKB	Topological domain	80	84	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53928	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53928	UniProtKB	Topological domain	106	116	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53928	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53928	UniProtKB	Topological domain	138	153	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53928	UniProtKB	Transmembrane	154	174	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53928	UniProtKB	Topological domain	175	181	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53910 1 189
+P53910	UniProtKB	Chain	1	189	.	.	.	ID=PRO_0000203425;Note=Uncharacterized protein YNL140C	
+P53910	UniProtKB	Sequence conflict	18	18	.	.	.	Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53891 1 406
+P53891	UniProtKB	Chain	1	406	.	.	.	ID=PRO_0000203412;Note=Uncharacterized protein YNL165W	
+##sequence-region P53884 1 190
+P53884	UniProtKB	Chain	1	190	.	.	.	ID=PRO_0000203408;Note=Putative uncharacterized protein YNL174W	
+P53884	UniProtKB	Transmembrane	15	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53884	UniProtKB	Transmembrane	58	78	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53884	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53884	UniProtKB	Transmembrane	148	168	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53884	UniProtKB	Compositional bias	61	65	.	.	.	Note=Poly-Phe	
+##sequence-region P53876 1 108
+P53876	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000203404;Note=Uncharacterized protein YNL184C	
+##sequence-region P53870 1 558
+P53870	UniProtKB	Chain	1	558	.	.	.	ID=PRO_0000203400;Note=Uncharacterized protein YNL193W	
+P53870	UniProtKB	Sequence conflict	122	122	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40166 1 100
+P40166	UniProtKB	Transit peptide	1	45	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40166	UniProtKB	Chain	46	100	.	.	.	ID=PRO_0000203396;Note=Uncharacterized protein YNL198C%2C mitochondrial	
+##sequence-region P40152 1 326
+P40152	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40152	UniProtKB	Chain	27	326	.	.	.	ID=PRO_0000042987;Note=Putative metallophosphoesterase YNL217W	
+##sequence-region P53864 1 136
+P53864	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000203387;Note=Putative uncharacterized protein YNL226W	
+##sequence-region Q12351 1 137
+Q12351	UniProtKB	Chain	1	137	.	.	.	ID=PRO_0000235937;Note=Uncharacterized protein YOR012W	
+##sequence-region Q08172 1 172
+Q08172	UniProtKB	Chain	1	172	.	.	.	ID=PRO_0000245274;Note=Putative uncharacterized protein YOL024W	
+##sequence-region Q3E824 1 90
+Q3E824	UniProtKB	Chain	1	90	.	.	.	ID=PRO_0000235939;Note=Uncharacterized protein YOR020W-A	
+Q3E824	UniProtKB	Transmembrane	15	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E824	UniProtKB	Glycosylation	44	44	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08222 1 106
+Q08222	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000299691;Note=Putative uncharacterized protein YOL050C	
+##sequence-region Q08232 1 322
+Q08232	UniProtKB	Chain	1	322	.	.	.	ID=PRO_0000235926;Note=Uncharacterized membrane protein YOL073C	
+Q08232	UniProtKB	Topological domain	1	19	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08232	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08232	UniProtKB	Topological domain	41	54	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08232	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08232	UniProtKB	Topological domain	76	90	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08232	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08232	UniProtKB	Topological domain	112	120	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08232	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08232	UniProtKB	Topological domain	142	189	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08232	UniProtKB	Transmembrane	190	210	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08232	UniProtKB	Topological domain	211	322	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08232	UniProtKB	Compositional bias	244	269	.	.	.	Note=Ala-rich	
+##sequence-region Q6B0V7 1 65
+Q6B0V7	UniProtKB	Chain	1	65	.	.	.	ID=PRO_0000299755;Note=Putative uncharacterized protein YPR002C-A	
+Q6B0V7	UniProtKB	Sequence conflict	35	35	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06104 1 294
+Q06104	UniProtKB	Chain	1	294	.	.	.	ID=PRO_0000242625;Note=Uncharacterized membrane protein YPR109W	
+Q06104	UniProtKB	Topological domain	1	139	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06104	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06104	UniProtKB	Topological domain	161	215	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06104	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06104	UniProtKB	Topological domain	237	294	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06104	UniProtKB	Sequence conflict	11	11	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12458 1 312
+Q12458	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000124612;Note=Putative reductase 1	
+Q12458	UniProtKB	Nucleotide binding	220	274	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12458	UniProtKB	Active site	56	56	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12458	UniProtKB	Binding site	112	112	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12458	UniProtKB	Site	81	81	.	.	.	Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P32329 1 569
+P32329	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Propeptide	22	67	.	.	.	ID=PRO_0000025838;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9417119;Dbxref=PMID:9417119	
+P32329	UniProtKB	Chain	68	548	.	.	.	ID=PRO_0000025839;Note=Aspartic proteinase 3	
+P32329	UniProtKB	Chain	68	128	.	.	.	ID=PRO_0000372455;Note=Aspartic proteinase 3 subunit alpha	
+P32329	UniProtKB	Chain	145	548	.	.	.	ID=PRO_0000372456;Note=Aspartic proteinase 3 subunit beta	
+P32329	UniProtKB	Propeptide	549	569	.	.	.	ID=PRO_0000025840;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Domain	83	475	.	.	.	Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
+P32329	UniProtKB	Active site	101	101	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P32329	UniProtKB	Active site	371	371	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P32329	UniProtKB	Site	128	129	.	.	.	Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32329	UniProtKB	Site	144	145	.	.	.	Note=Cleavage%3B by autolysis	
+P32329	UniProtKB	Lipidation	548	548	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Glycosylation	95	95	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Glycosylation	203	203	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Glycosylation	232	232	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Glycosylation	242	242	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Glycosylation	245	245	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Glycosylation	299	299	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Glycosylation	358	358	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Glycosylation	480	480	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Glycosylation	522	522	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Glycosylation	532	532	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32329	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Loss of function. D->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9417119;Dbxref=PMID:9417119	
+P32329	UniProtKB	Sequence conflict	370	370	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P01123 1 206
+P01123	UniProtKB	Chain	1	206	.	.	.	ID=PRO_0000121318;Note=GTP-binding protein YPT1	
+P01123	UniProtKB	Nucleotide binding	15	23	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820	
+P01123	UniProtKB	Nucleotide binding	33	40	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820	
+P01123	UniProtKB	Nucleotide binding	63	67	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820	
+P01123	UniProtKB	Nucleotide binding	121	124	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820	
+P01123	UniProtKB	Nucleotide binding	151	153	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820	
+P01123	UniProtKB	Region	63	80	.	.	.	Note=Interaction with GDI1	
+P01123	UniProtKB	Region	189	195	.	.	.	Note=Interaction with GDI1	
+P01123	UniProtKB	Motif	37	45	.	.	.	Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P01123	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5	
+P01123	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P01123	UniProtKB	Modified residue	174	174	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P01123	UniProtKB	Lipidation	23	23	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P01123	UniProtKB	Lipidation	123	123	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P01123	UniProtKB	Lipidation	205	205	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10071213;Dbxref=PMID:10071213	
+P01123	UniProtKB	Lipidation	206	206	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10071213;Dbxref=PMID:10071213	
+P01123	UniProtKB	Cross-link	144	144	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P01123	UniProtKB	Mutagenesis	17	17	.	.	.	Note=Decreases GTP binding and increases GTP hydrolysis. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3311726;Dbxref=PMID:3311726	
+P01123	UniProtKB	Mutagenesis	21	21	.	.	.	Note=Abolishes GTP binding. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3311726;Dbxref=PMID:3311726	
+P01123	UniProtKB	Mutagenesis	37	37	.	.	.	Note=No change. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858	
+P01123	UniProtKB	Mutagenesis	39	39	.	.	.	Note=No change. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858	
+P01123	UniProtKB	Mutagenesis	40	40	.	.	.	Note=No change. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858	
+P01123	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Lethal. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858	
+P01123	UniProtKB	Mutagenesis	43	43	.	.	.	Note=No change. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858	
+P01123	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Temperature-sensitive phenotype. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858	
+P01123	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Decreases GTP binding and GTP hydrolysis. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3311726;Dbxref=PMID:3311726	
+P01123	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Locks YPT1 in the GTP-bound form by reducing GTP hydrolysis rate 40-fold. Q->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15082776,ECO:0000269|PubMed:9447979;Dbxref=PMID:15082776,PMID:9447979	
+P01123	UniProtKB	Mutagenesis	121	121	.	.	.	Note=Abolishes GTP binding. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3311726;Dbxref=PMID:3311726	
+P01123	UniProtKB	Mutagenesis	136	136	.	.	.	Note=Loss of function at 37 degrees Celsius. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593181;Dbxref=PMID:7593181	
+P01123	UniProtKB	Mutagenesis	205	205	.	.	.	Note=Abolishes membrane association. Lethal%3B when associated with S-206. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10071213,ECO:0000269|PubMed:3042385;Dbxref=PMID:10071213,PMID:3042385	
+P01123	UniProtKB	Mutagenesis	206	206	.	.	.	Note=Abolishes membrane association. Lethal%3B when associated with S-205. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10071213,ECO:0000269|PubMed:3042385;Dbxref=PMID:10071213,PMID:3042385	
+P01123	UniProtKB	Sequence conflict	171	171	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P01123	UniProtKB	Beta strand	6	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Helix	21	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Beta strand	45	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Beta strand	55	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Turn	65	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Helix	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Beta strand	82	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Helix	93	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Beta strand	115	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Turn	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Helix	133	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Beta strand	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Turn	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Helix	158	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Helix	175	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P01123	UniProtKB	Helix	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+##sequence-region P40105 1 1681
+P40105	UniProtKB	Chain	1	1681	.	.	.	ID=PRO_0000102202;Note=Y' element ATP-dependent helicase protein 1 copy 2	
+P40105	UniProtKB	Domain	683	860	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P40105	UniProtKB	Domain	917	1066	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P40105	UniProtKB	Nucleotide binding	696	703	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region P0CX15 1 1859
+P0CX15	UniProtKB	Chain	1	1859	.	.	.	ID=PRO_0000409751;Note=Y' element ATP-dependent helicase protein 1 copy 7	
+P0CX15	UniProtKB	Domain	861	1038	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P0CX15	UniProtKB	Domain	1095	1244	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P0CX15	UniProtKB	Nucleotide binding	874	881	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region Q12340 1 786
+Q12340	UniProtKB	Chain	1	786	.	.	.	ID=PRO_0000269650;Note=Zinc finger transcription factor YRM1	
+Q12340	UniProtKB	DNA binding	31	59	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+Q12340	UniProtKB	Sequence conflict	158	158	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12340	UniProtKB	Sequence conflict	604	604	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47043 1 880
+P47043	UniProtKB	Chain	1	880	.	.	.	ID=PRO_0000046859;Note=Zinc-responsive transcriptional regulator ZAP1	
+P47043	UniProtKB	Zinc finger	579	604	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P47043	UniProtKB	Zinc finger	616	641	.	.	.	Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P47043	UniProtKB	Zinc finger	705	730	.	.	.	Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P47043	UniProtKB	Zinc finger	738	762	.	.	.	Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P47043	UniProtKB	Zinc finger	768	790	.	.	.	Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P47043	UniProtKB	Zinc finger	796	818	.	.	.	Note=C2H2-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P47043	UniProtKB	Zinc finger	824	846	.	.	.	Note=C2H2-type 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P47043	UniProtKB	Modified residue	156	156	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47043	UniProtKB	Modified residue	166	166	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47043	UniProtKB	Modified residue	515	515	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47043	UniProtKB	Helix	593	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW8	
+P47043	UniProtKB	Beta strand	626	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW8	
+P47043	UniProtKB	Helix	630	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW8	
+##sequence-region P54786 1 942
+P54786	UniProtKB	Chain	1	942	.	.	.	ID=PRO_0000066570;Note=Protein ZDS2	
+P54786	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P54786	UniProtKB	Sequence conflict	7	7	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54786	UniProtKB	Sequence conflict	23	23	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54786	UniProtKB	Sequence conflict	530	530	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54786	UniProtKB	Sequence conflict	546	546	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54786	UniProtKB	Sequence conflict	633	633	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54786	UniProtKB	Sequence conflict	668	668	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54786	UniProtKB	Sequence conflict	711	711	.	.	.	Note=V->VNC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54786	UniProtKB	Sequence conflict	723	723	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54786	UniProtKB	Sequence conflict	729	729	.	.	.	Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54786	UniProtKB	Sequence conflict	833	833	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54786	UniProtKB	Sequence conflict	914	942	.	.	.	Note=TGDIAFNGDSALGMMDKNDSDGTILIPDI->HWRYSLQW;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25650 1 117
+P25650	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000202576;Note=Uncharacterized protein YCR085W	
+##sequence-region P25657 1 155
+P25657	UniProtKB	Chain	1	155	.	.	.	ID=PRO_0000202582;Note=Uncharacterized protein YCR099C	
+##sequence-region P25606 1 316
+P25606	UniProtKB	Chain	1	316	.	.	.	ID=PRO_0000202583;Note=Uncharacterized protein YCR100C	
+P25606	UniProtKB	Repeat	62	73	.	.	.	Note=BNR 1	
+P25606	UniProtKB	Repeat	124	135	.	.	.	Note=BNR 2	
+P25606	UniProtKB	Repeat	196	207	.	.	.	Note=BNR 3	
+P25606	UniProtKB	Repeat	242	253	.	.	.	Note=BNR 4	
+##sequence-region Q12210 1 107
+Q12210	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000299842;Note=Uncharacterized protein YDL009C	
+Q12210	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12111 1 104
+Q12111	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000299870;Note=Uncharacterized protein YDR029W	
+Q12111	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12111	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12025 1 205
+Q12025	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12025	UniProtKB	Chain	18	205	.	.	.	ID=PRO_0000244437;Note=Uncharacterized protein YDR056C	
+Q12025	UniProtKB	Glycosylation	47	47	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07435 1 109
+Q07435	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299853;Note=Putative uncharacterized protein YDL068W	
+Q07435	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07435	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38966 1 869
+P38966	UniProtKB	Chain	1	869	.	.	.	ID=PRO_0000202595;Note=Uncharacterized protein YDR089W	
+P38966	UniProtKB	Domain	1	154	.	.	.	Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714	
+P38966	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38966	UniProtKB	Modified residue	241	241	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38966	UniProtKB	Modified residue	316	316	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38966	UniProtKB	Modified residue	324	324	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38966	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38966	UniProtKB	Modified residue	609	609	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38966	UniProtKB	Modified residue	612	612	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38966	UniProtKB	Modified residue	668	668	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38966	UniProtKB	Modified residue	760	760	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q07530 1 308
+Q07530	UniProtKB	Chain	1	308	.	.	.	ID=PRO_0000240705;Note=Uncharacterized oxidoreductase YDL114W	
+Q07530	UniProtKB	Nucleotide binding	42	66	.	.	.	Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07530	UniProtKB	Active site	182	182	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001	
+Q07530	UniProtKB	Binding site	169	169	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04608 1 324
+Q04608	UniProtKB	Chain	1	324	.	.	.	ID=PRO_0000253830;Note=Uncharacterized protein YDR124W	
+##sequence-region Q03899 1 556
+Q03899	UniProtKB	Chain	1	556	.	.	.	ID=PRO_0000253804;Note=F-box protein YDR131C	
+Q03899	UniProtKB	Domain	1	44	.	.	.	Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080	
+##sequence-region A0A023PZA4 1 116
+A0A023PZA4	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000430982;Note=Putative uncharacterized protein YDR154C	
+##sequence-region Q07613 1 109
+Q07613	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299863;Note=Putative uncharacterized protein YDL187C	
+##sequence-region Q12121 1 372
+Q12121	UniProtKB	Chain	1	372	.	.	.	ID=PRO_0000242481;Note=Uncharacterized protein YDL211C	
+Q12121	UniProtKB	Transmembrane	224	244	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12121	UniProtKB	Compositional bias	104	193	.	.	.	Note=Thr-rich	
+Q12121	UniProtKB	Modified residue	329	329	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q07658 1 213
+Q07658	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000299866;Note=Putative uncharacterized protein YDL228C	
+##sequence-region Q3E763 1 66
+Q3E763	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E763	UniProtKB	Chain	20	66	.	.	.	ID=PRO_0000253840;Note=Uncharacterized protein YDR246W-A	
+##sequence-region P87283 1 123
+P87283	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000299749;Note=Uncharacterized protein YDR274C	
+##sequence-region Q05530 1 114
+Q05530	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000253812;Note=Glutaredoxin-like protein YDR286C	
+Q05530	UniProtKB	Disulfide bond	31	34	.	.	.	Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P87288 1 108
+P87288	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000299883;Note=Putative uncharacterized protein YDR327W	
+##sequence-region P0C289 1 58
+P0C289	UniProtKB	Chain	1	58	.	.	.	ID=PRO_0000269763;Note=Putative uncharacterized protein YDR034C-A	
+P0C289	UniProtKB	Transmembrane	5	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13523 1 187
+O13523	UniProtKB	Chain	1	187	.	.	.	ID=PRO_0000299889;Note=Putative uncharacterized protein YDR401W	
+O13523	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13523	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P87267 1 123
+P87267	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87267	UniProtKB	Chain	25	123	.	.	.	ID=PRO_0000299750;Note=Putative uncharacterized protein YDR417C	
+P87267	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87267	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04093 1 687
+Q04093	UniProtKB	Chain	1	687	.	.	.	ID=PRO_0000253824;Note=Putative lipase YDR444W	
+Q04093	UniProtKB	Active site	284	284	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037	
+##sequence-region P87264 1 108
+P87264	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000299898;Note=Putative uncharacterized protein YDR467C	
+P87264	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87264	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGR7 1 38
+Q8TGR7	UniProtKB	Chain	1	38	.	.	.	ID=PRO_0000299901;Note=Putative uncharacterized protein YDR510C-A	
+Q8TGR7	UniProtKB	Transmembrane	10	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P87263 1 166
+P87263	UniProtKB	Chain	1	166	.	.	.	ID=PRO_0000299912;Note=Putative uncharacterized protein YER066C-A	
+##sequence-region A0A023PYE9 1 183
+A0A023PYE9	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PYE9	UniProtKB	Chain	18	183	.	.	.	ID=PRO_0000430997;Note=Putative uncharacterized protein YER087C-A	
+##sequence-region A0A023PXJ7 1 106
+A0A023PXJ7	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000430998;Note=Putative uncharacterized membrane protein YER107W-A	
+A0A023PXJ7	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXJ7	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXD5 1 136
+A0A023PXD5	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXD5	UniProtKB	Chain	20	136	.	.	.	ID=PRO_0000431002;Note=Putative uncharacterized membrane protein YER147C-A	
+A0A023PXD5	UniProtKB	Transmembrane	75	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZC7 1 188
+A0A023PZC7	UniProtKB	Chain	1	188	.	.	.	ID=PRO_0000431004;Note=Putative uncharacterized protein YER152W-A	
+##sequence-region A0A023PZH1 1 118
+A0A023PZH1	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000431005;Note=Putative uncharacterized membrane protein YER165C-A	
+A0A023PZH1	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZH1	UniProtKB	Transmembrane	34	58	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40101 1 306
+P40101	UniProtKB	Chain	1	306	.	.	.	ID=PRO_0000202662;Note=Uncharacterized protein YER186C	
+##sequence-region P0C0V2 1 99
+P0C0V2	UniProtKB	Chain	1	99	.	.	.	ID=PRO_0000211371;Note=UPF0320 protein YER188C-A	
+##sequence-region P0C270 1 34
+P0C270	UniProtKB	Chain	1	34	.	.	.	ID=PRO_0000268625;Note=Putative uncharacterized protein YER138W-A	
+##sequence-region A0A023PXC2 1 115
+A0A023PXC2	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXC2	UniProtKB	Chain	25	115	.	.	.	ID=PRO_0000431007;Note=Putative uncharacterized membrane protein YEL053W-A	
+A0A023PXC2	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXC2	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXJ3 1 115
+A0A023PXJ3	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000431008;Note=Putative uncharacterized membrane protein YER076W-A	
+A0A023PXJ3	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39994 1 560
+P39994	UniProtKB	Chain	1	560	.	.	.	ID=PRO_0000090826;Note=Putative 2-hydroxyacyl-CoA lyase	
+##sequence-region P39983 1 233
+P39983	UniProtKB	Chain	1	233	.	.	.	ID=PRO_0000202604;Note=Uncharacterized protein YEL057C	
+##sequence-region P39973 1 112
+P39973	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000211370;Note=Putative UPF0320 protein YEL074W	
+##sequence-region P40022 1 185
+P40022	UniProtKB	Chain	1	185	.	.	.	ID=PRO_0000202625;Note=Uncharacterized protein YER034W	
+P40022	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P35723 1 206
+P35723	UniProtKB	Chain	1	206	.	.	.	ID=PRO_0000203174;Note=Endoplasmic reticulum transmembrane protein 1	
+P35723	UniProtKB	Topological domain	1	7	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35723	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35723	UniProtKB	Topological domain	29	45	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35723	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35723	UniProtKB	Topological domain	67	104	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35723	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35723	UniProtKB	Topological domain	126	206	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35723	UniProtKB	Motif	203	206	.	.	.	Note=Di-lysine motif	
+P35723	UniProtKB	Cross-link	190	190	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538	
+P35723	UniProtKB	Sequence conflict	16	16	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35723	UniProtKB	Sequence conflict	16	16	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35723	UniProtKB	Sequence conflict	16	16	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39959 1 443
+P39959	UniProtKB	Chain	1	443	.	.	.	ID=PRO_0000046862;Note=Zinc finger protein YER130C	
+P39959	UniProtKB	Zinc finger	389	412	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39959	UniProtKB	Zinc finger	418	440	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+##sequence-region P10356 1 443
+P10356	UniProtKB	Chain	1	443	.	.	.	ID=PRO_0000202655;Note=Uncharacterized protein YER152C	
+##sequence-region Q03187 1 267
+Q03187	UniProtKB	Signal peptide	1	27	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03187	UniProtKB	Chain	28	267	.	.	.	ID=PRO_0000299917;Note=Putative uncharacterized protein YFL013W-A	
+Q03187	UniProtKB	Transmembrane	125	145	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03187	UniProtKB	Transmembrane	165	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03187	UniProtKB	Compositional bias	190	267	.	.	.	Note=Ser-rich	
+##sequence-region Q8TGR2 1 95
+Q8TGR2	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q8TGR2	UniProtKB	Chain	18	95	.	.	.	ID=PRO_0000299919;Note=Putative uncharacterized protein YFR034W-A	
+##sequence-region P0CX63 1 1770
+P0CX63	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000279308;Note=Transposon Ty2-F Gag-Pol polyprotein	
+P0CX63	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279309;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX63	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000279310;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX63	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000279311;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX63	UniProtKB	Chain	1233	1770	.	.	.	ID=PRO_0000279312;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX63	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX63	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+P0CX63	UniProtKB	Domain	1625	1767	.	.	.	Note=RNase H Ty1/copia-type	
+P0CX63	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX63	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+P0CX63	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX63	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX63	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX63	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX63	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX63	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX63	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX63	UniProtKB	Metal binding	1625	1625	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX63	UniProtKB	Metal binding	1667	1667	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX63	UniProtKB	Metal binding	1700	1700	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+P0CX63	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX63	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX63	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P43578 1 164
+P43578	UniProtKB	Chain	1	164	.	.	.	ID=PRO_0000202678;Note=Uncharacterized protein YFL015C	
+P43578	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43578	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43566 1 106
+P43566	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000202675;Note=Putative uncharacterized protein YFL032W	
+P43566	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43566	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43599 1 363
+P43599	UniProtKB	Chain	1	363	.	.	.	ID=PRO_0000202688;Note=Uncharacterized protein YFR018C	
+##sequence-region Q3E802 1 36
+Q3E802	UniProtKB	Chain	1	36	.	.	.	ID=PRO_0000245381;Note=Uncharacterized protein YGL006W-A	
+##sequence-region P0C5N2 1 42
+P0C5N2	UniProtKB	Chain	1	42	.	.	.	ID=PRO_0000309030;Note=Putative uncharacterized protein YGR122C-A	
+##sequence-region Q8TGT9 1 53
+Q8TGT9	UniProtKB	Chain	1	53	.	.	.	ID=PRO_0000245384;Note=Uncharacterized protein YGR146C-A	
+Q8TGT9	UniProtKB	Transmembrane	13	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53208 1 328
+P53208	UniProtKB	Chain	1	328	.	.	.	ID=PRO_0000202782;Note=Uncharacterized abhydrolase domain-containing protein YGR015C	
+P53208	UniProtKB	Domain	39	309	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53208	UniProtKB	Active site	115	115	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53208	UniProtKB	Active site	302	302	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53210 1 297
+P53210	UniProtKB	Chain	1	297	.	.	.	ID=PRO_0000202784;Note=Uncharacterized protein YGR017W	
+##sequence-region P53222 1 116
+P53222	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000202792;Note=Uncharacterized protein YGR035C	
+##sequence-region P53247 1 123
+P53247	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000202807;Note=Putative uncharacterized protein YGR073C	
+P53247	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53247	UniProtKB	Transmembrane	103	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12173 1 290
+Q12173	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15956549;Dbxref=PMID:15956549	
+Q12173	UniProtKB	Chain	2	290	.	.	.	ID=PRO_5000143279;Note=Transposon Ty3-G Gag polyprotein	
+Q12173	UniProtKB	Chain	2	207	.	.	.	ID=PRO_0000279365;Note=Capsid protein	
+Q12173	UniProtKB	Peptide	208	233	.	.	.	ID=PRO_0000279366;Note=Spacer peptide p3	
+Q12173	UniProtKB	Chain	234	290	.	.	.	ID=PRO_5000143280;Note=Nucleocapsid protein p9	
+Q12173	UniProtKB	Zinc finger	265	282	.	.	.	Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+Q12173	UniProtKB	Site	207	208	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q12173	UniProtKB	Site	233	234	.	.	.	Note=Cleavage%3B by Ty3 protease	
+Q12173	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15956549;Dbxref=PMID:15956549	
+Q12173	UniProtKB	Mutagenesis	267	267	.	.	.	Note=Reduces level of VLP formation and maturation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7515969;Dbxref=PMID:7515969	
+Q12173	UniProtKB	Mutagenesis	275	275	.	.	.	Note=Reduces level of VLP formation and maturation. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7515969;Dbxref=PMID:7515969	
+##sequence-region P53269 1 259
+P53269	UniProtKB	Chain	1	259	.	.	.	ID=PRO_0000202816;Note=Putative uncharacterized protein YGR115C	
+P53269	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53269	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53269	UniProtKB	Transmembrane	221	241	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53269	UniProtKB	Compositional bias	38	42	.	.	.	Note=Poly-Ser	
+P53269	UniProtKB	Compositional bias	45	48	.	.	.	Note=Poly-Ser	
+P53269	UniProtKB	Compositional bias	68	73	.	.	.	Note=Poly-Ser	
+P53269	UniProtKB	Compositional bias	87	93	.	.	.	Note=Poly-Ser	
+P53269	UniProtKB	Compositional bias	152	163	.	.	.	Note=Poly-Ser	
+P53269	UniProtKB	Compositional bias	179	185	.	.	.	Note=Poly-Ser	
+P53269	UniProtKB	Compositional bias	197	208	.	.	.	Note=Poly-Ser	
+P53269	UniProtKB	Compositional bias	214	220	.	.	.	Note=Poly-Ser	
+P53269	UniProtKB	Compositional bias	233	236	.	.	.	Note=Poly-Ser	
+##sequence-region P53284 1 112
+P53284	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000202827;Note=Putative uncharacterized protein YGR139W	
+##sequence-region P53293 1 376
+P53293	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000202838;Note=Uncharacterized protein YGR168C	
+P53293	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53293	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53300 1 117
+P53300	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000202840;Note=Putative uncharacterized protein YGR182C	
+##sequence-region P50089 1 785
+P50089	UniProtKB	Chain	1	785	.	.	.	ID=PRO_0000202854;Note=Uncharacterized protein YGR237C	
+P50089	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50089	UniProtKB	Modified residue	667	667	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P53325 1 136
+P53325	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000202863;Note=Putative uncharacterized protein YGR265W	
+P53325	UniProtKB	Transmembrane	102	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53325	UniProtKB	Compositional bias	106	111	.	.	.	Note=Poly-Phe	
+##sequence-region P53342 1 153
+P53342	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000202874;Note=Putative uncharacterized protein YGR293C	
+P53342	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53342	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P33199 1 130
+P33199	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000202775;Note=Uncharacterized protein YGL015C	
+##sequence-region P53183 1 348
+P53183	UniProtKB	Chain	1	348	.	.	.	ID=PRO_0000215577;Note=Putative uncharacterized oxidoreductase YGL039W	
+P53183	UniProtKB	Modified residue	339	339	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12068	
+##sequence-region P53155 1 381
+P53155	UniProtKB	Chain	1	381	.	.	.	ID=PRO_0000202757;Note=Uncharacterized protein YGL082W	
+P53155	UniProtKB	Sequence conflict	263	263	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53133 1 265
+P53133	UniProtKB	Chain	1	265	.	.	.	ID=PRO_0000202747;Note=Uncharacterized protein YGL117W	
+P53133	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P38616 1 354
+P38616	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Propeptide	20	37	.	.	.	ID=PRO_0000022705;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8139573;Dbxref=PMID:8139573	
+P38616	UniProtKB	Chain	38	354	.	.	.	ID=PRO_0000022706;Note=Protein YGP1	
+P38616	UniProtKB	Domain	50	354	.	.	.	Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068	
+P38616	UniProtKB	Glycosylation	40	40	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	50	50	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	53	53	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	58	58	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	61	61	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	65	65	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	87	87	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	94	94	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	100	100	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	106	106	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	118	118	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	172	172	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	239	239	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Glycosylation	286	286	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38616	UniProtKB	Sequence conflict	47	47	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38616	UniProtKB	Sequence conflict	79	79	.	.	.	Note=T->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53103 1 107
+P53103	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000202725;Note=Putative uncharacterized protein YGL182C	
+##sequence-region P53092 1 156
+P53092	UniProtKB	Chain	1	156	.	.	.	ID=PRO_0000202720;Note=Putative uncharacterized protein YGL199C	
+##sequence-region P53054 1 175
+P53054	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000202702;Note=Putative uncharacterized protein YGL262W	
+##sequence-region A0A023PYH5 1 124
+A0A023PYH5	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000431029;Note=Putative uncharacterized protein YHR193C-A	
+##sequence-region P0CX89 1 111
+P0CX89	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000410449;Note=Putative uncharacterized protein YHR212C	
+##sequence-region P0CL34 1 160
+P0CL34	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000299786;Note=Putative UPF0479 protein YHR219C-A	
+P0CL34	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL34	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL34	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region P0C5N8 1 60
+P0C5N8	UniProtKB	Chain	1	60	.	.	.	ID=PRO_0000309036;Note=Putative uncharacterized protein YHR180W-A	
+P0C5N8	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38729 1 150
+P38729	UniProtKB	Signal peptide	1	39	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38729	UniProtKB	Chain	40	150	.	.	.	ID=PRO_0000014324;Note=Putative uncharacterized protein YHL042W	
+##sequence-region P38721 1 697
+P38721	UniProtKB	Chain	1	697	.	.	.	ID=PRO_0000202875;Note=Uncharacterized protein YHL050C	
+P38721	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	163	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	194	214	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	227	247	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	286	306	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	316	336	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	361	381	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	394	414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	419	439	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	450	470	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	487	507	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38721	UniProtKB	Transmembrane	558	578	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38776 1 514
+P38776	UniProtKB	Chain	1	514	.	.	.	ID=PRO_0000173440;Note=Probable drug/proton antiporter YHK8	
+P38776	UniProtKB	Topological domain	1	74	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	96	111	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	133	141	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	163	170	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	192	200	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	201	221	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	222	227	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	228	248	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	249	307	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	308	328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	329	342	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	343	363	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	364	386	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	387	407	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	408	412	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	413	433	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	434	447	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	448	468	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	469	477	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Transmembrane	478	498	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38776	UniProtKB	Topological domain	499	514	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38829 1 231
+P38829	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38829	UniProtKB	Chain	2	231	.	.	.	ID=PRO_0000212699;Note=MIP18 family protein YHR122W	
+P38829	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P40556 1 373
+P40556	UniProtKB	Chain	1	373	.	.	.	ID=PRO_0000090698;Note=Mitochondrial nicotinamide adenine dinucleotide transporter 1	
+P40556	UniProtKB	Topological domain	1	80	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Topological domain	102	141	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Topological domain	163	176	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Transmembrane	177	199	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Topological domain	200	235	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Transmembrane	236	256	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Topological domain	257	280	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Transmembrane	281	297	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Topological domain	298	335	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Transmembrane	336	358	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Topological domain	359	373	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40556	UniProtKB	Repeat	75	166	.	.	.	Note=Solcar 1	
+P40556	UniProtKB	Repeat	174	263	.	.	.	Note=Solcar 2	
+P40556	UniProtKB	Repeat	276	364	.	.	.	Note=Solcar 3	
+##sequence-region P40524 1 105
+P40524	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000202990;Note=Uncharacterized membrane protein YIL054W	
+P40524	UniProtKB	Topological domain	1	48	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40524	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40524	UniProtKB	Topological domain	70	70	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40524	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40524	UniProtKB	Topological domain	92	105	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40503 1 102
+P40503	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000202978;Note=Uncharacterized protein YIL086C	
+##sequence-region P28625 1 365
+P28625	UniProtKB	Chain	1	365	.	.	.	ID=PRO_0000203310;Note=Protein YIM1	
+P28625	UniProtKB	Sequence conflict	121	121	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28625	UniProtKB	Sequence conflict	234	234	.	.	.	Note=S->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28625	UniProtKB	Sequence conflict	280	280	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28625	UniProtKB	Sequence conflict	296	296	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40449 1 235
+P40449	UniProtKB	Chain	1	235	.	.	.	ID=PRO_0000202952;Note=Uncharacterized protein YIL161W	
+P40449	UniProtKB	Cross-link	16	16	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40449	UniProtKB	Cross-link	35	35	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P40587 1 230
+P40587	UniProtKB	Chain	1	230	.	.	.	ID=PRO_0000207534;Note=Putative uncharacterized protein YIR043C	
+P40587	UniProtKB	Transmembrane	93	115	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47105 1 127
+P47105	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000203091;Note=Putative uncharacterized protein YJR037W	
+##sequence-region P47107 1 1121
+P47107	UniProtKB	Chain	1	1121	.	.	.	ID=PRO_0000203093;Note=Uncharacterized protein YJR039W	
+##sequence-region P47099 1 440
+P47099	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000203497;Note=Transposon Ty1-JR2 Gag polyprotein	
+P47099	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279092;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47099	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279093;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47099	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47099	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47099	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region P47115 1 236
+P47115	UniProtKB	Chain	1	236	.	.	.	ID=PRO_0000203097;Note=Uncharacterized protein YJR056C	
+P47115	UniProtKB	Modified residue	221	221	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40355 1 935
+P40355	UniProtKB	Chain	1	935	.	.	.	ID=PRO_0000203098;Note=Uncharacterized protein YJR061W	
+P40355	UniProtKB	Sequence conflict	197	197	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40355	UniProtKB	Sequence conflict	312	312	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47132 1 116
+P47132	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000203106;Note=Putative uncharacterized protein YJR087W	
+##sequence-region P47181 1 346
+P47181	UniProtKB	Chain	1	346	.	.	.	ID=PRO_0000215232;Note=Uncharacterized protein YJR154W	
+P47181	UniProtKB	Sequence conflict	300	300	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47066 1 102
+P47066	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000203073;Note=Putative uncharacterized protein YJL009W	
+##sequence-region P47053 1 257
+P47053	UniProtKB	Chain	1	257	.	.	.	ID=PRO_0000203067;Note=Uncharacterized protein YJL043W	
+P47053	UniProtKB	Sequence conflict	251	251	.	.	.	Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47038 1 131
+P47038	UniProtKB	Chain	1	131	.	.	.	ID=PRO_0000203058;Note=Putative uncharacterized protein YJL064W	
+##sequence-region P0CL26 1 75
+P0CL26	UniProtKB	Chain	1	75	.	.	.	ID=PRO_0000406045;Note=Putative UPF0377 protein YJL222W-A	
+##sequence-region P46987 1 611
+P46987	UniProtKB	Chain	1	611	.	.	.	ID=PRO_0000203023;Note=UPF0508 protein YJL181W	
+P46987	UniProtKB	Compositional bias	6	10	.	.	.	Note=Poly-Glu	
+##sequence-region P40896 1 331
+P40896	UniProtKB	Chain	1	331	.	.	.	ID=PRO_0000203013;Note=Uncharacterized protein YJL213W	
+##sequence-region P47091 1 120
+P47091	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000203086;Note=Putative uncharacterized protein YJR018W	
+P47091	UniProtKB	Transmembrane	93	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q2V2P3 1 75
+Q2V2P3	UniProtKB	Chain	1	75	.	.	.	ID=PRO_0000245423;Note=Uncharacterized protein YKL023C-A	
+Q2V2P3	UniProtKB	Transmembrane	47	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12336 1 168
+Q12336	UniProtKB	Chain	1	168	.	.	.	ID=PRO_0000299607;Note=Putative uncharacterized protein YLL059C	
+Q12336	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12336	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12259 1 485
+Q12259	UniProtKB	Chain	1	485	.	.	.	ID=PRO_0000247339;Note=BTB/POZ domain-containing protein YLR108C	
+Q12259	UniProtKB	Domain	26	121	.	.	.	Note=BTB	
+##sequence-region Q12327 1 114
+Q12327	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000299616;Note=Putative uncharacterized protein YLR124W	
+Q12327	UniProtKB	Compositional bias	77	82	.	.	.	Note=Poly-Lys	
+##sequence-region P0C2I8 1 440
+P0C2I8	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279114;Note=Transposon Ty1-LR4 Gag polyprotein	
+P0C2I8	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279115;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I8	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279116;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I8	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I8	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0C2I8	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2I8	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region O13561 1 117
+O13561	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000299618;Note=Putative uncharacterized protein YLR169W	
+O13561	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13561	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13562 1 129
+O13562	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000299619;Note=Putative uncharacterized protein YLR171W	
+O13562	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13562	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13562	UniProtKB	Transmembrane	101	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06247 1 608
+Q06247	UniProtKB	Chain	1	608	.	.	.	ID=PRO_0000247113;Note=Putative uncharacterized protein YLR173W	
+Q06247	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06247	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06247	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06247	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06247	UniProtKB	Glycosylation	141	141	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06247	UniProtKB	Glycosylation	169	169	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06247	UniProtKB	Glycosylation	407	407	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06247	UniProtKB	Glycosylation	425	425	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06247	UniProtKB	Glycosylation	449	449	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06247	UniProtKB	Glycosylation	453	453	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06247	UniProtKB	Glycosylation	527	527	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06247	UniProtKB	Glycosylation	580	580	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06252 1 201
+Q06252	UniProtKB	Chain	1	201	.	.	.	ID=PRO_0000204754;Note=Uncharacterized protein YLR179C	
+##sequence-region O13530 1 119
+O13530	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000299621;Note=Putative uncharacterized protein YLR198C	
+O13530	UniProtKB	Transmembrane	19	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13530	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13532 1 107
+O13532	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000299623;Note=Putative uncharacterized protein YLR217W	
+##sequence-region P0C5P7 1 76
+P0C5P7	UniProtKB	Chain	1	76	.	.	.	ID=PRO_0000309045;Note=Putative uncharacterized protein YLR222C-A	
+##sequence-region Q05947 1 369
+Q05947	UniProtKB	Chain	1	369	.	.	.	ID=PRO_0000269758;Note=F-box protein YLR224W	
+Q05947	UniProtKB	Domain	8	45	.	.	.	Note=F-box	
+##sequence-region P0C2J6 1 438
+P0C2J6	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000279337;Note=Transposon Ty2-LR2 Gag polyprotein	
+P0C2J6	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279338;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J6	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000279339;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J6	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C2J6	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q05881 1 355
+Q05881	UniProtKB	Chain	1	355	.	.	.	ID=PRO_0000247209;Note=Uncharacterized protein YLR287C	
+##sequence-region O13543 1 109
+O13543	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299632;Note=Putative uncharacterized protein YLR294C	
+O13543	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13543	UniProtKB	Compositional bias	86	89	.	.	.	Note=Poly-Leu	
+##sequence-region Q05899 1 129
+Q05899	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000247161;Note=Uncharacterized vacuolar protein YLR297W	
+Q05899	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06158 1 115
+Q06158	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000262740;Note=Putative uncharacterized membrane protein YLR311C	
+Q06158	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06158	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06158	UniProtKB	Topological domain	33	52	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06158	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06158	UniProtKB	Topological domain	74	78	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06158	UniProtKB	Transmembrane	79	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06158	UniProtKB	Topological domain	99	115	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06170 1 240
+Q06170	UniProtKB	Chain	1	240	.	.	.	ID=PRO_0000247210;Note=Uncharacterized membrane protein YLR326W	
+Q06170	UniProtKB	Topological domain	1	85	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06170	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06170	UniProtKB	Topological domain	107	131	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06170	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06170	UniProtKB	Topological domain	153	240	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06127 1 126
+Q06127	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000299637;Note=Putative uncharacterized protein YLR334C	
+Q06127	UniProtKB	Transmembrane	4	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06127	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06127	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O94086 1 168
+O94086	UniProtKB	Chain	1	168	.	.	.	ID=PRO_0000299640;Note=Putative uncharacterized protein YLR349W	
+##sequence-region O13565 1 187
+O13565	UniProtKB	Chain	1	187	.	.	.	ID=PRO_0000299641;Note=Uncharacterized protein YLR358C	
+O13565	UniProtKB	Compositional bias	50	81	.	.	.	Note=Ser-rich	
+##sequence-region Q7LIF1 1 101
+Q7LIF1	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000299643;Note=Putative uncharacterized protein YLR366W	
+##sequence-region O13556 1 202
+O13556	UniProtKB	Chain	1	202	.	.	.	ID=PRO_0000268171;Note=Putative uncharacterized protein YLR462W	
+##sequence-region P0CL38 1 160
+P0CL38	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000406012;Note=Putative UPF0479 protein YLR466C-A	
+P0CL38	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL38	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL38	UniProtKB	Compositional bias	103	106	.	.	.	Note=Poly-Ser	
+##sequence-region Q04978 1 212
+Q04978	UniProtKB	Chain	1	212	.	.	.	ID=PRO_0000203254;Note=Uncharacterized protein YML053C	
+##sequence-region Q12204 1 715
+Q12204	UniProtKB	Transit peptide	1	22	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12204	UniProtKB	Chain	23	715	.	.	.	ID=PRO_0000237644;Note=Probable phospholipase YOR022C%2C mitochondrial	
+Q12204	UniProtKB	Domain	519	700	.	.	.	Note=DDHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00378	
+Q12204	UniProtKB	Active site	501	501	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q08419 1 115
+Q08419	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000299706;Note=Putative uncharacterized protein YOR050C	
+##sequence-region Q08486 1 104
+Q08486	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000299709;Note=Uncharacterized protein YOR072W	
+##sequence-region Q08994 1 102
+Q08994	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000268173;Note=Putative uncharacterized protein YPR203W	
+##sequence-region Q08974 1 193
+Q08974	UniProtKB	Chain	1	193	.	.	.	ID=PRO_0000242486;Note=Uncharacterized membrane protein YPL257W	
+Q08974	UniProtKB	Topological domain	1	58	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08974	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08974	UniProtKB	Topological domain	80	119	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08974	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08974	UniProtKB	Topological domain	141	147	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08974	UniProtKB	Transmembrane	148	168	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08974	UniProtKB	Topological domain	169	193	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08989 1 487
+Q08989	UniProtKB	Signal peptide	1	31	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08989	UniProtKB	Chain	32	487	.	.	.	ID=PRO_0000269760;Note=Uncharacterized protein YPL277C	
+Q08989	UniProtKB	Glycosylation	40	40	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08989	UniProtKB	Glycosylation	68	68	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08989	UniProtKB	Glycosylation	150	150	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08989	UniProtKB	Glycosylation	220	220	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08989	UniProtKB	Glycosylation	304	304	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08989	UniProtKB	Glycosylation	367	367	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08989	UniProtKB	Glycosylation	442	442	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08989	UniProtKB	Glycosylation	448	448	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX20 1 1796
+P0CX20	UniProtKB	Chain	1	1796	.	.	.	ID=PRO_0000102201;Note=Y' element ATP-dependent helicase protein 1 copy 1	
+P0CX20	UniProtKB	Domain	797	974	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P0CX20	UniProtKB	Domain	1031	1180	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P0CX20	UniProtKB	Nucleotide binding	810	817	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region P0CX21 1 1796
+P0CX21	UniProtKB	Chain	1	1796	.	.	.	ID=PRO_0000409756;Note=Y' element ATP-dependent helicase protein 1 copy 5	
+P0CX21	UniProtKB	Domain	797	974	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P0CX21	UniProtKB	Domain	1031	1180	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P0CX21	UniProtKB	Nucleotide binding	810	817	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region P42844 1 174
+P42844	UniProtKB	Transit peptide	1	47	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15719019;Dbxref=PMID:15719019	
+P42844	UniProtKB	Chain	48	174	.	.	.	ID=PRO_0000203367;Note=Mitochondrial protein import protein ZIM17	
+P42844	UniProtKB	Zinc finger	64	159	.	.	.	Note=DNL-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00834	
+P42844	UniProtKB	Metal binding	75	75	.	.	.	Note=Zinc	
+P42844	UniProtKB	Metal binding	78	78	.	.	.	Note=Zinc	
+P42844	UniProtKB	Metal binding	100	100	.	.	.	Note=Zinc	
+P42844	UniProtKB	Metal binding	103	103	.	.	.	Note=Zinc	
+P42844	UniProtKB	Mutagenesis	106	107	.	.	.	Note=In TIM15-2RH%3B Abolishes interaction with SSC1%2C and leads to self-aggregation of mtHSP70 and accumulation of uncleaved precursor proteins. RH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17571076;Dbxref=PMID:17571076	
+P42844	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Abolishes interaction with SSC1%2C and leads to self-aggregation of mtHSP70 and accumulation of uncleaved precursor proteins. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17571076;Dbxref=PMID:17571076	
+P42844	UniProtKB	Mutagenesis	133	137	.	.	.	Note=Temperature sensitive%3B only partly prevents self-aggregation of mtHSP70 and leads to accumulation of uncleaved precursor proteins at high temperatures. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17571076;Dbxref=PMID:17571076	
+P42844	UniProtKB	Mutagenesis	140	148	.	.	.	Note=In TIM15-5DE%3B no effect. DLEFEDIPD->ALAFAAIPA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17571076;Dbxref=PMID:17571076	
+P42844	UniProtKB	Beta strand	68	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+P42844	UniProtKB	Turn	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+P42844	UniProtKB	Beta strand	80	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+P42844	UniProtKB	Helix	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+P42844	UniProtKB	Beta strand	94	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+P42844	UniProtKB	Beta strand	106	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+P42844	UniProtKB	Helix	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+P42844	UniProtKB	Helix	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+P42844	UniProtKB	Beta strand	135	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+P42844	UniProtKB	Beta strand	140	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+P42844	UniProtKB	Helix	148	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+P42844	UniProtKB	Beta strand	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z	
+##sequence-region Q8TGS0 1 48
+Q8TGS0	UniProtKB	Chain	1	48	.	.	.	ID=PRO_0000237660;Note=Uncharacterized protein YOR161C-C	
+Q8TGS0	UniProtKB	Transmembrane	20	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08543 1 101
+Q08543	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000299720;Note=Putative uncharacterized protein YOR170W	
+##sequence-region Q08604 1 109
+Q08604	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299722;Note=Putative uncharacterized protein YOR199W	
+Q08604	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08604	UniProtKB	Compositional bias	9	12	.	.	.	Note=Poly-Lys	
+##sequence-region Q08748 1 1289
+Q08748	UniProtKB	Chain	1	1289	.	.	.	ID=PRO_0000245284;Note=Uncharacterized protein YOR296W	
+Q08748	UniProtKB	Domain	615	733	.	.	.	Note=MHD1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00587	
+Q08748	UniProtKB	Domain	843	947	.	.	.	Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+Q08748	UniProtKB	Domain	1044	1184	.	.	.	Note=MHD2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00588	
+##sequence-region Q12444 1 126
+Q12444	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000299734;Note=Putative uncharacterized protein YOR309C	
+Q12444	UniProtKB	Compositional bias	44	83	.	.	.	Note=Arg/Lys-rich	
+##sequence-region Q08816 1 343
+Q08816	UniProtKB	Chain	1	343	.	.	.	ID=PRO_0000245290;Note=Uncharacterized protein YOR352W	
+Q08816	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08816	UniProtKB	Modified residue	105	105	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08816	UniProtKB	Modified residue	108	108	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08816	UniProtKB	Modified residue	342	342	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q08909 1 290
+Q08909	UniProtKB	Chain	1	290	.	.	.	ID=PRO_0000244636;Note=Uncharacterized protein YOR385W	
+##sequence-region Q8TGJ0 1 55
+Q8TGJ0	UniProtKB	Chain	1	55	.	.	.	ID=PRO_0000240708;Note=Uncharacterized protein YOR394C-A	
+##sequence-region Q8TGL4 1 86
+Q8TGL4	UniProtKB	Chain	1	86	.	.	.	ID=PRO_0000299718;Note=Putative uncharacterized protein YOR161W-B	
+##sequence-region Q8TGL3 1 69
+Q8TGL3	UniProtKB	Chain	1	69	.	.	.	ID=PRO_0000299721;Note=Putative uncharacterized protein YOR186C-A	
+##sequence-region Q08259 1 102
+Q08259	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000299695;Note=Uncharacterized protein YOL118C	
+##sequence-region Q12070 1 107
+Q12070	UniProtKB	Signal peptide	1	34	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12070	UniProtKB	Chain	35	107	.	.	.	ID=PRO_0000299703;Note=Putative uncharacterized protein YOR024W	
+##sequence-region Q08900 1 122
+Q08900	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000262745;Note=Uncharacterized membrane protein YOR376W	
+Q08900	UniProtKB	Topological domain	1	24	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258	
+Q08900	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08900	UniProtKB	Topological domain	46	57	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258	
+Q08900	UniProtKB	Transmembrane	58	78	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08900	UniProtKB	Topological domain	79	122	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12524434,ECO:0000269|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258	
+##sequence-region Q12274 1 175
+Q12274	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000237654;Note=Uncharacterized protein YOR097C	
+Q12274	UniProtKB	Transmembrane	21	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12274	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A5Z2X5 1 72
+A5Z2X5	UniProtKB	Chain	1	72	.	.	.	ID=PRO_0000306772;Note=UPF0495 protein YPR010C-A	
+A5Z2X5	UniProtKB	Transmembrane	20	42	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04203 1 84
+Q04203	UniProtKB	Chain	1	84	.	.	.	ID=PRO_0000299814;Note=Putative uncharacterized protein YPR012W	
+Q04203	UniProtKB	Transmembrane	10	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12531 1 247
+Q12531	UniProtKB	Chain	1	247	.	.	.	ID=PRO_0000255975;Note=Zinc finger protein YPR015C	
+Q12531	UniProtKB	Zinc finger	185	207	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q12531	UniProtKB	Zinc finger	213	237	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q12531	UniProtKB	Sequence conflict	184	184	.	.	.	Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02606 1 381
+Q02606	UniProtKB	Chain	1	381	.	.	.	ID=PRO_0000240703;Note=Uncharacterized protein YPL014W	
+##sequence-region Q12492 1 139
+Q12492	UniProtKB	Chain	1	139	.	.	.	ID=PRO_0000299819;Note=Uncharacterized protein YPR064W	
+Q12492	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12492	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12492	UniProtKB	Compositional bias	118	138	.	.	.	Note=Cys-rich	
+##sequence-region P0C5R6 1 56
+P0C5R6	UniProtKB	Chain	1	56	.	.	.	ID=PRO_0000309064;Note=Putative uncharacterized protein YPR074W-A	
+##sequence-region Q02872 1 168
+Q02872	UniProtKB	Chain	1	168	.	.	.	ID=PRO_0000238647;Note=Uncharacterized protein YPL108W	
+##sequence-region Q06107 1 315
+Q06107	UniProtKB	Chain	1	315	.	.	.	ID=PRO_0000242487;Note=Uncharacterized TLC domain-containing protein YPR114W	
+Q06107	UniProtKB	Topological domain	1	38	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Topological domain	60	101	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Transmembrane	102	122	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Topological domain	123	144	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Topological domain	166	170	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Transmembrane	171	190	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Topological domain	191	225	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Transmembrane	226	246	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Topological domain	247	264	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Transmembrane	265	285	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Topological domain	286	315	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06107	UniProtKB	Domain	95	302	.	.	.	Note=TLC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00205	
+##sequence-region Q12414 1 1755
+Q12414	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279169;Note=Transposon Ty1-PL Gag-Pol polyprotein	
+Q12414	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279170;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12414	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279171;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12414	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279172;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12414	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279173;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12414	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12414	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12414	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q12414	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12414	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q12414	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12414	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q12414	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q12414	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12414	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12414	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12414	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12414	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12414	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12414	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12414	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12414	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12414	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12414	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12414	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region Q08916 1 105
+Q08916	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000299754;Note=Putative uncharacterized protein YPL142C	
+##sequence-region P0C5R7 1 72
+P0C5R7	UniProtKB	Chain	1	72	.	.	.	ID=PRO_0000309065;Note=Putative uncharacterized protein YPR169W-A	
+P0C5R7	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06595 1 470
+Q06595	UniProtKB	Chain	1	470	.	.	.	ID=PRO_0000257819;Note=Maltose fermentation regulatory protein YPR196W	
+Q06595	UniProtKB	DNA binding	8	34	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+Q06595	UniProtKB	Motif	41	49	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08964 1 1102
+Q08964	UniProtKB	Chain	1	1102	.	.	.	ID=PRO_0000242161;Note=Putative ISWI chromatin-remodeling complex subunit YPL216W	
+Q08964	UniProtKB	Domain	23	131	.	.	.	Note=WAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00475	
+Q08964	UniProtKB	Domain	375	435	.	.	.	Note=DDT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00063	
+Q08964	UniProtKB	Coiled coil	673	743	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CL31 1 191
+P0CL31	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL31	UniProtKB	Chain	18	191	.	.	.	ID=PRO_0000406008;Note=Putative uncharacterized protein YPL283W-A	
+P0CL31	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL31	UniProtKB	Compositional bias	13	159	.	.	.	Note=Gly/Ser-rich	
+##sequence-region Q12010 1 308
+Q12010	UniProtKB	Chain	1	308	.	.	.	ID=PRO_0000235929;Note=Probable vacuolar amino acid transporter YPQ1	
+Q12010	UniProtKB	Topological domain	1	12	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Topological domain	34	44	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Topological domain	66	68	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Transmembrane	69	89	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Topological domain	90	167	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Topological domain	189	205	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Transmembrane	206	226	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Topological domain	227	244	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Transmembrane	245	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Topological domain	266	277	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Transmembrane	278	298	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Topological domain	299	308	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Domain	10	76	.	.	.	Note=PQ-loop 1	
+Q12010	UniProtKB	Domain	211	274	.	.	.	Note=PQ-loop 2	
+Q12010	UniProtKB	Glycosylation	9	9	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Glycosylation	189	189	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12010	UniProtKB	Glycosylation	275	275	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O13559 1 1382
+O13559	UniProtKB	Chain	1	1382	.	.	.	ID=PRO_0000102204;Note=Y' element ATP-dependent helicase protein 1 copy 4	
+O13559	UniProtKB	Domain	383	560	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+O13559	UniProtKB	Domain	617	766	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+O13559	UniProtKB	Nucleotide binding	396	403	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region P32793 1 468
+P32793	UniProtKB	Chain	1	468	.	.	.	ID=PRO_0000202887;Note=Protein YSC84	
+P32793	UniProtKB	Domain	409	468	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P32793	UniProtKB	Compositional bias	222	307	.	.	.	Note=Asp-rich	
+P32793	UniProtKB	Modified residue	301	301	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32793	UniProtKB	Modified residue	311	311	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32793	UniProtKB	Beta strand	413	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08	
+P32793	UniProtKB	Beta strand	435	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08	
+P32793	UniProtKB	Beta strand	447	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08	
+P32793	UniProtKB	Beta strand	456	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08	
+P32793	UniProtKB	Helix	462	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08	
+P32793	UniProtKB	Beta strand	465	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08	
+##sequence-region P0C074 1 85
+P0C074	UniProtKB	Chain	1	85	.	.	.	ID=PRO_0000097203;Note=RDS3 complex subunit 10	
+##sequence-region P26725 1 428
+P26725	UniProtKB	Chain	1	428	.	.	.	ID=PRO_0000208250;Note=Probable mannosyltransferase YUR1	
+P26725	UniProtKB	Topological domain	1	3	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P26725	UniProtKB	Transmembrane	4	24	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P26725	UniProtKB	Topological domain	25	428	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P26725	UniProtKB	Region	25	88	.	.	.	Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26725	UniProtKB	Region	89	428	.	.	.	Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26725	UniProtKB	Active site	313	313	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P26725	UniProtKB	Glycosylation	77	77	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P26725	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P26725	UniProtKB	Glycosylation	92	92	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P26725	UniProtKB	Glycosylation	167	167	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P26725	UniProtKB	Glycosylation	414	414	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53735 1 605
+P53735	UniProtKB	Chain	1	605	.	.	.	ID=PRO_0000203477;Note=Protein ZRG17	
+P53735	UniProtKB	Topological domain	1	225	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Transmembrane	226	246	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Topological domain	247	254	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Topological domain	276	287	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Transmembrane	288	308	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Topological domain	309	309	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Transmembrane	310	330	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Topological domain	331	363	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Transmembrane	364	384	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Topological domain	385	399	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Transmembrane	400	420	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Topological domain	421	422	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Transmembrane	423	443	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Topological domain	444	545	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Transmembrane	546	566	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Topological domain	567	605	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53735	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53735	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53735	UniProtKB	Modified residue	498	498	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53735	UniProtKB	Sequence conflict	239	239	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P20107 1 442
+P20107	UniProtKB	Chain	1	442	.	.	.	ID=PRO_0000206103;Note=Zinc/cadmium resistance protein	
+P20107	UniProtKB	Topological domain	1	9	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Transmembrane	10	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Topological domain	27	41	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Transmembrane	42	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Topological domain	59	79	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Transmembrane	80	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Topological domain	97	112	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Transmembrane	113	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Topological domain	130	239	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Transmembrane	240	256	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Topological domain	257	269	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Transmembrane	270	286	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Topological domain	287	442	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20107	UniProtKB	Compositional bias	141	145	.	.	.	Note=His-rich (could be involved in coordination of zinc or cadmium ions)	
+P20107	UniProtKB	Compositional bias	163	167	.	.	.	Note=His-rich (could be involved in coordination of zinc or cadmium ions)	
+P20107	UniProtKB	Compositional bias	216	220	.	.	.	Note=His-rich (could be involved in coordination of zinc or cadmium ions)	
+P20107	UniProtKB	Modified residue	387	387	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P20107	UniProtKB	Modified residue	393	393	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P20107	UniProtKB	Modified residue	397	397	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P20107	UniProtKB	Cross-link	357	357	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P20107	UniProtKB	Sequence conflict	414	414	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20107	UniProtKB	Sequence conflict	417	417	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32804 1 376
+P32804	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000068768;Note=Zinc-regulated transporter 1	
+P32804	UniProtKB	Topological domain	1	50	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Topological domain	72	80	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Topological domain	102	122	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Topological domain	144	216	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Topological domain	238	242	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Topological domain	264	278	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Transmembrane	279	299	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Topological domain	300	310	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Transmembrane	311	331	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Topological domain	332	354	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Transmembrane	355	375	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Topological domain	376	376	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32804	UniProtKB	Region	232	233	.	.	.	Note=Heavy metals binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P34240 1 503
+P34240	UniProtKB	Chain	1	503	.	.	.	ID=PRO_0000203140;Note=Zinc-regulated transporter 3	
+P34240	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34240	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34240	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34240	UniProtKB	Transmembrane	336	356	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34240	UniProtKB	Transmembrane	371	391	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34240	UniProtKB	Transmembrane	398	418	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34240	UniProtKB	Transmembrane	438	458	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34240	UniProtKB	Transmembrane	482	502	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34240	UniProtKB	Compositional bias	102	139	.	.	.	Note=His-rich	
+P34240	UniProtKB	Compositional bias	153	158	.	.	.	Note=Poly-Ser	
+P34240	UniProtKB	Compositional bias	322	325	.	.	.	Note=Poly-His	
+P34240	UniProtKB	Compositional bias	464	467	.	.	.	Note=Poly-His	
+P34240	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34240	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P0CX14 1 1859
+P0CX14	UniProtKB	Chain	1	1859	.	.	.	ID=PRO_0000102203;Note=Y' element ATP-dependent helicase protein 1 copy 3	
+P0CX14	UniProtKB	Domain	861	1038	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P0CX14	UniProtKB	Domain	1095	1244	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P0CX14	UniProtKB	Nucleotide binding	874	881	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region Q06681 1 1438
+Q06681	UniProtKB	Chain	1	1438	.	.	.	ID=PRO_0000253815;Note=Membrane-anchored lipid-binding protein YSP2	
+Q06681	UniProtKB	Topological domain	1	1277	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06681	UniProtKB	Transmembrane	1278	1298	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06681	UniProtKB	Topological domain	1299	1438	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06681	UniProtKB	Domain	648	716	.	.	.	Note=GRAM;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06681	UniProtKB	Domain	851	1018	.	.	.	Note=VASt 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114	
+Q06681	UniProtKB	Domain	1059	1225	.	.	.	Note=VASt 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114	
+Q06681	UniProtKB	Compositional bias	219	232	.	.	.	Note=Asn-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00003	
+Q06681	UniProtKB	Compositional bias	770	815	.	.	.	Note=Asp-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00004	
+Q06681	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+Q06681	UniProtKB	Modified residue	411	411	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06681	UniProtKB	Modified residue	596	596	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06681	UniProtKB	Modified residue	1032	1032	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06681	UniProtKB	Glycosylation	1306	1306	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q06681	UniProtKB	Glycosylation	1373	1373	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q06681	UniProtKB	Glycosylation	1430	1430	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q06681	UniProtKB	Mutagenesis	1205	1205	.	.	.	Note=Reduces the ability to bind sterol. G->A%2CT;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26001273;Dbxref=PMID:26001273	
+Q06681	UniProtKB	Mutagenesis	1205	1205	.	.	.	Note=Abolishes the ability to bind sterol. G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26001273;Dbxref=PMID:26001273	
+##sequence-region P40341 1 825
+P40341	UniProtKB	Chain	1	825	.	.	.	ID=PRO_0000084676;Note=Mitochondrial respiratory chain complexes assembly protein YTA12	
+P40341	UniProtKB	Transmembrane	178	194	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40341	UniProtKB	Transmembrane	294	311	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40341	UniProtKB	Nucleotide binding	388	395	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40341	UniProtKB	Active site	614	614	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40341	UniProtKB	Metal binding	613	613	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40341	UniProtKB	Metal binding	617	617	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40341	UniProtKB	Metal binding	689	689	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40341	UniProtKB	Mutagenesis	614	614	.	.	.	Note=Abolishes proteolytic activity%3B impairs synthesis of respiratory chain proteins COB and COX1. No effect on m-AAA protease assembly. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9707443;Dbxref=PMID:9707443	
+P40341	UniProtKB	Sequence conflict	195	195	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40341	UniProtKB	Sequence conflict	349	350	.	.	.	Note=DV->EL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40341	UniProtKB	Sequence conflict	653	653	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P31383 1 635
+P31383	UniProtKB	Chain	1	635	.	.	.	ID=PRO_0000071414;Note=Protein phosphatase PP2A regulatory subunit A	
+P31383	UniProtKB	Repeat	34	72	.	.	.	Note=HEAT 1	
+P31383	UniProtKB	Repeat	73	111	.	.	.	Note=HEAT 2	
+P31383	UniProtKB	Repeat	112	150	.	.	.	Note=HEAT 3	
+P31383	UniProtKB	Repeat	151	189	.	.	.	Note=HEAT 4	
+P31383	UniProtKB	Repeat	190	228	.	.	.	Note=HEAT 5	
+P31383	UniProtKB	Repeat	229	273	.	.	.	Note=HEAT 6	
+P31383	UniProtKB	Repeat	274	316	.	.	.	Note=HEAT 7	
+P31383	UniProtKB	Repeat	317	356	.	.	.	Note=HEAT 8	
+P31383	UniProtKB	Repeat	357	395	.	.	.	Note=HEAT 9	
+P31383	UniProtKB	Repeat	396	434	.	.	.	Note=HEAT 10	
+P31383	UniProtKB	Repeat	435	473	.	.	.	Note=HEAT 11	
+P31383	UniProtKB	Repeat	474	512	.	.	.	Note=HEAT 12	
+P31383	UniProtKB	Repeat	513	553	.	.	.	Note=HEAT 13	
+P31383	UniProtKB	Repeat	554	598	.	.	.	Note=HEAT 14	
+P31383	UniProtKB	Repeat	599	632	.	.	.	Note=HEAT 15	
+P31383	UniProtKB	Sequence conflict	336	336	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31383	UniProtKB	Sequence conflict	356	356	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31383	UniProtKB	Sequence conflict	366	366	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31383	UniProtKB	Sequence conflict	611	611	.	.	.	Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08361 1 143
+Q08361	UniProtKB	Chain	1	143	.	.	.	ID=PRO_0000070370;Note=Putative aryl-alcohol dehydrogenase AAD15	
+##sequence-region P43547 1 212
+P43547	UniProtKB	Chain	1	212	.	.	.	ID=PRO_0000070367;Note=Putative aryl-alcohol dehydrogenase AAD6	
+P43547	UniProtKB	Active site	76	76	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43547	UniProtKB	Sequence conflict	208	208	.	.	.	Note=V->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P15891 1 592
+P15891	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378	
+P15891	UniProtKB	Chain	2	592	.	.	.	ID=PRO_0000064429;Note=Actin-binding protein	
+P15891	UniProtKB	Domain	7	136	.	.	.	Note=ADF-H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00599	
+P15891	UniProtKB	Repeat	200	209	.	.	.	Note=1	
+P15891	UniProtKB	Repeat	436	445	.	.	.	Note=2	
+P15891	UniProtKB	Domain	532	592	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P15891	UniProtKB	Repeat	566	575	.	.	.	Note=3	
+P15891	UniProtKB	Region	200	575	.	.	.	Note=3 X 10 AA approximate repeats (acidic)	
+P15891	UniProtKB	Compositional bias	518	522	.	.	.	Note=Poly-Pro	
+P15891	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378	
+P15891	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P15891	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P15891	UniProtKB	Modified residue	169	169	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P15891	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P15891	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P15891	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P15891	UniProtKB	Modified residue	365	365	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P15891	UniProtKB	Modified residue	389	389	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P15891	UniProtKB	Modified residue	458	458	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P15891	UniProtKB	Modified residue	481	481	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P15891	UniProtKB	Cross-link	464	464	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P15891	UniProtKB	Mutagenesis	21	21	.	.	.	Note=In ABP1-1%3B moderately reduces actin binding and partially reduces ARP2/3 complex activation%3B when associated with A-24. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087	
+P15891	UniProtKB	Mutagenesis	24	24	.	.	.	Note=In ABP1-1%3B moderately reduces actin binding and partially reduces ARP2/3 complex activation%3B when associated with A-21. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087	
+P15891	UniProtKB	Mutagenesis	80	80	.	.	.	Note=In ABP1-2%3B strongly reduces actin binding and abolishes ARP2/3 complex activation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087	
+P15891	UniProtKB	Mutagenesis	94	94	.	.	.	Note=In ABP1-3%3B reduces actin binding and abolishes ARP2/3 complex activation%3B when associated with A-96. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087	
+P15891	UniProtKB	Mutagenesis	96	96	.	.	.	Note=In ABP1-3%3B reduces actin binding and abolishes ARP2/3 complex activation%3B when associated with A-94. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087	
+P15891	UniProtKB	Mutagenesis	122	122	.	.	.	Note=In ABP1-4%3B no effect%3B when associated with A-125. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087	
+P15891	UniProtKB	Mutagenesis	125	125	.	.	.	Note=In ABP1-4%3B no effect%3B when associated with A-122. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087	
+P15891	UniProtKB	Mutagenesis	134	134	.	.	.	Note=In ABP1-5%3B moderately reduces actin binding and abolishes ARP2/3 complex activation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087	
+P15891	UniProtKB	Mutagenesis	201	203	.	.	.	Note=Abolishes ARP2/3 complex activation%2C but not actin binding. DDW->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11331312;Dbxref=PMID:11331312	
+P15891	UniProtKB	Mutagenesis	437	439	.	.	.	Note=Abolishes ARP2/3 complex activation%2C but not actin binding. DDW->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11331312;Dbxref=PMID:11331312	
+P15891	UniProtKB	Mutagenesis	569	569	.	.	.	Note=Abolishes protein binding. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11668184;Dbxref=PMID:11668184	
+P15891	UniProtKB	Sequence conflict	58	58	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15891	UniProtKB	Sequence conflict	312	312	.	.	.	Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15891	UniProtKB	Helix	12	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ	
+P15891	UniProtKB	Beta strand	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ	
+P15891	UniProtKB	Beta strand	43	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ	
+P15891	UniProtKB	Helix	52	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ	
+P15891	UniProtKB	Beta strand	65	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ	
+P15891	UniProtKB	Beta strand	80	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ	
+P15891	UniProtKB	Helix	93	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ	
+P15891	UniProtKB	Beta strand	115	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ	
+P15891	UniProtKB	Helix	123	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ	
+P15891	UniProtKB	Helix	128	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ	
+P15891	UniProtKB	Beta strand	537	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8	
+P15891	UniProtKB	Beta strand	546	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RPN	
+P15891	UniProtKB	Beta strand	558	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8	
+P15891	UniProtKB	Beta strand	566	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8	
+P15891	UniProtKB	Turn	575	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8	
+P15891	UniProtKB	Beta strand	580	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8	
+P15891	UniProtKB	Helix	585	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8	
+P15891	UniProtKB	Beta strand	588	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8	
+##sequence-region P39970 1 489
+P39970	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000076537;Note=ATF/CREB activator 1	
+P39970	UniProtKB	Domain	384	447	.	.	.	Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P39970	UniProtKB	Region	386	406	.	.	.	Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P39970	UniProtKB	Region	412	419	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P39970	UniProtKB	Compositional bias	258	267	.	.	.	Note=Poly-Ser	
+##sequence-region P32316 1 526
+P32316	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1970569;Dbxref=PMID:1970569	
+P32316	UniProtKB	Chain	2	526	.	.	.	ID=PRO_0000215524;Note=Acetyl-CoA hydrolase	
+P32316	UniProtKB	Region	277	281	.	.	.	Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B3EY95	
+P32316	UniProtKB	Active site	302	302	.	.	.	Note=5-glutamyl coenzyme A thioester intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B3EY95	
+P32316	UniProtKB	Binding site	392	392	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B3EY95	
+P32316	UniProtKB	Binding site	396	396	.	.	.	Note=Coenzyme A%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B3EY95	
+P32316	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1970569;Dbxref=PMID:1970569	
+P32316	UniProtKB	Modified residue	350	350	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P32316	UniProtKB	Sequence conflict	308	308	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32316	UniProtKB	Sequence conflict	320	320	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32316	UniProtKB	Sequence conflict	363	364	.	.	.	Note=LG->FP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q01574 1 713
+Q01574	UniProtKB	Chain	1	713	.	.	.	ID=PRO_0000208420;Note=Acetyl-coenzyme A synthetase 1	
+Q01574	UniProtKB	Nucleotide binding	443	445	.	.	.	Note=ATP	
+Q01574	UniProtKB	Nucleotide binding	467	472	.	.	.	Note=ATP	
+Q01574	UniProtKB	Region	248	251	.	.	.	Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01574	UniProtKB	Motif	711	713	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01574	UniProtKB	Binding site	367	367	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01574	UniProtKB	Binding site	559	559	.	.	.	Note=ATP	
+Q01574	UniProtKB	Binding site	574	574	.	.	.	Note=ATP	
+Q01574	UniProtKB	Binding site	582	582	.	.	.	Note=Coenzyme A%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01574	UniProtKB	Binding site	585	585	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01574	UniProtKB	Binding site	650	650	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01574	UniProtKB	Sequence conflict	34	34	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01574	UniProtKB	Sequence conflict	328	328	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01574	UniProtKB	Helix	75	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	87	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	133	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	139	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	148	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	166	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	191	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	200	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	215	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	225	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	238	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	255	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	271	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	287	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	293	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	316	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	323	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	328	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	335	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	356	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	366	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	374	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	381	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	397	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	408	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	414	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	427	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	438	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	448	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	461	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	465	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Turn	472	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	478	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Turn	483	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	503	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	508	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	520	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	540	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	549	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	554	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	569	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	581	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	588	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	601	607	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	619	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	641	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Turn	655	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Beta strand	660	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	678	683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Helix	702	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+Q01574	UniProtKB	Turn	710	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2	
+##sequence-region Q00362 1 526
+Q00362	UniProtKB	Chain	1	526	.	.	.	ID=PRO_0000071442;Note=Protein phosphatase PP2A regulatory subunit B	
+Q00362	UniProtKB	Repeat	23	62	.	.	.	Note=WD 1	
+Q00362	UniProtKB	Repeat	82	123	.	.	.	Note=WD 2	
+Q00362	UniProtKB	Repeat	182	220	.	.	.	Note=WD 3	
+Q00362	UniProtKB	Repeat	231	271	.	.	.	Note=WD 4	
+Q00362	UniProtKB	Repeat	290	328	.	.	.	Note=WD 5	
+Q00362	UniProtKB	Repeat	345	386	.	.	.	Note=WD 6	
+Q00362	UniProtKB	Repeat	495	525	.	.	.	Note=WD 7	
+Q00362	UniProtKB	Compositional bias	416	419	.	.	.	Note=Poly-Ser	
+Q00362	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q00362	UniProtKB	Sequence conflict	500	500	.	.	.	Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47096 1 177
+P47096	UniProtKB	Chain	1	177	.	.	.	ID=PRO_0000064375;Note=3-hydroxyanthranilate 3%2C4-dioxygenase	
+P47096	UniProtKB	Metal binding	49	49	.	.	.	Note=Iron%3B catalytic	
+P47096	UniProtKB	Metal binding	55	55	.	.	.	Note=Iron%3B catalytic	
+P47096	UniProtKB	Metal binding	97	97	.	.	.	Note=Iron%3B catalytic	
+P47096	UniProtKB	Metal binding	126	126	.	.	.	Note=Divalent metal cation	
+P47096	UniProtKB	Metal binding	129	129	.	.	.	Note=Divalent metal cation	
+P47096	UniProtKB	Metal binding	163	163	.	.	.	Note=Divalent metal cation	
+P47096	UniProtKB	Metal binding	166	166	.	.	.	Note=Divalent metal cation	
+P47096	UniProtKB	Binding site	45	45	.	.	.	Note=Dioxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03019	
+P47096	UniProtKB	Binding site	55	55	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03019	
+P47096	UniProtKB	Binding site	101	101	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03019	
+P47096	UniProtKB	Binding site	111	111	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03019	
+P47096	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47096	UniProtKB	Helix	9	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Helix	17	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	26	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	32	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	55	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	64	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	72	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	87	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	97	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	106	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	121	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Turn	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	132	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Beta strand	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Helix	145	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Helix	158	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+P47096	UniProtKB	Turn	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF	
+##sequence-region P42884 1 376
+P42884	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000070369;Note=Putative aryl-alcohol dehydrogenase AAD14	
+P42884	UniProtKB	Nucleotide binding	236	246	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42884	UniProtKB	Active site	76	76	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42884	UniProtKB	Binding site	151	151	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42884	UniProtKB	Site	103	103	.	.	.	Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P32357 1 355
+P32357	UniProtKB	Chain	1	355	.	.	.	ID=PRO_0000209705;Note=A1 cistron-splicing factor AAR2	
+P32357	UniProtKB	Region	261	282	.	.	.	Note=Leucine-zipper	
+P32357	UniProtKB	Compositional bias	332	341	.	.	.	Note=Asp/Glu-rich (acidic)	
+P32357	UniProtKB	Modified residue	253	253	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848	
+P32357	UniProtKB	Modified residue	274	274	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848	
+P32357	UniProtKB	Modified residue	328	328	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848	
+P32357	UniProtKB	Modified residue	331	331	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848	
+P32357	UniProtKB	Modified residue	345	345	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848	
+P32357	UniProtKB	Mutagenesis	253	253	.	.	.	Note=No effect on interaction with PRP8. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848	
+P32357	UniProtKB	Mutagenesis	253	253	.	.	.	Note=Disrupts interaction with PRP8. S->D%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848	
+P32357	UniProtKB	Beta strand	2	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	13	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	20	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	32	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBS	
+P32357	UniProtKB	Beta strand	42	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	51	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	66	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Turn	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	86	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	113	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	123	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	136	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Turn	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ILI	
+P32357	UniProtKB	Helix	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ILH	
+P32357	UniProtKB	Turn	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	194	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	202	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	207	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	217	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	237	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	258	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	277	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	280	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	286	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Turn	297	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	303	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Helix	314	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P32357	UniProtKB	Beta strand	345	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+##sequence-region P47146 1 123
+P47146	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000203111;Note=Aberrant microtubules protein 1	
+##sequence-region Q12031 1 575
+Q12031	UniProtKB	Chain	1	575	.	.	.	ID=PRO_0000068800;Note=Mitochondrial 2-methylisocitrate lyase	
+Q12031	UniProtKB	Active site	238	238	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07248 1 1323
+P07248	UniProtKB	Chain	1	1323	.	.	.	ID=PRO_0000046801;Note=Regulatory protein ADR1	
+P07248	UniProtKB	Zinc finger	104	126	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P07248	UniProtKB	Zinc finger	132	155	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P07248	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07248	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07248	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07248	UniProtKB	Modified residue	230	230	.	.	.	Note=Phosphoserine%3B by PKA%3B in vitro;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:1549108;Dbxref=PMID:17287358,PMID:19779198,PMID:1549108	
+P07248	UniProtKB	Modified residue	258	258	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07248	UniProtKB	Modified residue	259	259	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07248	UniProtKB	Modified residue	299	299	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07248	UniProtKB	Modified residue	323	323	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07248	UniProtKB	Modified residue	325	325	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07248	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07248	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Suppresses activity. C->Y	
+P07248	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Suppresses activity. C->Y	
+P07248	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Lowers activity. A->V	
+P07248	UniProtKB	Mutagenesis	118	118	.	.	.	Note=Suppresses activity. H->Y	
+P07248	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Suppresses activity. H->Y	
+P07248	UniProtKB	Mutagenesis	134	134	.	.	.	Note=Suppresses activity. C->Y	
+P07248	UniProtKB	Mutagenesis	142	142	.	.	.	Note=Lowers activity. T->I	
+P07248	UniProtKB	Sequence conflict	1216	1216	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07248	UniProtKB	Beta strand	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ARF	
+P07248	UniProtKB	Turn	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ARD	
+P07248	UniProtKB	Beta strand	111	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ARF	
+P07248	UniProtKB	Helix	116	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ARD	
+P07248	UniProtKB	Beta strand	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ADR	
+P07248	UniProtKB	Turn	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAA	
+P07248	UniProtKB	Beta strand	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAA	
+P07248	UniProtKB	Helix	145	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAA	
+P07248	UniProtKB	Turn	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ADR	
+##sequence-region P39925 1 761
+P39925	UniProtKB	Chain	1	761	.	.	.	ID=PRO_0000084670;Note=Mitochondrial respiratory chain complexes assembly protein AFG3	
+P39925	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39925	UniProtKB	Transmembrane	224	244	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39925	UniProtKB	Nucleotide binding	328	335	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39925	UniProtKB	Active site	559	559	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39925	UniProtKB	Metal binding	558	558	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39925	UniProtKB	Metal binding	562	562	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39925	UniProtKB	Metal binding	634	634	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39925	UniProtKB	Mutagenesis	559	559	.	.	.	Note=Abolishes proteolytic activity%3B impairs synthesis of respiratory chain proteins COB and COX1. No effect on m-AAA protease assembly. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9707443;Dbxref=PMID:9707443	
+P39925	UniProtKB	Sequence conflict	411	411	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38903 1 757
+P38903	UniProtKB	Chain	1	757	.	.	.	ID=PRO_0000071471;Note=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform	
+P38903	UniProtKB	Compositional bias	16	22	.	.	.	Note=Poly-Ser	
+P38903	UniProtKB	Compositional bias	46	51	.	.	.	Note=Poly-Ser	
+P38903	UniProtKB	Compositional bias	98	110	.	.	.	Note=Poly-Ser	
+P38903	UniProtKB	Compositional bias	143	147	.	.	.	Note=Poly-Ser	
+P38903	UniProtKB	Compositional bias	202	213	.	.	.	Note=Poly-Asn	
+P38903	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38903	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38903	UniProtKB	Sequence conflict	95	95	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38903	UniProtKB	Sequence conflict	529	529	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38903	UniProtKB	Sequence conflict	581	581	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47129 1 309
+P47129	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000203104;Note=Assembly-complementing factor 4	
+P47129	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P47129	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P47129	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47129	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47129	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47129	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P14164 1 731
+P14164	UniProtKB	Chain	1	731	.	.	.	ID=PRO_0000064807;Note=ARS-binding factor 1	
+P14164	UniProtKB	Region	624	628	.	.	.	Note=C-terminal sequence 1	
+P14164	UniProtKB	Region	639	662	.	.	.	Note=C-terminal sequence 2	
+P14164	UniProtKB	Compositional bias	94	294	.	.	.	Note=Asn-rich	
+P14164	UniProtKB	Compositional bias	449	510	.	.	.	Note=Asn-rich	
+P14164	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14164	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14164	UniProtKB	Modified residue	467	467	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P14164	UniProtKB	Modified residue	554	554	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14164	UniProtKB	Modified residue	618	618	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14164	UniProtKB	Modified residue	624	624	.	.	.	Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14164	UniProtKB	Modified residue	720	720	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:7608180;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:7608180	
+P14164	UniProtKB	Cross-link	18	18	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14164	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Loss of DNA binding. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2686983;Dbxref=PMID:2686983	
+P14164	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Loss of DNA binding. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2686983;Dbxref=PMID:2686983	
+P14164	UniProtKB	Mutagenesis	625	625	.	.	.	Note=Leads to mislocalization into the cytoplasm. K->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15522095;Dbxref=PMID:15522095	
+P14164	UniProtKB	Mutagenesis	720	720	.	.	.	Note=Strongly reduces phosphorylation by CK2. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7608180;Dbxref=PMID:7608180	
+P14164	UniProtKB	Sequence conflict	125	125	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	128	128	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	128	128	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	128	128	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	148	148	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	148	148	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	148	148	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	279	280	.	.	.	Note=NT->TN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	279	280	.	.	.	Note=NT->TN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	279	280	.	.	.	Note=NT->TN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	690	690	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	690	690	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14164	UniProtKB	Sequence conflict	690	690	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40535 1 587
+P40535	UniProtKB	Chain	1	587	.	.	.	ID=PRO_0000076530;Note=ATF/CREB activator 2	
+P40535	UniProtKB	Domain	425	488	.	.	.	Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P40535	UniProtKB	Region	427	447	.	.	.	Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P40535	UniProtKB	Region	453	467	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P40535	UniProtKB	Modified residue	171	171	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40535	UniProtKB	Modified residue	179	179	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40535	UniProtKB	Modified residue	399	399	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P40535	UniProtKB	Modified residue	557	557	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40535	UniProtKB	Modified residue	559	559	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P31787 1 87
+P31787	UniProtKB	Chain	1	87	.	.	.	ID=PRO_0000214013;Note=Acyl-CoA-binding protein	
+P31787	UniProtKB	Domain	2	87	.	.	.	Note=ACB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00573	
+P31787	UniProtKB	Region	29	33	.	.	.	Note=Acyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P31787	UniProtKB	Binding site	51	51	.	.	.	Note=Acyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P31787	UniProtKB	Binding site	55	55	.	.	.	Note=Acyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P31787	UniProtKB	Binding site	74	74	.	.	.	Note=Acyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P31787	UniProtKB	Cross-link	51	51	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P31787	UniProtKB	Cross-link	72	72	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P31787	UniProtKB	Helix	3	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ST7	
+P31787	UniProtKB	Helix	22	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ST7	
+P31787	UniProtKB	Helix	50	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ST7	
+P31787	UniProtKB	Turn	61	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ST7	
+P31787	UniProtKB	Helix	66	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ST7	
+##sequence-region P53930 1 226
+P53930	UniProtKB	Chain	1	226	.	.	.	ID=PRO_0000215934;Note=Protein AF-9 homolog	
+P53930	UniProtKB	Domain	15	123	.	.	.	Note=YEATS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00376	
+P53930	UniProtKB	Coiled coil	187	224	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53930	UniProtKB	Sequence conflict	65	65	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53930	UniProtKB	Beta strand	8	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FK3	
+P53930	UniProtKB	Beta strand	14	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Beta strand	41	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Helix	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Turn	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Beta strand	59	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Beta strand	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Beta strand	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Beta strand	79	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Beta strand	93	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Helix	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Beta strand	109	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Beta strand	145	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+P53930	UniProtKB	Helix	160	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS	
+##sequence-region P32317 1 509
+P32317	UniProtKB	Chain	1	509	.	.	.	ID=PRO_0000064477;Note=Protein AFG1	
+P32317	UniProtKB	Nucleotide binding	126	133	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32317	UniProtKB	Sequence conflict	210	210	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32317	UniProtKB	Sequence conflict	210	210	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32317	UniProtKB	Sequence conflict	373	373	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32317	UniProtKB	Sequence conflict	373	373	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32317	UniProtKB	Sequence conflict	399	399	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32323 1 725
+P32323	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32323	UniProtKB	Chain	25	699	.	.	.	ID=PRO_0000020641;Note=A-agglutinin anchorage subunit	
+P32323	UniProtKB	Propeptide	700	725	.	.	.	ID=PRO_0000296627;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32323	UniProtKB	Repeat	53	149	.	.	.	Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	182	188	.	.	.	Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	189	195	.	.	.	Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	196	202	.	.	.	Note=2-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	203	209	.	.	.	Note=2-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	210	216	.	.	.	Note=2-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	217	223	.	.	.	Note=2-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	224	230	.	.	.	Note=2-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	231	237	.	.	.	Note=2-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	238	244	.	.	.	Note=2-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	245	251	.	.	.	Note=2-10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	252	258	.	.	.	Note=2-11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	259	265	.	.	.	Note=2-12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	266	272	.	.	.	Note=2-13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	273	279	.	.	.	Note=2-14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	280	286	.	.	.	Note=2-15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	287	293	.	.	.	Note=2-16;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	294	300	.	.	.	Note=2-17;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	301	307	.	.	.	Note=2-18;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Repeat	395	493	.	.	.	Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32323	UniProtKB	Region	53	493	.	.	.	Note=2 X approximate repeats	
+P32323	UniProtKB	Region	182	307	.	.	.	Note=18 X approximate tandem repeats%2C Ser/Thr-rich	
+P32323	UniProtKB	Lipidation	699	699	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32323	UniProtKB	Disulfide bond	133	133	.	.	.	Note=Interchain (with AGA2);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278672;Dbxref=PMID:11278672	
+P32323	UniProtKB	Disulfide bond	136	136	.	.	.	Note=Interchain (with AGA2);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278672;Dbxref=PMID:11278672	
+##sequence-region Q12482 1 902
+Q12482	UniProtKB	Chain	1	902	.	.	.	ID=PRO_0000227601;Note=Mitochondrial aspartate-glutamate transporter AGC1	
+Q12482	UniProtKB	Transmembrane	534	554	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12482	UniProtKB	Transmembrane	591	611	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12482	UniProtKB	Transmembrane	622	642	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12482	UniProtKB	Transmembrane	681	702	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12482	UniProtKB	Transmembrane	731	751	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12482	UniProtKB	Transmembrane	786	806	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12482	UniProtKB	Repeat	528	614	.	.	.	Note=Solcar 1	
+Q12482	UniProtKB	Repeat	622	710	.	.	.	Note=Solcar 2	
+Q12482	UniProtKB	Repeat	725	813	.	.	.	Note=Solcar 3	
+##sequence-region Q04412 1 482
+Q04412	UniProtKB	Chain	1	482	.	.	.	ID=PRO_0000074222;Note=ADP-ribosylation factor GTPase-activating protein effector protein 1	
+Q04412	UniProtKB	Domain	170	297	.	.	.	Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+Q04412	UniProtKB	Zinc finger	186	210	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+##sequence-region P38090 1 596
+P38090	UniProtKB	Chain	1	596	.	.	.	ID=PRO_0000054143;Note=General amino acid permease AGP2	
+P38090	UniProtKB	Topological domain	1	94	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	95	115	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	116	117	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	139	165	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	166	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	187	199	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	221	227	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	228	248	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	249	288	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	289	309	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	310	326	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	327	347	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	348	379	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	380	400	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	401	427	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	428	448	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	449	459	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	460	480	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	481	505	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	506	526	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	527	534	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Transmembrane	535	555	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38090	UniProtKB	Topological domain	556	596	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P03876 1 854
+P03876	UniProtKB	Chain	1	854	.	.	.	ID=PRO_0000196881;Note=Putative COX1/OXI3 intron 2 protein	
+P03876	UniProtKB	Domain	329	613	.	.	.	Note=Reverse transcriptase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405	
+P03876	UniProtKB	Sequence conflict	236	236	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03876	UniProtKB	Sequence conflict	724	724	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12471 1 397
+Q12471	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000179977;Note=6-phosphofructo-2-kinase 2	
+Q12471	UniProtKB	Nucleotide binding	103	110	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12471	UniProtKB	Region	85	305	.	.	.	Note=6-phosphofructo-2-kinase	
+Q12471	UniProtKB	Active site	197	197	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12471	UniProtKB	Active site	235	235	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12471	UniProtKB	Binding site	269	269	.	.	.	Note=Fructose-6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12471	UniProtKB	Cross-link	55	55	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P53319 1 492
+P53319	UniProtKB	Chain	1	492	.	.	.	ID=PRO_0000090076;Note=6-phosphogluconate dehydrogenase%2C decarboxylating 2	
+P53319	UniProtKB	Nucleotide binding	12	17	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Nucleotide binding	35	37	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Nucleotide binding	77	79	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Region	131	133	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Region	188	189	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Active site	185	185	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Active site	192	192	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Binding site	105	105	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Binding site	105	105	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Binding site	193	193	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Binding site	262	262	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Binding site	289	289	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Binding site	449	449	.	.	.	Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53319	UniProtKB	Binding site	455	455	.	.	.	Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P23542 1 418
+P23542	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1859361,ECO:0000269|PubMed:2199266;Dbxref=PMID:22814378,PMID:1859361,PMID:2199266	
+P23542	UniProtKB	Chain	2	418	.	.	.	ID=PRO_0000123875;Note=Aspartate aminotransferase%2C cytoplasmic	
+P23542	UniProtKB	Binding site	38	38	.	.	.	Note=Aspartate%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9655342;Dbxref=PMID:9655342	
+P23542	UniProtKB	Binding site	135	135	.	.	.	Note=Aspartate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9655342;Dbxref=PMID:9655342	
+P23542	UniProtKB	Binding site	188	188	.	.	.	Note=Aspartate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9655342;Dbxref=PMID:9655342	
+P23542	UniProtKB	Binding site	387	387	.	.	.	Note=Aspartate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9655342;Dbxref=PMID:9655342	
+P23542	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1859361;Dbxref=PMID:22814378,PMID:1859361	
+P23542	UniProtKB	Modified residue	255	255	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9655342;Dbxref=PMID:9655342	
+P23542	UniProtKB	Modified residue	389	389	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P23542	UniProtKB	Sequence conflict	95	95	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23542	UniProtKB	Sequence conflict	95	95	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23542	UniProtKB	Sequence conflict	413	414	.	.	.	Note=TI->AT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23542	UniProtKB	Sequence conflict	413	414	.	.	.	Note=TI->AT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23542	UniProtKB	Turn	3	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	18	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	51	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	77	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Beta strand	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	107	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Beta strand	128	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	138	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Turn	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Beta strand	149	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Turn	157	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	164	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Beta strand	179	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Turn	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	196	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Beta strand	212	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Turn	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Beta strand	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	227	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	232	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Turn	241	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Beta strand	247	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Turn	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Beta strand	264	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	277	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Turn	294	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	301	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	314	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	353	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Beta strand	359	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	368	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Beta strand	386	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	390	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Turn	395	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+P23542	UniProtKB	Helix	398	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA	
+##sequence-region Q07622 1 623
+Q07622	UniProtKB	Chain	1	623	.	.	.	ID=PRO_0000242166;Note=Activator of C kinase protein 1	
+Q07622	UniProtKB	Repeat	318	361	.	.	.	Note=Sel1-like 1	
+Q07622	UniProtKB	Repeat	408	444	.	.	.	Note=Sel1-like 2	
+Q07622	UniProtKB	Repeat	495	531	.	.	.	Note=Sel1-like 3	
+Q07622	UniProtKB	Repeat	576	611	.	.	.	Note=Sel1-like 4	
+Q07622	UniProtKB	Compositional bias	68	76	.	.	.	Note=Poly-Ser	
+Q07622	UniProtKB	Cross-link	184	184	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q07622	UniProtKB	Cross-link	191	191	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q03771 1 387
+Q03771	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03771	UniProtKB	Chain	2	387	.	.	.	ID=PRO_0000253808;Note=Assembly chaperone of RPL4	
+Q03771	UniProtKB	Repeat	42	75	.	.	.	Note=TPR 1	
+Q03771	UniProtKB	Repeat	163	196	.	.	.	Note=TPR 2	
+Q03771	UniProtKB	Repeat	224	257	.	.	.	Note=TPR 3	
+Q03771	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q07747 1 329
+Q07747	UniProtKB	Chain	1	329	.	.	.	ID=PRO_0000070366;Note=Probable aryl-alcohol dehydrogenase AAD4	
+Q07747	UniProtKB	Nucleotide binding	190	200	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07747	UniProtKB	Active site	30	30	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07747	UniProtKB	Binding site	105	105	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07747	UniProtKB	Site	57	57	.	.	.	Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P08521 1 25
+P08521	UniProtKB	Peptide	1	25	.	.	.	ID=PRO_0000043974;Note=Arginine attenuator peptide	
+P08521	UniProtKB	Mutagenesis	13	13	.	.	.	Note=Eliminates arginine-specific stalling of ribosomes at the termination codon. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3555844;Dbxref=PMID:3555844	
+##sequence-region P21192 1 770
+P21192	UniProtKB	Chain	1	770	.	.	.	ID=PRO_0000046800;Note=Metallothionein expression activator	
+P21192	UniProtKB	Zinc finger	603	627	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P21192	UniProtKB	Zinc finger	633	657	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P21192	UniProtKB	Zinc finger	662	685	.	.	.	Note=C2H2-type 3%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P21192	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+P21192	UniProtKB	Modified residue	122	122	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P21192	UniProtKB	Modified residue	247	247	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21192	UniProtKB	Modified residue	249	249	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21192	UniProtKB	Modified residue	253	253	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21192	UniProtKB	Modified residue	259	259	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21192	UniProtKB	Modified residue	385	385	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21192	UniProtKB	Modified residue	392	392	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21192	UniProtKB	Modified residue	483	483	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21192	UniProtKB	Modified residue	486	486	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21192	UniProtKB	Modified residue	501	501	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21192	UniProtKB	Modified residue	564	564	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21192	UniProtKB	Modified residue	709	709	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P21192	UniProtKB	Modified residue	714	714	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P47182 1 288
+P47182	UniProtKB	Chain	1	288	.	.	.	ID=PRO_0000070368;Note=Putative aryl-alcohol dehydrogenase AAD10	
+##sequence-region P25612 1 363
+P25612	UniProtKB	Chain	1	363	.	.	.	ID=PRO_0000070365;Note=Putative aryl-alcohol dehydrogenase AAD3	
+##sequence-region P37898 1 856
+P37898	UniProtKB	Chain	1	856	.	.	.	ID=PRO_0000095105;Note=Alanine/arginine aminopeptidase	
+P37898	UniProtKB	Region	264	268	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P37898	UniProtKB	Active site	301	301	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P37898	UniProtKB	Metal binding	300	300	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P37898	UniProtKB	Metal binding	304	304	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P37898	UniProtKB	Metal binding	323	323	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P37898	UniProtKB	Binding site	132	132	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P37898	UniProtKB	Site	386	386	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P37898	UniProtKB	Sequence conflict	550	569	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37898	UniProtKB	Sequence conflict	646	646	.	.	.	Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P28240 1 557
+P28240	UniProtKB	Chain	1	557	.	.	.	ID=PRO_0000068799;Note=Isocitrate lyase	
+P28240	UniProtKB	Region	106	108	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7	
+P28240	UniProtKB	Region	218	219	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7	
+P28240	UniProtKB	Region	437	441	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7	
+P28240	UniProtKB	Active site	217	217	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28240	UniProtKB	Metal binding	179	179	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7	
+P28240	UniProtKB	Binding site	254	254	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7	
+P28240	UniProtKB	Binding site	471	471	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7	
+P28240	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28240	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Abolishes short-term enzyme inactivation by glucose addition. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8641464;Dbxref=PMID:8641464	
+P28240	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Reduces activity by 45%25%3B when associated with L-220. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8923733;Dbxref=PMID:8923733	
+P28240	UniProtKB	Mutagenesis	220	220	.	.	.	Note=Reduces activity by 45%25%3B when associated with R-216. M->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8923733;Dbxref=PMID:8923733	
+##sequence-region P38720 1 489
+P38720	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000090075;Note=6-phosphogluconate dehydrogenase%2C decarboxylating 1	
+P38720	UniProtKB	Nucleotide binding	9	14	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Nucleotide binding	32	34	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Nucleotide binding	74	76	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Region	128	130	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Region	185	186	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Active site	182	182	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Active site	189	189	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Binding site	102	102	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Binding site	102	102	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Binding site	190	190	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Binding site	259	259	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Binding site	286	286	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Binding site	446	446	.	.	.	Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Binding site	452	452	.	.	.	Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38720	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38720	UniProtKB	Beta strand	4	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	12	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Beta strand	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Beta strand	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	36	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Turn	44	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Beta strand	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	57	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Beta strand	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	78	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Beta strand	96	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	105	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Beta strand	121	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	130	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Beta strand	139	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	149	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Beta strand	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	177	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	211	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Turn	223	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	229	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Beta strand	245	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	248	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	261	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	277	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	292	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	315	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	354	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Beta strand	363	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	370	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	388	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	392	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	420	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	439	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Helix	458	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+P38720	UniProtKB	Beta strand	463	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q	
+##sequence-region Q02895 1 342
+Q02895	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000238634;Note=Putative aryl-alcohol dehydrogenase AAD16	
+##sequence-region Q01802 1 451
+Q01802	UniProtKB	Binding site	52	52	.	.	.	Note=Aspartate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01802	UniProtKB	Binding site	155	155	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01802	UniProtKB	Binding site	216	216	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01802	UniProtKB	Binding site	423	423	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01802	UniProtKB	Modified residue	286	286	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01802	UniProtKB	Sequence conflict	41	41	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01802	UniProtKB	Sequence conflict	414	414	.	.	.	Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08641 1 628
+Q08641	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9467951;Dbxref=PMID:9467951	
+Q08641	UniProtKB	Chain	2	628	.	.	.	ID=PRO_0000204458;Note=tRNA(Thr) (cytosine(32)-N(3))-methyltransferase	
+Q08641	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q08641	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08641	UniProtKB	Modified residue	321	321	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q08641	UniProtKB	Modified residue	326	326	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08641	UniProtKB	Modified residue	347	347	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P47177 1 404
+P47177	UniProtKB	Chain	1	404	.	.	.	ID=PRO_0000203128;Note=Putative nitronate monooxygenase	
+P47177	UniProtKB	Nucleotide binding	41	43	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47177	UniProtKB	Nucleotide binding	270	272	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47177	UniProtKB	Nucleotide binding	293	294	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47177	UniProtKB	Active site	224	224	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47177	UniProtKB	Binding site	224	224	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47177	UniProtKB	Sequence conflict	402	402	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40433 1 827
+P40433	UniProtKB	Chain	1	827	.	.	.	ID=PRO_0000179976;Note=6-phosphofructo-2-kinase 1	
+P40433	UniProtKB	Nucleotide binding	190	197	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40433	UniProtKB	Active site	277	277	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40433	UniProtKB	Active site	309	309	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40433	UniProtKB	Active site	404	404	.	.	.	Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40433	UniProtKB	Active site	497	497	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40433	UniProtKB	Active site	565	565	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40433	UniProtKB	Binding site	343	343	.	.	.	Note=Fructose-6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40433	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40433	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40433	UniProtKB	Modified residue	644	644	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40433	UniProtKB	Modified residue	652	652	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40433	UniProtKB	Modified residue	659	659	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P40433	UniProtKB	Modified residue	667	667	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40433	UniProtKB	Sequence conflict	382	382	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40433	UniProtKB	Sequence conflict	477	477	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P12904 1 322
+P12904	UniProtKB	Chain	1	322	.	.	.	ID=PRO_0000204389;Note=5'-AMP-activated protein kinase subunit gamma	
+P12904	UniProtKB	Domain	37	97	.	.	.	Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P12904	UniProtKB	Domain	118	181	.	.	.	Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P12904	UniProtKB	Domain	194	253	.	.	.	Note=CBS 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P12904	UniProtKB	Domain	262	322	.	.	.	Note=CBS 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P12904	UniProtKB	Nucleotide binding	166	169	.	.	.	Note=ADP 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343	
+P12904	UniProtKB	Nucleotide binding	221	222	.	.	.	Note=AMP%2C ADP or ATP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22019086;Dbxref=PMID:22019086	
+P12904	UniProtKB	Nucleotide binding	291	293	.	.	.	Note=ADP 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343	
+P12904	UniProtKB	Nucleotide binding	309	312	.	.	.	Note=AMP%2C ADP or ATP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22019086;Dbxref=PMID:22019086	
+P12904	UniProtKB	Binding site	146	146	.	.	.	Note=ADP 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343	
+P12904	UniProtKB	Binding site	195	195	.	.	.	Note=AMP%2C ADP or ATP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22019086;Dbxref=PMID:22019086	
+P12904	UniProtKB	Binding site	200	200	.	.	.	Note=AMP%2C ADP or ATP 2%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22019086;Dbxref=PMID:22019086	
+P12904	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. V->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591	
+P12904	UniProtKB	Mutagenesis	136	136	.	.	.	Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591	
+P12904	UniProtKB	Mutagenesis	145	145	.	.	.	Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591	
+P12904	UniProtKB	Mutagenesis	146	146	.	.	.	Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. R->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591	
+P12904	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. T->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591	
+P12904	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. N->A%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591	
+P12904	UniProtKB	Mutagenesis	242	242	.	.	.	Note=Decreases SNF1-activation efficiency%3B when associated with A-291 and E-293. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17223533;Dbxref=PMID:17223533	
+P12904	UniProtKB	Mutagenesis	251	251	.	.	.	Note=Leads to resistance to 2-deoxyglucose. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591	
+P12904	UniProtKB	Mutagenesis	291	291	.	.	.	Note=Decreases SNF1-activation efficiency%3B when associated with E-242 and E-293. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17223533;Dbxref=PMID:17223533	
+P12904	UniProtKB	Mutagenesis	293	293	.	.	.	Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17223533,ECO:0000269|PubMed:18474591;Dbxref=PMID:17223533,PMID:18474591	
+P12904	UniProtKB	Mutagenesis	293	293	.	.	.	Note=Decreases SNF1-activation efficiency%3B when associated with E-242 and A-291. H->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17223533,ECO:0000269|PubMed:18474591;Dbxref=PMID:17223533,PMID:18474591	
+P12904	UniProtKB	Helix	8	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Helix	31	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Beta strand	37	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Helix	50	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Beta strand	65	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Turn	70	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Beta strand	74	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Helix	81	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Helix	95	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Helix	106	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Helix	132	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Beta strand	145	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Turn	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Beta strand	159	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Helix	167	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Helix	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV	
+P12904	UniProtKB	Helix	182	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC	
+P12904	UniProtKB	Helix	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC	
+P12904	UniProtKB	Helix	208	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC	
+P12904	UniProtKB	Beta strand	221	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC	
+P12904	UniProtKB	Beta strand	231	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC	
+P12904	UniProtKB	Helix	238	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC	
+P12904	UniProtKB	Helix	249	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Helix	257	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC	
+P12904	UniProtKB	Beta strand	272	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P12904	UniProtKB	Helix	280	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC	
+P12904	UniProtKB	Beta strand	293	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC	
+P12904	UniProtKB	Beta strand	302	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC	
+P12904	UniProtKB	Helix	310	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC	
+##sequence-region Q02486 1 183
+Q02486	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1881919;Dbxref=PMID:1881919	
+Q02486	UniProtKB	Chain	27	183	.	.	.	ID=PRO_0000013477;Note=ARS-binding factor 2%2C mitochondrial	
+Q02486	UniProtKB	DNA binding	43	111	.	.	.	Note=HMG box 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267	
+Q02486	UniProtKB	DNA binding	116	183	.	.	.	Note=HMG box 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267	
+Q02486	UniProtKB	Helix	30	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0	
+Q02486	UniProtKB	Helix	49	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0	
+Q02486	UniProtKB	Helix	70	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0	
+Q02486	UniProtKB	Helix	86	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0	
+Q02486	UniProtKB	Helix	122	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0	
+Q02486	UniProtKB	Helix	143	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0	
+Q02486	UniProtKB	Helix	159	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0	
+##sequence-region Q00955 1 2233
+Q00955	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q00955	UniProtKB	Chain	2	2233	.	.	.	ID=PRO_0000146770;Note=Acetyl-CoA carboxylase	
+Q00955	UniProtKB	Domain	58	567	.	.	.	Note=Biotin carboxylation	
+Q00955	UniProtKB	Domain	216	408	.	.	.	Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+Q00955	UniProtKB	Domain	694	768	.	.	.	Note=Biotinyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066	
+Q00955	UniProtKB	Domain	1486	1822	.	.	.	Note=CoA carboxyltransferase N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01136	
+Q00955	UniProtKB	Domain	1826	2141	.	.	.	Note=CoA carboxyltransferase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01137	
+Q00955	UniProtKB	Nucleotide binding	256	261	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+Q00955	UniProtKB	Region	1486	2141	.	.	.	Note=Carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01138	
+Q00955	UniProtKB	Region	1627	1629	.	.	.	Note=Acetyl-CoA binding	
+Q00955	UniProtKB	Active site	383	383	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00955	UniProtKB	Metal binding	365	365	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00955	UniProtKB	Metal binding	379	379	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00955	UniProtKB	Metal binding	379	379	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00955	UniProtKB	Metal binding	381	381	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00955	UniProtKB	Binding site	1731	1731	.	.	.	Note=Coenzyme A	
+Q00955	UniProtKB	Binding site	1998	1998	.	.	.	Note=Acetyl-CoA%3B via amide nitrogen	
+Q00955	UniProtKB	Binding site	2034	2034	.	.	.	Note=Coenzyme A	
+Q00955	UniProtKB	Binding site	2036	2036	.	.	.	Note=Coenzyme A	
+Q00955	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q00955	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q00955	UniProtKB	Modified residue	735	735	.	.	.	Note=N6-biotinyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066	
+Q00955	UniProtKB	Modified residue	790	790	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00955	UniProtKB	Modified residue	1148	1148	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198	
+Q00955	UniProtKB	Modified residue	1157	1157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q00955	UniProtKB	Modified residue	1162	1162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00955	UniProtKB	Mutagenesis	1705	1705	.	.	.	Note=Raises KM for malonyl-CoA by a factor of 20. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926	
+Q00955	UniProtKB	Mutagenesis	1731	1731	.	.	.	Note=Raises KM for malonyl-CoA by a factor of 15. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926	
+Q00955	UniProtKB	Mutagenesis	1738	1738	.	.	.	Note=Does not affect catalytic activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926	
+Q00955	UniProtKB	Mutagenesis	1954	1954	.	.	.	Note=Raises KM for malonyl-CoA by a factor of 70. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926	
+Q00955	UniProtKB	Mutagenesis	1994	1994	.	.	.	Note=Does not affect catalytic activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926	
+Q00955	UniProtKB	Mutagenesis	2026	2026	.	.	.	Note=Does not affect catalytic activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926	
+Q00955	UniProtKB	Mutagenesis	2036	2036	.	.	.	Note=Affects only slightly binding of Co-A. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926	
+Q00955	UniProtKB	Sequence conflict	1523	1523	.	.	.	Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00955	UniProtKB	Sequence conflict	1755	1755	.	.	.	Note=I->IWYRCL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00955	UniProtKB	Sequence conflict	1761	1766	.	.	.	Note=AINKML->ESTNA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00955	UniProtKB	Helix	22	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	45	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	68	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	91	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	100	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	108	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	113	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Turn	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	131	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	144	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Turn	152	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	158	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	171	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	177	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	186	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Turn	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Turn	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	224	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	235	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	247	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Turn	258	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	268	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	287	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	297	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Turn	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W93	
+Q00955	UniProtKB	Beta strand	311	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	326	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	339	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	360	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Turn	370	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	375	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	388	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	399	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	412	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	416	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	439	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	452	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	466	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W93	
+Q00955	UniProtKB	Beta strand	472	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	484	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	503	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	516	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Beta strand	531	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSK	
+Q00955	UniProtKB	Helix	541	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	550	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	561	565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96	
+Q00955	UniProtKB	Helix	577	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Helix	612	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	618	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	626	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	638	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	650	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	659	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	663	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	671	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	682	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	690	695	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	702	704	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	709	716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	727	733	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	736	741	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	746	750	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	763	767	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Helix	772	774	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	793	795	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I6E	
+Q00955	UniProtKB	Helix	798	813	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	818	833	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	838	850	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	851	853	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	856	871	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	878	889	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Turn	892	894	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Beta strand	896	898	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	900	913	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Turn	914	916	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	918	937	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	938	940	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	942	944	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSL	
+Q00955	UniProtKB	Helix	947	957	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Helix	962	972	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	975	995	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	997	1002	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	1004	1011	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	1016	1018	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	1019	1030	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0	
+Q00955	UniProtKB	Helix	1037	1052	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1054	1056	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Beta strand	1057	1059	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1062	1066	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA	
+Q00955	UniProtKB	Helix	1069	1076	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1083	1086	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1087	1090	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Turn	1095	1097	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1098	1109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Turn	1110	1112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1113	1122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1124	1134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1138	1140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I6E	
+Q00955	UniProtKB	Beta strand	1155	1157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSL	
+Q00955	UniProtKB	Helix	1158	1160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSL	
+Q00955	UniProtKB	Beta strand	1167	1170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I6E	
+Q00955	UniProtKB	Beta strand	1173	1178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1183	1185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1186	1194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1220	1225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1235	1255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1258	1265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1268	1270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1274	1279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Turn	1280	1283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1287	1289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1294	1300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1303	1305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1308	1313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1320	1327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1334	1342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1349	1351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1353	1372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1378	1380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I6E	
+Q00955	UniProtKB	Beta strand	1382	1389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1397	1403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Turn	1404	1408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1409	1411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Helix	1412	1418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1420	1430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Turn	1432	1434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1437	1445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1447	1450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I6E	
+Q00955	UniProtKB	Beta strand	1453	1461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1463	1465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1467	1474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Turn	1477	1480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC	
+Q00955	UniProtKB	Beta strand	1482	1484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1490	1493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1495	1502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1508	1510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1511	1526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1534	1536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1537	1544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1546	1548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OD2	
+Q00955	UniProtKB	Beta strand	1550	1553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1561	1571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1580	1587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1592	1594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1598	1614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1618	1622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Turn	1633	1638	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1640	1645	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1649	1651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1653	1658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1660	1668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1672	1674	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1675	1682	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1685	1693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1696	1698	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1702	1719	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1724	1728	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1735	1742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1745	1749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1754	1757	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1759	1766	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1775	1778	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1780	1783	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Turn	1784	1787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1788	1795	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1796	1807	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1812	1816	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSK	
+Q00955	UniProtKB	Beta strand	1827	1829	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CTE	
+Q00955	UniProtKB	Beta strand	1837	1839	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8X	
+Q00955	UniProtKB	Helix	1843	1848	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1850	1852	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1855	1857	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1867	1870	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1877	1884	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1887	1894	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1899	1903	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1909	1911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OD4	
+Q00955	UniProtKB	Beta strand	1915	1919	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1926	1940	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Turn	1941	1943	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1947	1950	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1953	1956	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CTE	
+Q00955	UniProtKB	Helix	1960	1964	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	1967	1979	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1985	1989	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	1994	1996	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8X	
+Q00955	UniProtKB	Helix	1997	2000	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Turn	2001	2003	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	2005	2008	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Turn	2009	2011	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	2012	2017	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	2021	2025	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8X	
+Q00955	UniProtKB	Helix	2027	2034	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	2039	2047	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	2049	2058	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	2059	2063	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CTB	
+Q00955	UniProtKB	Helix	2065	2072	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	2078	2095	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	2100	2106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	2108	2113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	2115	2117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	2118	2139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Beta strand	2142	2144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	2148	2157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Helix	2168	2186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8	
+Q00955	UniProtKB	Turn	2189	2191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TVU	
+Q00955	UniProtKB	Turn	2196	2199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UYV	
+Q00955	UniProtKB	Turn	2203	2205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UYR	
+Q00955	UniProtKB	Helix	2206	2215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CTE	
+Q00955	UniProtKB	Helix	2223	2233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CTE	
+##sequence-region P40529 1 298
+P40529	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40529	UniProtKB	Chain	2	298	.	.	.	ID=PRO_0000074228;Note=ADP-ribosylation factor GTPase-activating protein effector protein 2	
+P40529	UniProtKB	Domain	8	130	.	.	.	Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+P40529	UniProtKB	Zinc finger	23	47	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+P40529	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40529	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40529	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40529	UniProtKB	Modified residue	207	207	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P52923 1 378
+P52923	UniProtKB	Chain	1	378	.	.	.	ID=PRO_0000203486;Note=Apoptosis-inducing factor 1	
+P52923	UniProtKB	Transmembrane	7	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52923	UniProtKB	Nucleotide binding	12	16	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52923	UniProtKB	Binding site	51	51	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52923	UniProtKB	Binding site	56	56	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52923	UniProtKB	Binding site	283	283	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P23180 1 465
+P23180	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23180	UniProtKB	Chain	17	465	.	.	.	ID=PRO_0000207092;Note=Probable oxidoreductase AIM17	
+P23180	UniProtKB	Metal binding	246	246	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23180	UniProtKB	Metal binding	248	248	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23180	UniProtKB	Metal binding	428	428	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38884 1 321
+P38884	UniProtKB	Transit peptide	1	72	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38884	UniProtKB	Chain	73	321	.	.	.	ID=PRO_0000202939;Note=Altered inheritance of mitochondria protein 18%2C mitochondrial	
+##sequence-region P40451 1 204
+P40451	UniProtKB	Chain	1	204	.	.	.	ID=PRO_0000202953;Note=Altered inheritance of mitochondria protein 20	
+P40451	UniProtKB	Transmembrane	6	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32858 1 118
+P32858	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000203183;Note=Altered inheritance of mitochondria protein 26%2C mitochondrial	
+P32858	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32858	UniProtKB	Transmembrane	41	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32858	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03673 1 198
+Q03673	UniProtKB	Transit peptide	1	55	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03673	UniProtKB	Chain	56	198	.	.	.	ID=PRO_0000203268;Note=Altered inheritance of mitochondria protein 34%2C mitochondrial	
+Q03673	UniProtKB	Transmembrane	172	187	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03673	UniProtKB	Domain	69	103	.	.	.	Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186	
+##sequence-region Q03798 1 255
+Q03798	UniProtKB	Transit peptide	1	40	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03798	UniProtKB	Chain	41	255	.	.	.	ID=PRO_0000203312;Note=Altered inheritance of mitochondria protein 36%2C mitochondrial	
+Q03798	UniProtKB	Transmembrane	64	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12032 1 185
+Q12032	UniProtKB	Transit peptide	1	53	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12032	UniProtKB	Chain	54	185	.	.	.	ID=PRO_0000237666;Note=Altered inheritance of mitochondria protein 41%2C mitochondrial	
+##sequence-region P38305 1 123
+P38305	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000202507;Note=Altered inheritance of mitochondria protein 4	
+##sequence-region P46680 1 615
+P46680	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P46680	UniProtKB	Chain	2	615	.	.	.	ID=PRO_0000050841;Note=Actin-interacting protein 1	
+P46680	UniProtKB	Repeat	2	45	.	.	.	Note=WD 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	46	94	.	.	.	Note=WD 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	95	146	.	.	.	Note=WD 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	147	189	.	.	.	Note=WD 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	190	235	.	.	.	Note=WD 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	236	280	.	.	.	Note=WD 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	281	325	.	.	.	Note=WD 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	326	363	.	.	.	Note=WD 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	364	399	.	.	.	Note=WD 9;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	400	433	.	.	.	Note=WD 10;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	434	473	.	.	.	Note=WD 11;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	474	516	.	.	.	Note=WD 12;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	517	569	.	.	.	Note=WD 13;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Repeat	570	611	.	.	.	Note=WD 14;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914	
+P46680	UniProtKB	Compositional bias	363	366	.	.	.	Note=Poly-Ser	
+P46680	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P46680	UniProtKB	Beta strand	4	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	40	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	55	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	67	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	80	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	88	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	99	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	103	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	119	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	128	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	141	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	152	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	163	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	170	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	175	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	184	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	193	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	209	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	221	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	231	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	241	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	256	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	274	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	281	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	285	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Helix	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	301	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	311	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	321	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	328	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	342	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	347	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	351	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	359	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	362	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	366	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	375	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	387	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	391	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	394	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	400	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	409	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	416	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	427	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	434	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	439	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	449	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	456	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	464	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	469	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	476	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	491	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	500	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	512	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Turn	517	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	521	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	534	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	555	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	565	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	577	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	587	594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	597	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+P46680	UniProtKB	Beta strand	607	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU	
+##sequence-region P52893 1 592
+P52893	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P52893	UniProtKB	Modified residue	412	412	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P47019 1 175
+P47019	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000203041;Note=Ribosome biogenesis protein ALB1	
+##sequence-region P40047 1 520
+P40047	UniProtKB	Transit peptide	1	23	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40047	UniProtKB	Chain	24	520	.	.	.	ID=PRO_0000007166;Note=Aldehyde dehydrogenase 5%2C mitochondrial	
+P40047	UniProtKB	Nucleotide binding	266	271	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40047	UniProtKB	Active site	288	288	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P40047	UniProtKB	Active site	322	322	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P40047	UniProtKB	Site	190	190	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40047	UniProtKB	Sequence conflict	48	48	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40047	UniProtKB	Sequence conflict	90	90	.	.	.	Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40047	UniProtKB	Sequence conflict	93	104	.	.	.	Note=AFETKWSIVEPE->LLKRSVYCRAG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40047	UniProtKB	Sequence conflict	411	411	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53178 1 202
+P53178	UniProtKB	Chain	1	202	.	.	.	ID=PRO_0000215605;Note=UDP-N-acetylglucosamine transferase subunit ALG13	
+P53178	UniProtKB	Beta strand	9	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Beta strand	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KS6	
+P53178	UniProtKB	Helix	20	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Helix	29	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Turn	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Beta strand	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Helix	58	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Beta strand	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KS6	
+P53178	UniProtKB	Turn	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KS6	
+P53178	UniProtKB	Beta strand	83	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Turn	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Beta strand	91	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Beta strand	99	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Helix	103	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Beta strand	114	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Helix	120	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Beta strand	133	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KS6	
+P53178	UniProtKB	Helix	145	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Beta strand	157	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KS6	
+P53178	UniProtKB	Turn	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Helix	169	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Beta strand	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+P53178	UniProtKB	Helix	192	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC	
+##sequence-region P38179 1 458
+P38179	UniProtKB	Chain	1	458	.	.	.	ID=PRO_0000080565;Note=Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1%2C3-mannosyltransferase	
+P38179	UniProtKB	Topological domain	1	41	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Topological domain	63	95	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Transmembrane	96	116	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Topological domain	117	137	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Transmembrane	138	158	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Topological domain	159	171	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Transmembrane	172	192	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Topological domain	193	216	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Topological domain	238	242	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Topological domain	264	302	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Transmembrane	303	323	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Topological domain	324	345	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Transmembrane	346	366	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Topological domain	367	381	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Transmembrane	382	402	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Topological domain	403	415	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Transmembrane	416	436	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Topological domain	437	458	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38179	UniProtKB	Mutagenesis	275	275	.	.	.	Note=In ALG3-1%3B leads to an underglycosylation of secretory proteins. A->V	
+P38179	UniProtKB	Sequence conflict	86	86	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38179	UniProtKB	Sequence conflict	187	198	.	.	.	Note=LGAIVASRCHQR->FRGYRGQQVPSA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38179	UniProtKB	Sequence conflict	266	266	.	.	.	Note=S->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06497 1 328
+Q06497	UniProtKB	Chain	1	328	.	.	.	ID=PRO_0000227603;Note=Peroxisomal adenine nucleotide transporter 1	
+Q06497	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06497	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06497	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06497	UniProtKB	Transmembrane	185	202	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06497	UniProtKB	Transmembrane	226	246	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06497	UniProtKB	Transmembrane	277	297	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06497	UniProtKB	Repeat	1	101	.	.	.	Note=Solcar 1	
+Q06497	UniProtKB	Repeat	122	208	.	.	.	Note=Solcar 2	
+Q06497	UniProtKB	Repeat	220	304	.	.	.	Note=Solcar 3	
+##sequence-region P38856 1 637
+P38856	UniProtKB	Chain	1	637	.	.	.	ID=PRO_0000202930;Note=Clathrin coat assembly protein AP180A	
+P38856	UniProtKB	Domain	1	126	.	.	.	Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243	
+P38856	UniProtKB	Region	587	637	.	.	.	Note=Clathrin-binding	
+P38856	UniProtKB	Compositional bias	560	579	.	.	.	Note=Poly-Gln	
+##sequence-region Q12028 1 832
+Q12028	UniProtKB	Chain	1	832	.	.	.	ID=PRO_0000193764;Note=AP-1 complex subunit gamma-1	
+Q12028	UniProtKB	Domain	733	832	.	.	.	Note=GAE	
+##sequence-region P38065 1 1025
+P38065	UniProtKB	Chain	1	1025	.	.	.	ID=PRO_0000193737;Note=AP-2 complex subunit alpha	
+P38065	UniProtKB	Modified residue	727	727	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38065	UniProtKB	Modified residue	733	733	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53886 1 1748
+P53886	UniProtKB	Chain	1	1748	.	.	.	ID=PRO_0000215875;Note=Anaphase-promoting complex subunit 1	
+P53886	UniProtKB	Compositional bias	353	357	.	.	.	Note=Poly-Gln	
+P53886	UniProtKB	Modified residue	1462	1462	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53886	UniProtKB	Sequence conflict	1547	1547	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12440 1 853
+Q12440	UniProtKB	Chain	1	853	.	.	.	ID=PRO_0000119814;Note=Anaphase-promoting complex subunit 2	
+Q12440	UniProtKB	Helix	775	792	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD	
+Q12440	UniProtKB	Beta strand	794	796	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD	
+Q12440	UniProtKB	Helix	797	807	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD	
+Q12440	UniProtKB	Helix	810	812	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD	
+Q12440	UniProtKB	Helix	819	831	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD	
+Q12440	UniProtKB	Beta strand	834	836	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD	
+Q12440	UniProtKB	Turn	839	841	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD	
+Q12440	UniProtKB	Beta strand	842	845	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD	
+##sequence-region Q12449 1 350
+Q12449	UniProtKB	Chain	1	350	.	.	.	ID=PRO_0000215822;Note=Hsp90 co-chaperone AHA1	
+Q12449	UniProtKB	Mutagenesis	53	53	.	.	.	Note=No effect on Hsp90 ATPase activity but reduces Hsp90 binding affinity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935	
+Q12449	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Decreases activation of Hsp90 ATPase activity and substantially reduces Hsp90 binding affinity. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935	
+Q12449	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Decreases activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935	
+Q12449	UniProtKB	Mutagenesis	60	60	.	.	.	Note=Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935	
+Q12449	UniProtKB	Mutagenesis	62	62	.	.	.	Note=Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935	
+Q12449	UniProtKB	Sequence conflict	28	28	.	.	.	Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12449	UniProtKB	Helix	17	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+Q12449	UniProtKB	Beta strand	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USV	
+Q12449	UniProtKB	Beta strand	41	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+Q12449	UniProtKB	Beta strand	49	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+Q12449	UniProtKB	Beta strand	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USV	
+Q12449	UniProtKB	Beta strand	68	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+Q12449	UniProtKB	Beta strand	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USV	
+Q12449	UniProtKB	Beta strand	88	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+Q12449	UniProtKB	Helix	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+Q12449	UniProtKB	Beta strand	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+Q12449	UniProtKB	Helix	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+Q12449	UniProtKB	Helix	132	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU	
+##sequence-region Q9ZZX0 1 354
+Q9ZZX0	UniProtKB	Chain	1	354	.	.	.	ID=PRO_0000270561;Note=Intron-encoded DNA endonuclease aI5 beta	
+##sequence-region P47015 1 356
+P47015	UniProtKB	Transit peptide	1	32	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47015	UniProtKB	Chain	33	356	.	.	.	ID=PRO_0000203039;Note=Altered inheritance of mitochondria protein 23%2C mitochondrial	
+##sequence-region P36154 1 155
+P36154	UniProtKB	Chain	1	155	.	.	.	ID=PRO_0000203221;Note=Altered inheritance rate of mitochondria protein 29	
+P36154	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36154	UniProtKB	Sequence conflict	153	153	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08223 1 395
+Q08223	UniProtKB	Transmembrane	156	176	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07716 1 390
+Q07716	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07716	UniProtKB	Chain	27	390	.	.	.	ID=PRO_0000242484;Note=Altered inheritance of mitochondria protein 6	
+Q07716	UniProtKB	Sequence conflict	44	44	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47771 1 506
+P47771	UniProtKB	Chain	1	506	.	.	.	ID=PRO_0000056439;Note=Aldehyde dehydrogenase [NAD(P)+] 1	
+P47771	UniProtKB	Active site	268	268	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P47771	UniProtKB	Active site	302	302	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P47771	UniProtKB	Site	169	169	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47771	UniProtKB	Sequence conflict	23	23	.	.	.	Note=L->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47771	UniProtKB	Sequence conflict	462	462	.	.	.	Note=S->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47771	UniProtKB	Sequence conflict	486	488	.	.	.	Note=QSG->DNV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47771	UniProtKB	Sequence conflict	497	497	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47771	UniProtKB	Sequence conflict	500	501	.	.	.	Note=IN->MD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P54114 1 506
+P54114	UniProtKB	Chain	1	506	.	.	.	ID=PRO_0000056440;Note=Aldehyde dehydrogenase [NAD(P)+] 2	
+P54114	UniProtKB	Active site	268	268	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P54114	UniProtKB	Active site	302	302	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P54114	UniProtKB	Site	169	169	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P46367 1 519
+P46367	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1989592,ECO:0000269|PubMed:9150920;Dbxref=PMID:1989592,PMID:9150920	
+P46367	UniProtKB	Chain	25	519	.	.	.	ID=PRO_0000007165;Note=Potassium-activated aldehyde dehydrogenase%2C mitochondrial	
+P46367	UniProtKB	Nucleotide binding	268	273	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46367	UniProtKB	Active site	290	290	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P46367	UniProtKB	Active site	324	324	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P46367	UniProtKB	Site	192	192	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46367	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46367	UniProtKB	Modified residue	216	216	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P46367	UniProtKB	Modified residue	500	500	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:19779198	
+P46367	UniProtKB	Sequence conflict	51	51	.	.	.	Note=N->NN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46367	UniProtKB	Sequence conflict	63	63	.	.	.	Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38242 1 237
+P38242	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000123818;Note=UDP-N-acetylglucosamine transferase subunit ALG14	
+P38242	UniProtKB	Topological domain	1	7	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17686769;Dbxref=PMID:17686769	
+P38242	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38242	UniProtKB	Topological domain	29	237	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17686769;Dbxref=PMID:17686769	
+##sequence-region P40350 1 334
+P40350	UniProtKB	Chain	1	334	.	.	.	ID=PRO_0000059097;Note=Dolichyl-phosphate beta-glucosyltransferase	
+P40350	UniProtKB	Topological domain	1	12	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40350	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40350	UniProtKB	Topological domain	34	334	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40350	UniProtKB	Glycosylation	83	83	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40350	UniProtKB	Glycosylation	119	119	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40351 1 577
+P40351	UniProtKB	Chain	1	577	.	.	.	ID=PRO_0000174168;Note=Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1%2C3-glucosyltransferase	
+P40351	UniProtKB	Topological domain	1	42	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	64	92	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	114	139	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	161	168	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	169	189	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	190	219	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	220	240	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	241	266	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	288	307	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	308	328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	329	382	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	383	403	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	404	419	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	420	440	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	441	447	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	448	468	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	469	470	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	471	491	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	492	504	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	505	525	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	526	543	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Transmembrane	544	564	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40351	UniProtKB	Topological domain	565	577	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43633 1 760
+P43633	UniProtKB	Chain	1	760	.	.	.	ID=PRO_0000064557;Note=Serine/threonine-protein kinase Haspin homolog ALK1	
+P43633	UniProtKB	Domain	468	760	.	.	.	Note=Protein kinase	
+P43633	UniProtKB	Nucleotide binding	474	482	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43633	UniProtKB	Motif	200	202	.	.	.	Note=KEN box	
+P43633	UniProtKB	Motif	224	232	.	.	.	Note=D box	
+P43633	UniProtKB	Compositional bias	94	449	.	.	.	Note=Ser-rich	
+P43633	UniProtKB	Compositional bias	240	245	.	.	.	Note=Poly-Gln	
+P43633	UniProtKB	Compositional bias	264	269	.	.	.	Note=Poly-Ser	
+P43633	UniProtKB	Compositional bias	351	356	.	.	.	Note=Poly-Ser	
+P43633	UniProtKB	Binding site	510	510	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43633	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43633	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43633	UniProtKB	Mutagenesis	606	610	.	.	.	Note=Reduces strongly kinase activity. EHRNL->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16855400;Dbxref=PMID:16855400	
+P43633	UniProtKB	Sequence conflict	758	760	.	.	.	Note=LYK->AL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32459 1 195
+P32459	UniProtKB	Chain	1	195	.	.	.	ID=PRO_0000120562;Note=Ureidoglycolate lyase	
+##sequence-region Q08269 1 859
+Q08269	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08269	UniProtKB	Chain	2	859	.	.	.	ID=PRO_0000201535;Note=Magnesium transporter ALR1	
+Q08269	UniProtKB	Transmembrane	744	764	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08269	UniProtKB	Transmembrane	773	793	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08269	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08269	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08269	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08269	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08269	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08269	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08269	UniProtKB	Modified residue	221	221	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08269	UniProtKB	Modified residue	236	236	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08269	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08269	UniProtKB	Modified residue	850	850	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08269	UniProtKB	Sequence conflict	13	13	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P14904 1 514
+P14904	UniProtKB	Propeptide	1	45	.	.	.	ID=PRO_0000026806;Note=Required for vacuolar localization. Mediates aggregation and vesicle formation in Cvt pathway;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2651436,ECO:0000269|PubMed:8521804,ECO:0000269|PubMed:8601598;Dbxref=PMID:2651436,PMID:8521804,PMID:8601598	
+P14904	UniProtKB	Chain	46	514	.	.	.	ID=PRO_0000026807;Note=Vacuolar aminopeptidase 1	
+P14904	UniProtKB	Metal binding	132	132	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0	
+P14904	UniProtKB	Metal binding	303	303	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0	
+P14904	UniProtKB	Metal binding	303	303	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0	
+P14904	UniProtKB	Metal binding	340	340	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0	
+P14904	UniProtKB	Metal binding	385	385	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0	
+P14904	UniProtKB	Metal binding	479	479	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0	
+P14904	UniProtKB	Binding site	210	210	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0	
+P14904	UniProtKB	Binding site	339	339	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0	
+P14904	UniProtKB	Binding site	385	385	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0	
+P14904	UniProtKB	Binding site	388	388	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0	
+P14904	UniProtKB	Site	45	46	.	.	.	Note=Cleavage%3B by protease B (PrB/PRB1);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1400574;Dbxref=PMID:1400574	
+P14904	UniProtKB	Modified residue	356	356	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14904	UniProtKB	Glycosylation	107	107	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P14904	UniProtKB	Glycosylation	110	110	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P14904	UniProtKB	Glycosylation	448	448	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P14904	UniProtKB	Sequence conflict	233	233	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14904	UniProtKB	Sequence conflict	323	323	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14904	UniProtKB	Sequence conflict	328	328	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14904	UniProtKB	Sequence conflict	369	369	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14904	UniProtKB	Helix	1	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGE	
+P14904	UniProtKB	Helix	34	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH9	
+P14904	UniProtKB	Beta strand	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH9	
+P14904	UniProtKB	Helix	48	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	66	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Turn	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Turn	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	110	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	127	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	136	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	157	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	173	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	190	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Turn	221	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Turn	250	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R8F	
+P14904	UniProtKB	Helix	257	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	271	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	274	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	296	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	302	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Turn	324	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	330	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	339	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	349	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	353	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	372	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	380	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	395	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	411	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	418	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	424	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	442	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	457	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	467	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	474	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Beta strand	480	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	489	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF	
+P14904	UniProtKB	Helix	509	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH9	
+##sequence-region P47064 1 194
+P47064	UniProtKB	Chain	1	194	.	.	.	ID=PRO_0000193822;Note=AP-3 complex subunit sigma	
+##sequence-region P60010 1 375
+P60010	UniProtKB	Chain	1	375	.	.	.	ID=PRO_0000089051;Note=Actin	
+P60010	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1885608;Dbxref=PMID:22814378,PMID:1885608	
+P60010	UniProtKB	Cross-link	191	191	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P60010	UniProtKB	Natural variant	143	143	.	.	.	Note=In strain: CBS 1907. Y->F	
+P60010	UniProtKB	Sequence conflict	178	178	.	.	.	Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P60010	UniProtKB	Sequence conflict	308	308	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P60010	UniProtKB	Beta strand	8	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	14	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	28	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	35	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Turn	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YVN	
+P60010	UniProtKB	Helix	56	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YVN	
+P60010	UniProtKB	Beta strand	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YVN	
+P60010	UniProtKB	Helix	79	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Turn	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	103	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	113	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	130	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	137	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	148	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	160	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	176	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	182	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Turn	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	203	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	223	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Turn	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	238	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	247	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	253	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	258	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	264	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	274	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	287	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	297	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	302	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	309	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Turn	333	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	338	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	350	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Beta strand	356	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	359	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	367	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+P60010	UniProtKB	Helix	370	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG	
+##sequence-region P25371 1 1049
+P25371	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Chain	26	1049	.	.	.	ID=PRO_0000000257;Note=Probable ATP-dependent permease	
+P25371	UniProtKB	Topological domain	26	324	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Transmembrane	325	345	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Topological domain	346	463	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Transmembrane	464	481	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Topological domain	482	793	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Transmembrane	794	814	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Topological domain	815	828	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Transmembrane	829	849	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Topological domain	850	877	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Transmembrane	878	898	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Topological domain	899	909	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Transmembrane	910	930	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Topological domain	931	937	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Transmembrane	938	958	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Topological domain	959	1000	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Transmembrane	1001	1021	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Topological domain	1022	1024	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Transmembrane	1025	1045	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Topological domain	1046	1049	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Domain	384	631	.	.	.	Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P25371	UniProtKB	Domain	793	1044	.	.	.	Note=ABC transmembrane type-2	
+P25371	UniProtKB	Nucleotide binding	423	430	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P25371	UniProtKB	Modified residue	659	659	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25371	UniProtKB	Modified residue	702	702	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25371	UniProtKB	Glycosylation	50	50	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Glycosylation	114	114	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Glycosylation	165	165	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Glycosylation	221	221	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Glycosylation	935	935	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25371	UniProtKB	Sequence conflict	29	29	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25613 1 283
+P25613	UniProtKB	Chain	1	283	.	.	.	ID=PRO_0000135706;Note=Accumulation of dyads protein 2	
+P25613	UniProtKB	Topological domain	1	89	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Topological domain	111	120	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Topological domain	142	151	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Transmembrane	152	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Topological domain	173	185	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Transmembrane	186	206	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Topological domain	207	208	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Topological domain	230	240	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25613	UniProtKB	Topological domain	262	283	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P33304 1 620
+P33304	UniProtKB	Chain	1	620	.	.	.	ID=PRO_0000064485;Note=Protein AFR1	
+P33304	UniProtKB	Modified residue	472	472	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P33304	UniProtKB	Modified residue	526	526	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P22149 1 690
+P22149	UniProtKB	Chain	1	690	.	.	.	ID=PRO_0000064487;Note=Iron-regulated transcriptional activator AFT1	
+P22149	UniProtKB	Natural variant	291	291	.	.	.	Note=In allele AFT1-1UP%3B which is constitutively activated. C->F	
+P22149	UniProtKB	Sequence conflict	8	8	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	71	71	.	.	.	Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	136	136	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	236	236	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	329	329	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	378	378	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	416	416	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	416	416	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	468	468	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	507	507	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	507	507	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	538	538	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	538	538	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	568	568	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	568	568	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	579	579	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	579	579	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	644	644	.	.	.	Note=H->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	644	644	.	.	.	Note=H->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	649	649	.	.	.	Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22149	UniProtKB	Sequence conflict	649	649	.	.	.	Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P87275 1 137
+P87275	UniProtKB	Chain	1	137	.	.	.	ID=PRO_0000202641;Note=Altered inheritance of mitochondria protein 11	
+P87275	UniProtKB	Transmembrane	20	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87275	UniProtKB	Transmembrane	66	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53109 1 570
+P53109	UniProtKB	Chain	1	570	.	.	.	ID=PRO_0000202731;Note=Probable metalloreductase AIM14	
+P53109	UniProtKB	Topological domain	1	20	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53109	UniProtKB	Transmembrane	21	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53109	UniProtKB	Topological domain	42	69	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53109	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53109	UniProtKB	Topological domain	91	141	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53109	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53109	UniProtKB	Topological domain	163	176	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53109	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53109	UniProtKB	Topological domain	198	373	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53109	UniProtKB	Transmembrane	374	394	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53109	UniProtKB	Topological domain	395	570	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53109	UniProtKB	Domain	101	219	.	.	.	Note=Ferric oxidoreductase	
+P53109	UniProtKB	Domain	250	388	.	.	.	Note=FAD-binding FR-type	
+##sequence-region P47140 1 327
+P47140	UniProtKB	Chain	1	327	.	.	.	ID=PRO_0000203109;Note=Altered inheritance rate of mitochondria protein 25	
+##sequence-region P39721 1 246
+P39721	UniProtKB	Chain	1	246	.	.	.	ID=PRO_0000202423;Note=Protein AIM2	
+##sequence-region Q04689 1 311
+Q04689	UniProtKB	Chain	1	311	.	.	.	ID=PRO_0000203255;Note=Altered inheritance of mitochondria protein 32	
+##sequence-region P53730 1 551
+P53730	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000215786;Note=Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1%2C6-mannosyltransferase	
+P53730	UniProtKB	Topological domain	1	2	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	24	61	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	83	89	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	111	136	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	137	157	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	158	178	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	200	202	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	203	223	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	224	227	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	228	248	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	249	275	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	276	296	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	297	303	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	304	324	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	325	331	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	332	352	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	353	365	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	366	386	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	387	417	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Transmembrane	418	438	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53730	UniProtKB	Topological domain	439	551	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43636 1 503
+P43636	UniProtKB	Chain	1	503	.	.	.	ID=PRO_0000080271;Note=Alpha-1%2C3/1%2C6-mannosyltransferase ALG2	
+P43636	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43636	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43636	UniProtKB	Transmembrane	443	463	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43636	UniProtKB	Glycosylation	170	170	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43636	UniProtKB	Glycosylation	303	303	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43636	UniProtKB	Glycosylation	371	371	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43636	UniProtKB	Glycosylation	400	400	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43636	UniProtKB	Mutagenesis	335	335	.	.	.	Note=Severly affects activity%2C especially the second mannosylation step. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16878994;Dbxref=PMID:16878994	
+P43636	UniProtKB	Mutagenesis	343	343	.	.	.	Note=No activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16878994;Dbxref=PMID:16878994	
+P43636	UniProtKB	Sequence conflict	8	8	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43636	UniProtKB	Sequence conflict	237	238	.	.	.	Note=KA->NG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43636	UniProtKB	Sequence conflict	302	302	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43636	UniProtKB	Sequence conflict	457	457	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43636	UniProtKB	Sequence conflict	470	503	.	.	.	Note=FLFMATFMVLYFKNYLWGIYWAFVFALSYPYEEI->SYLWPLLWYYILRTTYGEFTGHLYSLSPTLMKKYNVYLNKQCIPPEEKIIYIGEEISKCK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32789 1 676
+P32789	UniProtKB	Chain	1	676	.	.	.	ID=PRO_0000202464;Note=Serine/threonine-protein kinase Haspin homolog ALK2	
+P32789	UniProtKB	Domain	383	672	.	.	.	Note=Protein kinase	
+P32789	UniProtKB	Nucleotide binding	389	397	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32789	UniProtKB	Motif	116	118	.	.	.	Note=KEN box	
+P32789	UniProtKB	Motif	150	158	.	.	.	Note=D box	
+P32789	UniProtKB	Compositional bias	29	309	.	.	.	Note=Ser-rich	
+P32789	UniProtKB	Binding site	430	430	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32789	UniProtKB	Mutagenesis	528	532	.	.	.	Note=Reduces strongly kinase activity. EHRNL->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16855400;Dbxref=PMID:16855400	
+##sequence-region P43553 1 858
+P43553	UniProtKB	Chain	1	858	.	.	.	ID=PRO_0000201536;Note=Magnesium transporter ALR2	
+P43553	UniProtKB	Topological domain	1	741	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43553	UniProtKB	Transmembrane	742	762	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43553	UniProtKB	Topological domain	763	771	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43553	UniProtKB	Transmembrane	772	792	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43553	UniProtKB	Topological domain	793	858	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47029 1 1046
+P47029	UniProtKB	Chain	1	1046	.	.	.	ID=PRO_0000203049;Note=Arrestin-related trafficking adapter 3	
+P47029	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47029	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P47029	UniProtKB	Modified residue	213	213	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P47029	UniProtKB	Modified residue	586	586	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47029	UniProtKB	Modified residue	826	826	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47029	UniProtKB	Modified residue	838	838	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47029	UniProtKB	Modified residue	900	900	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47029	UniProtKB	Modified residue	1022	1022	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47029	UniProtKB	Modified residue	1023	1023	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47029	UniProtKB	Sequence conflict	852	852	.	.	.	Note=P->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P50082 1 593
+P50082	UniProtKB	Chain	1	593	.	.	.	ID=PRO_0000050842;Note=Meiosis-specific APC/C activator protein AMA1	
+P50082	UniProtKB	Repeat	226	264	.	.	.	Note=WD 1	
+P50082	UniProtKB	Repeat	271	310	.	.	.	Note=WD 2	
+P50082	UniProtKB	Repeat	323	364	.	.	.	Note=WD 3	
+P50082	UniProtKB	Repeat	388	427	.	.	.	Note=WD 4	
+P50082	UniProtKB	Repeat	432	474	.	.	.	Note=WD 5	
+P50082	UniProtKB	Repeat	525	564	.	.	.	Note=WD 6	
+P50082	UniProtKB	Motif	29	35	.	.	.	Note=C-box;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50082	UniProtKB	Compositional bias	94	100	.	.	.	Note=Poly-Ser	
+##sequence-region P38285 1 549
+P38285	UniProtKB	Chain	1	549	.	.	.	ID=PRO_0000202500;Note=Antagonist of mitotic exit network protein 1	
+##sequence-region P40502 1 157
+P40502	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40502	UniProtKB	Chain	2	157	.	.	.	ID=PRO_0000202977;Note=Altered inheritance of mitochondria protein 19%2C mitochondrial	
+P40502	UniProtKB	Transmembrane	31	48	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40502	UniProtKB	Transmembrane	80	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40502	UniProtKB	Transmembrane	103	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40502	UniProtKB	Transmembrane	131	147	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40502	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P40563 1 679
+P40563	UniProtKB	Chain	1	679	.	.	.	ID=PRO_0000203003;Note=Altered inheritance of mitochondria protein 21	
+P40563	UniProtKB	Region	383	396	.	.	.	Note=Interaction with SH3 domain of ABP1	
+P40563	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40563	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40563	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40563	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40563	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40563	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40563	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40563	UniProtKB	Modified residue	206	206	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40563	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40563	UniProtKB	Modified residue	277	277	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40563	UniProtKB	Modified residue	284	284	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40563	UniProtKB	Modified residue	324	324	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40563	UniProtKB	Modified residue	552	552	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40563	UniProtKB	Modified residue	576	576	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40563	UniProtKB	Modified residue	620	620	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40563	UniProtKB	Modified residue	623	623	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40563	UniProtKB	Modified residue	625	625	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40563	UniProtKB	Modified residue	627	627	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40563	UniProtKB	Modified residue	667	667	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40563	UniProtKB	Modified residue	671	671	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40563	UniProtKB	Modified residue	675	675	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40563	UniProtKB	Modified residue	678	678	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P40053 1 627
+P40053	UniProtKB	Transit peptide	1	43	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40053	UniProtKB	Chain	44	627	.	.	.	ID=PRO_0000202637;Note=Altered inheritance of mitochondria protein 9%2C mitochondrial	
+##sequence-region P25335 1 343
+P25335	UniProtKB	Chain	1	343	.	.	.	ID=PRO_0000205914;Note=Allantoicase	
+P25335	UniProtKB	Sequence conflict	93	93	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25335	UniProtKB	Sequence conflict	134	135	.	.	.	Note=WV->SL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25335	UniProtKB	Beta strand	2	4	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Helix	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Helix	9	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Turn	17	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Helix	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	33	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Helix	45	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	82	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	93	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	106	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	111	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	135	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	148	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	162	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	174	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Helix	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	206	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Helix	218	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Helix	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	246	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	257	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	275	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	297	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	311	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	323	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+P25335	UniProtKB	Beta strand	337	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59	
+##sequence-region Q00776 1 475
+Q00776	UniProtKB	Chain	1	475	.	.	.	ID=PRO_0000193778;Note=AP-1 complex subunit mu-1-I	
+Q00776	UniProtKB	Domain	175	473	.	.	.	Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404	
+Q00776	UniProtKB	Sequence conflict	214	214	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00776	UniProtKB	Sequence conflict	216	216	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00776	UniProtKB	Sequence conflict	222	222	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00776	UniProtKB	Sequence conflict	433	433	.	.	.	Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00776	UniProtKB	Sequence conflict	440	440	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00776	UniProtKB	Sequence conflict	450	450	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35181 1 156
+P35181	UniProtKB	Chain	1	156	.	.	.	ID=PRO_0000193803;Note=AP-1 complex subunit sigma-1	
+##sequence-region P16550 1 321
+P16550	UniProtKB	Chain	1	321	.	.	.	ID=PRO_0000064611;Note=Protein APA1	
+P16550	UniProtKB	Region	93	94	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108	
+P16550	UniProtKB	Region	151	154	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108	
+P16550	UniProtKB	Region	273	275	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108	
+P16550	UniProtKB	Active site	158	158	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108	
+P16550	UniProtKB	Binding site	54	54	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108	
+P16550	UniProtKB	Binding site	145	145	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108	
+P16550	UniProtKB	Binding site	160	160	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108	
+P16550	UniProtKB	Binding site	280	280	.	.	.	Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108	
+P16550	UniProtKB	Binding site	284	284	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108	
+P16550	UniProtKB	Site	160	160	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108	
+P16550	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P16550	UniProtKB	Sequence conflict	100	100	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38281 1 316
+P38281	UniProtKB	Chain	1	316	.	.	.	ID=PRO_0000202497;Note=Actin patches distal protein 1	
+##sequence-region P40532 1 138
+P40532	UniProtKB	Chain	1	138	.	.	.	ID=PRO_0000202992;Note=Nuclear membrane organization protein APQ12	
+P40532	UniProtKB	Topological domain	1	39	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40532	UniProtKB	Transmembrane	40	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40532	UniProtKB	Topological domain	59	67	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40532	UniProtKB	Transmembrane	68	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40532	UniProtKB	Topological domain	85	138	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53909 1 347
+P53909	UniProtKB	Chain	1	347	.	.	.	ID=PRO_0000194360;Note=Adenine deaminase	
+P53909	UniProtKB	Active site	207	207	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145	
+P53909	UniProtKB	Metal binding	16	16	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145	
+P53909	UniProtKB	Metal binding	18	18	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145	
+P53909	UniProtKB	Metal binding	204	204	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145	
+P53909	UniProtKB	Metal binding	285	285	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145	
+P53909	UniProtKB	Binding site	286	286	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145	
+P53909	UniProtKB	Site	228	228	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145	
+P53909	UniProtKB	Mutagenesis	69	69	.	.	.	Note=In aah1-2%3B impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+P53909	UniProtKB	Mutagenesis	72	72	.	.	.	Note=In aah1-3%3B impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+P53909	UniProtKB	Mutagenesis	219	219	.	.	.	Note=In aah1-4%3B impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+P53909	UniProtKB	Mutagenesis	237	237	.	.	.	Note=In aah1-6%3B impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+P53909	UniProtKB	Mutagenesis	329	329	.	.	.	Note=In aah1-7%3B impairs AAH1 degradation during postdiauxic growth. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+##sequence-region Q2V2Q1 1 113
+Q2V2Q1	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000248450;Note=Antisense of depressing factor protein 1	
+##sequence-region P00330 1 348
+P00330	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:320000;Dbxref=PMID:320000	
+P00330	UniProtKB	Chain	2	348	.	.	.	ID=PRO_0000160730;Note=Alcohol dehydrogenase 1	
+P00330	UniProtKB	Nucleotide binding	178	184	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00330	UniProtKB	Nucleotide binding	269	271	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00330	UniProtKB	Metal binding	44	44	.	.	.	Note=Zinc 1%3B catalytic	
+P00330	UniProtKB	Metal binding	67	67	.	.	.	Note=Zinc 1%3B catalytic	
+P00330	UniProtKB	Metal binding	98	98	.	.	.	Note=Zinc 2	
+P00330	UniProtKB	Metal binding	101	101	.	.	.	Note=Zinc 2	
+P00330	UniProtKB	Metal binding	104	104	.	.	.	Note=Zinc 2	
+P00330	UniProtKB	Metal binding	112	112	.	.	.	Note=Zinc 2	
+P00330	UniProtKB	Metal binding	154	154	.	.	.	Note=Zinc 1%3B catalytic	
+P00330	UniProtKB	Binding site	202	202	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00330	UniProtKB	Binding site	207	207	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00330	UniProtKB	Binding site	341	341	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00330	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:320000;Dbxref=PMID:320000	
+P00330	UniProtKB	Modified residue	213	213	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00330	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00330	UniProtKB	Modified residue	279	279	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00330	UniProtKB	Modified residue	316	316	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+P00330	UniProtKB	Cross-link	226	226	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00330	UniProtKB	Cross-link	234	234	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00330	UniProtKB	Cross-link	287	287	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00330	UniProtKB	Cross-link	319	319	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00330	UniProtKB	Natural variant	236	236	.	.	.	Note=T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:320000;Dbxref=PMID:320000	
+P00330	UniProtKB	Sequence conflict	21	21	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00330	UniProtKB	Sequence conflict	21	21	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00330	UniProtKB	Sequence conflict	59	59	.	.	.	Note=V->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00330	UniProtKB	Sequence conflict	148	148	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00330	UniProtKB	Sequence conflict	152	152	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00330	UniProtKB	Sequence conflict	237	237	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00330	UniProtKB	Sequence conflict	314	314	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00330	UniProtKB	Sequence conflict	338	338	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00330	UniProtKB	Beta strand	5	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	20	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	33	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	45	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	68	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	88	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	102	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Turn	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	125	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Turn	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	137	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	155	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	173	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Turn	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	184	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	197	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	207	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Turn	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	228	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	240	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	250	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	260	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	276	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	281	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	290	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	299	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	318	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	323	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Helix	326	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+P00330	UniProtKB	Beta strand	339	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z	
+##sequence-region P00331 1 348
+P00331	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P00331	UniProtKB	Chain	2	348	.	.	.	ID=PRO_0000160731;Note=Alcohol dehydrogenase 2	
+P00331	UniProtKB	Nucleotide binding	178	184	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00331	UniProtKB	Nucleotide binding	269	271	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00331	UniProtKB	Metal binding	44	44	.	.	.	Note=Zinc 1%3B catalytic	
+P00331	UniProtKB	Metal binding	67	67	.	.	.	Note=Zinc 1%3B catalytic	
+P00331	UniProtKB	Metal binding	98	98	.	.	.	Note=Zinc 2	
+P00331	UniProtKB	Metal binding	101	101	.	.	.	Note=Zinc 2	
+P00331	UniProtKB	Metal binding	104	104	.	.	.	Note=Zinc 2	
+P00331	UniProtKB	Metal binding	112	112	.	.	.	Note=Zinc 2	
+P00331	UniProtKB	Metal binding	154	154	.	.	.	Note=Zinc 1%3B catalytic	
+P00331	UniProtKB	Binding site	202	202	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00331	UniProtKB	Binding site	207	207	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00331	UniProtKB	Binding site	341	341	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00331	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P00331	UniProtKB	Modified residue	213	213	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P00331	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P00331	UniProtKB	Modified residue	279	279	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P00331	UniProtKB	Modified residue	316	316	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P00331	UniProtKB	Cross-link	226	226	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P00331	UniProtKB	Cross-link	234	234	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P00331	UniProtKB	Cross-link	287	287	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P00331	UniProtKB	Cross-link	319	319	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P00331	UniProtKB	Sequence conflict	16	16	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00331	UniProtKB	Sequence conflict	31	31	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00331	UniProtKB	Sequence conflict	233	233	.	.	.	Note=V->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P10127 1 382
+P10127	UniProtKB	Chain	1	382	.	.	.	ID=PRO_0000087817;Note=Alcohol dehydrogenase 4	
+P10127	UniProtKB	Sequence conflict	60	60	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10127	UniProtKB	Sequence conflict	88	88	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10127	UniProtKB	Sequence conflict	310	310	.	.	.	Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10127	UniProtKB	Sequence conflict	339	339	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10127	UniProtKB	Sequence conflict	348	348	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04894 1 360
+Q04894	UniProtKB	Chain	1	360	.	.	.	ID=PRO_0000160734;Note=NADP-dependent alcohol dehydrogenase 6	
+Q04894	UniProtKB	Nucleotide binding	187	192	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04894	UniProtKB	Nucleotide binding	275	277	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04894	UniProtKB	Metal binding	46	46	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04894	UniProtKB	Metal binding	68	68	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04894	UniProtKB	Metal binding	100	100	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04894	UniProtKB	Metal binding	103	103	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04894	UniProtKB	Metal binding	106	106	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04894	UniProtKB	Metal binding	114	114	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04894	UniProtKB	Metal binding	163	163	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04894	UniProtKB	Binding site	215	215	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04894	UniProtKB	Binding site	348	348	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04894	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04894	UniProtKB	Modified residue	315	315	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25377	
+Q04894	UniProtKB	Modified residue	359	359	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q04894	UniProtKB	Turn	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	7	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	22	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	35	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	47	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Turn	54	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	70	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	90	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1N	
+Q04894	UniProtKB	Helix	104	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	118	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	134	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	155	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	159	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	164	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	182	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	190	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	205	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	216	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	225	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	236	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	244	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PS0	
+Q04894	UniProtKB	Turn	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	266	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	284	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	288	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	295	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	304	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	323	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	330	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Beta strand	346	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+Q04894	UniProtKB	Helix	355	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW	
+##sequence-region P47143 1 340
+P47143	UniProtKB	Chain	1	340	.	.	.	ID=PRO_0000080062;Note=Adenosine kinase	
+P47143	UniProtKB	Active site	293	293	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q01976 1 231
+Q01976	UniProtKB	Chain	1	231	.	.	.	ID=PRO_0000057050;Note=ADP-ribose pyrophosphatase	
+Q01976	UniProtKB	Domain	75	214	.	.	.	Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794	
+Q01976	UniProtKB	Region	64	65	.	.	.	Note=Substrate binding%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Motif	116	137	.	.	.	Note=Nudix box	
+Q01976	UniProtKB	Metal binding	115	115	.	.	.	Note=Magnesium 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Metal binding	131	131	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Metal binding	131	131	.	.	.	Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Metal binding	135	135	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Metal binding	135	135	.	.	.	Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Metal binding	185	185	.	.	.	Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Binding site	46	46	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Binding site	69	69	.	.	.	Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Binding site	103	103	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Binding site	117	117	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Binding site	152	152	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q01976	UniProtKB	Alternative sequence	1	19	.	.	.	ID=VSP_058126;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P18239 1 318
+P18239	UniProtKB	Chain	1	318	.	.	.	ID=PRO_0000090594;Note=ADP%2CATP carrier protein 2	
+P18239	UniProtKB	Transmembrane	20	54	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18239	UniProtKB	Transmembrane	91	115	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18239	UniProtKB	Transmembrane	123	157	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18239	UniProtKB	Transmembrane	192	219	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18239	UniProtKB	Transmembrane	224	258	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18239	UniProtKB	Transmembrane	287	312	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18239	UniProtKB	Repeat	21	114	.	.	.	Note=Solcar 1	
+P18239	UniProtKB	Repeat	125	217	.	.	.	Note=Solcar 2	
+P18239	UniProtKB	Repeat	225	311	.	.	.	Note=Solcar 3	
+P18239	UniProtKB	Motif	252	257	.	.	.	Note=Substrate recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18239	UniProtKB	Binding site	96	96	.	.	.	Note=Nucleotide;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18239	UniProtKB	Sequence conflict	58	58	.	.	.	Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18239	UniProtKB	Sequence conflict	65	65	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18239	UniProtKB	Sequence conflict	68	68	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18239	UniProtKB	Sequence conflict	71	71	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18239	UniProtKB	Sequence conflict	79	79	.	.	.	Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18239	UniProtKB	Sequence conflict	83	83	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18239	UniProtKB	Sequence conflict	113	113	.	.	.	Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18239	UniProtKB	Sequence conflict	124	124	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18239	UniProtKB	Helix	25	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	54	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	70	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	84	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	90	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	97	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	123	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	173	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Turn	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	193	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	229	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	246	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Turn	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	268	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	281	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Helix	288	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G	
+P18239	UniProtKB	Beta strand	313	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9H	
+##sequence-region P18238 1 307
+P18238	UniProtKB	Chain	1	307	.	.	.	ID=PRO_0000090595;Note=ADP%2CATP carrier protein 3	
+P18238	UniProtKB	Transmembrane	9	43	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18238	UniProtKB	Transmembrane	80	104	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18238	UniProtKB	Transmembrane	112	146	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18238	UniProtKB	Transmembrane	181	208	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18238	UniProtKB	Transmembrane	213	247	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18238	UniProtKB	Transmembrane	276	301	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18238	UniProtKB	Repeat	10	103	.	.	.	Note=Solcar 1	
+P18238	UniProtKB	Repeat	114	206	.	.	.	Note=Solcar 2	
+P18238	UniProtKB	Repeat	214	300	.	.	.	Note=Solcar 3	
+P18238	UniProtKB	Motif	241	246	.	.	.	Note=Substrate recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18238	UniProtKB	Binding site	85	85	.	.	.	Note=Nucleotide;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18238	UniProtKB	Helix	5	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	31	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	43	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	59	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	79	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Turn	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9J	
+P18238	UniProtKB	Helix	112	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	162	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	175	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Turn	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	182	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	217	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	235	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Turn	247	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	257	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	270	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Helix	277	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q	
+P18238	UniProtKB	Beta strand	302	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9J	
+##sequence-region Q07732 1 790
+Q07732	UniProtKB	Chain	1	790	.	.	.	ID=PRO_0000064461;Note=Accumulates dyads protein 3	
+Q07732	UniProtKB	Coiled coil	241	328	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07732	UniProtKB	Coiled coil	361	430	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07732	UniProtKB	Coiled coil	477	498	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07732	UniProtKB	Coiled coil	540	658	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07732	UniProtKB	Sequence conflict	569	569	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32493 1 518
+P32493	UniProtKB	Transit peptide	1	19	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32493	UniProtKB	Chain	20	518	.	.	.	ID=PRO_0000021791;Note=ATPase expression protein 1%2C mitochondrial	
+P32493	UniProtKB	Sequence conflict	51	51	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	51	51	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	113	113	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	113	113	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	159	159	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	159	159	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	197	197	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	197	197	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	212	212	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	212	212	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	225	225	.	.	.	Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	225	225	.	.	.	Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	240	240	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	240	240	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	295	295	.	.	.	Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	295	295	.	.	.	Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	392	392	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32493	UniProtKB	Sequence conflict	392	392	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P22136 1 580
+P22136	UniProtKB	Transit peptide	1	40	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22136	UniProtKB	Chain	41	580	.	.	.	ID=PRO_0000002536;Note=ATPase expression protein 2%2C mitochondrial	
+P22136	UniProtKB	Mutagenesis	413	413	.	.	.	Note=Suppresses a T-to-C nucleotide transition mutation in the 5' untranslated region of OLI1 mRNA localized 16 nucleotides upstream of the OLI1 reading frame. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101162;Dbxref=PMID:10101162	
+P22136	UniProtKB	Sequence conflict	214	214	.	.	.	Note=G->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22136	UniProtKB	Sequence conflict	481	481	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08957 1 416
+Q08957	UniProtKB	Chain	1	416	.	.	.	ID=PRO_0000227599;Note=Iron-regulated transcriptional activator AFT2	
+Q08957	UniProtKB	Helix	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG	
+Q08957	UniProtKB	Helix	57	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG	
+Q08957	UniProtKB	Helix	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG	
+Q08957	UniProtKB	Beta strand	72	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG	
+Q08957	UniProtKB	Beta strand	81	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG	
+Q08957	UniProtKB	Beta strand	112	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG	
+Q08957	UniProtKB	Turn	119	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG	
+Q08957	UniProtKB	Beta strand	123	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG	
+Q08957	UniProtKB	Helix	139	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG	
+Q08957	UniProtKB	Helix	146	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG	
+Q08957	UniProtKB	Helix	161	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG	
+##sequence-region P43548 1 558
+P43548	UniProtKB	Chain	1	558	.	.	.	ID=PRO_0000054144;Note=General amino acid permease AGP3	
+P43548	UniProtKB	Topological domain	1	57	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	58	78	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	79	81	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	103	126	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	127	147	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	148	168	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	169	189	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	190	193	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	194	214	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	215	241	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	263	280	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	281	301	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	302	324	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	325	345	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	346	375	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	376	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	397	402	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	403	423	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	424	446	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	447	467	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	468	480	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Transmembrane	481	501	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43548	UniProtKB	Topological domain	502	558	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25649 1 128
+P25649	UniProtKB	Chain	1	128	.	.	.	ID=PRO_0000202575;Note=ADA histone acetyltransferase complex component 2	
+##sequence-region P29589 1 182
+P29589	UniProtKB	Chain	1	182	.	.	.	ID=PRO_0000064511;Note=Hexose transport activator protein	
+##sequence-region P38266 1 947
+P38266	UniProtKB	Chain	1	947	.	.	.	ID=PRO_0000202486;Note=Altered inheritance of mitochondria protein 3	
+P38266	UniProtKB	Compositional bias	95	398	.	.	.	Note=Gln-rich	
+P38266	UniProtKB	Compositional bias	371	447	.	.	.	Note=Pro-rich	
+P38266	UniProtKB	Compositional bias	862	907	.	.	.	Note=Pro-rich	
+P38266	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38266	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38266	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38266	UniProtKB	Modified residue	476	476	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38266	UniProtKB	Modified residue	729	729	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P38266	UniProtKB	Modified residue	861	861	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38266	UniProtKB	Sequence conflict	515	515	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38266	UniProtKB	Sequence conflict	515	515	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99299 1 758
+Q99299	UniProtKB	Chain	1	758	.	.	.	ID=PRO_0000203491;Note=Altered inheritance of mitochondria protein 44	
+Q99299	UniProtKB	Coiled coil	648	711	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99299	UniProtKB	Compositional bias	253	263	.	.	.	Note=Poly-Ser	
+Q99299	UniProtKB	Compositional bias	652	658	.	.	.	Note=Poly-Glu	
+Q99299	UniProtKB	Compositional bias	664	669	.	.	.	Note=Poly-Glu	
+Q99299	UniProtKB	Compositional bias	686	690	.	.	.	Note=Poly-Glu	
+Q99299	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38885 1 310
+P38885	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38885	UniProtKB	Chain	21	310	.	.	.	ID=PRO_0000202940;Note=Altered inheritance of mitochondria protein 46%2C mitochondrial	
+##sequence-region P53954 1 548
+P53954	UniProtKB	Chain	1	548	.	.	.	ID=PRO_0000080280;Note=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1%2C2-mannosyltransferase	
+P53954	UniProtKB	Topological domain	1	20	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53954	UniProtKB	Transmembrane	21	41	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53954	UniProtKB	Topological domain	42	548	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53954	UniProtKB	Compositional bias	84	87	.	.	.	Note=Poly-Gly	
+P53954	UniProtKB	Compositional bias	543	546	.	.	.	Note=Poly-Glu	
+P53954	UniProtKB	Glycosylation	262	262	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53954	UniProtKB	Glycosylation	393	393	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53954	UniProtKB	Glycosylation	480	480	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53954	UniProtKB	Glycosylation	490	490	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53954	UniProtKB	Mutagenesis	84	84	.	.	.	Note=No effect. G->A%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855	
+P53954	UniProtKB	Mutagenesis	85	85	.	.	.	Note=No effect. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855	
+P53954	UniProtKB	Mutagenesis	85	85	.	.	.	Note=No activity. G->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855	
+P53954	UniProtKB	Mutagenesis	87	87	.	.	.	Note=No effect. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855	
+P53954	UniProtKB	Mutagenesis	87	87	.	.	.	Note=No activity. G->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855	
+P53954	UniProtKB	Mutagenesis	319	319	.	.	.	Note=Almost no activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855	
+P53954	UniProtKB	Mutagenesis	405	405	.	.	.	Note=Almost no activity. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16878994,ECO:0000269|PubMed:19929855;Dbxref=PMID:16878994,PMID:19929855	
+P53954	UniProtKB	Mutagenesis	406	406	.	.	.	Note=Almost no activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855	
+P53954	UniProtKB	Mutagenesis	407	407	.	.	.	Note=Impaired activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855	
+P53954	UniProtKB	Mutagenesis	413	413	.	.	.	Note=No effect. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16878994,ECO:0000269|PubMed:19929855;Dbxref=PMID:16878994,PMID:19929855	
+##sequence-region Q12001 1 544
+Q12001	UniProtKB	Chain	1	544	.	.	.	ID=PRO_0000174161;Note=Dolichyl pyrophosphate Man9GlcNAc2 alpha-1%2C3-glucosyltransferase	
+Q12001	UniProtKB	Topological domain	1	35	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	57	104	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	126	145	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	167	171	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	172	192	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	193	223	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	224	244	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	245	263	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	264	284	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	285	332	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	333	353	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	354	356	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	357	377	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	378	398	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	399	419	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	420	425	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	426	446	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	447	481	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	482	502	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	503	508	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Transmembrane	509	529	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Topological domain	530	544	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12001	UniProtKB	Sequence conflict	203	203	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53868 1 555
+P53868	UniProtKB	Chain	1	555	.	.	.	ID=PRO_0000215789;Note=Alpha-1%2C2-mannosyltransferase ALG9	
+P53868	UniProtKB	Topological domain	1	7	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Topological domain	29	62	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Topological domain	84	86	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Transmembrane	87	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Topological domain	108	113	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Topological domain	135	176	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Topological domain	198	213	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Topological domain	235	268	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Transmembrane	269	289	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Topological domain	290	316	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Transmembrane	317	337	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Topological domain	338	349	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Transmembrane	350	370	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53868	UniProtKB	Topological domain	371	555	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38313 1 324
+P38313	UniProtKB	Chain	1	324	.	.	.	ID=PRO_0000064578;Note=Central kinetochore subunit AME1	
+P38313	UniProtKB	Coiled coil	199	263	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38313	UniProtKB	Modified residue	41	41	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38313	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38313	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38313	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38313	UniProtKB	Modified residue	101	101	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P39533 1 789
+P39533	UniProtKB	Transit peptide	1	14	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39533	UniProtKB	Chain	15	789	.	.	.	ID=PRO_0000076649;Note=Homocitrate dehydratase%2C mitochondrial	
+P39533	UniProtKB	Region	189	191	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39533	UniProtKB	Region	672	673	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39533	UniProtKB	Metal binding	385	385	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39533	UniProtKB	Metal binding	448	448	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39533	UniProtKB	Metal binding	451	451	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39533	UniProtKB	Binding site	96	96	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39533	UniProtKB	Binding site	476	476	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39533	UniProtKB	Binding site	481	481	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39533	UniProtKB	Mutagenesis	610	610	.	.	.	Note=Reduces catalytic activity towards homoaconitate by 45%25 and increases the activity towards aconitate by a factor 116. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23106124;Dbxref=PMID:23106124	
+##sequence-region P52910 1 683
+P52910	UniProtKB	Chain	1	683	.	.	.	ID=PRO_0000208421;Note=Acetyl-coenzyme A synthetase 2	
+P52910	UniProtKB	Nucleotide binding	401	403	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Nucleotide binding	425	430	.	.	.	Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Nucleotide binding	425	430	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Region	206	209	.	.	.	Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Binding site	325	325	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Binding site	516	516	.	.	.	Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Binding site	516	516	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Binding site	531	531	.	.	.	Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Binding site	531	531	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Binding site	539	539	.	.	.	Note=Coenzyme A%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Binding site	542	542	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Binding site	612	612	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52910	UniProtKB	Modified residue	679	679	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P52910	UniProtKB	Cross-link	506	506	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region P48360 1 493
+P48360	UniProtKB	Nucleotide binding	177	180	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165	
+P48360	UniProtKB	Nucleotide binding	223	224	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165	
+P48360	UniProtKB	Nucleotide binding	414	416	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165	
+P48360	UniProtKB	Binding site	26	26	.	.	.	Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165	
+P48360	UniProtKB	Binding site	48	48	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165	
+P48360	UniProtKB	Binding site	56	56	.	.	.	Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165	
+P48360	UniProtKB	Binding site	100	100	.	.	.	Note=FAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165	
+P48360	UniProtKB	Binding site	235	235	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165	
+P48360	UniProtKB	Binding site	407	407	.	.	.	Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165	
+P48360	UniProtKB	Binding site	414	414	.	.	.	Note=NADP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165	
+P48360	UniProtKB	Sequence conflict	33	33	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48360	UniProtKB	Sequence conflict	132	132	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25376 1 633
+P25376	UniProtKB	Chain	1	633	.	.	.	ID=PRO_0000054142;Note=General amino acid permease AGP1	
+P25376	UniProtKB	Topological domain	1	124	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	125	145	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	146	148	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	149	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	170	197	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	219	231	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	253	260	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	261	281	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	282	313	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	314	334	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	335	352	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	353	373	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	374	402	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	403	425	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	426	452	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	453	473	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	474	477	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	478	498	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	499	531	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	532	552	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	553	560	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Transmembrane	561	581	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Topological domain	582	633	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25376	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48813	
+P25376	UniProtKB	Lipidation	633	633	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25376	UniProtKB	Cross-link	11	11	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48813	
+##sequence-region P10869 1 527
+P10869	UniProtKB	Chain	1	527	.	.	.	ID=PRO_0000066690;Note=Aspartokinase	
+P10869	UniProtKB	Domain	367	440	.	.	.	Note=ACT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007	
+P10869	UniProtKB	Domain	442	527	.	.	.	Note=ACT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007	
+P10869	UniProtKB	Modified residue	333	333	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q08548 1 619
+Q08548	UniProtKB	Chain	1	619	.	.	.	ID=PRO_0000245257;Note=Lysophospholipid acyltransferase	
+Q08548	UniProtKB	Topological domain	1	19	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Transmembrane	20	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Topological domain	40	51	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Topological domain	73	92	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Topological domain	114	231	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Topological domain	253	274	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Transmembrane	275	295	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Topological domain	296	429	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Transmembrane	430	450	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Topological domain	451	456	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Transmembrane	457	477	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Topological domain	478	619	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Coiled coil	545	593	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Active site	382	382	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08548	UniProtKB	Modified residue	513	513	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q08548	UniProtKB	Modified residue	605	605	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+Q08548	UniProtKB	Modified residue	610	610	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08548	UniProtKB	Modified residue	615	615	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P36117 1 915
+P36117	UniProtKB	Chain	1	915	.	.	.	ID=PRO_0000203200;Note=Arrestin-related trafficking adapter 6	
+P36117	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P22580 1 549
+P22580	UniProtKB	Chain	1	549	.	.	.	ID=PRO_0000105130;Note=Probable amidase	
+P22580	UniProtKB	Active site	132	132	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22580	UniProtKB	Active site	209	209	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22580	UniProtKB	Active site	233	233	.	.	.	Note=Acyl-ester intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22580	UniProtKB	Sequence conflict	525	525	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38113 1 351
+P38113	UniProtKB	Chain	1	351	.	.	.	ID=PRO_0000160733;Note=Alcohol dehydrogenase 5	
+P38113	UniProtKB	Nucleotide binding	181	187	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Nucleotide binding	272	274	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Metal binding	47	47	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Metal binding	70	70	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Metal binding	101	101	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Metal binding	104	104	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Metal binding	107	107	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Metal binding	115	115	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Metal binding	183	183	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Binding site	205	205	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Binding site	210	210	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Binding site	344	344	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38113	UniProtKB	Modified residue	226	226	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P38113	UniProtKB	Modified residue	282	282	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P38113	UniProtKB	Modified residue	319	319	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P38113	UniProtKB	Cross-link	229	229	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P38113	UniProtKB	Cross-link	237	237	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+P38113	UniProtKB	Cross-link	290	290	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330	
+##sequence-region P04710 1 309
+P04710	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000090593;Note=ADP%2CATP carrier protein 1	
+P04710	UniProtKB	Transmembrane	10	44	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04710	UniProtKB	Transmembrane	81	105	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04710	UniProtKB	Transmembrane	114	148	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04710	UniProtKB	Transmembrane	183	210	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04710	UniProtKB	Transmembrane	215	249	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04710	UniProtKB	Transmembrane	278	303	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04710	UniProtKB	Repeat	11	104	.	.	.	Note=Solcar 1	
+P04710	UniProtKB	Repeat	116	208	.	.	.	Note=Solcar 2	
+P04710	UniProtKB	Repeat	216	302	.	.	.	Note=Solcar 3	
+P04710	UniProtKB	Motif	243	248	.	.	.	Note=Substrate recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04710	UniProtKB	Binding site	86	86	.	.	.	Note=Nucleotide;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P47127 1 394
+P47127	UniProtKB	Transit peptide	1	111	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47127	UniProtKB	Chain	112	394	.	.	.	ID=PRO_0000203103;Note=Altered inheritance of mitochondria protein 24%2C mitochondrial	
+##sequence-region Q12013 1 749
+Q12013	UniProtKB	Chain	1	749	.	.	.	ID=PRO_0000212936;Note=Probable palmitoyltransferase AKR2	
+Q12013	UniProtKB	Topological domain	1	306	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Transmembrane	307	327	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Transmembrane	328	348	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Topological domain	349	360	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Transmembrane	361	381	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Topological domain	382	392	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Transmembrane	393	413	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Topological domain	414	489	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Transmembrane	490	510	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Topological domain	511	546	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Transmembrane	547	567	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Topological domain	568	749	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12013	UniProtKB	Repeat	49	79	.	.	.	Note=ANK 1	
+Q12013	UniProtKB	Repeat	83	112	.	.	.	Note=ANK 2	
+Q12013	UniProtKB	Repeat	117	146	.	.	.	Note=ANK 3	
+Q12013	UniProtKB	Repeat	150	183	.	.	.	Note=ANK 4	
+Q12013	UniProtKB	Repeat	189	218	.	.	.	Note=ANK 5	
+Q12013	UniProtKB	Repeat	222	251	.	.	.	Note=ANK 6	
+Q12013	UniProtKB	Domain	446	496	.	.	.	Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067	
+Q12013	UniProtKB	Active site	476	476	.	.	.	Note=S-palmitoyl cysteine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12013	UniProtKB	Glycosylation	534	534	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P52892 1 507
+P52892	UniProtKB	Chain	1	507	.	.	.	ID=PRO_0000123937;Note=Probable alanine aminotransferase	
+P52892	UniProtKB	Modified residue	327	327	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52892	UniProtKB	Sequence conflict	420	420	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P14540 1 359
+P14540	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8935650;Dbxref=PMID:8935650	
+P14540	UniProtKB	Chain	2	359	.	.	.	ID=PRO_0000178762;Note=Fructose-bisphosphate aldolase	
+P14540	UniProtKB	Region	266	268	.	.	.	Note=Dihydroxyacetone phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14540	UniProtKB	Region	287	290	.	.	.	Note=Dihydroxyacetone phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14540	UniProtKB	Active site	110	110	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14540	UniProtKB	Metal binding	111	111	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14540	UniProtKB	Metal binding	145	145	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14540	UniProtKB	Metal binding	175	175	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14540	UniProtKB	Metal binding	227	227	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14540	UniProtKB	Metal binding	265	265	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14540	UniProtKB	Binding site	63	63	.	.	.	Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14540	UniProtKB	Binding site	228	228	.	.	.	Note=Dihydroxyacetone phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14540	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P14540	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14540	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14540	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14540	UniProtKB	Modified residue	83	83	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14540	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14540	UniProtKB	Modified residue	147	147	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P14540	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P14540	UniProtKB	Modified residue	179	179	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P14540	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P14540	UniProtKB	Modified residue	290	290	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14540	UniProtKB	Modified residue	310	310	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P14540	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P14540	UniProtKB	Cross-link	27	27	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14540	UniProtKB	Cross-link	73	73	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14540	UniProtKB	Cross-link	85	85	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14540	UniProtKB	Cross-link	308	308	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P50076 1 525
+P50076	UniProtKB	Chain	1	525	.	.	.	ID=PRO_0000215463;Note=Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1%2C2-glucosyltransferase	
+P50076	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	95	115	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	151	171	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	257	277	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	295	315	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	334	354	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	376	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	424	444	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	448	468	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Transmembrane	493	513	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Glycosylation	31	31	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Glycosylation	278	278	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Glycosylation	372	372	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50076	UniProtKB	Sequence conflict	266	266	.	.	.	Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50076	UniProtKB	Sequence conflict	266	266	.	.	.	Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32375 1 460
+P32375	UniProtKB	Chain	1	460	.	.	.	ID=PRO_0000165939;Note=Allantoinase	
+P32375	UniProtKB	Metal binding	70	70	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32375	UniProtKB	Metal binding	72	72	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32375	UniProtKB	Metal binding	157	157	.	.	.	Note=Zinc 1%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32375	UniProtKB	Metal binding	157	157	.	.	.	Note=Zinc 2%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32375	UniProtKB	Metal binding	193	193	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32375	UniProtKB	Metal binding	250	250	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32375	UniProtKB	Metal binding	323	323	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32375	UniProtKB	Modified residue	157	157	.	.	.	Note=N6-carboxylysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32375	UniProtKB	Sequence conflict	438	460	.	.	.	Note=VVYTNANGVSKTPLGQTLLDSRR->WYIRMPTESRKHHWVKLCLILDVKLKLQIFIKEIL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P54783 1 526
+P54783	UniProtKB	Chain	1	526	.	.	.	ID=PRO_0000128171;Note=D-arabinono-1%2C4-lactone oxidase	
+P54783	UniProtKB	Domain	19	193	.	.	.	Note=FAD-binding PCMH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00718	
+P54783	UniProtKB	Modified residue	56	56	.	.	.	Note=Pros-8alpha-FAD histidine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54783	UniProtKB	Sequence conflict	417	417	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38971 1 573
+P38971	UniProtKB	Chain	1	573	.	.	.	ID=PRO_0000054145;Note=Basic amino-acid permease	
+P38971	UniProtKB	Topological domain	1	73	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	74	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	94	95	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	96	116	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	117	153	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	154	174	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	175	179	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	180	200	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	201	209	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	210	230	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	231	265	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	266	286	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	287	306	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	307	327	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	328	359	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	360	380	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	381	403	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	404	424	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	425	431	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	432	452	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	453	477	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	478	498	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	499	510	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Transmembrane	511	531	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Topological domain	532	573	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38971	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32487	
+P38971	UniProtKB	Sequence conflict	51	51	.	.	.	Note=D->DD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38971	UniProtKB	Sequence conflict	126	126	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38971	UniProtKB	Sequence conflict	260	260	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38971	UniProtKB	Sequence conflict	517	517	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38971	UniProtKB	Sequence conflict	548	548	.	.	.	Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08981 1 209
+Q08981	UniProtKB	Chain	1	209	.	.	.	ID=PRO_0000268174;Note=APC/C-CDH1 modulator 1	
+Q08981	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q08981	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+Q08981	UniProtKB	Modified residue	202	202	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+Q08981	UniProtKB	Helix	68	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+Q08981	UniProtKB	Helix	95	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+Q08981	UniProtKB	Helix	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+##sequence-region P13711 1 748
+P13711	UniProtKB	Chain	1	748	.	.	.	ID=PRO_0000204704;Note=Acyl-coenzyme A oxidase	
+P13711	UniProtKB	Sequence conflict	443	443	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32463 1 125
+P32463	UniProtKB	Transit peptide	1	36	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32463	UniProtKB	Chain	37	125	.	.	.	ID=PRO_0000000566;Note=Acyl carrier protein%2C mitochondrial	
+P32463	UniProtKB	Domain	43	122	.	.	.	Note=Carrier;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258	
+P32463	UniProtKB	Modified residue	82	82	.	.	.	Note=O-(pantetheine 4'-phosphoryl)serine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258	
+##sequence-region Q02336 1 434
+Q02336	UniProtKB	Chain	1	434	.	.	.	ID=PRO_0000197082;Note=Transcriptional adapter 2	
+Q02336	UniProtKB	Domain	60	112	.	.	.	Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624	
+Q02336	UniProtKB	Domain	349	434	.	.	.	Note=SWIRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00247	
+Q02336	UniProtKB	Zinc finger	1	48	.	.	.	Note=ZZ-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00228	
+Q02336	UniProtKB	Helix	358	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ	
+Q02336	UniProtKB	Beta strand	367	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ	
+Q02336	UniProtKB	Helix	371	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ	
+Q02336	UniProtKB	Helix	384	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ	
+Q02336	UniProtKB	Helix	407	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ	
+Q02336	UniProtKB	Helix	418	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ	
+##sequence-region P07246 1 375
+P07246	UniProtKB	Transit peptide	1	27	.	.	.	Note=Mitochondrion	
+P07246	UniProtKB	Chain	28	375	.	.	.	ID=PRO_0000000879;Note=Alcohol dehydrogenase 3%2C mitochondrial	
+P07246	UniProtKB	Nucleotide binding	205	211	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07246	UniProtKB	Nucleotide binding	296	298	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07246	UniProtKB	Metal binding	71	71	.	.	.	Note=Zinc 1%3B catalytic	
+P07246	UniProtKB	Metal binding	94	94	.	.	.	Note=Zinc 1%3B catalytic	
+P07246	UniProtKB	Metal binding	125	125	.	.	.	Note=Zinc 2	
+P07246	UniProtKB	Metal binding	128	128	.	.	.	Note=Zinc 2	
+P07246	UniProtKB	Metal binding	131	131	.	.	.	Note=Zinc 2	
+P07246	UniProtKB	Metal binding	139	139	.	.	.	Note=Zinc 2	
+P07246	UniProtKB	Metal binding	181	181	.	.	.	Note=Zinc 1%3B catalytic	
+P07246	UniProtKB	Binding site	229	229	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07246	UniProtKB	Binding site	234	234	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07246	UniProtKB	Binding site	368	368	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07246	UniProtKB	Sequence conflict	10	10	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07246	UniProtKB	Sequence conflict	45	45	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25377 1 361
+P25377	UniProtKB	Chain	1	361	.	.	.	ID=PRO_0000160735;Note=NADP-dependent alcohol dehydrogenase 7	
+P25377	UniProtKB	Nucleotide binding	188	193	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25377	UniProtKB	Nucleotide binding	276	278	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25377	UniProtKB	Metal binding	46	46	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25377	UniProtKB	Metal binding	68	68	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25377	UniProtKB	Metal binding	100	100	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25377	UniProtKB	Metal binding	103	103	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25377	UniProtKB	Metal binding	106	106	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25377	UniProtKB	Metal binding	114	114	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25377	UniProtKB	Metal binding	164	164	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25377	UniProtKB	Binding site	216	216	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25377	UniProtKB	Binding site	349	349	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25377	UniProtKB	Modified residue	132	132	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04894	
+P25377	UniProtKB	Modified residue	316	316	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q12184 1 172
+Q12184	UniProtKB	Domain	61	163	.	.	.	Note=2Fe-2S ferredoxin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465	
+Q12184	UniProtKB	Metal binding	98	98	.	.	.	Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465	
+Q12184	UniProtKB	Metal binding	104	104	.	.	.	Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465	
+Q12184	UniProtKB	Metal binding	107	107	.	.	.	Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465	
+Q12184	UniProtKB	Metal binding	144	144	.	.	.	Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465	
+Q12184	UniProtKB	Beta strand	61	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+Q12184	UniProtKB	Beta strand	72	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+Q12184	UniProtKB	Helix	83	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+Q12184	UniProtKB	Beta strand	101	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+Q12184	UniProtKB	Beta strand	108	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+Q12184	UniProtKB	Turn	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+Q12184	UniProtKB	Turn	124	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+Q12184	UniProtKB	Helix	128	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+Q12184	UniProtKB	Beta strand	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+Q12184	UniProtKB	Beta strand	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+Q12184	UniProtKB	Turn	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+Q12184	UniProtKB	Helix	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJE	
+Q12184	UniProtKB	Beta strand	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD	
+##sequence-region P38872 1 237
+P38872	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000064460;Note=Prospore formation at selected spindle poles protein 1	
+##sequence-region Q05955 1 493
+Q05955	UniProtKB	Chain	1	493	.	.	.	ID=PRO_0000064462;Note=Accumulates dyads protein 4	
+##sequence-region Q12089 1 606
+Q12089	UniProtKB	Chain	1	606	.	.	.	ID=PRO_0000064466;Note=ATPase expression protein 3	
+Q12089	UniProtKB	Repeat	220	254	.	.	.	Note=PPR 1	
+Q12089	UniProtKB	Repeat	397	432	.	.	.	Note=PPR 2	
+Q12089	UniProtKB	Repeat	433	467	.	.	.	Note=PPR 3	
+##sequence-region Q99222 1 893
+Q99222	UniProtKB	Chain	1	893	.	.	.	ID=PRO_0000066256;Note=ARF3-interacting protein 1	
+Q99222	UniProtKB	Domain	28	335	.	.	.	Note=uDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304	
+Q99222	UniProtKB	Domain	365	492	.	.	.	Note=cDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304	
+Q99222	UniProtKB	Domain	494	640	.	.	.	Note=dDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304	
+Q99222	UniProtKB	Region	25	488	.	.	.	Note=Interaction with active ARF3	
+Q99222	UniProtKB	Coiled coil	152	172	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99222	UniProtKB	Coiled coil	872	892	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99222	UniProtKB	Mutagenesis	38	41	.	.	.	Note=Abolishes interaction with ARF3. KLGP->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18397879;Dbxref=PMID:18397879	
+##sequence-region P32781 1 87
+P32781	UniProtKB	Signal peptide	1	18	.	.	.	.	
+P32781	UniProtKB	Chain	19	87	.	.	.	ID=PRO_0000020642;Note=A-agglutinin-binding subunit	
+P32781	UniProtKB	Glycosylation	22	22	.	.	.	Note=O-linked (Man...) threonine	
+P32781	UniProtKB	Glycosylation	30	30	.	.	.	Note=O-linked (Man...) serine	
+P32781	UniProtKB	Glycosylation	32	32	.	.	.	Note=O-linked (Man...) threonine	
+P32781	UniProtKB	Glycosylation	39	39	.	.	.	Note=O-linked (Man...) serine	
+P32781	UniProtKB	Glycosylation	63	63	.	.	.	Note=O-linked (Man...) threonine	
+P32781	UniProtKB	Glycosylation	66	66	.	.	.	Note=O-linked (Man...) serine	
+P32781	UniProtKB	Glycosylation	75	75	.	.	.	Note=O-linked (Man...) threonine	
+P32781	UniProtKB	Disulfide bond	25	25	.	.	.	Note=Interchain (with AGA1);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32781	UniProtKB	Disulfide bond	68	68	.	.	.	Note=Interchain (with AGA1);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32781	UniProtKB	Mutagenesis	25	25	.	.	.	Note=Abolishes agglutination%3B when associated with S-68. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7957044;Dbxref=PMID:7957044	
+P32781	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Abolishes agglutination%3B when associated with S-25. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7957044;Dbxref=PMID:7957044	
+##sequence-region P38628 1 557
+P38628	UniProtKB	Chain	1	557	.	.	.	ID=PRO_0000148019;Note=Phosphoacetylglucosamine mutase	
+P38628	UniProtKB	Region	395	397	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2	
+P38628	UniProtKB	Region	522	526	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2	
+P38628	UniProtKB	Active site	67	67	.	.	.	Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2	
+P38628	UniProtKB	Metal binding	67	67	.	.	.	Note=Magnesium%3B via phosphate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2	
+P38628	UniProtKB	Metal binding	298	298	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2	
+P38628	UniProtKB	Metal binding	300	300	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2	
+P38628	UniProtKB	Metal binding	302	302	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2	
+P38628	UniProtKB	Binding site	531	531	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2	
+P38628	UniProtKB	Modified residue	67	67	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38628	UniProtKB	Sequence conflict	15	15	.	.	.	Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38628	UniProtKB	Sequence conflict	196	196	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38628	UniProtKB	Sequence conflict	406	406	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43567 1 385
+P43567	UniProtKB	Chain	1	385	.	.	.	ID=PRO_0000150239;Note=Alanine--glyoxylate aminotransferase 1	
+P43567	UniProtKB	Binding site	354	354	.	.	.	Note=Substrate	
+P43567	UniProtKB	Modified residue	201	201	.	.	.	Note=N6-(pyridoxal phosphate)lysine	
+P43567	UniProtKB	Beta strand	10	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	18	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	34	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Beta strand	60	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	70	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Beta strand	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	96	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Beta strand	111	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	126	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Beta strand	139	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Turn	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	156	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Beta strand	170	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Turn	177	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Turn	187	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Beta strand	193	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Beta strand	209	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	216	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	225	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	238	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	261	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	279	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Turn	299	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Beta strand	304	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Beta strand	309	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Beta strand	319	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	326	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Turn	346	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	349	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Beta strand	352	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	359	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+P43567	UniProtKB	Helix	369	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW	
+##sequence-region Q04516 1 312
+Q04516	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000167629;Note=Uncharacterized oxidoreductase AIM33	
+Q04516	UniProtKB	Topological domain	1	14	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04516	UniProtKB	Transmembrane	15	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04516	UniProtKB	Topological domain	36	41	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04516	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04516	UniProtKB	Topological domain	63	179	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04516	UniProtKB	Transmembrane	180	200	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04516	UniProtKB	Topological domain	201	312	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04516	UniProtKB	Domain	70	173	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+##sequence-region Q12476 1 344
+Q12476	UniProtKB	Chain	1	344	.	.	.	ID=PRO_0000227604;Note=Protein AIR2	
+Q12476	UniProtKB	Zinc finger	61	78	.	.	.	Note=CCHC-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+Q12476	UniProtKB	Zinc finger	99	116	.	.	.	Note=CCHC-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+Q12476	UniProtKB	Zinc finger	162	179	.	.	.	Note=CCHC-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+Q12476	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12476	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12476	UniProtKB	Beta strand	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+Q12476	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+Q12476	UniProtKB	Helix	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+Q12476	UniProtKB	Helix	36	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+Q12476	UniProtKB	Beta strand	67	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI	
+Q12476	UniProtKB	Turn	73	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI	
+Q12476	UniProtKB	Turn	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI	
+Q12476	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI	
+Q12476	UniProtKB	Turn	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI	
+Q12476	UniProtKB	Helix	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI	
+Q12476	UniProtKB	Beta strand	101	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI	
+Q12476	UniProtKB	Beta strand	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI	
+Q12476	UniProtKB	Turn	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI	
+Q12476	UniProtKB	Beta strand	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+Q12476	UniProtKB	Beta strand	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+Q12476	UniProtKB	Helix	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+Q12476	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+Q12476	UniProtKB	Beta strand	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI	
+Q12476	UniProtKB	Beta strand	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+Q12476	UniProtKB	Beta strand	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+Q12476	UniProtKB	Helix	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+##sequence-region P21147 1 510
+P21147	UniProtKB	Chain	1	510	.	.	.	ID=PRO_0000185406;Note=Acyl-CoA desaturase 1	
+P21147	UniProtKB	Topological domain	1	112	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21147	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21147	UniProtKB	Topological domain	134	138	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21147	UniProtKB	Transmembrane	139	159	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21147	UniProtKB	Topological domain	160	255	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21147	UniProtKB	Transmembrane	256	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21147	UniProtKB	Topological domain	277	280	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21147	UniProtKB	Transmembrane	281	301	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21147	UniProtKB	Topological domain	302	510	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21147	UniProtKB	Domain	409	487	.	.	.	Note=Cytochrome b5 heme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+P21147	UniProtKB	Motif	161	166	.	.	.	Note=Histidine box-1;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21147	UniProtKB	Motif	198	202	.	.	.	Note=Histidine box-2;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21147	UniProtKB	Motif	335	339	.	.	.	Note=Histidine box-3;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21147	UniProtKB	Metal binding	161	161	.	.	.	Note=Iron 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516	
+P21147	UniProtKB	Metal binding	166	166	.	.	.	Note=Iron 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516	
+P21147	UniProtKB	Metal binding	198	198	.	.	.	Note=Iron 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516	
+P21147	UniProtKB	Metal binding	201	201	.	.	.	Note=Iron 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516	
+P21147	UniProtKB	Metal binding	202	202	.	.	.	Note=Iron 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516	
+P21147	UniProtKB	Metal binding	306	306	.	.	.	Note=Iron 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516	
+P21147	UniProtKB	Metal binding	335	335	.	.	.	Note=Iron 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516	
+P21147	UniProtKB	Metal binding	338	338	.	.	.	Note=Iron 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516	
+P21147	UniProtKB	Metal binding	339	339	.	.	.	Note=Iron 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516	
+P21147	UniProtKB	Metal binding	444	444	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+P21147	UniProtKB	Metal binding	470	470	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+P21147	UniProtKB	Sequence conflict	67	67	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21147	UniProtKB	Sequence conflict	304	304	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P19414 1 778
+P19414	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975908;Dbxref=PMID:15975908	
+P19414	UniProtKB	Chain	17	778	.	.	.	ID=PRO_0000000547;Note=Aconitate hydratase%2C mitochondrial	
+P19414	UniProtKB	Region	188	190	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19414	UniProtKB	Region	667	668	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19414	UniProtKB	Metal binding	382	382	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19414	UniProtKB	Metal binding	445	445	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19414	UniProtKB	Metal binding	448	448	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19414	UniProtKB	Binding site	95	95	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19414	UniProtKB	Binding site	471	471	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19414	UniProtKB	Binding site	476	476	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19414	UniProtKB	Binding site	604	604	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19414	UniProtKB	Modified residue	391	391	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19414	UniProtKB	Modified residue	409	409	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P19414	UniProtKB	Modified residue	556	556	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P19414	UniProtKB	Mutagenesis	604	604	.	.	.	Note=Strongly diminishes the catalytic activity towards both known substrates%2C aconitate and homoaconitate. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23106124;Dbxref=PMID:23106124	
+P19414	UniProtKB	Sequence conflict	527	549	.	.	.	Note=DGLPQRGYDAGENTYQAPPADRS->RWFASKEVMMLVRTLTKLHLQTVA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03233 1 198
+Q03233	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000203321;Note=Alpha1-proteinase inhibitor-degradation deficient protein 37	
+Q03233	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P32794 1 780
+P32794	UniProtKB	Chain	1	780	.	.	.	ID=PRO_0000084592;Note=ATPase family gene 2 protein	
+P32794	UniProtKB	Nucleotide binding	286	293	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32794	UniProtKB	Nucleotide binding	557	564	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12433 1 566
+Q12433	UniProtKB	Chain	1	566	.	.	.	ID=PRO_0000227804;Note=Protein AHC1	
+Q12433	UniProtKB	Modified residue	282	282	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12433	UniProtKB	Modified residue	505	505	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+##sequence-region P38013 1 176
+P38013	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+P38013	UniProtKB	Chain	2	176	.	.	.	ID=PRO_0000056610;Note=Peroxiredoxin AHP1	
+P38013	UniProtKB	Domain	9	176	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P38013	UniProtKB	Active site	62	62	.	.	.	Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:22474296;Dbxref=PMID:22474296	
+P38013	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+P38013	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38013	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38013	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38013	UniProtKB	Disulfide bond	31	31	.	.	.	Note=Interchain (with C-31 in TRX2)%3B transient;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296	
+P38013	UniProtKB	Disulfide bond	31	31	.	.	.	Note=Interchain (with C-62)%3B in linked form;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4DSQ,ECO:0000244|PDB:4OWY,ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296	
+P38013	UniProtKB	Disulfide bond	62	62	.	.	.	Note=Interchain (with C-31)%3B in linked form;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4DSQ,ECO:0000244|PDB:4OWY,ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296	
+P38013	UniProtKB	Cross-link	32	32	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21209336;Dbxref=PMID:21209336	
+P38013	UniProtKB	Cross-link	48	48	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38013	UniProtKB	Cross-link	113	113	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38013	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Abolishes catalytic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296	
+P38013	UniProtKB	Mutagenesis	32	32	.	.	.	Note=Prevents urmylation of AHP1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21209336;Dbxref=PMID:21209336	
+P38013	UniProtKB	Mutagenesis	62	62	.	.	.	Note=Abolishes catalytic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296	
+P38013	UniProtKB	Mutagenesis	120	120	.	.	.	Note=No effect on tert-butyl hydroperoxide consumption. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296	
+P38013	UniProtKB	Sequence conflict	21	21	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38013	UniProtKB	Sequence conflict	65	65	.	.	.	Note=S->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38013	UniProtKB	Sequence conflict	87	87	.	.	.	Note=I->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38013	UniProtKB	Turn	3	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Beta strand	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Beta strand	23	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Beta strand	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OWY	
+P38013	UniProtKB	Helix	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Beta strand	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Helix	39	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Beta strand	47	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Helix	60	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Helix	67	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Beta strand	85	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Helix	94	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Beta strand	110	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Helix	121	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Beta strand	129	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Beta strand	136	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Beta strand	141	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Beta strand	150	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Turn	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+P38013	UniProtKB	Helix	169	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86	
+##sequence-region P03875 1 834
+P03875	UniProtKB	Chain	1	834	.	.	.	ID=PRO_0000196880;Note=Putative COX1/OXI3 intron 1 protein	
+P03875	UniProtKB	Domain	296	577	.	.	.	Note=Reverse transcriptase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405	
+P03875	UniProtKB	Sequence conflict	118	118	.	.	.	Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03875	UniProtKB	Sequence conflict	118	118	.	.	.	Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12156 1 149
+Q12156	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12156	UniProtKB	Chain	2	149	.	.	.	ID=PRO_0000244441;Note=Protein AIM7	
+Q12156	UniProtKB	Domain	3	147	.	.	.	Note=ADF-H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00599	
+Q12156	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12156	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P40507 1 360
+P40507	UniProtKB	Chain	1	360	.	.	.	ID=PRO_0000202979;Note=Protein AIR1	
+P40507	UniProtKB	Zinc finger	74	91	.	.	.	Note=CCHC-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+P40507	UniProtKB	Zinc finger	112	129	.	.	.	Note=CCHC-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+P40507	UniProtKB	Zinc finger	134	151	.	.	.	Note=CCHC-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+P40507	UniProtKB	Zinc finger	173	190	.	.	.	Note=CCHC-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+P40507	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P39010 1 764
+P39010	UniProtKB	Chain	1	764	.	.	.	ID=PRO_0000212934;Note=Palmitoyltransferase AKR1	
+P39010	UniProtKB	Topological domain	1	321	.	.	.	Note=Cytoplasmic	
+P39010	UniProtKB	Transmembrane	322	341	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39010	UniProtKB	Topological domain	342	346	.	.	.	Note=Lumenal	
+P39010	UniProtKB	Transmembrane	347	364	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39010	UniProtKB	Topological domain	365	384	.	.	.	Note=Cytoplasmic	
+P39010	UniProtKB	Transmembrane	385	405	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39010	UniProtKB	Topological domain	406	418	.	.	.	Note=Lumenal	
+P39010	UniProtKB	Transmembrane	419	439	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39010	UniProtKB	Topological domain	440	513	.	.	.	Note=Cytoplasmic	
+P39010	UniProtKB	Transmembrane	514	534	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39010	UniProtKB	Topological domain	535	570	.	.	.	Note=Lumenal	
+P39010	UniProtKB	Transmembrane	571	591	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39010	UniProtKB	Topological domain	592	764	.	.	.	Note=Cytoplasmic	
+P39010	UniProtKB	Repeat	72	102	.	.	.	Note=ANK 1	
+P39010	UniProtKB	Repeat	108	137	.	.	.	Note=ANK 2	
+P39010	UniProtKB	Repeat	142	171	.	.	.	Note=ANK 3	
+P39010	UniProtKB	Repeat	175	204	.	.	.	Note=ANK 4	
+P39010	UniProtKB	Repeat	213	242	.	.	.	Note=ANK 5	
+P39010	UniProtKB	Repeat	246	275	.	.	.	Note=ANK 6	
+P39010	UniProtKB	Domain	470	520	.	.	.	Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067	
+P39010	UniProtKB	Active site	500	500	.	.	.	Note=S-palmitoyl cysteine intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12370247;Dbxref=PMID:12370247	
+P39010	UniProtKB	Modified residue	51	51	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39010	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39010	UniProtKB	Mutagenesis	497	498	.	.	.	Note=Abolishes YCK2 palmitoylation. DH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12370247;Dbxref=PMID:12370247	
+P39010	UniProtKB	Mutagenesis	500	500	.	.	.	Note=Abolishes YCK2 palmitoylation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12370247;Dbxref=PMID:12370247	
+##sequence-region P38207 1 520
+P38207	UniProtKB	Chain	1	520	.	.	.	ID=PRO_0000200020;Note=DNA-(apurinic or apyrimidinic site) lyase 2	
+P38207	UniProtKB	Active site	181	181	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38207	UniProtKB	Active site	222	222	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38207	UniProtKB	Metal binding	59	59	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38207	UniProtKB	Metal binding	222	222	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38207	UniProtKB	Metal binding	224	224	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38207	UniProtKB	Metal binding	353	353	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38207	UniProtKB	Site	224	224	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38207	UniProtKB	Site	328	328	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38207	UniProtKB	Site	354	354	.	.	.	Note=Interaction with DNA substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38207	UniProtKB	Sequence conflict	15	15	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12354 1 227
+Q12354	UniProtKB	Chain	1	227	.	.	.	ID=PRO_0000229015;Note=Acyl-protein thioesterase 1	
+Q12354	UniProtKB	Active site	119	119	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12354	UniProtKB	Active site	173	173	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12354	UniProtKB	Active site	207	207	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q08702 1 217
+Q08702	UniProtKB	Chain	1	217	.	.	.	ID=PRO_0000109802;Note=Aprataxin-like protein	
+Q08702	UniProtKB	Domain	6	139	.	.	.	Note=HIT	
+Q08702	UniProtKB	Region	34	38	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859	
+Q08702	UniProtKB	Region	121	132	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859	
+Q08702	UniProtKB	Region	144	148	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859	
+Q08702	UniProtKB	Active site	130	130	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859	
+Q08702	UniProtKB	Metal binding	188	188	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859	
+Q08702	UniProtKB	Metal binding	191	191	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859	
+Q08702	UniProtKB	Metal binding	205	205	.	.	.	Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859	
+Q08702	UniProtKB	Metal binding	209	209	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859	
+Q08702	UniProtKB	Site	10	10	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859	
+Q08702	UniProtKB	Sequence conflict	80	80	.	.	.	Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08702	UniProtKB	Sequence conflict	157	157	.	.	.	Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04212 1 335
+Q04212	UniProtKB	Chain	1	335	.	.	.	ID=PRO_0000070372;Note=D-arabinose 1-dehydrogenase	
+Q04212	UniProtKB	Nucleotide binding	221	287	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04212	UniProtKB	Active site	58	58	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04212	UniProtKB	Binding site	124	124	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04212	UniProtKB	Site	86	86	.	.	.	Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38724 1 620
+P38724	UniProtKB	Chain	1	620	.	.	.	ID=PRO_0000084863;Note=Siderophore iron transporter ARN2	
+P38724	UniProtKB	Transmembrane	71	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	106	128	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	135	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	162	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	191	213	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	223	245	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	286	308	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	318	335	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	355	377	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	392	414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	421	438	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	448	470	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	491	513	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38724	UniProtKB	Transmembrane	561	578	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38840 1 513
+P38840	UniProtKB	Chain	1	513	.	.	.	ID=PRO_0000064679;Note=Aromatic amino acid aminotransferase 2	
+P38840	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38840	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38840	UniProtKB	Sequence conflict	460	460	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04549 1 284
+Q04549	UniProtKB	Chain	1	284	.	.	.	ID=PRO_0000089130;Note=Actin-like protein ARP10	
+##sequence-region P80428 1 489
+P80428	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000089103;Note=Actin-related protein 4	
+P80428	UniProtKB	Modified residue	349	349	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P80428	UniProtKB	Mutagenesis	23	23	.	.	.	Note=Lethal%3B when associated with D-161. Formamide-%2C hydroxyurea and UV-hypersensitivity%2C suppressor of TY phenotype%3B when associated with A-159. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622406;Dbxref=PMID:14622406	
+P80428	UniProtKB	Mutagenesis	155	155	.	.	.	Note=No histone acetyltransferase activity at 37 degrees Celsius. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10911987;Dbxref=PMID:10911987	
+P80428	UniProtKB	Mutagenesis	159	159	.	.	.	Note=Formamide-%2C hydroxyurea and UV-hypersensitivity%2C suppressor of TY phenotype%3B when associated with S-23. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622406;Dbxref=PMID:14622406	
+P80428	UniProtKB	Mutagenesis	161	161	.	.	.	Note=Formamide-%2C hydroxyurea and UV-hypersensitivity%2C destabilization of ARP4%2C suppressor of TY phenotype and elevated levels of MSN2/MSN4-regulated genes. Lethal%3B when associated with A-23. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622406;Dbxref=PMID:14622406	
+P80428	UniProtKB	Mutagenesis	187	187	.	.	.	Note=Defect in promoter association and change in chromatin structure. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11937627;Dbxref=PMID:11937627	
+P80428	UniProtKB	Mutagenesis	455	455	.	.	.	Note=No histone acetyltransferase activity at 37 degrees Celsius. Defect in promoter association and change in chromatin structure. G->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10911987,ECO:0000269|PubMed:11937627;Dbxref=PMID:10911987,PMID:11937627	
+P80428	UniProtKB	Beta strand	9	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	17	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	23	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	37	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	67	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	83	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	107	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	118	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	135	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	142	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	153	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	165	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0	
+P80428	UniProtKB	Beta strand	181	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	187	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Turn	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0	
+P80428	UniProtKB	Beta strand	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	227	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	238	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	258	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	268	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0	
+P80428	UniProtKB	Beta strand	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0	
+P80428	UniProtKB	Beta strand	277	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0	
+P80428	UniProtKB	Helix	282	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Turn	291	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Turn	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	308	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0	
+P80428	UniProtKB	Helix	385	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	398	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	408	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	413	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	420	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	446	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	451	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Helix	463	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Beta strand	469	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0	
+P80428	UniProtKB	Helix	472	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+P80428	UniProtKB	Turn	479	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+##sequence-region P40467 1 964
+P40467	UniProtKB	Chain	1	964	.	.	.	ID=PRO_0000114997;Note=Activator of stress genes 1	
+P40467	UniProtKB	DNA binding	21	47	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P40467	UniProtKB	Compositional bias	832	837	.	.	.	Note=Poly-Asn	
+P40467	UniProtKB	Compositional bias	840	869	.	.	.	Note=Poly-Asn	
+P40467	UniProtKB	Compositional bias	875	887	.	.	.	Note=Poly-Asn	
+P40467	UniProtKB	Modified residue	166	166	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40467	UniProtKB	Modified residue	186	186	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40467	UniProtKB	Modified residue	963	963	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40467	UniProtKB	Natural variant	77	77	.	.	.	Note=In strain: SK1. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40467	UniProtKB	Natural variant	149	149	.	.	.	Note=In strain: SK1. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40467	UniProtKB	Natural variant	353	353	.	.	.	Note=In strain: SK1. I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40467	UniProtKB	Natural variant	682	682	.	.	.	Note=In strain: SK1. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40467	UniProtKB	Natural variant	707	707	.	.	.	Note=In strain: SK1. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40467	UniProtKB	Natural variant	770	770	.	.	.	Note=In strain: SK1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40467	UniProtKB	Natural variant	811	811	.	.	.	Note=In strain: SK1. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40467	UniProtKB	Natural variant	852	852	.	.	.	Note=In strain: SK1. D->NDNNN	
+P40467	UniProtKB	Natural variant	887	887	.	.	.	Note=In strain: SK1. N->NN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40467	UniProtKB	Natural variant	926	933	.	.	.	Note=In strain: SK1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+##sequence-region P34233 1 588
+P34233	UniProtKB	Chain	1	588	.	.	.	ID=PRO_0000083492;Note=Transcriptional regulatory protein ASH1	
+P34233	UniProtKB	Zinc finger	499	526	.	.	.	Note=GATA-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094	
+P34233	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34233	UniProtKB	Modified residue	465	465	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q06834 1 288
+Q06834	UniProtKB	Chain	1	288	.	.	.	ID=PRO_0000055760;Note=Alcohol-sensitive RING finger protein 1	
+Q06834	UniProtKB	Zinc finger	4	48	.	.	.	Note=RING-type 1%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q06834	UniProtKB	Zinc finger	121	168	.	.	.	Note=RING-type 2%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+##sequence-region P49435 1 187
+P49435	UniProtKB	Chain	1	187	.	.	.	ID=PRO_0000149517;Note=Adenine phosphoribosyltransferase 1	
+P49435	UniProtKB	Nucleotide binding	133	137	.	.	.	Note=AMP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P49435	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P49435	UniProtKB	Mutagenesis	69	69	.	.	.	Note=4-fold decrease in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055	
+P49435	UniProtKB	Mutagenesis	89	89	.	.	.	Note=2-fold decrease in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055	
+P49435	UniProtKB	Mutagenesis	90	90	.	.	.	Note=30-fold decrease in activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055	
+P49435	UniProtKB	Mutagenesis	93	93	.	.	.	Note=Small increase in activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055	
+P49435	UniProtKB	Mutagenesis	103	103	.	.	.	Note=4-fold increase in activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055	
+P49435	UniProtKB	Mutagenesis	106	106	.	.	.	Note=1 million-fold decrease in activity. E->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055	
+P49435	UniProtKB	Mutagenesis	106	106	.	.	.	Note=2-fold decrease in activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055	
+P49435	UniProtKB	Mutagenesis	107	107	.	.	.	Note=2/3-fold decrease in activity. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055	
+P49435	UniProtKB	Mutagenesis	107	107	.	.	.	Note=Small decrease in activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055	
+P49435	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Small decrease in activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055	
+P49435	UniProtKB	Mutagenesis	108	108	.	.	.	Note=2/3-fold decrease in activity. G->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055	
+P49435	UniProtKB	Sequence conflict	37	37	.	.	.	Note=P->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P49435	UniProtKB	Helix	2	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Beta strand	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Beta strand	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Helix	31	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Helix	37	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Beta strand	62	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Turn	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Helix	70	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Beta strand	84	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Beta strand	96	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Beta strand	109	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Beta strand	124	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Helix	136	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Beta strand	151	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+P49435	UniProtKB	Helix	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2P	
+P49435	UniProtKB	Helix	166	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2P	
+P49435	UniProtKB	Beta strand	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q	
+##sequence-region P07347 1 238
+P07347	UniProtKB	Chain	1	238	.	.	.	ID=PRO_0000074529;Note=N-terminal acetyltransferase A complex catalytic subunit ARD1	
+P07347	UniProtKB	Domain	35	195	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+P07347	UniProtKB	Sequence conflict	37	37	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07347	UniProtKB	Beta strand	3	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Helix	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Helix	13	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Helix	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY	
+P07347	UniProtKB	Helix	30	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Turn	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Beta strand	45	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Helix	66	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY	
+P07347	UniProtKB	Turn	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY	
+P07347	UniProtKB	Beta strand	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Beta strand	90	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Helix	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNX	
+P07347	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNW	
+P07347	UniProtKB	Beta strand	112	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Helix	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Beta strand	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Helix	129	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Beta strand	148	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Helix	159	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Turn	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Beta strand	172	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Beta strand	187	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Helix	196	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Helix	201	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P07347	UniProtKB	Turn	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY	
+P07347	UniProtKB	Beta strand	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY	
+P07347	UniProtKB	Helix	224	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY	
+##sequence-region P18544 1 423
+P18544	UniProtKB	Modified residue	276	276	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53974 1 638
+P53974	UniProtKB	Chain	1	638	.	.	.	ID=PRO_0000085635;Note=Actin-regulating kinase 1	
+P53974	UniProtKB	Domain	22	298	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53974	UniProtKB	Nucleotide binding	28	36	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53974	UniProtKB	Region	602	615	.	.	.	Note=Interaction with SH3 domain of ABP1	
+P53974	UniProtKB	Active site	159	159	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P53974	UniProtKB	Binding site	56	56	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53974	UniProtKB	Modified residue	478	478	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P53974	UniProtKB	Modified residue	522	522	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53974	UniProtKB	Modified residue	535	535	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53974	UniProtKB	Mutagenesis	56	56	.	.	.	Note=Abolishes protein kinase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10087264;Dbxref=PMID:10087264	
+##sequence-region P38116 1 183
+P38116	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+P38116	UniProtKB	Chain	2	183	.	.	.	ID=PRO_0000207421;Note=ADP-ribosylation factor-like protein 1	
+P38116	UniProtKB	Nucleotide binding	25	32	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38116	UniProtKB	Nucleotide binding	68	72	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38116	UniProtKB	Nucleotide binding	127	130	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38116	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9388248;Dbxref=PMID:9388248	
+P38116	UniProtKB	Helix	3	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Helix	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Beta strand	19	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Helix	31	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Beta strand	41	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Beta strand	54	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Beta strand	62	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Helix	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Turn	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Beta strand	86	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Turn	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Helix	101	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Beta strand	121	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Helix	137	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Turn	144	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Beta strand	154	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Helix	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+P38116	UniProtKB	Helix	167	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ	
+##sequence-region P38696 1 384
+P38696	UniProtKB	Chain	1	384	.	.	.	ID=PRO_0000089066;Note=Centractin	
+P38696	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Temperature-sensitive%3B when associated with A-6. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Temperature-sensitive%3B when associated with A-2. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	46	46	.	.	.	Note=Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis%3B when associated with 48-A-A-49. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	48	49	.	.	.	Note=Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis%3B when associated with A-46. DK->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Reduces spindle formation%3B when associated with A-75. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	75	75	.	.	.	Note=Reduces spindle formation%3B when associated with A-73. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	79	80	.	.	.	Note=Reduces nuclear migration in mitosis. KH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	84	85	.	.	.	Note=Reduces spindle formation. Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis%3B when associated with A-87. ED->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Reduces spindle formation. Reduces nuclear migration in mitosis%3B when associated with 84-A-A-85. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	108	109	.	.	.	Note=Reduces nuclear migration in mitosis. EH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	133	133	.	.	.	Note=Lethal. Strongly reduces interaction with JNM1%3B when associated with A-136. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	136	136	.	.	.	Note=Lethal. Strongly reduces interaction with JNM1%3B when associated with A-133. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	162	162	.	.	.	Note=Reduces spindle formation. Reduces nuclear migration in mitosis%3B when associated with A-165. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	165	165	.	.	.	Note=Reduces spindle formation. Reduces nuclear migration in mitosis%3B when associated with A-162. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	185	185	.	.	.	Note=Temperature-sensitive. Strongly reduces interaction with JNM1%3B when associated with A-187. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	187	187	.	.	.	Note=Temperature-sensitive. Strongly reduces interaction with JNM1%3B when associated with A-185. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	214	216	.	.	.	Note=Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis. Alters complex assembly%3B when associated with A-219. ERE->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	219	219	.	.	.	Note=Lethal%3B when associated with 214-A--A-216. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	222	224	.	.	.	Note=Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis. KEK->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	233	238	.	.	.	Note=Temperature-sensitive. Strongly reduces interaction with JNM1. KKEEEK->AAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	233	235	.	.	.	Note=Reduces spindle formation. KKE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	236	238	.	.	.	Note=Reduces spindle formation. EEK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	251	251	.	.	.	Note=Lethal and dominant cold-sensitive. Reduces nuclear migration in mitosis%3B when associated with A-254. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	254	254	.	.	.	Note=Lethal and dominant cold-sensitive. Reduces nuclear migration in mitosis%3B when associated with A-251. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	263	264	.	.	.	Note=Reduces spindle formation. DR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	266	266	.	.	.	Note=Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis%3B when associated with A-269. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	269	269	.	.	.	Note=Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis%3B when associated with A-266. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	294	294	.	.	.	Note=Reduces nuclear migration in mitosis%3B when associated with A-296 and A-298. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	296	296	.	.	.	Note=Reduces nuclear migration in mitosis%3B when associated with A-294 and A-298. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	298	298	.	.	.	Note=Reduces nuclear migration in mitosis%3B when associated with A-294 and A-296. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	321	322	.	.	.	Note=Lethal. Strongly reduces interaction with JNM1. DR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	326	326	.	.	.	Note=Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1%3B when associated with A-328. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	328	328	.	.	.	Note=Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1%3B when associated with A-326. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	336	336	.	.	.	Note=Strongly reduces interaction with JNM1%3B when associated with A-338. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	338	338	.	.	.	Note=Strongly reduces interaction with JNM1%3B when associated with A-336. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	344	346	.	.	.	Note=Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1. ERK->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	368	369	.	.	.	Note=Reduces nuclear migration in mitosis%3B when associated with A-371. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535	
+P38696	UniProtKB	Mutagenesis	369	369	.	.	.	Note=Lethal. Strongly reduces interaction with JNM1%3B when associated with A-371. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	371	371	.	.	.	Note=Lethal. Strongly reduces interaction with JNM1%3B when associated with A-369. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	371	371	.	.	.	Note=Reduces nuclear migration in mitosis%3B when associated with 368-A-A-369. D->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535	
+P38696	UniProtKB	Mutagenesis	374	375	.	.	.	Note=Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1%3B when associated with A-378. ED->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Mutagenesis	378	378	.	.	.	Note=Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1%3B when associated with 374-A-A-375. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903	
+P38696	UniProtKB	Sequence conflict	3	3	.	.	.	Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06597 1 130
+Q06597	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000064439;Note=Arsenical-resistance protein 2	
+Q06597	UniProtKB	Domain	17	124	.	.	.	Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+##sequence-region P40994 1 183
+P40994	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+P40994	UniProtKB	Chain	2	183	.	.	.	ID=PRO_0000207420;Note=ADP-ribosylation factor 3	
+P40994	UniProtKB	Nucleotide binding	24	31	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40994	UniProtKB	Nucleotide binding	67	71	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40994	UniProtKB	Nucleotide binding	126	129	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40994	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04728 1 441
+Q04728	UniProtKB	Transit peptide	1	8	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03124,ECO:0000269|PubMed:7705341;Dbxref=PMID:7705341	
+Q04728	UniProtKB	Chain	9	214	.	.	.	ID=PRO_0000002283;Note=Arginine biosynthesis bifunctional protein ArgJ alpha chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124	
+Q04728	UniProtKB	Chain	215	441	.	.	.	ID=PRO_0000002284;Note=Arginine biosynthesis bifunctional protein ArgJ beta chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124	
+Q04728	UniProtKB	Active site	215	215	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124	
+Q04728	UniProtKB	Binding site	177	177	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124	
+Q04728	UniProtKB	Binding site	204	204	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124	
+Q04728	UniProtKB	Binding site	215	215	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124	
+Q04728	UniProtKB	Binding site	301	301	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124	
+Q04728	UniProtKB	Binding site	436	436	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124	
+Q04728	UniProtKB	Binding site	441	441	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124	
+Q04728	UniProtKB	Site	136	136	.	.	.	Note=Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124	
+Q04728	UniProtKB	Site	137	137	.	.	.	Note=Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124	
+Q04728	UniProtKB	Site	214	215	.	.	.	Note=Cleavage%3B by autolysis	
+Q04728	UniProtKB	Mutagenesis	215	215	.	.	.	Note=Blocks autocatalytic processing of the precursor protein. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10753950;Dbxref=PMID:10753950	
+##sequence-region P07249 1 177
+P07249	UniProtKB	Chain	1	177	.	.	.	ID=PRO_0000199438;Note=Arginine metabolism regulation protein I	
+P07249	UniProtKB	Domain	80	134	.	.	.	Note=MADS-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00251	
+P07249	UniProtKB	Mutagenesis	94	94	.	.	.	Note=Decreases the physical interaction with ARG82. Abolishes the physical interaction with ARG82 and impairs function%3B when associated with D-95 and R-103. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10632874;Dbxref=PMID:10632874	
+P07249	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Decreases the physical interaction with ARG82. Abolishes the physical interaction with ARG82 and impairs function%3B when associated with G-94 and R-103. H->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10632874;Dbxref=PMID:10632874	
+P07249	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Abolishes the physical interaction with ARG82 and impairs function%3B when associated with G-94 and D-95. H->R	
+P07249	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Decreases the physical interaction with ARG82. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10632874;Dbxref=PMID:10632874	
+P07249	UniProtKB	Mutagenesis	115	115	.	.	.	Note=Decreases the physical interaction with ARG82. L->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10632874;Dbxref=PMID:10632874	
+P07249	UniProtKB	Mutagenesis	148	148	.	.	.	Note=Decreases the physical interaction with ARG82. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10632874;Dbxref=PMID:10632874	
+##sequence-region P38731 1 627
+P38731	UniProtKB	Chain	1	627	.	.	.	ID=PRO_0000084862;Note=Siderophore iron transporter ARN1	
+P38731	UniProtKB	Topological domain	1	70	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	92	110	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	132	135	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	157	167	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	189	197	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	219	231	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	253	290	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	291	311	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	312	323	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	324	344	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	345	367	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	368	388	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	389	398	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	399	419	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	420	424	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	425	445	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	446	454	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	455	475	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	476	563	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Transmembrane	564	584	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38731	UniProtKB	Topological domain	585	627	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53090 1 500
+P53090	UniProtKB	Chain	1	500	.	.	.	ID=PRO_0000064678;Note=Aromatic/aminoadipate aminotransferase 1	
+P53090	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53090	UniProtKB	Helix	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	15	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	24	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Turn	30	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	53	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	78	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	99	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	112	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	133	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	141	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	158	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	167	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	179	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	192	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	211	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Turn	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	228	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	244	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	263	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	277	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	293	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	297	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Turn	304	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	309	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	314	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	320	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Turn	332	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	339	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	395	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	406	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Turn	410	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	420	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	441	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	456	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Beta strand	466	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+P53090	UniProtKB	Helix	478	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5	
+##sequence-region P32449 1 370
+P32449	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32449	UniProtKB	Chain	2	370	.	.	.	ID=PRO_0000140851;Note=Phospho-2-dehydro-3-deoxyheptonate aldolase%2C tyrosine-inhibited	
+P32449	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32449	UniProtKB	Beta strand	25	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	34	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	45	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	68	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	81	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Turn	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	102	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	115	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Turn	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	134	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Turn	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	155	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	173	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Turn	179	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	185	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	198	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	209	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	223	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	231	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	244	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	259	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	276	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	282	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	292	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	309	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Beta strand	319	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	330	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF6	
+P32449	UniProtKB	Beta strand	339	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+P32449	UniProtKB	Helix	347	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8	
+##sequence-region P53946 1 755
+P53946	UniProtKB	Chain	1	755	.	.	.	ID=PRO_0000089104;Note=Actin-related protein 5	
+P53946	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53946	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53946	UniProtKB	Modified residue	383	383	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53946	UniProtKB	Cross-link	12	12	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q12386 1 881
+Q12386	UniProtKB	Chain	1	881	.	.	.	ID=PRO_0000089128;Note=Actin-like protein ARP8	
+Q12386	UniProtKB	Nucleotide binding	502	505	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12386	UniProtKB	Compositional bias	22	27	.	.	.	Note=Poly-Asp	
+Q12386	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12386	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12386	UniProtKB	Helix	265	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	268	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	275	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	285	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	289	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	295	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	299	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	321	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	352	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM7	
+Q12386	UniProtKB	Beta strand	357	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	367	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	386	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Turn	394	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	397	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	402	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	418	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	434	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	442	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	449	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	460	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	477	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	484	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	498	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	508	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	520	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	524	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	530	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	556	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	574	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	579	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	589	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	593	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	603	609	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	610	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	615	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	628	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Turn	640	642	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	651	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	662	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	668	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	703	716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	720	722	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	723	727	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	730	734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	735	738	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM7	
+Q12386	UniProtKB	Helix	742	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Turn	757	759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	763	778	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Beta strand	786	788	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Turn	793	797	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM7	
+Q12386	UniProtKB	Helix	798	817	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	838	840	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	841	849	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	853	858	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	862	868	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+Q12386	UniProtKB	Helix	869	874	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6	
+##sequence-region Q05123 1 467
+Q05123	UniProtKB	Chain	1	467	.	.	.	ID=PRO_0000089129;Note=Actin-like protein ARP9	
+Q05123	UniProtKB	Mutagenesis	337	337	.	.	.	Note=Impaired heterodimerization with ARP7%3B when associated with L-338. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12805231;Dbxref=PMID:12805231	
+Q05123	UniProtKB	Mutagenesis	338	338	.	.	.	Note=Impaired heterodimerization with ARP7%3B when associated with V-337. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12805231;Dbxref=PMID:12805231	
+Q05123	UniProtKB	Helix	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	10	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	16	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	35	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	41	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	51	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	76	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Turn	101	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	111	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	121	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	139	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	145	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	157	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	169	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	185	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	191	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	207	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	224	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE	
+Q05123	UniProtKB	Beta strand	229	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE	
+Q05123	UniProtKB	Beta strand	251	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE	
+Q05123	UniProtKB	Helix	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	282	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	291	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	296	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	303	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	323	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	333	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	338	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	345	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	363	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	379	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE	
+Q05123	UniProtKB	Beta strand	401	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	417	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Turn	425	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	428	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Beta strand	448	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	451	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q05123	UniProtKB	Helix	458	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+##sequence-region P38328 1 384
+P38328	UniProtKB	Chain	1	384	.	.	.	ID=PRO_0000050859;Note=Actin-related protein 2/3 complex subunit 1	
+P38328	UniProtKB	Repeat	61	99	.	.	.	Note=WD 1	
+P38328	UniProtKB	Repeat	105	146	.	.	.	Note=WD 2	
+P38328	UniProtKB	Repeat	151	190	.	.	.	Note=WD 3	
+P38328	UniProtKB	Repeat	212	251	.	.	.	Note=WD 4	
+P38328	UniProtKB	Repeat	349	383	.	.	.	Note=WD 5	
+##sequence-region P53731 1 342
+P53731	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000124041;Note=Actin-related protein 2/3 complex subunit 2	
+P53731	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53731	UniProtKB	Modified residue	324	324	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32447 1 279
+P32447	UniProtKB	Chain	1	279	.	.	.	ID=PRO_0000064695;Note=Histone chaperone ASF1	
+P32447	UniProtKB	Region	1	155	.	.	.	Note=Interaction with histone H3%2C histone H4%2C RAD53 and the RF-C complex	
+P32447	UniProtKB	Region	1	143	.	.	.	Note=Interaction with HIR1	
+P32447	UniProtKB	Coiled coil	192	243	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32447	UniProtKB	Compositional bias	170	242	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P32447	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Enhances transcriptional silencing. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17081973;Dbxref=PMID:17081973	
+P32447	UniProtKB	Mutagenesis	36	37	.	.	.	Note=Abrogates stimulation of replication-independent chromatin assembly by the HIR complex and abrogates telomeric silencing. HD->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14680630,ECO:0000269|PubMed:16303565;Dbxref=PMID:14680630,PMID:16303565	
+P32447	UniProtKB	Mutagenesis	37	37	.	.	.	Note=Reduces transcriptional silencing%3B when associated with R-39. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15840725;Dbxref=PMID:15840725	
+P32447	UniProtKB	Mutagenesis	39	39	.	.	.	Note=Reduces transcriptional silencing%3B when associated with R-37. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15840725;Dbxref=PMID:15840725	
+P32447	UniProtKB	Mutagenesis	45	45	.	.	.	Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16627621;Dbxref=PMID:16627621	
+P32447	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Abrogates interaction with histone H3 and histone H4 and enhances transcriptional silencing. Reduces acetylation of histone H3 on 'K-9' and 'K-56'%3B when associated with E-145 or E-147. S->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:17081973,PMID:17107956	
+P32447	UniProtKB	Mutagenesis	53	54	.	.	.	Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. HD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16627621;Dbxref=PMID:16627621	
+P32447	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Reduces transcriptional silencing. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15840725;Dbxref=PMID:15840725	
+P32447	UniProtKB	Mutagenesis	94	94	.	.	.	Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin%2C camptothecin%2C HU and MMS%3B when associated with D-96. V->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15840725,ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:15840725,PMID:16627621,PMID:17081973,PMID:17107956	
+P32447	UniProtKB	Mutagenesis	94	94	.	.	.	Note=Abrogates interaction with histone H3 and histone H4%2C abrogates transcriptional silencing%2C reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS. V->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15840725,ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:15840725,PMID:16627621,PMID:17081973,PMID:17107956	
+P32447	UniProtKB	Mutagenesis	96	96	.	.	.	Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin%2C camptothecin%2C HU and MMS%3B when associated with D-94. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16627621;Dbxref=PMID:16627621	
+P32447	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Reduces transcriptional silencing. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15840725;Dbxref=PMID:15840725	
+P32447	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Reduces interaction with histone H3 and histone H4%2C enhances transcriptional silencing and reduces transcriptional activation. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17081973;Dbxref=PMID:17081973	
+P32447	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Abrogates interaction with histone H3 and histone H4 and enhances transcriptional silencing. Abrogates transcriptional silencing%2C reduces transcriptional activation%2C reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS%3B when associated with E-145 or E-147. Y->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956	
+P32447	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin%2C camptothecin%2C HU and MMS. Y->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956	
+P32447	UniProtKB	Mutagenesis	145	145	.	.	.	Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin%2C camptothecin%2C HU and MMS%3B when associated with A-147. R->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956	
+P32447	UniProtKB	Mutagenesis	145	145	.	.	.	Note=Abrogates interaction with histone H3 and histone H4%2C abrogates transcriptional silencing%2C reduces transcriptional activation%2C reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS%3B when associated with R-48%3B E-112 or E-147. R->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956	
+P32447	UniProtKB	Mutagenesis	146	146	.	.	.	Note=Reduces interaction with histone H3 and histone H4%2C enhances transcriptional silencing and reduces transcriptional activation. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17081973;Dbxref=PMID:17081973	
+P32447	UniProtKB	Mutagenesis	147	147	.	.	.	Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin%2C camptothecin%2C HU and MMS%3B when associated with A-145. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956	
+P32447	UniProtKB	Mutagenesis	147	147	.	.	.	Note=Enhances transcriptional silencing. Abrogates interaction with histone H3 and histone H4%2C abrogates transcriptional silencing%2C reduces transcriptional activation%2C reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS%3B when associated with R-48%3B A-112 or E-145. T->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956	
+P32447	UniProtKB	Mutagenesis	152	152	.	.	.	Note=Impairs interaction with histone H3 and RAD53 and enhances silencing at telomeres and mating-type loci. V->VVFLHY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16582440;Dbxref=PMID:16582440	
+P32447	UniProtKB	Beta strand	3	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Beta strand	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Beta strand	22	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Beta strand	38	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Helix	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HUE	
+P32447	UniProtKB	Beta strand	55	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Beta strand	67	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Helix	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Helix	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Beta strand	93	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Beta strand	104	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Helix	120	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Beta strand	135	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Beta strand	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC	
+P32447	UniProtKB	Turn	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HUE	
+##sequence-region P38986 1 381
+P38986	UniProtKB	Chain	1	381	.	.	.	ID=PRO_0000171091;Note=L-asparaginase 1	
+P38986	UniProtKB	Domain	54	378	.	.	.	Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068	
+P38986	UniProtKB	Region	141	142	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38986	UniProtKB	Active site	64	64	.	.	.	Note=O-isoaspartyl threonine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10099,ECO:0000255|PROSITE-ProRule:PRU10100	
+P38986	UniProtKB	Binding site	110	110	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38986	UniProtKB	Modified residue	350	350	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38986	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Almost no activity. A->V	
+##sequence-region P40024 1 610
+P40024	UniProtKB	Chain	1	610	.	.	.	ID=PRO_0000093463;Note=ABC transporter ATP-binding protein ARB1	
+P40024	UniProtKB	Domain	82	323	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P40024	UniProtKB	Domain	393	610	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P40024	UniProtKB	Nucleotide binding	114	121	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P40024	UniProtKB	Nucleotide binding	428	435	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P40024	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40024	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40024	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40024	UniProtKB	Modified residue	446	446	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P11076 1 181
+P11076	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+P11076	UniProtKB	Chain	2	181	.	.	.	ID=PRO_0000207418;Note=ADP-ribosylation factor 1	
+P11076	UniProtKB	Nucleotide binding	25	32	.	.	.	Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20601958;Dbxref=PMID:20601958	
+P11076	UniProtKB	Nucleotide binding	126	129	.	.	.	Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20601958;Dbxref=PMID:20601958	
+P11076	UniProtKB	Nucleotide binding	160	161	.	.	.	Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20601958;Dbxref=PMID:20601958	
+P11076	UniProtKB	Binding site	48	48	.	.	.	Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20601958;Dbxref=PMID:20601958	
+P11076	UniProtKB	Binding site	70	70	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20601958;Dbxref=PMID:20601958	
+P11076	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19141284,ECO:0000269|PubMed:20601958;Dbxref=PMID:19141284,PMID:20601958	
+P11076	UniProtKB	Cross-link	127	127	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P11076	UniProtKB	Beta strand	4	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K5U	
+P11076	UniProtKB	Helix	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KSQ	
+P11076	UniProtKB	Turn	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KSQ	
+P11076	UniProtKB	Beta strand	19	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Turn	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KSQ	
+P11076	UniProtKB	Helix	30	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Beta strand	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K5U	
+P11076	UniProtKB	Beta strand	49	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Beta strand	61	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Helix	72	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Helix	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Helix	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Beta strand	86	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Beta strand	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Helix	100	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Beta strand	120	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Helix	136	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Helix	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Beta strand	153	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Turn	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Helix	166	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ	
+P11076	UniProtKB	Turn	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KSQ	
+##sequence-region P00812 1 333
+P00812	UniProtKB	Chain	1	333	.	.	.	ID=PRO_0000173711;Note=Arginase	
+P00812	UniProtKB	Region	148	152	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53608	
+P00812	UniProtKB	Region	159	161	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53608	
+P00812	UniProtKB	Metal binding	123	123	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742	
+P00812	UniProtKB	Metal binding	146	146	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742	
+P00812	UniProtKB	Metal binding	146	146	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742	
+P00812	UniProtKB	Metal binding	148	148	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742	
+P00812	UniProtKB	Metal binding	150	150	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742	
+P00812	UniProtKB	Metal binding	256	256	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742	
+P00812	UniProtKB	Metal binding	256	256	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742	
+P00812	UniProtKB	Metal binding	258	258	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742	
+P00812	UniProtKB	Binding site	205	205	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53608	
+P00812	UniProtKB	Binding site	270	270	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53608	
+P00812	UniProtKB	Binding site	301	301	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53608	
+P00812	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P00812	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00812	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00812	UniProtKB	Modified residue	270	270	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P08566 1 1588
+P08566	UniProtKB	Chain	1	1588	.	.	.	ID=PRO_0000140862;Note=Pentafunctional AROM polypeptide	
+P08566	UniProtKB	Nucleotide binding	43	45	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Nucleotide binding	78	81	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Nucleotide binding	109	111	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Nucleotide binding	134	135	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Nucleotide binding	174	177	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Nucleotide binding	895	902	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Region	1	392	.	.	.	Note=3-dehydroquinate synthase	
+P08566	UniProtKB	Region	189	192	.	.	.	Note=Substrate binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Region	272	276	.	.	.	Note=Substrate binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Region	405	871	.	.	.	Note=EPSP synthase	
+P08566	UniProtKB	Region	890	1080	.	.	.	Note=Shikimate kinase	
+P08566	UniProtKB	Region	1081	1293	.	.	.	Note=3-dehydroquinase	
+P08566	UniProtKB	Region	1306	1588	.	.	.	Note=Shikimate dehydrogenase	
+P08566	UniProtKB	Active site	268	268	.	.	.	Note=Proton acceptor%3B for 3-dehydroquinate synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Active site	283	283	.	.	.	Note=Proton acceptor%3B for 3-dehydroquinate synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Active site	853	853	.	.	.	Note=For EPSP synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Active site	1198	1198	.	.	.	Note=Proton acceptor%3B for 3-dehydroquinate dehydratase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Active site	1227	1227	.	.	.	Note=Schiff-base intermediate with substrate%3B for 3-dehydroquinate dehydratase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Metal binding	189	189	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Metal binding	279	279	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Metal binding	295	295	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Binding site	114	114	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Binding site	125	125	.	.	.	Note=Substrate 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Binding site	141	141	.	.	.	Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Binding site	147	147	.	.	.	Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Binding site	156	156	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Binding site	157	157	.	.	.	Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Binding site	185	185	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Binding site	258	258	.	.	.	Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Binding site	279	279	.	.	.	Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Binding site	295	295	.	.	.	Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+P08566	UniProtKB	Binding site	364	364	.	.	.	Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143	
+##sequence-region P15274 1 810
+P15274	UniProtKB	Chain	1	810	.	.	.	ID=PRO_0000194414;Note=AMP deaminase	
+P15274	UniProtKB	Region	433	438	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15274	UniProtKB	Region	708	711	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15274	UniProtKB	Active site	652	652	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10104	
+P15274	UniProtKB	Metal binding	362	362	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15274	UniProtKB	Metal binding	364	364	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15274	UniProtKB	Metal binding	630	630	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15274	UniProtKB	Metal binding	707	707	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15274	UniProtKB	Binding site	364	364	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15274	UniProtKB	Binding site	633	633	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15274	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P15274	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P15274	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P15274	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950	
+P15274	UniProtKB	Sequence conflict	568	568	.	.	.	Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08951 1 932
+Q08951	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08951	UniProtKB	Chain	2	932	.	.	.	ID=PRO_0000227676;Note=AP-3 complex subunit delta	
+Q08951	UniProtKB	Repeat	157	194	.	.	.	Note=HEAT 1	
+Q08951	UniProtKB	Repeat	196	231	.	.	.	Note=HEAT 2	
+Q08951	UniProtKB	Repeat	233	269	.	.	.	Note=HEAT 3	
+Q08951	UniProtKB	Repeat	270	307	.	.	.	Note=HEAT 4	
+Q08951	UniProtKB	Repeat	310	346	.	.	.	Note=HEAT 5	
+Q08951	UniProtKB	Repeat	347	384	.	.	.	Note=HEAT 6	
+Q08951	UniProtKB	Repeat	386	425	.	.	.	Note=HEAT 7	
+Q08951	UniProtKB	Repeat	427	466	.	.	.	Note=HEAT 8	
+Q08951	UniProtKB	Repeat	490	527	.	.	.	Note=HEAT 9	
+Q08951	UniProtKB	Repeat	528	564	.	.	.	Note=HEAT 10	
+Q08951	UniProtKB	Repeat	570	601	.	.	.	Note=HEAT 11	
+Q08951	UniProtKB	Repeat	602	638	.	.	.	Note=HEAT 12	
+Q08951	UniProtKB	Coiled coil	858	878	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08951	UniProtKB	Compositional bias	784	791	.	.	.	Note=Poly-Lys	
+Q08951	UniProtKB	Compositional bias	897	916	.	.	.	Note=Poly-Lys	
+Q08951	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08951	UniProtKB	Modified residue	700	700	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08951	UniProtKB	Modified residue	727	727	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08951	UniProtKB	Modified residue	767	767	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q08951	UniProtKB	Modified residue	770	770	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08951	UniProtKB	Modified residue	773	773	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08951	UniProtKB	Modified residue	798	798	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08951	UniProtKB	Modified residue	888	888	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q08951	UniProtKB	Modified residue	918	918	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P22108 1 325
+P22108	UniProtKB	Chain	1	325	.	.	.	ID=PRO_0000064613;Note=Diadenosine 5'%2C5'''-P1%2CP4-tetraphosphate phosphorylase 2	
+P22108	UniProtKB	Region	92	93	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156	
+P22108	UniProtKB	Region	154	157	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156	
+P22108	UniProtKB	Region	277	279	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156	
+P22108	UniProtKB	Active site	161	161	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156	
+P22108	UniProtKB	Binding site	53	53	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156	
+P22108	UniProtKB	Binding site	148	148	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156	
+P22108	UniProtKB	Binding site	163	163	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156	
+P22108	UniProtKB	Binding site	284	284	.	.	.	Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156	
+P22108	UniProtKB	Binding site	288	288	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156	
+P22108	UniProtKB	Mutagenesis	161	161	.	.	.	Note=Completely abolishes catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156	
+P22108	UniProtKB	Helix	6	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5W	
+P22108	UniProtKB	Beta strand	29	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Turn	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	41	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Helix	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Turn	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Helix	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	81	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	101	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Helix	117	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	143	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Turn	151	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	161	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Helix	174	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5V	
+P22108	UniProtKB	Beta strand	197	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Helix	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Helix	217	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Turn	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	249	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	255	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Turn	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Helix	278	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Beta strand	284	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Helix	290	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Helix	301	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+P22108	UniProtKB	Helix	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T	
+##sequence-region Q04601 1 652
+Q04601	UniProtKB	Chain	1	652	.	.	.	ID=PRO_0000064623;Note=Anaphase-promoting complex subunit 4	
+##sequence-region Q08683 1 685
+Q08683	UniProtKB	Chain	1	685	.	.	.	ID=PRO_0000064625;Note=Anaphase-promoting complex subunit 5	
+Q08683	UniProtKB	Compositional bias	497	500	.	.	.	Note=Poly-Ser	
+##sequence-region Q12107 1 265
+Q12107	UniProtKB	Chain	1	265	.	.	.	ID=PRO_0000064626;Note=Anaphase-promoting complex subunit 9	
+##sequence-region P53933 1 587
+P53933	UniProtKB	Chain	1	587	.	.	.	ID=PRO_0000076180;Note=Phosphatidate phosphatase APP1	
+P53933	UniProtKB	Region	467	483	.	.	.	Note=Interaction with SH3 domain of ABP1	
+P53933	UniProtKB	Motif	281	285	.	.	.	Note=DXDXT motif	
+P53933	UniProtKB	Compositional bias	469	475	.	.	.	Note=Poly-Pro	
+P53933	UniProtKB	Mutagenesis	281	281	.	.	.	Note=Abolishes PAP activity. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23071111;Dbxref=PMID:23071111	
+##sequence-region P47036 1 138
+P47036	UniProtKB	Chain	1	138	.	.	.	ID=PRO_0000203053;Note=Putative uncharacterized protein APQ13	
+P47036	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36973 1 181
+P36973	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36973	UniProtKB	Chain	2	181	.	.	.	ID=PRO_0000149518;Note=Adenine phosphoribosyltransferase 2	
+P36973	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36973	UniProtKB	Sequence conflict	57	57	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25628 1 610
+P25628	UniProtKB	Chain	1	610	.	.	.	ID=PRO_0000207648;Note=Sterol O-acyltransferase 1	
+P25628	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25628	UniProtKB	Transmembrane	229	249	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25628	UniProtKB	Transmembrane	264	284	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25628	UniProtKB	Transmembrane	371	391	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25628	UniProtKB	Transmembrane	409	429	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25628	UniProtKB	Transmembrane	535	555	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25628	UniProtKB	Transmembrane	590	610	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25628	UniProtKB	Active site	547	547	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25628	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P25628	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P53111 1 347
+P53111	UniProtKB	Chain	1	347	.	.	.	ID=PRO_0000215578;Note=NADPH-dependent aldehyde reductase ARI1	
+##sequence-region P36090 1 516
+P36090	UniProtKB	Chain	1	516	.	.	.	ID=PRO_0000203181;Note=Uncharacterized protein ANR2	
+P36090	UniProtKB	Domain	31	185	.	.	.	Note=uDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304	
+P36090	UniProtKB	Domain	211	365	.	.	.	Note=cDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304	
+P36090	UniProtKB	Domain	367	513	.	.	.	Note=dDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304	
+P36090	UniProtKB	Lipidation	511	511	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36090	UniProtKB	Lipidation	516	516	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46682 1 809
+P46682	UniProtKB	Chain	1	809	.	.	.	ID=PRO_0000193757;Note=AP-3 complex subunit beta	
+P46682	UniProtKB	Repeat	37	76	.	.	.	Note=HEAT 1	
+P46682	UniProtKB	Repeat	112	151	.	.	.	Note=HEAT 2	
+P46682	UniProtKB	Repeat	153	186	.	.	.	Note=HEAT 3	
+P46682	UniProtKB	Repeat	187	224	.	.	.	Note=HEAT 4	
+P46682	UniProtKB	Repeat	524	561	.	.	.	Note=HEAT 5	
+P46682	UniProtKB	Compositional bias	771	789	.	.	.	Note=Asp/Glu-rich (acidic)	
+P46682	UniProtKB	Modified residue	693	693	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46682	UniProtKB	Modified residue	698	698	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46682	UniProtKB	Modified residue	724	724	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46682	UniProtKB	Modified residue	726	726	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P46682	UniProtKB	Sequence conflict	27	35	.	.	.	Note=TSKLGESSY->PLSWVNPP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46682	UniProtKB	Sequence conflict	724	724	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46682	UniProtKB	Sequence conflict	798	802	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12157 1 165
+Q12157	UniProtKB	Chain	1	165	.	.	.	ID=PRO_0000055751;Note=Anaphase-promoting complex subunit 11	
+Q12157	UniProtKB	Zinc finger	52	95	.	.	.	Note=RING-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q12157	UniProtKB	Mutagenesis	10	10	.	.	.	Note=In APC11-13%3B G2/M cell cycle arrest at 37 degrees Celsius. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888670;Dbxref=PMID:10888670	
+Q12157	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888670;Dbxref=PMID:10888670	
+Q12157	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888670;Dbxref=PMID:10888670	
+Q12157	UniProtKB	Mutagenesis	81	81	.	.	.	Note=Loss of function. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888670;Dbxref=PMID:10888670	
+Q12157	UniProtKB	Mutagenesis	91	91	.	.	.	Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888670;Dbxref=PMID:10888670	
+##sequence-region Q04413 1 109
+Q04413	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299768;Note=Uncharacterized protein API2	
+##sequence-region P04076 1 463
+P04076	UniProtKB	Chain	1	463	.	.	.	ID=PRO_0000137727;Note=Argininosuccinate lyase	
+P04076	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04076	UniProtKB	Sequence conflict	103	103	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P08019 1 549
+P08019	UniProtKB	Chain	1	549	.	.	.	ID=PRO_0000186120;Note=Glucoamylase%2C intracellular sporulation-specific	
+P08019	UniProtKB	Active site	261	261	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10051	
+P08019	UniProtKB	Active site	264	264	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10051	
+P08019	UniProtKB	Binding site	198	198	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08019	UniProtKB	Sequence conflict	184	184	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08019	UniProtKB	Sequence conflict	504	549	.	.	.	Note=HVGTDGELSEQFNKYTGFMQGAQHLTWSYTSFWDAYQIRQEVLQSL->TWEQTGN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32629 1 500
+P32629	UniProtKB	Chain	1	500	.	.	.	ID=PRO_0000193668;Note=Mannan polymerase II complex ANP1 subunit	
+P32629	UniProtKB	Topological domain	1	15	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32629	UniProtKB	Transmembrane	16	27	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P32629	UniProtKB	Topological domain	28	500	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32629	UniProtKB	Compositional bias	446	473	.	.	.	Note=Gln-rich	
+P32629	UniProtKB	Sequence conflict	220	224	.	.	.	Note=HHDKD->QSGQGN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32629	UniProtKB	Sequence conflict	220	224	.	.	.	Note=HHDKD->QSGQGN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32629	UniProtKB	Sequence conflict	313	313	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32629	UniProtKB	Sequence conflict	313	313	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32629	UniProtKB	Sequence conflict	313	313	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32629	UniProtKB	Sequence conflict	313	313	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32629	UniProtKB	Sequence conflict	472	500	.	.	.	Note=PQGKPLDDNDKNKKKHPKEVPLDFDPDRN->RRGNLLMTTTRTRKNILKKFH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32629	UniProtKB	Sequence conflict	472	500	.	.	.	Note=PQGKPLDDNDKNKKKHPKEVPLDFDPDRN->RRGNLLMTTTRTRKNILKKFH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38832 1 159
+P38832	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38832	UniProtKB	Chain	21	137	.	.	.	ID=PRO_0000203777;Note=Probable GPI-anchored protein ANS1	
+P38832	UniProtKB	Propeptide	138	159	.	.	.	ID=PRO_0000402190;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38832	UniProtKB	Repeat	101	114	.	.	.	Note=PIR1/2/3	
+P38832	UniProtKB	Lipidation	137	137	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38153 1 483
+P38153	UniProtKB	Chain	1	483	.	.	.	ID=PRO_0000193794;Note=AP-3 complex subunit mu	
+P38153	UniProtKB	Domain	211	482	.	.	.	Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404	
+P38153	UniProtKB	Sequence conflict	35	36	.	.	.	Note=QS->RT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38153	UniProtKB	Sequence conflict	35	36	.	.	.	Note=QS->RT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P37302 1 537
+P37302	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37302	UniProtKB	Propeptide	22	56	.	.	.	ID=PRO_0000026847;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37302	UniProtKB	Chain	57	537	.	.	.	ID=PRO_0000026848;Note=Aminopeptidase Y	
+P37302	UniProtKB	Active site	358	358	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P37302	UniProtKB	Metal binding	314	314	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P37302	UniProtKB	Metal binding	326	326	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P37302	UniProtKB	Metal binding	326	326	.	.	.	Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P37302	UniProtKB	Metal binding	359	359	.	.	.	Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P37302	UniProtKB	Metal binding	387	387	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P37302	UniProtKB	Metal binding	472	472	.	.	.	Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P37302	UniProtKB	Site	471	471	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P37302	UniProtKB	Glycosylation	85	85	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37302	UniProtKB	Glycosylation	96	96	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37302	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37302	UniProtKB	Glycosylation	150	150	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37302	UniProtKB	Glycosylation	162	162	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37302	UniProtKB	Glycosylation	371	371	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37302	UniProtKB	Glycosylation	427	427	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37302	UniProtKB	Glycosylation	480	480	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37302	UniProtKB	Sequence conflict	14	15	.	.	.	Note=YA->LR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53940 1 528
+P53940	UniProtKB	Chain	1	528	.	.	.	ID=PRO_0000071155;Note=J domain-containing protein APJ1	
+P53940	UniProtKB	Domain	4	73	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P53940	UniProtKB	Repeat	206	213	.	.	.	Note=CXXCXGXG motif	
+P53940	UniProtKB	Repeat	218	225	.	.	.	Note=CXXCXGXG motif	
+P53940	UniProtKB	Repeat	246	253	.	.	.	Note=CXXCXGXG motif	
+P53940	UniProtKB	Repeat	262	269	.	.	.	Note=CXXCXGXG motif	
+P53940	UniProtKB	Zinc finger	193	274	.	.	.	Note=CR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00546	
+##sequence-region P38700 1 605
+P38700	UniProtKB	Chain	1	605	.	.	.	ID=PRO_0000193793;Note=Adaptin medium chain homolog APM2	
+P38700	UniProtKB	Domain	269	604	.	.	.	Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404	
+##sequence-region P22936 1 367
+P22936	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3056935;Dbxref=PMID:3056935	
+P22936	UniProtKB	Chain	2	367	.	.	.	ID=PRO_0000190898;Note=DNA-(apurinic or apyrimidinic site) lyase 1	
+P22936	UniProtKB	Metal binding	83	83	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22936	UniProtKB	Metal binding	123	123	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22936	UniProtKB	Metal binding	158	158	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22936	UniProtKB	Metal binding	158	158	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22936	UniProtKB	Metal binding	192	192	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22936	UniProtKB	Metal binding	195	195	.	.	.	Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22936	UniProtKB	Metal binding	229	229	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22936	UniProtKB	Metal binding	242	242	.	.	.	Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22936	UniProtKB	Metal binding	244	244	.	.	.	Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22936	UniProtKB	Metal binding	274	274	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22936	UniProtKB	Modified residue	356	356	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22936	UniProtKB	Sequence conflict	239	239	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53943 1 586
+P53943	UniProtKB	Chain	1	586	.	.	.	ID=PRO_0000173443;Note=Probable transporter AQR1	
+P53943	UniProtKB	Topological domain	1	99	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Topological domain	121	139	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Topological domain	161	166	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Transmembrane	167	187	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Topological domain	188	188	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Topological domain	210	225	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Transmembrane	226	246	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Topological domain	247	255	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Transmembrane	256	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Topological domain	277	334	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Transmembrane	335	355	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Topological domain	356	374	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Transmembrane	375	395	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Topological domain	396	433	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Transmembrane	434	454	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Topological domain	455	459	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Transmembrane	460	480	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Topological domain	481	523	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Transmembrane	524	544	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Topological domain	545	586	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53943	UniProtKB	Sequence conflict	174	174	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CD90 1 149
+P0CD90	UniProtKB	Chain	1	149	.	.	.	ID=PRO_0000391651;Note=Aquaporin-like protein 2	
+P0CD90	UniProtKB	Topological domain	1	47	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD90	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD90	UniProtKB	Topological domain	69	89	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD90	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD90	UniProtKB	Topological domain	111	149	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04371 1 470
+Q04371	UniProtKB	Chain	1	470	.	.	.	ID=PRO_0000203271;Note=Protein-glutamate O-methyltransferase	
+Q04371	UniProtKB	Binding site	259	259	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H993	
+Q04371	UniProtKB	Binding site	292	292	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H993	
+Q04371	UniProtKB	Helix	15	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	23	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	47	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	77	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	88	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	106	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Turn	125	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	134	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	145	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	175	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	191	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	196	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	204	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	210	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	223	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	228	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	248	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	258	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	277	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Turn	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	295	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Turn	308	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	319	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	339	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	346	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	354	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	363	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	366	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	377	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	383	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	402	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	407	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	416	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	434	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	444	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Helix	450	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	456	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+Q04371	UniProtKB	Beta strand	460	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1	
+##sequence-region Q06408 1 635
+Q06408	UniProtKB	Chain	1	635	.	.	.	ID=PRO_0000090835;Note=Transaminated amino acid decarboxylase	
+Q06408	UniProtKB	Cross-link	588	588	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region Q04052 1 950
+Q04052	UniProtKB	Chain	1	950	.	.	.	ID=PRO_0000114938;Note=Transcriptional activator ARO80	
+Q04052	UniProtKB	DNA binding	25	58	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+Q04052	UniProtKB	Compositional bias	921	943	.	.	.	Note=Asn-rich	
+##sequence-region P38080 1 1108
+P38080	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38080	UniProtKB	Chain	2	1108	.	.	.	ID=PRO_0000085603;Note=Serine/threonine-protein kinase AKL1	
+P38080	UniProtKB	Domain	35	319	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38080	UniProtKB	Nucleotide binding	41	49	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38080	UniProtKB	Active site	181	181	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P38080	UniProtKB	Binding site	70	70	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38080	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38080	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38080	UniProtKB	Modified residue	407	407	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38080	UniProtKB	Modified residue	471	471	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38080	UniProtKB	Modified residue	504	504	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38080	UniProtKB	Modified residue	541	541	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38080	UniProtKB	Modified residue	574	574	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38080	UniProtKB	Modified residue	801	801	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38080	UniProtKB	Modified residue	846	846	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38080	UniProtKB	Modified residue	953	953	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38080	UniProtKB	Modified residue	960	960	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38080	UniProtKB	Modified residue	1048	1048	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38080	UniProtKB	Modified residue	1072	1072	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38080	UniProtKB	Cross-link	1008	1008	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P38080	UniProtKB	Cross-link	1046	1046	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region P54115 1 500
+P54115	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9392076;Dbxref=PMID:9392076	
+P54115	UniProtKB	Chain	2	500	.	.	.	ID=PRO_0000056441;Note=Magnesium-activated aldehyde dehydrogenase%2C cytosolic	
+P54115	UniProtKB	Nucleotide binding	249	254	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54115	UniProtKB	Active site	272	272	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007	
+P54115	UniProtKB	Active site	306	306	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007	
+P54115	UniProtKB	Site	173	173	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54115	UniProtKB	Cross-link	3	3	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P54115	UniProtKB	Cross-link	142	142	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P54115	UniProtKB	Cross-link	196	196	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P54115	UniProtKB	Sequence conflict	121	121	.	.	.	Note=L->FK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P16661 1 449
+P16661	UniProtKB	Chain	1	449	.	.	.	ID=PRO_0000080259;Note=Chitobiosyldiphosphodolichol beta-mannosyltransferase	
+P16661	UniProtKB	Topological domain	1	7	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16661	UniProtKB	Transmembrane	8	34	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16661	UniProtKB	Topological domain	35	449	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16661	UniProtKB	Region	435	449	.	.	.	Note=Required for oligomerization	
+P16661	UniProtKB	Motif	21	32	.	.	.	Note=Dolichol recognition;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16661	UniProtKB	Glycosylation	88	88	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16661	UniProtKB	Glycosylation	199	199	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16661	UniProtKB	Glycosylation	425	425	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16661	UniProtKB	Mutagenesis	278	278	.	.	.	Note=Abolishes enzymatic activity. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044395;Dbxref=PMID:15044395	
+P16661	UniProtKB	Mutagenesis	310	310	.	.	.	Note=Abolishes enzymatic activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044395;Dbxref=PMID:15044395	
+P16661	UniProtKB	Mutagenesis	356	356	.	.	.	Note=Abolishes enzymatic activity. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044395;Dbxref=PMID:15044395	
+P16661	UniProtKB	Mutagenesis	363	363	.	.	.	Note=No effect on enzymatic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044395;Dbxref=PMID:15044395	
+P16661	UniProtKB	Mutagenesis	370	370	.	.	.	Note=No effect on enzymatic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044395;Dbxref=PMID:15044395	
+##sequence-region P36000 1 726
+P36000	UniProtKB	Chain	1	726	.	.	.	ID=PRO_0000193753;Note=AP-1 complex subunit beta-1	
+##sequence-region P19880 1 650
+P19880	UniProtKB	Chain	1	650	.	.	.	ID=PRO_0000076521;Note=AP-1-like transcription factor YAP1	
+P19880	UniProtKB	Domain	64	127	.	.	.	Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P19880	UniProtKB	Region	67	90	.	.	.	Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P19880	UniProtKB	Region	92	120	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P19880	UniProtKB	Region	220	378	.	.	.	Note=Transcription activation 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8182076;Dbxref=PMID:8182076	
+P19880	UniProtKB	Region	303	315	.	.	.	Note=n-CRD;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15318225;Dbxref=PMID:15318225	
+P19880	UniProtKB	Region	430	537	.	.	.	Note=Transcription activation 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8182076;Dbxref=PMID:8182076	
+P19880	UniProtKB	Region	598	629	.	.	.	Note=c-CRD;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15318225;Dbxref=PMID:15318225	
+P19880	UniProtKB	Motif	35	42	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00768	
+P19880	UniProtKB	Motif	68	75	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00768	
+P19880	UniProtKB	Motif	614	621	.	.	.	Note=Nuclear export signal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9857197;Dbxref=PMID:9857197	
+P19880	UniProtKB	Compositional bias	411	414	.	.	.	Note=Poly-Asn	
+P19880	UniProtKB	Compositional bias	517	521	.	.	.	Note=Poly-Asp	
+P19880	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19880	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+P19880	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19880	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19880	UniProtKB	Modified residue	204	204	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19880	UniProtKB	Modified residue	372	372	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P19880	UniProtKB	Modified residue	528	528	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P19880	UniProtKB	Disulfide bond	303	598	.	.	.	Note=In peroxide stress-induced nuclear retained form%3B alternate;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1SSE,ECO:0000269|PubMed:12437921,ECO:0000269|PubMed:14556629,ECO:0000269|PubMed:15318225,ECO:0000269|PubMed:17707237;Dbxref=PMID:12437921,PMID:14556629,PMID:15318225,PMID:17707237	
+P19880	UniProtKB	Disulfide bond	310	629	.	.	.	Note=In peroxide stress-induced nuclear retained form%3B alternate;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1SSE,ECO:0000269|PubMed:14556629,ECO:0000269|PubMed:15318225,ECO:0000269|PubMed:17707237;Dbxref=PMID:14556629,PMID:15318225,PMID:17707237	
+P19880	UniProtKB	Disulfide bond	598	629	.	.	.	Note=In diamide-induced nuclear retained form%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11509657;Dbxref=PMID:11509657	
+P19880	UniProtKB	Disulfide bond	598	620	.	.	.	Note=In diamide-induced nuclear retained form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11509657;Dbxref=PMID:11509657	
+P19880	UniProtKB	Disulfide bond	598	598	.	.	.	Note=Interchain (with C-36 in HYR1)%3B transient%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12437921,ECO:0000269|PubMed:14556629,ECO:0000269|PubMed:17720812;Dbxref=PMID:12437921,PMID:14556629,PMID:17720812	
+P19880	UniProtKB	Disulfide bond	620	629	.	.	.	Note=In diamide-induced nuclear retained form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11509657;Dbxref=PMID:11509657	
+P19880	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Dominant negative transcription activator. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8182076;Dbxref=PMID:8182076	
+P19880	UniProtKB	Mutagenesis	598	598	.	.	.	Note=Does not alter nuclear location and transcription activation. Constitutively cytoplasmic%3B when associated with A-620 and T-629. C->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9130715;Dbxref=PMID:9130715	
+P19880	UniProtKB	Mutagenesis	620	620	.	.	.	Note=Does not alter nuclear location and transcription activation. Constitutively cytoplasmic%3B when associated with T-598 and T-629. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9130715;Dbxref=PMID:9130715	
+P19880	UniProtKB	Mutagenesis	620	620	.	.	.	Note=Constitutive nuclear location and transcription activation. C->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9130715;Dbxref=PMID:9130715	
+P19880	UniProtKB	Mutagenesis	629	629	.	.	.	Note=Does not alter nuclear location and transcription activation. Constitutively cytoplasmic%3B when associated with T-598 and T-620. C->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9130715;Dbxref=PMID:9130715	
+P19880	UniProtKB	Sequence conflict	316	316	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19880	UniProtKB	Sequence conflict	586	586	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19880	UniProtKB	Sequence conflict	648	648	.	.	.	Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19880	UniProtKB	Helix	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE	
+P19880	UniProtKB	Beta strand	292	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE	
+P19880	UniProtKB	Beta strand	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE	
+P19880	UniProtKB	Helix	301	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE	
+P19880	UniProtKB	Helix	598	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE	
+P19880	UniProtKB	Helix	616	623	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE	
+P19880	UniProtKB	Turn	624	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE	
+P19880	UniProtKB	Helix	638	646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE	
+##sequence-region P27351 1 700
+P27351	UniProtKB	Chain	1	700	.	.	.	ID=PRO_0000193755;Note=AP-2 complex subunit beta	
+P27351	UniProtKB	Modified residue	649	649	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P27351	UniProtKB	Modified residue	652	652	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P27351	UniProtKB	Modified residue	683	683	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P27351	UniProtKB	Sequence conflict	55	55	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27351	UniProtKB	Sequence conflict	484	484	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27351	UniProtKB	Sequence conflict	504	504	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27351	UniProtKB	Sequence conflict	521	521	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27351	UniProtKB	Sequence conflict	629	629	.	.	.	Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99186 1 491
+Q99186	UniProtKB	Chain	1	491	.	.	.	ID=PRO_0000193780;Note=AP-2 complex subunit mu	
+Q99186	UniProtKB	Domain	209	490	.	.	.	Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404	
+Q99186	UniProtKB	Modified residue	179	179	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q99186	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q99186	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53068 1 250
+P53068	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000174016;Note=Anaphase-promoting complex subunit DOC1	
+P53068	UniProtKB	Domain	60	246	.	.	.	Note=DOC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00614	
+P53068	UniProtKB	Mutagenesis	94	94	.	.	.	Note=In DOC1-1%3B G2/M cell cycle arrest at 37 degrees Celsius. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9348530;Dbxref=PMID:9348530	
+P53068	UniProtKB	Beta strand	31	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Turn	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Helix	62	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Beta strand	79	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Helix	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Beta strand	88	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Helix	101	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Beta strand	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Beta strand	117	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Beta strand	135	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Helix	142	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Helix	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Beta strand	149	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Turn	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Beta strand	165	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Beta strand	176	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Beta strand	193	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Beta strand	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+P53068	UniProtKB	Beta strand	217	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP	
+##sequence-region P0CD91 1 305
+P0CD91	UniProtKB	Chain	1	305	.	.	.	ID=PRO_0000064076;Note=Aquaporin-1	
+P0CD91	UniProtKB	Topological domain	1	48	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Topological domain	70	91	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Topological domain	113	136	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Transmembrane	137	157	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Topological domain	158	176	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Topological domain	198	203	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Topological domain	225	248	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Transmembrane	249	269	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Topological domain	270	305	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD91	UniProtKB	Motif	118	120	.	.	.	Note=NPA 1	
+P0CD91	UniProtKB	Motif	230	232	.	.	.	Note=NPA 2	
+P0CD91	UniProtKB	Mutagenesis	121	121	.	.	.	Note=Restores water permeability%3B when associated with P-255. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9765289;Dbxref=PMID:9765289	
+P0CD91	UniProtKB	Mutagenesis	255	255	.	.	.	Note=Restores water permeability%3B when associated with V-121. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9765289;Dbxref=PMID:9765289	
+##sequence-region P38115 1 344
+P38115	UniProtKB	Chain	1	344	.	.	.	ID=PRO_0000124610;Note=D-arabinose dehydrogenase [NAD(P)+] heavy chain	
+P38115	UniProtKB	Nucleotide binding	241	295	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38115	UniProtKB	Active site	71	71	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38115	UniProtKB	Binding site	131	131	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38115	UniProtKB	Site	100	100	.	.	.	Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38115	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P38115	UniProtKB	Sequence conflict	56	62	.	.	.	Note=AAIKAGY->LQSKLDN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38115	UniProtKB	Sequence conflict	71	73	.	.	.	Note=YET->SR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38115	UniProtKB	Helix	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Beta strand	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Beta strand	32	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	44	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	50	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Beta strand	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	74	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Beta strand	96	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	109	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Beta strand	126	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	167	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Beta strand	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJC	
+P38115	UniProtKB	Beta strand	189	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	196	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Beta strand	211	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	224	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Beta strand	236	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	249	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	254	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	267	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	289	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	303	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	324	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+P38115	UniProtKB	Helix	339	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR	
+##sequence-region P46672 1 376
+P46672	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000087409;Note=tRNA-aminoacylation cofactor ARC1	
+P46672	UniProtKB	Domain	205	307	.	.	.	Note=tRNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00209	
+P46672	UniProtKB	Region	22	46	.	.	.	Note=Interaction with methionyl-tRNA synthetase MES1	
+P46672	UniProtKB	Region	52	61	.	.	.	Note=Interaction with glutamyl-tRNA synthetase GUS1	
+P46672	UniProtKB	Region	91	121	.	.	.	Note=Interaction with glutamyl-tRNA synthetase GUS1	
+P46672	UniProtKB	Mutagenesis	26	26	.	.	.	Note=Abolishes interaction with MES1. A->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16914447;Dbxref=PMID:16914447	
+P46672	UniProtKB	Mutagenesis	100	100	.	.	.	Note=Abolishes interaction with GUS1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16914447;Dbxref=PMID:16914447	
+P46672	UniProtKB	Sequence conflict	137	149	.	.	.	Note=PAGGAADAAAKAD->LRVALLMLQQGS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46672	UniProtKB	Sequence conflict	181	182	.	.	.	Note=KK->LL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46672	UniProtKB	Helix	3	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT	
+P46672	UniProtKB	Helix	12	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRK	
+P46672	UniProtKB	Helix	22	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT	
+P46672	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT	
+P46672	UniProtKB	Helix	44	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT	
+P46672	UniProtKB	Helix	65	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT	
+P46672	UniProtKB	Helix	88	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT	
+P46672	UniProtKB	Helix	96	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT	
+P46672	UniProtKB	Turn	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT	
+P46672	UniProtKB	Helix	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	211	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	229	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	242	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Turn	249	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Helix	254	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	261	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	271	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	284	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	291	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	305	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Helix	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Helix	326	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Helix	331	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	341	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	354	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+P46672	UniProtKB	Beta strand	374	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J	
+##sequence-region P53309 1 568
+P53309	UniProtKB	Chain	1	568	.	.	.	ID=PRO_0000202856;Note=Clathrin coat assembly protein AP180B	
+P53309	UniProtKB	Domain	1	127	.	.	.	Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243	
+P53309	UniProtKB	Compositional bias	379	383	.	.	.	Note=Poly-Gln	
+P53309	UniProtKB	Compositional bias	464	467	.	.	.	Note=Poly-Gln	
+P53309	UniProtKB	Compositional bias	551	560	.	.	.	Note=Poly-Gln	
+P53309	UniProtKB	Modified residue	449	449	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53309	UniProtKB	Cross-link	282	282	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q00381 1 147
+Q00381	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000193814;Note=AP-2 complex subunit sigma	
+##sequence-region P24813 1 409
+P24813	UniProtKB	Chain	1	409	.	.	.	ID=PRO_0000076522;Note=AP-1-like transcription factor YAP2	
+P24813	UniProtKB	Domain	43	106	.	.	.	Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P24813	UniProtKB	Region	46	69	.	.	.	Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P24813	UniProtKB	Region	71	99	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P24813	UniProtKB	Region	356	387	.	.	.	Note=c-CRD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19880	
+P24813	UniProtKB	Motif	17	24	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00768	
+P24813	UniProtKB	Motif	47	54	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00768	
+P24813	UniProtKB	Motif	372	379	.	.	.	Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19880	
+P24813	UniProtKB	Mutagenesis	356	356	.	.	.	Note=Only partially accumulates in the nucleus in response to cadmium. Does not accumulate in the nucleus%3B when associated with A-387. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17187783;Dbxref=PMID:17187783	
+P24813	UniProtKB	Mutagenesis	378	378	.	.	.	Note=No effect. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17187783;Dbxref=PMID:17187783	
+P24813	UniProtKB	Mutagenesis	387	387	.	.	.	Note=Only partially accumulates in the nucleus in response to cadmium. Does not accumulate in the nucleus%3B when associated with A-356. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17187783;Dbxref=PMID:17187783	
+P24813	UniProtKB	Mutagenesis	391	391	.	.	.	Note=Does not accumulate in the nucleus in response to cadmium. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17187783;Dbxref=PMID:17187783	
+P24813	UniProtKB	Sequence conflict	36	36	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24813	UniProtKB	Sequence conflict	90	90	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24813	UniProtKB	Sequence conflict	102	102	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24813	UniProtKB	Sequence conflict	125	125	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24813	UniProtKB	Sequence conflict	131	131	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24813	UniProtKB	Sequence conflict	142	142	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24813	UniProtKB	Sequence conflict	145	145	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24813	UniProtKB	Sequence conflict	327	327	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24813	UniProtKB	Sequence conflict	337	337	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24813	UniProtKB	Sequence conflict	347	347	.	.	.	Note=S->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24813	UniProtKB	Sequence conflict	354	354	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q8TGM5 1 67
+Q8TGM5	UniProtKB	Chain	1	67	.	.	.	ID=PRO_0000262871;Note=Putative uncharacterized protein ART3	
+##sequence-region Q03862 1 593
+Q03862	UniProtKB	Chain	1	593	.	.	.	ID=PRO_0000148999;Note=Probable metalloprotease ARX1	
+##sequence-region P22768 1 420
+P22768	UniProtKB	Chain	1	420	.	.	.	ID=PRO_0000148559;Note=Argininosuccinate synthase	
+P22768	UniProtKB	Nucleotide binding	9	17	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Nucleotide binding	114	122	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	35	35	.	.	.	Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	86	86	.	.	.	Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	91	91	.	.	.	Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	118	118	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	122	122	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	122	122	.	.	.	Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	123	123	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	126	126	.	.	.	Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	179	179	.	.	.	Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	188	188	.	.	.	Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	273	273	.	.	.	Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Binding site	285	285	.	.	.	Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22768	UniProtKB	Sequence conflict	27	28	.	.	.	Note=GY->AT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22768	UniProtKB	Sequence conflict	27	28	.	.	.	Note=GY->AT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22768	UniProtKB	Sequence conflict	48	49	.	.	.	Note=EK->VL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22768	UniProtKB	Sequence conflict	48	49	.	.	.	Note=EK->VL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22768	UniProtKB	Sequence conflict	61	64	.	.	.	Note=VDCR->GGLS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22768	UniProtKB	Sequence conflict	169	169	.	.	.	Note=P->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22768	UniProtKB	Sequence conflict	316	316	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22768	UniProtKB	Sequence conflict	329	332	.	.	.	Note=SYFT->FLLH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22768	UniProtKB	Sequence conflict	329	332	.	.	.	Note=SYFT->FLLH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22768	UniProtKB	Sequence conflict	329	332	.	.	.	Note=SYFT->FLLH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P13586 1 950
+P13586	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P13586	UniProtKB	Chain	2	950	.	.	.	ID=PRO_0000046231;Note=Calcium-transporting ATPase 1	
+P13586	UniProtKB	Topological domain	2	92	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Transmembrane	93	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Topological domain	112	116	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Transmembrane	117	133	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Topological domain	134	288	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Transmembrane	289	309	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Topological domain	310	323	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Transmembrane	324	344	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Topological domain	345	814	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Transmembrane	815	835	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Topological domain	836	844	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Transmembrane	845	862	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Topological domain	863	884	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Transmembrane	885	905	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Topological domain	906	909	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Transmembrane	910	930	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Topological domain	931	950	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13586	UniProtKB	Active site	371	371	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13586	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P13586	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q12675 1 1612
+Q12675	UniProtKB	Chain	1	1612	.	.	.	ID=PRO_0000046234;Note=Phospholipid-transporting ATPase DNF2	
+Q12675	UniProtKB	Topological domain	1	252	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Transmembrane	253	273	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Topological domain	274	277	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Transmembrane	278	298	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Topological domain	299	598	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Transmembrane	599	619	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Topological domain	620	639	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Transmembrane	640	660	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Topological domain	661	1231	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Transmembrane	1232	1252	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Topological domain	1253	1262	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Transmembrane	1263	1283	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Topological domain	1284	1313	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Transmembrane	1314	1334	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Topological domain	1335	1350	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Transmembrane	1351	1371	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Topological domain	1372	1377	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Transmembrane	1378	1398	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Topological domain	1399	1418	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Transmembrane	1419	1439	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Topological domain	1440	1612	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12675	UniProtKB	Active site	712	712	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12675	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12675	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12675	UniProtKB	Modified residue	389	389	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12675	UniProtKB	Modified residue	392	392	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12675	UniProtKB	Modified residue	396	396	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12675	UniProtKB	Modified residue	403	403	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12675	UniProtKB	Modified residue	406	406	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12675	UniProtKB	Modified residue	782	782	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12675	UniProtKB	Modified residue	1542	1542	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q12675	UniProtKB	Modified residue	1592	1592	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12675	UniProtKB	Cross-link	938	938	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P40527 1 1151
+P40527	UniProtKB	Chain	1	1151	.	.	.	ID=PRO_0000046236;Note=Probable phospholipid-transporting ATPase NEO1	
+P40527	UniProtKB	Topological domain	1	184	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Topological domain	206	209	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Transmembrane	210	230	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Topological domain	231	367	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Transmembrane	368	388	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Topological domain	389	416	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Transmembrane	417	437	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Topological domain	438	438	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Transmembrane	439	459	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Topological domain	460	947	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Transmembrane	948	968	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Topological domain	969	970	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Transmembrane	971	991	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Topological domain	992	1020	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Transmembrane	1021	1041	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Topological domain	1042	1052	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Transmembrane	1053	1073	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Topological domain	1074	1078	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Transmembrane	1079	1099	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Topological domain	1100	1109	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Transmembrane	1110	1130	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Topological domain	1131	1151	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40527	UniProtKB	Region	1131	1151	.	.	.	Note=Required for endosomal targeting	
+P40527	UniProtKB	Active site	503	503	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40527	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40527	UniProtKB	Modified residue	551	551	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P16639 1 503
+P16639	UniProtKB	Chain	1	503	.	.	.	ID=PRO_0000195092;Note=Arginyl-tRNA--protein transferase 1	
+P16639	UniProtKB	Sequence conflict	122	122	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16639	UniProtKB	Sequence conflict	122	122	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16639	UniProtKB	Sequence conflict	402	402	.	.	.	Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38316 1 186
+P38316	UniProtKB	Chain	1	186	.	.	.	ID=PRO_0000212485;Note=Ubiquitin-like protein ATG12	
+P38316	UniProtKB	Cross-link	186	186	.	.	.	Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-149 in ATG5)	
+P38316	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Decreases protein stability. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16874032;Dbxref=PMID:16874032	
+P38316	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Decreases protein stability. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16874032;Dbxref=PMID:16874032	
+P38316	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Impairs conjugation to ATG5 and autophagic activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16874032;Dbxref=PMID:16874032	
+P38316	UniProtKB	Mutagenesis	154	154	.	.	.	Note=Impairs conjugation to ATG5 and autophagic activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16874032;Dbxref=PMID:16874032	
+P38316	UniProtKB	Mutagenesis	186	186	.	.	.	Note=Strong decrease of conjugation with ATG5. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9759731;Dbxref=PMID:9759731	
+P38316	UniProtKB	Beta strand	103	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S	
+P38316	UniProtKB	Beta strand	121	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S	
+P38316	UniProtKB	Helix	130	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S	
+P38316	UniProtKB	Beta strand	147	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S	
+P38316	UniProtKB	Turn	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S	
+P38316	UniProtKB	Helix	162	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S	
+P38316	UniProtKB	Beta strand	174	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S	
+##sequence-region Q06628 1 738
+Q06628	UniProtKB	Chain	1	738	.	.	.	ID=PRO_0000157972;Note=Autophagy-related protein 13	
+Q06628	UniProtKB	Region	432	520	.	.	.	Note=Interaction with ATG1	
+Q06628	UniProtKB	Compositional bias	306	338	.	.	.	Note=Poly-Gln	
+Q06628	UniProtKB	Compositional bias	622	625	.	.	.	Note=Poly-Asp	
+Q06628	UniProtKB	Compositional bias	699	708	.	.	.	Note=Poly-Asn	
+Q06628	UniProtKB	Modified residue	344	344	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805182;Dbxref=PMID:19805182	
+Q06628	UniProtKB	Modified residue	348	348	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Modified residue	355	355	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06628	UniProtKB	Modified residue	437	437	.	.	.	Note=Phosphoserine%3B by TORC1 and PKA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19805182,ECO:0000269|PubMed:19995911;Dbxref=PMID:19805182,PMID:19995911	
+Q06628	UniProtKB	Modified residue	438	438	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Modified residue	461	461	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06628	UniProtKB	Modified residue	496	496	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Modified residue	535	535	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Modified residue	541	541	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Modified residue	554	554	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06628	UniProtKB	Modified residue	581	581	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805182;Dbxref=PMID:19805182	
+Q06628	UniProtKB	Modified residue	646	646	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Modified residue	649	649	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:19995911;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198,PMID:19995911	
+Q06628	UniProtKB	Mutagenesis	344	344	.	.	.	Note=Decreases phosphorylation by PKA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805182;Dbxref=PMID:19805182	
+Q06628	UniProtKB	Mutagenesis	348	348	.	.	.	Note=Leads to constitutive activation of autophagy%3B when associated with A-437%3B A-438%3B A-496%3B A-535%3B A-541%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Mutagenesis	437	437	.	.	.	Note=Decreases phosphorylation by PKA. Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-438%3B A-496%3B A-535%3B A-541%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19805182,ECO:0000269|PubMed:19995911;Dbxref=PMID:19805182,PMID:19995911	
+Q06628	UniProtKB	Mutagenesis	438	438	.	.	.	Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-496%3B A-535%3B A-541%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Mutagenesis	468	468	.	.	.	Note=Impairs binding to ATG1%3B when associated with A-469. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22885598;Dbxref=PMID:22885598	
+Q06628	UniProtKB	Mutagenesis	469	469	.	.	.	Note=Impairs binding to ATG1%3B when associated with A-468. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22885598;Dbxref=PMID:22885598	
+Q06628	UniProtKB	Mutagenesis	496	496	.	.	.	Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-438%3B A-535%3B A-541%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Mutagenesis	535	535	.	.	.	Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-438%3B A-496%3B A-541%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Mutagenesis	541	541	.	.	.	Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-438%3B A-496%3B A-535%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Mutagenesis	581	581	.	.	.	Note=Decreases phosphorylation by PKA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805182;Dbxref=PMID:19805182	
+Q06628	UniProtKB	Mutagenesis	646	646	.	.	.	Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-438%3B A-496%3B A-535%3B A-541 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+Q06628	UniProtKB	Mutagenesis	649	649	.	.	.	Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-438%3B A-496%3B A-535%3B A-541%2C and A-646. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911	
+##sequence-region Q06671 1 453
+Q06671	UniProtKB	Chain	1	453	.	.	.	ID=PRO_0000064727;Note=Autophagy-related protein 23	
+Q06671	UniProtKB	Coiled coil	144	213	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06671	UniProtKB	Coiled coil	272	302	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46989 1 271
+P46989	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46989	UniProtKB	Chain	20	271	.	.	.	ID=PRO_0000001780;Note=Autophagy-related protein 27	
+P46989	UniProtKB	Topological domain	20	199	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17135291;Dbxref=PMID:17135291	
+P46989	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46989	UniProtKB	Topological domain	221	271	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17135291;Dbxref=PMID:17135291	
+P46989	UniProtKB	Mutagenesis	188	193	.	.	.	Note=Abolishes the binding of phosphatidylinositol 3-phosphate and the cytoplasm to vacuole transport. KKPAKK->AAPAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12186856;Dbxref=PMID:12186856	
+##sequence-region P01097 1 85
+P01097	UniProtKB	Transit peptide	1	22	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2138617,ECO:0000269|PubMed:6458601;Dbxref=PMID:2138617,PMID:6458601	
+P01097	UniProtKB	Chain	23	85	.	.	.	ID=PRO_0000002554;Note=ATPase inhibitor%2C mitochondrial	
+P01097	UniProtKB	Coiled coil	41	84	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P01097	UniProtKB	Mutagenesis	41	41	.	.	.	Note=No loss of inhibitory activity. K->Q%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10705452;Dbxref=PMID:10705452	
+P01097	UniProtKB	Turn	24	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P01097	UniProtKB	Helix	38	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+##sequence-region P21306 1 62
+P21306	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1985960;Dbxref=PMID:1985960	
+P21306	UniProtKB	Chain	2	62	.	.	.	ID=PRO_0000071667;Note=ATP synthase subunit epsilon%2C mitochondrial	
+P21306	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P21306	UniProtKB	Turn	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P21306	UniProtKB	Helix	11	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P21306	UniProtKB	Helix	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P21306	UniProtKB	Helix	33	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P21306	UniProtKB	Beta strand	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+##sequence-region P00830 1 511
+P00830	UniProtKB	Transit peptide	1	33	.	.	.	Note=Mitochondrion	
+P00830	UniProtKB	Chain	34	511	.	.	.	ID=PRO_0000002454;Note=ATP synthase subunit beta%2C mitochondrial	
+P00830	UniProtKB	Nucleotide binding	190	197	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00830	UniProtKB	Modified residue	112	112	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P00830	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P00830	UniProtKB	Modified residue	373	373	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P00830	UniProtKB	Sequence conflict	201	201	.	.	.	Note=Q->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	218	218	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	218	218	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	232	237	.	.	.	Note=REMKET->HEMEDS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	260	260	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	287	288	.	.	.	Note=FI->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	354	358	.	.	.	Note=APATT->SPSTS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	365	366	.	.	.	Note=TT->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	365	366	.	.	.	Note=TT->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	469	473	.	.	.	Note=DTVAS->RTRCL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	489	489	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	501	501	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Sequence conflict	508	508	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00830	UniProtKB	Beta strand	43	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	53	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XOK	
+P00830	UniProtKB	Beta strand	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	79	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	91	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	108	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HLD	
+P00830	UniProtKB	Beta strand	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPD	
+P00830	UniProtKB	Beta strand	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	147	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEE	
+P00830	UniProtKB	Helix	172	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	180	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEH	
+P00830	UniProtKB	Beta strand	184	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	192	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPD	
+P00830	UniProtKB	Helix	196	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Turn	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEE	
+P00830	UniProtKB	Beta strand	215	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	224	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Turn	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	242	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OFN	
+P00830	UniProtKB	Beta strand	247	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	259	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	283	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	292	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	311	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	318	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	332	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEE	
+P00830	UniProtKB	Beta strand	335	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	346	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	353	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	359	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Beta strand	363	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	370	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Turn	383	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	393	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	398	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	426	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HLD	
+P00830	UniProtKB	Helix	431	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	455	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	467	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Turn	480	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	487	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Turn	490	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P00830	UniProtKB	Helix	496	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+##sequence-region P05626 1 244
+P05626	UniProtKB	Transit peptide	1	35	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2883007;Dbxref=PMID:2883007	
+P05626	UniProtKB	Chain	36	244	.	.	.	ID=PRO_0000002524;Note=ATP synthase subunit 4%2C mitochondrial	
+P05626	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P05626	UniProtKB	Sequence conflict	11	11	.	.	.	Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05626	UniProtKB	Sequence conflict	172	172	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05626	UniProtKB	Sequence conflict	172	172	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07879 1 167
+Q07879	UniProtKB	Chain	1	167	.	.	.	ID=PRO_0000096190;Note=Ubiquitin-like-conjugating enzyme ATG10	
+Q07879	UniProtKB	Active site	133	133	.	.	.	Note=Glycyl thioester intermediate	
+Q07879	UniProtKB	Mutagenesis	26	26	.	.	.	Note=No effect on conjugating activity. Normal autophagic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10508157;Dbxref=PMID:10508157	
+Q07879	UniProtKB	Mutagenesis	133	133	.	.	.	Note=Complete loss of covalent binding to ATG12. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10508157;Dbxref=PMID:10508157	
+Q07879	UniProtKB	Mutagenesis	133	133	.	.	.	Note=Strong decrease of binding to ATG12. No more formation of ATG12-ATG5 conjugate. Defect in autophagy. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10508157;Dbxref=PMID:10508157	
+Q07879	UniProtKB	Mutagenesis	137	137	.	.	.	Note=No effect on conjugating activity. Normal autophagic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10508157;Dbxref=PMID:10508157	
+Q07879	UniProtKB	Helix	4	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Turn	17	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Beta strand	26	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Beta strand	33	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSK	
+Q07879	UniProtKB	Beta strand	38	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Helix	46	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSK	
+Q07879	UniProtKB	Beta strand	61	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Turn	71	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Beta strand	75	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Beta strand	91	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Helix	99	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Turn	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Beta strand	115	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Beta strand	125	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Helix	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Helix	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Helix	150	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+Q07879	UniProtKB	Helix	159	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR	
+##sequence-region Q07528 1 640
+Q07528	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q07528	UniProtKB	Chain	2	640	.	.	.	ID=PRO_0000213824;Note=Autophagy-related protein 20	
+Q07528	UniProtKB	Domain	140	301	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
+Q07528	UniProtKB	Coiled coil	475	512	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07528	UniProtKB	Coiled coil	562	593	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07528	UniProtKB	Binding site	192	192	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07528	UniProtKB	Binding site	194	194	.	.	.	Note=Phosphatidylinositol 3-phosphate%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07528	UniProtKB	Binding site	218	218	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07528	UniProtKB	Binding site	267	267	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07528	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q07528	UniProtKB	Modified residue	361	361	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07528	UniProtKB	Modified residue	363	363	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07528	UniProtKB	Mutagenesis	193	193	.	.	.	Note=Abolishes the intracellular punctate localization and decreases the cytoplasm to vacuole transport. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12048214;Dbxref=PMID:12048214	
+##sequence-region Q12421 1 196
+Q12421	UniProtKB	Chain	1	196	.	.	.	ID=PRO_0000076210;Note=Autophagy-related protein 31	
+##sequence-region Q99325 1 256
+Q99325	UniProtKB	Signal peptide	1	16	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99325	UniProtKB	Chain	17	256	.	.	.	ID=PRO_0000245280;Note=Autophagy-related protein 40	
+Q99325	UniProtKB	Topological domain	17	67	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99325	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99325	UniProtKB	Topological domain	89	256	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99325	UniProtKB	Motif	242	245	.	.	.	Note=ATG8-binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26040717;Dbxref=PMID:26040717	
+Q99325	UniProtKB	Mutagenesis	242	242	.	.	.	Note=Impairs interaction with ATG8 and decreases subsequent reticulophagy%3B when associated with A-245. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26040717;Dbxref=PMID:26040717	
+Q99325	UniProtKB	Mutagenesis	245	245	.	.	.	Note=Impairs interaction with ATG8 and decreases subsequent reticulophagy%3B when associated with A-245. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26040717;Dbxref=PMID:26040717	
+##sequence-region P48016 1 1211
+P48016	UniProtKB	Region	513	514	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D6XZ22	
+P48016	UniProtKB	Region	711	712	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D6XZ22	
+P48016	UniProtKB	Active site	644	644	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D6XZ22	
+P48016	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	32	32	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	98	98	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	207	207	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	238	238	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	247	247	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	255	255	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	259	259	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	325	325	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	370	370	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	376	376	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	488	488	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	539	539	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	568	568	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	628	628	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	638	638	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	696	696	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	705	705	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	879	879	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	897	897	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	910	910	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	972	972	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	990	990	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	1031	1031	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	1049	1049	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	1064	1064	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	1147	1147	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Glycosylation	1157	1157	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48016	UniProtKB	Sequence conflict	1168	1211	.	.	.	Note=LQVGDKGNTDWRKTRYIVVAVQGVYDDYDDDNKGATIKEIVLND->FAGG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12233 1 115
+Q12233	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000071696;Note=ATP synthase subunit g%2C mitochondrial	
+Q12233	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+Q12233	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+Q12233	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+Q12233	UniProtKB	Mutagenesis	62	62	.	.	.	Note=No effect on ATP synthase dimerization. S->A	
+Q12233	UniProtKB	Mutagenesis	62	62	.	.	.	Note=Inhibits ATP synthase dimerization. S->E	
+##sequence-region P38111 1 2368
+P38111	UniProtKB	Chain	1	2368	.	.	.	ID=PRO_0000088836;Note=Serine/threonine-protein kinase MEC1	
+P38111	UniProtKB	Domain	1399	1944	.	.	.	Note=FAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534	
+P38111	UniProtKB	Domain	2082	2368	.	.	.	Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269	
+P38111	UniProtKB	Domain	2336	2368	.	.	.	Note=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535	
+P38111	UniProtKB	Region	2140	2368	.	.	.	Note=Binding to the RPA complex	
+P38111	UniProtKB	Mutagenesis	225	225	.	.	.	Note=In MEC1-101%3B impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint%3B when associated with P-552 and S-781. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899	
+P38111	UniProtKB	Mutagenesis	552	552	.	.	.	Note=In MEC1-101%3B impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint%3B when associated with S-225 and S-781. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899	
+P38111	UniProtKB	Mutagenesis	781	781	.	.	.	Note=In MEC1-101%3B impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint%3B when associated with S-225 and P-552. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899	
+P38111	UniProtKB	Mutagenesis	1179	1179	.	.	.	Note=In MEC1-100%3B impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint%3B when associated with S-1700. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899	
+P38111	UniProtKB	Mutagenesis	1700	1700	.	.	.	Note=In MEC1-100%3B impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint%3B when associated with S-1179. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899	
+P38111	UniProtKB	Mutagenesis	2224	2224	.	.	.	Note=Impairs kinase activity%3B when associated with K-2229. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11095737,ECO:0000269|PubMed:11359899;Dbxref=PMID:11095737,PMID:11359899	
+P38111	UniProtKB	Mutagenesis	2229	2229	.	.	.	Note=Impairs kinase activity%3B when associated with A-2224. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11095737;Dbxref=PMID:11095737	
+P38111	UniProtKB	Mutagenesis	2243	2243	.	.	.	Note=Impairs kinase activity. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899	
+P38111	UniProtKB	Mutagenesis	2360	2362	.	.	.	Note=In MEC1-85%3B disrupts interaction with RFA1 and severely impairs kinase activity. MYI->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16148046;Dbxref=PMID:16148046	
+P38111	UniProtKB	Mutagenesis	2367	2368	.	.	.	Note=In MEC1-87%3B decreases the level of MEC1 and impairs viability. FW->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16148046;Dbxref=PMID:16148046	
+P38111	UniProtKB	Sequence conflict	197	197	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38111	UniProtKB	Sequence conflict	716	716	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38111	UniProtKB	Sequence conflict	1255	1255	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38111	UniProtKB	Sequence conflict	1276	1276	.	.	.	Note=L->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08409 1 1394
+Q08409	UniProtKB	Chain	1	1394	.	.	.	ID=PRO_0000093434;Note=ATP-dependent permease AUS1	
+Q08409	UniProtKB	Topological domain	1	420	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	421	443	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	468	490	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	497	519	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	529	551	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	558	575	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	636	658	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Topological domain	659	1080	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	1081	1103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	1107	1129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	1156	1178	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	1193	1215	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	1224	1246	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Transmembrane	1346	1368	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Topological domain	1369	1394	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08409	UniProtKB	Domain	33	273	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q08409	UniProtKB	Domain	751	978	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q08409	UniProtKB	Nucleotide binding	782	789	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+##sequence-region Q12500 1 764
+Q12500	UniProtKB	Chain	1	764	.	.	.	ID=PRO_0000247424;Note=Late secretory pathway protein AVL9	
+Q12500	UniProtKB	Domain	10	173	.	.	.	Note=uDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304	
+Q12500	UniProtKB	Domain	195	360	.	.	.	Note=cDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304	
+Q12500	UniProtKB	Domain	362	464	.	.	.	Note=dDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304	
+Q12500	UniProtKB	Compositional bias	603	682	.	.	.	Note=Asp-rich	
+Q12500	UniProtKB	Modified residue	519	519	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12500	UniProtKB	Modified residue	524	524	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q05933 1 178
+Q05933	UniProtKB	Chain	1	178	.	.	.	ID=PRO_0000124048;Note=Actin-related protein 2/3 complex subunit 3	
+Q05933	UniProtKB	Cross-link	29	29	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P0CX79 1 362
+P0CX79	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786	
+P0CX79	UniProtKB	Chain	26	362	.	.	.	ID=PRO_0000410443;Note=L-asparaginase 2-4	
+P0CX79	UniProtKB	Domain	33	359	.	.	.	Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068	
+P0CX79	UniProtKB	Region	122	123	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX79	UniProtKB	Active site	43	43	.	.	.	Note=O-isoaspartyl threonine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10099,ECO:0000255|PROSITE-ProRule:PRU10100	
+P0CX79	UniProtKB	Binding site	89	89	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX79	UniProtKB	Glycosylation	29	29	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX79	UniProtKB	Glycosylation	93	93	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX79	UniProtKB	Glycosylation	239	239	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX79	UniProtKB	Natural variant	26	55	.	.	.	Note=Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786	
+##sequence-region P39945 1 430
+P39945	UniProtKB	Chain	1	430	.	.	.	ID=PRO_0000064711;Note=Protein AST2	
+##sequence-region P53296 1 535
+P53296	UniProtKB	Chain	1	535	.	.	.	ID=PRO_0000064721;Note=Alcohol O-acetyltransferase 2	
+P53296	UniProtKB	Sequence conflict	179	179	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12527 1 1178
+Q12527	UniProtKB	Chain	1	1178	.	.	.	ID=PRO_0000124554;Note=Autophagy-related protein 11	
+Q12527	UniProtKB	Coiled coil	538	572	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12527	UniProtKB	Coiled coil	696	850	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12527	UniProtKB	Compositional bias	598	610	.	.	.	Note=Asn-rich	
+Q12527	UniProtKB	Compositional bias	1050	1099	.	.	.	Note=Ser-rich	
+##sequence-region P38270 1 344
+P38270	UniProtKB	Chain	1	344	.	.	.	ID=PRO_0000212453;Note=Autophagy-related protein 14	
+P38270	UniProtKB	Region	3	18	.	.	.	Note=Cysteine repeats;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38270	UniProtKB	Coiled coil	25	156	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25641 1 520
+P25641	UniProtKB	Chain	1	520	.	.	.	ID=PRO_0000090372;Note=Putative lipase ATG15	
+P25641	UniProtKB	Topological domain	1	14	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12499386;Dbxref=PMID:12499386	
+P25641	UniProtKB	Transmembrane	15	35	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P25641	UniProtKB	Topological domain	36	520	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12499386;Dbxref=PMID:12499386	
+P25641	UniProtKB	Active site	332	332	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037	
+P25641	UniProtKB	Glycosylation	173	173	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25641	UniProtKB	Glycosylation	202	202	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25641	UniProtKB	Glycosylation	208	208	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25641	UniProtKB	Mutagenesis	332	332	.	.	.	Note=Loss of function. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11085977,ECO:0000269|PubMed:11566994;Dbxref=PMID:11085977,PMID:11566994	
+##sequence-region Q03818 1 150
+Q03818	UniProtKB	Chain	1	150	.	.	.	ID=PRO_0000218595;Note=Autophagy protein 16	
+Q03818	UniProtKB	Coiled coil	58	130	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03818	UniProtKB	Mutagenesis	35	35	.	.	.	Note=Impairs interaction with ATG5and autophagy. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17192262;Dbxref=PMID:17192262	
+Q03818	UniProtKB	Mutagenesis	46	46	.	.	.	Note=Impairs interaction with ATG5and autophagy. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17192262;Dbxref=PMID:17192262	
+Q03818	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Significantly reduces autophagic activity%3B when associated with A-102. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19889643;Dbxref=PMID:19889643	
+Q03818	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Significantly reduces autophagic activity%3B when associated with A-101. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19889643;Dbxref=PMID:19889643	
+Q03818	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Significantly reduces autophagic activity%3B when associated with A-108 and A-112. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19889643;Dbxref=PMID:19889643	
+Q03818	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Significantly reduces autophagic activity%3B when associated with A-104 and A-112. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19889643;Dbxref=PMID:19889643	
+Q03818	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Significantly reduces autophagic activity%3B when associated with A-104 and A-108. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19889643;Dbxref=PMID:19889643	
+Q03818	UniProtKB	Helix	23	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q03818	UniProtKB	Helix	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q03818	UniProtKB	Turn	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q03818	UniProtKB	Helix	61	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A7O	
+##sequence-region Q06410 1 417
+Q06410	UniProtKB	Chain	1	417	.	.	.	ID=PRO_0000124566;Note=Autophagy-related protein 17	
+Q06410	UniProtKB	Coiled coil	146	221	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06410	UniProtKB	Coiled coil	353	384	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06410	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Decreases affinity for ATG13. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15743910;Dbxref=PMID:15743910	
+##sequence-region P35193 1 415
+P35193	UniProtKB	Chain	1	415	.	.	.	ID=PRO_0000064722;Note=Autophagy-related protein 19	
+P35193	UniProtKB	Region	21	28	.	.	.	Note=ATG11-binding	
+P35193	UniProtKB	Region	254	367	.	.	.	Note=AMS1-binding	
+P35193	UniProtKB	Region	406	415	.	.	.	Note=ATG8-binding	
+P35193	UniProtKB	Coiled coil	157	187	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35193	UniProtKB	Motif	412	415	.	.	.	Note=WXXL	
+P35193	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P35193	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35193	UniProtKB	Modified residue	243	243	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P35193	UniProtKB	Cross-link	213	213	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16186126;Dbxref=PMID:16186126	
+P35193	UniProtKB	Cross-link	216	216	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16186126;Dbxref=PMID:16186126	
+P35193	UniProtKB	Mutagenesis	412	412	.	.	.	Note=Impairs vacuolar transport of LAP4. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19021777;Dbxref=PMID:19021777	
+P35193	UniProtKB	Mutagenesis	415	415	.	.	.	Note=Impairs vacuolar transport of LAP4. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19021777;Dbxref=PMID:19021777	
+P35193	UniProtKB	Sequence conflict	412	412	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35193	UniProtKB	Helix	161	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGE	
+P35193	UniProtKB	Beta strand	262	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB	
+P35193	UniProtKB	Beta strand	272	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB	
+P35193	UniProtKB	Beta strand	281	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB	
+P35193	UniProtKB	Beta strand	295	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB	
+P35193	UniProtKB	Beta strand	318	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB	
+P35193	UniProtKB	Beta strand	335	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB	
+P35193	UniProtKB	Beta strand	342	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB	
+P35193	UniProtKB	Beta strand	352	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB	
+##sequence-region P53104 1 897
+P53104	UniProtKB	Chain	1	897	.	.	.	ID=PRO_0000085655;Note=Serine/threonine-protein kinase ATG1	
+P53104	UniProtKB	Domain	24	325	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53104	UniProtKB	Nucleotide binding	30	38	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53104	UniProtKB	Region	880	886	.	.	.	Note=Required for Cvt trafficking	
+P53104	UniProtKB	Motif	429	432	.	.	.	Note=LIR	
+P53104	UniProtKB	Compositional bias	542	548	.	.	.	Note=Poly-Gln	
+P53104	UniProtKB	Active site	172	172	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P53104	UniProtKB	Binding site	54	54	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53104	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	226	226	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20439775;Dbxref=PMID:20439775	
+P53104	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	365	365	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	390	390	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:21460632;Dbxref=PMID:18407956,PMID:21460632	
+P53104	UniProtKB	Modified residue	508	508	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17699586;Dbxref=PMID:17699586	
+P53104	UniProtKB	Modified residue	515	515	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17699586,ECO:0000269|PubMed:21460632;Dbxref=PMID:17699586,PMID:21460632	
+P53104	UniProtKB	Modified residue	533	533	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	551	551	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	552	552	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	590	590	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	621	621	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	635	635	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53104	UniProtKB	Modified residue	638	638	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53104	UniProtKB	Modified residue	647	647	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53104	UniProtKB	Modified residue	677	677	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000269|PubMed:21460632;Dbxref=PMID:15665377,PMID:21460632	
+P53104	UniProtKB	Modified residue	680	680	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	683	683	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	769	769	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Modified residue	783	783	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Mutagenesis	34	34	.	.	.	Note=Impairs kinase activity. S->D%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Defect in the Cvt pathway. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10995454,ECO:0000269|PubMed:12589048,ECO:0000269|PubMed:23549786;Dbxref=PMID:10995454,PMID:12589048,PMID:23549786	
+P53104	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Enables the binding of the inhibitor of the kinase activity 1-NA-PP1. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12589048;Dbxref=PMID:12589048	
+P53104	UniProtKB	Mutagenesis	211	211	.	.	.	Note=Loss of cell viability under starvation. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23549786,ECO:0000269|PubMed:9224897;Dbxref=PMID:23549786,PMID:9224897	
+P53104	UniProtKB	Mutagenesis	226	226	.	.	.	Note=Leads to constitutive autophosphorylation activity. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20439775;Dbxref=PMID:20439775	
+P53104	UniProtKB	Mutagenesis	237	237	.	.	.	Note=Loss of cell viability under starvation. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9224897;Dbxref=PMID:9224897	
+P53104	UniProtKB	Mutagenesis	429	429	.	.	.	Note=Impairs interaction with ATG8 and decreases autophagy efficiency%3B when associated with A-432. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22778255;Dbxref=PMID:22778255	
+P53104	UniProtKB	Mutagenesis	432	432	.	.	.	Note=Impairs interaction with ATG8 and decreases autophagy efficiency%3B when associated with A-429. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22778255;Dbxref=PMID:22778255	
+P53104	UniProtKB	Mutagenesis	508	508	.	.	.	Note=Impairs autophagic activity%3B when associated with A-515. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17699586;Dbxref=PMID:17699586	
+P53104	UniProtKB	Mutagenesis	515	515	.	.	.	Note=Impairs autophagic activity%3B when associated with A-508. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17699586;Dbxref=PMID:17699586	
+P53104	UniProtKB	Mutagenesis	551	551	.	.	.	Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Mutagenesis	552	552	.	.	.	Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Mutagenesis	621	621	.	.	.	Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Mutagenesis	677	677	.	.	.	Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Mutagenesis	680	680	.	.	.	Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Mutagenesis	683	683	.	.	.	Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Mutagenesis	769	769	.	.	.	Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Mutagenesis	783	783	.	.	.	Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632	
+P53104	UniProtKB	Mutagenesis	884	884	.	.	.	Note=No effect. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12589048;Dbxref=PMID:12589048	
+P53104	UniProtKB	Mutagenesis	886	886	.	.	.	Note=Cvt pathway specific block. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12589048;Dbxref=PMID:12589048	
+##sequence-region Q06159 1 398
+Q06159	UniProtKB	Chain	1	398	.	.	.	ID=PRO_0000268627;Note=Autophagy-related protein 39	
+Q06159	UniProtKB	Transmembrane	148	164	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06159	UniProtKB	Motif	8	11	.	.	.	Note=ATG8-binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26040717;Dbxref=PMID:26040717	
+Q06159	UniProtKB	Motif	52	59	.	.	.	Note=ATG11-binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26040717;Dbxref=PMID:26040717	
+Q06159	UniProtKB	Mutagenesis	52	59	.	.	.	Note=Impairs interaction with ATG8 and decreases subsequent reticulophagy. DVLSNTSS->AAAAAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26040717;Dbxref=PMID:26040717	
+##sequence-region P53867 1 494
+P53867	UniProtKB	Chain	1	494	.	.	.	ID=PRO_0000215870;Note=Cysteine protease ATG4	
+P53867	UniProtKB	Active site	147	147	.	.	.	Note=Nucleophile	
+P53867	UniProtKB	Active site	322	322	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53867	UniProtKB	Active site	324	324	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53867	UniProtKB	Modified residue	488	488	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53867	UniProtKB	Mutagenesis	147	147	.	.	.	Note=Abolishes the proteolytic activity and decreases autophagy. C->S%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11038174;Dbxref=PMID:11038174	
+##sequence-region Q12380 1 294
+Q12380	UniProtKB	Chain	1	294	.	.	.	ID=PRO_0000219010;Note=Autophagy protein 5	
+Q12380	UniProtKB	Cross-link	149	149	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12)	
+Q12380	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Loss of conjugation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9759731;Dbxref=PMID:9759731	
+Q12380	UniProtKB	Helix	1	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	12	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	30	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	34	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	49	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Turn	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S	
+Q12380	UniProtKB	Beta strand	71	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYM	
+Q12380	UniProtKB	Helix	87	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Turn	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYM	
+Q12380	UniProtKB	Beta strand	115	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYM	
+Q12380	UniProtKB	Helix	139	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	167	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	182	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	202	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	208	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	233	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Turn	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	248	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	255	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Helix	263	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+Q12380	UniProtKB	Beta strand	277	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO	
+##sequence-region P53722 1 227
+P53722	UniProtKB	Chain	1	227	.	.	.	ID=PRO_0000203472;Note=Mitochondrial inner membrane protease ATP23	
+P53722	UniProtKB	Active site	125	125	.	.	.	.	
+P53722	UniProtKB	Metal binding	124	124	.	.	.	Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53722	UniProtKB	Metal binding	128	128	.	.	.	Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53722	UniProtKB	Mutagenesis	124	124	.	.	.	Note=Abolishes proteolytic processing of ATP6%2C but still promotes assembly of the ATP6 precursor into the ATPase CF(0) particle. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17135288;Dbxref=PMID:17135288	
+P53722	UniProtKB	Mutagenesis	125	125	.	.	.	Note=Abolishes proteolytic processing of ATP6%2C but still promotes assembly of the ATP6 precursor into the ATPase CF(0) particle. E->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17135288,ECO:0000269|PubMed:17135290;Dbxref=PMID:17135288,PMID:17135290	
+P53722	UniProtKB	Mutagenesis	128	128	.	.	.	Note=Abolishes proteolytic processing of ATP6%2C but still promotes assembly of the ATP6 precursor into the ATPase CF(0) particle. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17135288;Dbxref=PMID:17135288	
+##sequence-region Q12092 1 213
+Q12092	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000232994;Note=Autophagy-related protein 29	
+Q12092	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12092	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12092	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40458 1 529
+P40458	UniProtKB	Chain	1	529	.	.	.	ID=PRO_0000086920;Note=Autophagy-related protein 32	
+P40458	UniProtKB	Transmembrane	390	414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40458	UniProtKB	Modified residue	114	114	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21757540;Dbxref=PMID:21757540	
+P40458	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21757540;Dbxref=PMID:21757540	
+P40458	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Abolishes mitophagy and impairs interaction with ATG11. S->A%2CN%2CG%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21757540;Dbxref=PMID:21757540	
+P40458	UniProtKB	Mutagenesis	119	119	.	.	.	Note=Decreases mitophagy and impairs interaction with ATG11. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21757540;Dbxref=PMID:21757540	
+##sequence-region P46983 1 293
+P46983	UniProtKB	Chain	1	293	.	.	.	ID=PRO_0000203020;Note=Autophagy-related protein 36	
+##sequence-region Q12048 1 136
+Q12048	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000270559;Note=Autophagy-related protein 41	
+Q12048	UniProtKB	Region	127	136	.	.	.	Note=ATG9-binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26565778;Dbxref=PMID:26565778	
+##sequence-region P38862 1 630
+P38862	UniProtKB	Chain	1	630	.	.	.	ID=PRO_0000212822;Note=Ubiquitin-like modifier-activating enzyme ATG7	
+P38862	UniProtKB	Region	591	630	.	.	.	Note=Homodimerization	
+P38862	UniProtKB	Motif	331	336	.	.	.	Note=GXGXXG motif	
+P38862	UniProtKB	Active site	507	507	.	.	.	Note=Glycyl thioester intermediate	
+P38862	UniProtKB	Mutagenesis	333	333	.	.	.	Note=Loss of interaction with ATG8 and ATG12%2C and no more ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10233150,ECO:0000269|PubMed:11100732;Dbxref=PMID:10233150,PMID:11100732	
+P38862	UniProtKB	Mutagenesis	443	443	.	.	.	Note=Loss of interaction with ATG8. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22055191;Dbxref=PMID:22055191	
+P38862	UniProtKB	Mutagenesis	466	466	.	.	.	Note=Loss of interaction with ATG8%3B when associated with F-486 and A-490. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22055191;Dbxref=PMID:22055191	
+P38862	UniProtKB	Mutagenesis	486	486	.	.	.	Note=Loss of interaction with ATG8%3B when associated with A-466 and A-490. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22055191;Dbxref=PMID:22055191	
+P38862	UniProtKB	Mutagenesis	490	490	.	.	.	Note=Loss of interaction with ATG8%3B when associated with A-466 and F-486. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22055191;Dbxref=PMID:22055191	
+P38862	UniProtKB	Mutagenesis	507	507	.	.	.	Note=Loss of interaction with ATG8 and ATG12 and no more formation of ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10233150,ECO:0000269|PubMed:11100732,ECO:0000269|PubMed:15277523;Dbxref=PMID:10233150,PMID:11100732,PMID:15277523	
+P38862	UniProtKB	Mutagenesis	507	507	.	.	.	Note=Instead of the formation of an intermediate complex with a thiol ester bond between ATG7 (E1-like enzyme) and ATG8 (substrate) or between ATG7 and ATG12 (substrate)%2C a stable complex with an O-ester bond is formed. No more formation of ATG12-ATG5 conjugate. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10233150,ECO:0000269|PubMed:11100732,ECO:0000269|PubMed:15277523;Dbxref=PMID:10233150,PMID:11100732,PMID:15277523	
+P38862	UniProtKB	Mutagenesis	550	550	.	.	.	Note=Loss of interaction with ATG8. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22055191;Dbxref=PMID:22055191	
+P38862	UniProtKB	Beta strand	12	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Helix	19	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Turn	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7G	
+P38862	UniProtKB	Beta strand	36	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VH2	
+P38862	UniProtKB	Beta strand	56	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Helix	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSL	
+P38862	UniProtKB	Beta strand	78	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Helix	90	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Helix	98	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Helix	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Turn	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	135	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	151	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Helix	159	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Helix	165	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	179	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Helix	194	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	202	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Helix	219	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	235	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	243	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	248	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	263	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7F	
+P38862	UniProtKB	Beta strand	269	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Beta strand	284	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H	
+P38862	UniProtKB	Helix	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUJ	
+P38862	UniProtKB	Helix	294	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	319	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	326	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	334	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	350	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Turn	364	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	372	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	376	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VH1	
+P38862	UniProtKB	Helix	379	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	391	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSK	
+P38862	UniProtKB	Beta strand	395	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	413	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	431	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	438	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VH4	
+P38862	UniProtKB	Helix	441	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	444	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	456	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	464	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	486	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	490	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	494	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VH1	
+P38862	UniProtKB	Turn	498	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	504	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	513	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	537	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	547	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Turn	553	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Beta strand	557	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Turn	570	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	574	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	585	593	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	595	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	604	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38862	UniProtKB	Helix	616	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LI5	
+P38862	UniProtKB	Helix	627	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LI5	
+##sequence-region P38182 1 117
+P38182	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000017242;Note=Autophagy-related protein 8	
+P38182	UniProtKB	Propeptide	117	117	.	.	.	ID=PRO_0000017243;Note=Removed in mature form	
+P38182	UniProtKB	Site	116	117	.	.	.	Note=Cleavage%3B by ATG4	
+P38182	UniProtKB	Lipidation	116	116	.	.	.	Note=Phosphatidylethanolamine amidated glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11100732;Dbxref=PMID:11100732	
+P38182	UniProtKB	Mutagenesis	26	26	.	.	.	Note=No effect on autophagic activity. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20428927;Dbxref=PMID:20428927	
+P38182	UniProtKB	Mutagenesis	28	28	.	.	.	Note=Impairs ATG19-binding and autophagic activity. R->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19021777,ECO:0000269|PubMed:19398890;Dbxref=PMID:19021777,PMID:19398890	
+P38182	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Impairs autophagic activity. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19398890;Dbxref=PMID:19398890	
+P38182	UniProtKB	Mutagenesis	49	49	.	.	.	Note=Impairs ATG19-binding%2C PE-conjugation%2C and autophagic activity. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16680092,ECO:0000269|PubMed:19398890;Dbxref=PMID:16680092,PMID:19398890	
+P38182	UniProtKB	Mutagenesis	50	50	.	.	.	Note=Impairs ATG19-binding and autophagic activity. L->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16680092,ECO:0000269|PubMed:19398890;Dbxref=PMID:16680092,PMID:19398890	
+P38182	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Significantly decreases ATG19-binding and autophagic activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19021777;Dbxref=PMID:19021777	
+P38182	UniProtKB	Mutagenesis	55	55	.	.	.	Note=Impairs autophagic activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19398890;Dbxref=PMID:19398890	
+P38182	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Significantly decreases ATG19-binding and autophagic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19021777;Dbxref=PMID:19021777	
+P38182	UniProtKB	Mutagenesis	77	77	.	.	.	Note=Impairs interaction with ATG4%2C cleavage by ATG4%2C PAS localization%2C and autophagic activity%3B when associated with A-79. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16680092;Dbxref=PMID:16680092	
+P38182	UniProtKB	Mutagenesis	79	79	.	.	.	Note=Impairs interaction with ATG4%2C cleavage by ATG4%2C PAS localization%2C and autophagic activity%3B when associated with A-77. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16680092;Dbxref=PMID:16680092	
+P38182	UniProtKB	Mutagenesis	116	116	.	.	.	Note=No cleaving of the C-terminal R-117 by ATG4. Defect in Cvt pathway and autophagy. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11038174;Dbxref=PMID:11038174	
+P38182	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Normal processing after G-116 by ATG4. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11038174;Dbxref=PMID:11038174	
+P38182	UniProtKB	Helix	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VH3	
+P38182	UniProtKB	Helix	11	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38182	UniProtKB	Beta strand	26	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38182	UniProtKB	Beta strand	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KWC	
+P38182	UniProtKB	Beta strand	48	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38182	UniProtKB	Helix	57	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38182	UniProtKB	Beta strand	76	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38182	UniProtKB	Beta strand	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KWC	
+P38182	UniProtKB	Helix	91	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+P38182	UniProtKB	Beta strand	105	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI	
+##sequence-region Q12691 1 1091
+Q12691	UniProtKB	Chain	1	1091	.	.	.	ID=PRO_0000046244;Note=Sodium transport ATPase 5	
+Q12691	UniProtKB	Topological domain	1	63	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Topological domain	85	90	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Topological domain	112	282	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Transmembrane	283	303	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Topological domain	304	312	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Transmembrane	313	333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Topological domain	334	815	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Transmembrane	816	836	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Topological domain	837	848	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Transmembrane	849	869	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Topological domain	870	885	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Transmembrane	886	906	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Topological domain	907	943	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Transmembrane	944	964	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Topological domain	965	991	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Transmembrane	992	1012	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Topological domain	1013	1021	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Transmembrane	1022	1042	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Topological domain	1043	1091	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12691	UniProtKB	Active site	369	369	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P32453 1 318
+P32453	UniProtKB	Transit peptide	1	40	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32453	UniProtKB	Chain	41	318	.	.	.	ID=PRO_0000002535;Note=Protein ATP11%2C mitochondrial	
+P32453	UniProtKB	Modified residue	109	109	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P00854 1 259
+P00854	UniProtKB	Propeptide	1	10	.	.	.	ID=PRO_0000002626;Note=Removed in mature form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2894987;Dbxref=PMID:2894987	
+P00854	UniProtKB	Chain	11	259	.	.	.	ID=PRO_0000002627;Note=ATP synthase subunit a	
+P00854	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00854	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00854	UniProtKB	Transmembrane	125	145	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00854	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00854	UniProtKB	Transmembrane	191	211	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00854	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00854	UniProtKB	Natural variant	171	171	.	.	.	Note=In strain: D273-10B/A1. I->M	
+P00854	UniProtKB	Natural variant	177	177	.	.	.	Note=In strain: D273-10B/A1. F->I	
+P00854	UniProtKB	Natural variant	231	231	.	.	.	Note=In strain: D273-10B/A1. M->I	
+P00854	UniProtKB	Natural variant	241	241	.	.	.	Note=In strain: D273-10B/A1. G->S	
+P00854	UniProtKB	Natural variant	245	245	.	.	.	Note=In strain: D273-10B/A1. A->T	
+P00854	UniProtKB	Natural variant	255	256	.	.	.	Note=In strain: D273-10B/A1. AV->TL	
+##sequence-region Q12165 1 160
+Q12165	UniProtKB	Transit peptide	1	22	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8026496;Dbxref=PMID:8026496	
+Q12165	UniProtKB	Chain	23	160	.	.	.	ID=PRO_0000002671;Note=ATP synthase subunit delta%2C mitochondrial	
+Q12165	UniProtKB	Beta strand	34	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OFN	
+Q12165	UniProtKB	Beta strand	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Beta strand	56	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Beta strand	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Beta strand	70	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Beta strand	78	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Beta strand	86	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Beta strand	95	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Turn	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Beta strand	104	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Beta strand	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OFN	
+Q12165	UniProtKB	Helix	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Helix	120	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Beta strand	136	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+Q12165	UniProtKB	Helix	140	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+##sequence-region Q06405 1 101
+Q06405	UniProtKB	Transit peptide	1	6	.	.	.	Note=Mitochondrion	
+Q06405	UniProtKB	Chain	7	101	.	.	.	ID=PRO_0000002637;Note=ATP synthase subunit f%2C mitochondrial	
+##sequence-region P31386 1 333
+P31386	UniProtKB	Chain	1	333	.	.	.	ID=PRO_0000206648;Note=Protein ATS1	
+P31386	UniProtKB	Repeat	1	53	.	.	.	Note=RCC1 1	
+P31386	UniProtKB	Repeat	55	104	.	.	.	Note=RCC1 2	
+P31386	UniProtKB	Repeat	146	197	.	.	.	Note=RCC1 3	
+P31386	UniProtKB	Repeat	286	333	.	.	.	Note=RCC1 4	
+P31386	UniProtKB	Sequence conflict	305	305	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31386	UniProtKB	Sequence conflict	305	305	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31386	UniProtKB	Sequence conflict	305	305	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31386	UniProtKB	Sequence conflict	305	305	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31386	UniProtKB	Beta strand	3	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	16	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	23	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4D4O	
+P31386	UniProtKB	Beta strand	38	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	45	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	57	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	76	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	89	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	96	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	108	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	115	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4D4O	
+P31386	UniProtKB	Beta strand	132	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	140	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	148	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	158	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	165	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	182	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	189	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	201	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Helix	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	224	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	231	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Turn	237	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	241	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	263	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	270	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	281	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4D4O	
+P31386	UniProtKB	Beta strand	287	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	296	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4D4Q	
+P31386	UniProtKB	Beta strand	311	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+P31386	UniProtKB	Beta strand	326	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+##sequence-region P38636 1 73
+P38636	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000212535;Note=Metal homeostasis factor ATX1	
+P38636	UniProtKB	Domain	5	69	.	.	.	Note=HMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38636	UniProtKB	Metal binding	15	15	.	.	.	Note=Copper	
+P38636	UniProtKB	Metal binding	18	18	.	.	.	Note=Copper	
+P38636	UniProtKB	Sequence conflict	8	8	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38636	UniProtKB	Beta strand	5	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8	
+P38636	UniProtKB	Helix	16	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8	
+P38636	UniProtKB	Turn	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8	
+P38636	UniProtKB	Beta strand	32	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8	
+P38636	UniProtKB	Turn	40	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8	
+P38636	UniProtKB	Beta strand	44	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8	
+P38636	UniProtKB	Helix	53	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8	
+P38636	UniProtKB	Turn	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K7R	
+P38636	UniProtKB	Beta strand	67	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8	
+##sequence-region P40851 1 1208
+P40851	UniProtKB	Chain	1	1208	.	.	.	ID=PRO_0000074417;Note=Putative protease AXL1	
+P40851	UniProtKB	Active site	71	71	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096	
+P40851	UniProtKB	Metal binding	68	68	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096	
+P40851	UniProtKB	Metal binding	72	72	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096	
+P40851	UniProtKB	Metal binding	156	156	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096	
+P40851	UniProtKB	Modified residue	262	262	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P40851	UniProtKB	Sequence conflict	113	113	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06541 1 321
+Q06541	UniProtKB	Chain	1	321	.	.	.	ID=PRO_0000228135;Note=Protein ARV1	
+Q06541	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06541	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06541	UniProtKB	Transmembrane	248	270	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06541	UniProtKB	Transmembrane	272	292	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06541	UniProtKB	Glycosylation	296	296	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06822 1 443
+Q06822	UniProtKB	Chain	1	443	.	.	.	ID=PRO_0000252299;Note=ASTRA-associated protein 1	
+Q06822	UniProtKB	Repeat	23	67	.	.	.	Note=WD 1	
+Q06822	UniProtKB	Repeat	71	110	.	.	.	Note=WD 2	
+Q06822	UniProtKB	Repeat	258	295	.	.	.	Note=WD 3	
+Q06822	UniProtKB	Repeat	318	359	.	.	.	Note=WD 4	
+##sequence-region P46993 1 209
+P46993	UniProtKB	Chain	1	209	.	.	.	ID=PRO_0000203025;Note=Protein ASG7	
+P46993	UniProtKB	Topological domain	1	49	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46993	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46993	UniProtKB	Topological domain	71	184	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46993	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46993	UniProtKB	Topological domain	206	209	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46993	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P46993	UniProtKB	Modified residue	123	123	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P46993	UniProtKB	Modified residue	125	125	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P46993	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P54074 1 624
+P54074	UniProtKB	Chain	1	624	.	.	.	ID=PRO_0000203295;Note=Protein ASI1	
+P54074	UniProtKB	Topological domain	1	69	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54074	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54074	UniProtKB	Topological domain	91	116	.	.	.	Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54074	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54074	UniProtKB	Topological domain	138	152	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54074	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54074	UniProtKB	Topological domain	174	209	.	.	.	Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54074	UniProtKB	Transmembrane	210	230	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54074	UniProtKB	Topological domain	231	273	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54074	UniProtKB	Transmembrane	274	294	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54074	UniProtKB	Topological domain	295	624	.	.	.	Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54074	UniProtKB	Zinc finger	568	608	.	.	.	Note=RING-type%3B atypical	
+P54074	UniProtKB	Glycosylation	2	2	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16735580,ECO:0000269|PubMed:17085444;Dbxref=PMID:16735580,PMID:17085444	
+P54074	UniProtKB	Glycosylation	19	19	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16735580,ECO:0000269|PubMed:17085444;Dbxref=PMID:16735580,PMID:17085444	
+P54074	UniProtKB	Glycosylation	29	29	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16735580,ECO:0000269|PubMed:17085444;Dbxref=PMID:16735580,PMID:17085444	
+P54074	UniProtKB	Mutagenesis	583	583	.	.	.	Note=In ASI1-21HA%3B when associated with S-585%3B abolishes function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16735580;Dbxref=PMID:16735580	
+P54074	UniProtKB	Mutagenesis	585	585	.	.	.	Note=In ASI1-21HA%3B when associated with S-583%3B abolishes function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16735580;Dbxref=PMID:16735580	
+##sequence-region P48361 1 1146
+P48361	UniProtKB	Chain	1	1146	.	.	.	ID=PRO_0000064699;Note=Activator of SKN7 protein 10	
+P48361	UniProtKB	Domain	482	606	.	.	.	Note=PH	
+P48361	UniProtKB	Compositional bias	22	26	.	.	.	Note=Poly-Gly	
+P48361	UniProtKB	Compositional bias	625	628	.	.	.	Note=Poly-Ser	
+P48361	UniProtKB	Compositional bias	933	938	.	.	.	Note=Poly-Asn	
+P48361	UniProtKB	Compositional bias	958	961	.	.	.	Note=Poly-Gln	
+P48361	UniProtKB	Compositional bias	972	975	.	.	.	Note=Poly-Ser	
+P48361	UniProtKB	Modified residue	344	344	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P48361	UniProtKB	Modified residue	793	793	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P48361	UniProtKB	Modified residue	808	808	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P48361	UniProtKB	Modified residue	944	944	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48361	UniProtKB	Modified residue	969	969	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48361	UniProtKB	Modified residue	1017	1017	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P48361	UniProtKB	Modified residue	1070	1070	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P48361	UniProtKB	Modified residue	1095	1095	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48361	UniProtKB	Modified residue	1098	1098	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48361	UniProtKB	Sequence conflict	57	57	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48361	UniProtKB	Sequence conflict	346	346	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48361	UniProtKB	Sequence conflict	464	464	.	.	.	Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48361	UniProtKB	Sequence conflict	467	467	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48361	UniProtKB	Sequence conflict	603	603	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48361	UniProtKB	Sequence conflict	906	906	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32660 1 1571
+P32660	UniProtKB	Chain	1	1571	.	.	.	ID=PRO_0000046235;Note=Phospholipid-transporting ATPase DNF1	
+P32660	UniProtKB	Topological domain	1	214	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Transmembrane	215	235	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Topological domain	236	239	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Transmembrane	240	260	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Topological domain	261	553	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Transmembrane	554	574	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Topological domain	575	594	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Transmembrane	595	615	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Topological domain	616	1188	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Transmembrane	1189	1209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Topological domain	1210	1219	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Transmembrane	1220	1240	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Topological domain	1241	1270	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Transmembrane	1271	1291	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Topological domain	1292	1307	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Transmembrane	1308	1328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Topological domain	1329	1334	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Transmembrane	1335	1355	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Topological domain	1356	1375	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Transmembrane	1376	1396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Topological domain	1397	1571	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32660	UniProtKB	Active site	667	667	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32660	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P32660	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32660	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32660	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32660	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32660	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32660	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32660	UniProtKB	Modified residue	109	109	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32660	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32660	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12675	
+P32660	UniProtKB	Modified residue	358	358	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12675	
+P32660	UniProtKB	Modified residue	365	365	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32660	UniProtKB	Modified residue	368	368	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12675	
+P32660	UniProtKB	Modified residue	1506	1506	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32660	UniProtKB	Modified residue	1551	1551	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32660	UniProtKB	Modified residue	1552	1552	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32660	UniProtKB	Modified residue	1563	1563	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32660	UniProtKB	Cross-link	895	895	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12675	
+##sequence-region Q12674 1 1656
+Q12674	UniProtKB	Chain	1	1656	.	.	.	ID=PRO_0000046237;Note=Probable phospholipid-transporting ATPase DNF3	
+Q12674	UniProtKB	Topological domain	1	164	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12674	UniProtKB	Transmembrane	165	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Topological domain	186	451	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Transmembrane	452	472	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Topological domain	473	495	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12674	UniProtKB	Transmembrane	496	516	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Topological domain	517	1157	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Transmembrane	1158	1178	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Topological domain	1179	1318	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12674	UniProtKB	Transmembrane	1319	1339	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Topological domain	1340	1365	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Transmembrane	1366	1386	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Topological domain	1387	1395	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12674	UniProtKB	Transmembrane	1396	1416	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Topological domain	1417	1432	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Transmembrane	1433	1453	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Topological domain	1454	1473	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12674	UniProtKB	Transmembrane	1474	1494	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12674	UniProtKB	Topological domain	1495	1656	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+Q12674	UniProtKB	Active site	566	566	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12674	UniProtKB	Modified residue	627	627	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q03153 1 612
+Q03153	UniProtKB	Transit peptide	1	14	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03153	UniProtKB	Chain	15	612	.	.	.	ID=PRO_0000203288;Note=ATPase synthesis protein 25%2C mitochondrial	
+##sequence-region P30902 1 174
+P30902	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1832157;Dbxref=PMID:1832157	
+P30902	UniProtKB	Chain	2	174	.	.	.	ID=PRO_0000071681;Note=ATP synthase subunit d%2C mitochondrial	
+P30902	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1832157;Dbxref=PMID:1832157	
+##sequence-region P00856 1 48
+P00856	UniProtKB	Chain	1	48	.	.	.	ID=PRO_0000195607;Note=ATP synthase protein 8	
+P00856	UniProtKB	Transmembrane	13	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12406 1 477
+Q12406	UniProtKB	Chain	1	477	.	.	.	ID=PRO_0000089122;Note=Actin-related protein 7	
+Q12406	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. A->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12805231,ECO:0000269|PubMed:9844636;Dbxref=PMID:12805231,PMID:9844636	
+Q12406	UniProtKB	Mutagenesis	33	33	.	.	.	Note=Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. S->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12805231,ECO:0000269|PubMed:9844636;Dbxref=PMID:12805231,PMID:9844636	
+Q12406	UniProtKB	Mutagenesis	396	396	.	.	.	Note=Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9844636;Dbxref=PMID:9844636	
+Q12406	UniProtKB	Mutagenesis	411	411	.	.	.	Note=Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12805231,ECO:0000269|PubMed:9844636;Dbxref=PMID:12805231,PMID:9844636	
+Q12406	UniProtKB	Beta strand	8	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	14	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	28	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE	
+Q12406	UniProtKB	Beta strand	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE	
+Q12406	UniProtKB	Helix	51	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	66	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE	
+Q12406	UniProtKB	Helix	80	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Turn	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE	
+Q12406	UniProtKB	Beta strand	104	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE	
+Q12406	UniProtKB	Helix	116	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Turn	128	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	134	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	141	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Turn	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	152	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	164	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	186	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	217	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	227	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	243	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	287	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	293	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	297	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	303	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	316	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	329	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Turn	339	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	344	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE	
+Q12406	UniProtKB	Helix	381	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	391	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	397	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	404	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	423	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE	
+Q12406	UniProtKB	Helix	429	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	435	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	449	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Beta strand	454	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+Q12406	UniProtKB	Helix	457	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+##sequence-region P40518 1 154
+P40518	UniProtKB	Chain	1	154	.	.	.	ID=PRO_0000124059;Note=Actin-related protein 2/3 complex subunit 5	
+P40518	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q06598 1 404
+Q06598	UniProtKB	Chain	1	404	.	.	.	ID=PRO_0000064440;Note=Arsenical-resistance protein 3	
+Q06598	UniProtKB	Topological domain	1	34	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482	
+Q06598	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06598	UniProtKB	Topological domain	56	69	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482	
+Q06598	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06598	UniProtKB	Topological domain	91	113	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482	
+Q06598	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06598	UniProtKB	Topological domain	135	141	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482	
+Q06598	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06598	UniProtKB	Topological domain	163	169	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482	
+Q06598	UniProtKB	Transmembrane	170	190	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06598	UniProtKB	Topological domain	191	216	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482	
+Q06598	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06598	UniProtKB	Topological domain	238	245	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482	
+Q06598	UniProtKB	Transmembrane	246	266	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06598	UniProtKB	Topological domain	267	280	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482	
+Q06598	UniProtKB	Transmembrane	281	301	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06598	UniProtKB	Topological domain	302	343	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482	
+Q06598	UniProtKB	Transmembrane	344	364	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06598	UniProtKB	Topological domain	365	369	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482	
+Q06598	UniProtKB	Transmembrane	370	390	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06598	UniProtKB	Topological domain	391	404	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482	
+Q06598	UniProtKB	Glycosylation	201	201	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q06598	UniProtKB	Glycosylation	365	365	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q06598	UniProtKB	Mutagenesis	90	90	.	.	.	Note=Leads to ER retention and arsenite sensitivity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645	
+Q06598	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Impairs cell membrane localization%2C and leads to arsenite sensitivity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	150	150	.	.	.	Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	151	151	.	.	.	Note=Leads to complete loss of metalloid transport function. C->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645	
+Q06598	UniProtKB	Mutagenesis	158	158	.	.	.	Note=Impairs cell membrane localization%2C and leads to arsenite sensitivity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	169	169	.	.	.	Note=Greatly reduces arsenite efflux. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645	
+Q06598	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	192	192	.	.	.	Note=Results in moderate reduction of arsenite transport capacities and sorting perturbations. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645	
+Q06598	UniProtKB	Mutagenesis	230	230	.	.	.	Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	266	266	.	.	.	Note=Impairs arsenite resistance. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	283	283	.	.	.	Note=Does not alter the arsenite/proton exchange across the plasma membrane. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645	
+Q06598	UniProtKB	Mutagenesis	290	290	.	.	.	Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	316	316	.	.	.	Note=Results in moderate reduction of arsenite transport capacities and sorting perturbations. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645	
+Q06598	UniProtKB	Mutagenesis	318	318	.	.	.	Note=Results in moderate reduction of arsenite transport capacities and sorting perturbations. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645	
+Q06598	UniProtKB	Mutagenesis	333	333	.	.	.	Note=Results in moderate reduction of arsenite transport capacities and sorting perturbations. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645	
+Q06598	UniProtKB	Mutagenesis	344	344	.	.	.	Note=Results in moderate reduction of arsenite transport capacities and sorting perturbations. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645	
+Q06598	UniProtKB	Mutagenesis	345	345	.	.	.	Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	349	349	.	.	.	Note=Impairs arsenite resistance. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	351	351	.	.	.	Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	352	352	.	.	.	Note=Impairs arsenite resistance. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	353	353	.	.	.	Note=Impairs arsenite resistance. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+Q06598	UniProtKB	Mutagenesis	380	380	.	.	.	Note=Impairs arsenite resistance. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064	
+##sequence-region Q8TGM7 1 61
+Q8TGM7	UniProtKB	Chain	1	61	.	.	.	ID=PRO_0000262870;Note=Putative uncharacterized protein ART2	
+##sequence-region P35734 1 292
+P35734	UniProtKB	Chain	1	292	.	.	.	ID=PRO_0000211317;Note=DASH complex subunit ASK1	
+P35734	UniProtKB	Modified residue	26	26	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:12408861;Dbxref=PMID:18407956,PMID:12408861	
+P35734	UniProtKB	Modified residue	118	118	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861	
+P35734	UniProtKB	Modified residue	134	134	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:17330950,PMID:19779198,PMID:12408861	
+P35734	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861	
+P35734	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P35734	UniProtKB	Modified residue	156	156	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P35734	UniProtKB	Modified residue	200	200	.	.	.	Note=Phosphoserine%3B by IPL1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:12408861	
+P35734	UniProtKB	Modified residue	216	216	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35734	UniProtKB	Modified residue	250	250	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861	
+P35734	UniProtKB	Sequence conflict	14	14	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35734	UniProtKB	Sequence conflict	14	14	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35183 1 429
+P35183	UniProtKB	Chain	1	429	.	.	.	ID=PRO_0000064710;Note=Protein AST1	
+P35183	UniProtKB	Sequence conflict	326	429	.	.	.	Note=TVGDYVANYKEDIFDSWDNPSANARKMFGSIIWSYNYTHYYFDPNAKTASANNDWIEQCGDFLKNGTVKCVVDKVYDWKDHKEAFSYMATQRAQGKLIMNVEKF->HCR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40353 1 525
+P40353	UniProtKB	Chain	1	525	.	.	.	ID=PRO_0000064720;Note=Alcohol O-acetyltransferase 1	
+P40353	UniProtKB	Sequence conflict	84	84	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40353	UniProtKB	Sequence conflict	391	391	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53855 1 1592
+P53855	UniProtKB	Chain	1	1592	.	.	.	ID=PRO_0000215836;Note=Autophagy-related protein 2	
+P53855	UniProtKB	Coiled coil	1049	1075	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53855	UniProtKB	Modified residue	236	236	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53855	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Leads to a severely reduced activity of autophagy and a dispersed localization in the cytoplasm. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11382761;Dbxref=PMID:11382761	
+##sequence-region Q12292 1 412
+Q12292	UniProtKB	Chain	1	412	.	.	.	ID=PRO_0000235927;Note=Autophagy-related protein 34	
+Q12292	UniProtKB	Region	246	348	.	.	.	Note=AMS1-binding	
+Q12292	UniProtKB	Beta strand	251	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK	
+Q12292	UniProtKB	Beta strand	263	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK	
+Q12292	UniProtKB	Beta strand	269	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK	
+Q12292	UniProtKB	Beta strand	278	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK	
+Q12292	UniProtKB	Beta strand	284	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK	
+Q12292	UniProtKB	Beta strand	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK	
+Q12292	UniProtKB	Beta strand	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK	
+Q12292	UniProtKB	Beta strand	330	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK	
+Q12292	UniProtKB	Beta strand	338	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK	
+##sequence-region Q05789 1 226
+Q05789	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q05789	UniProtKB	Chain	2	226	.	.	.	ID=PRO_0000203237;Note=Autophagy-related protein 38	
+Q05789	UniProtKB	Coiled coil	52	85	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05789	UniProtKB	Coiled coil	161	215	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05789	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q05789	UniProtKB	Helix	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KC1	
+Q05789	UniProtKB	Helix	129	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KC1	
+Q05789	UniProtKB	Helix	156	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KC1	
+Q05789	UniProtKB	Helix	164	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KC1	
+##sequence-region Q01896 1 1091
+Q01896	UniProtKB	Chain	1	1091	.	.	.	ID=PRO_0000046243;Note=Sodium transport ATPase 2	
+Q01896	UniProtKB	Topological domain	1	63	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Topological domain	85	90	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Topological domain	112	282	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Transmembrane	283	303	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Topological domain	304	312	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Transmembrane	313	333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Topological domain	334	815	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Transmembrane	816	836	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Topological domain	837	848	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Transmembrane	849	869	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Topological domain	870	885	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Transmembrane	886	906	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Topological domain	907	943	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Transmembrane	944	964	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Topological domain	965	991	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Transmembrane	992	1012	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Topological domain	1013	1021	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Transmembrane	1022	1042	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Topological domain	1043	1091	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01896	UniProtKB	Active site	369	369	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P22135 1 325
+P22135	UniProtKB	Transit peptide	1	32	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22135	UniProtKB	Chain	33	325	.	.	.	ID=PRO_0000002421;Note=Protein ATP12%2C mitochondrial	
+P22135	UniProtKB	Sequence conflict	48	48	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38360 1 1216
+P38360	UniProtKB	Chain	1	1216	.	.	.	ID=PRO_0000046317;Note=P-type cation-transporting ATPase	
+P38360	UniProtKB	Topological domain	1	556	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Transmembrane	557	578	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Topological domain	579	592	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Transmembrane	593	612	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Topological domain	613	620	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Transmembrane	621	641	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Topological domain	642	659	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Transmembrane	660	680	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Topological domain	681	808	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Transmembrane	809	831	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Topological domain	832	847	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Transmembrane	848	865	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Topological domain	866	1161	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Transmembrane	1162	1181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Topological domain	1182	1190	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Transmembrane	1191	1209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Topological domain	1210	1216	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38360	UniProtKB	Domain	411	474	.	.	.	Note=HMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38360	UniProtKB	Region	250	350	.	.	.	Note=Metal-responding degradation signal	
+P38360	UniProtKB	Active site	903	903	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38360	UniProtKB	Metal binding	421	421	.	.	.	Note=Copper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38360	UniProtKB	Metal binding	424	424	.	.	.	Note=Copper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38360	UniProtKB	Metal binding	1107	1107	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38360	UniProtKB	Metal binding	1111	1111	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38360	UniProtKB	Mutagenesis	298	298	.	.	.	Note=Abolishes copper resistance but not cadmium resistance%3B when associated with A-300. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18753133;Dbxref=PMID:18753133	
+P38360	UniProtKB	Mutagenesis	300	300	.	.	.	Note=Abolishes copper resistance but not cadmium resistance%3B when associated with A-298. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18753133;Dbxref=PMID:18753133	
+P38360	UniProtKB	Mutagenesis	311	311	.	.	.	Note=Abolishes cadmium resistance yet retains the ability to confer copper resistance%3B when associated with A-312. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18753133;Dbxref=PMID:18753133	
+P38360	UniProtKB	Mutagenesis	312	312	.	.	.	Note=Abolishes cadmium resistance yet retains the ability to confer copper resistance%3B when associated with A-311. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18753133;Dbxref=PMID:18753133	
+P38360	UniProtKB	Mutagenesis	970	970	.	.	.	Note=Confers localization to the plasma membrane and cadmium transport function. R->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10743563,ECO:0000269|PubMed:17107946;Dbxref=PMID:10743563,PMID:17107946	
+P38360	UniProtKB	Sequence conflict	382	382	.	.	.	Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38360	UniProtKB	Sequence conflict	382	382	.	.	.	Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32450 1 94
+P32450	UniProtKB	Chain	1	94	.	.	.	ID=PRO_0000064762;Note=Ammonia regulation of amino acid uptake protein	
+P32450	UniProtKB	Repeat	48	57	.	.	.	.	
+P32450	UniProtKB	Repeat	58	67	.	.	.	.	
+P32450	UniProtKB	Compositional bias	41	94	.	.	.	Note=Arg/His/Lys-rich (basic)	
+##sequence-region P36107 1 401
+P36107	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000064766;Note=Inositol phosphorylceramide synthase catalytic subunit AUR1	
+P36107	UniProtKB	Topological domain	1	41	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Topological domain	63	64	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Topological domain	86	87	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Topological domain	109	155	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Transmembrane	156	176	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Topological domain	177	178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Topological domain	200	245	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Transmembrane	246	266	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Topological domain	267	268	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Transmembrane	269	289	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Topological domain	290	291	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Transmembrane	292	312	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Topological domain	313	401	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Modified residue	392	392	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P36107	UniProtKB	Modified residue	395	395	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P36107	UniProtKB	Glycosylation	132	132	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36107	UniProtKB	Mutagenesis	137	137	.	.	.	Note=AbA resistant%3B when associated with Y-157. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8593016;Dbxref=PMID:8593016	
+P36107	UniProtKB	Mutagenesis	157	157	.	.	.	Note=AbA resistant%3B when associated with F-137. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8593016;Dbxref=PMID:8593016	
+P36107	UniProtKB	Mutagenesis	158	158	.	.	.	Note=In AUR1-1%3B AbA resistant. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8668135;Dbxref=PMID:8668135	
+P36107	UniProtKB	Mutagenesis	294	294	.	.	.	Note=Abolishes catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888667;Dbxref=PMID:10888667	
+##sequence-region P39981 1 480
+P39981	UniProtKB	Chain	1	480	.	.	.	ID=PRO_0000093835;Note=Vacuolar amino acid transporter 2	
+P39981	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39981	UniProtKB	Transmembrane	95	115	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39981	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39981	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39981	UniProtKB	Transmembrane	263	283	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39981	UniProtKB	Transmembrane	297	317	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39981	UniProtKB	Transmembrane	338	358	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39981	UniProtKB	Transmembrane	394	414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39981	UniProtKB	Transmembrane	447	467	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36062 1 692
+P36062	UniProtKB	Chain	1	692	.	.	.	ID=PRO_0000093836;Note=Vacuolar amino acid transporter 3	
+P36062	UniProtKB	Transmembrane	302	322	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36062	UniProtKB	Transmembrane	329	349	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36062	UniProtKB	Transmembrane	374	394	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36062	UniProtKB	Transmembrane	412	432	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36062	UniProtKB	Transmembrane	443	463	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36062	UniProtKB	Transmembrane	483	503	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36062	UniProtKB	Transmembrane	519	539	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36062	UniProtKB	Transmembrane	561	581	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36062	UniProtKB	Transmembrane	607	627	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36062	UniProtKB	Transmembrane	630	650	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36062	UniProtKB	Transmembrane	665	685	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36062	UniProtKB	Compositional bias	261	276	.	.	.	Note=Poly-Glu	
+P36062	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P36062	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36062	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P36062	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53629 1 642
+P53629	UniProtKB	Chain	1	642	.	.	.	ID=PRO_0000207651;Note=Sterol O-acyltransferase 2	
+P53629	UniProtKB	Transmembrane	215	235	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53629	UniProtKB	Transmembrane	292	312	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53629	UniProtKB	Transmembrane	404	424	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53629	UniProtKB	Transmembrane	442	462	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53629	UniProtKB	Transmembrane	485	505	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53629	UniProtKB	Transmembrane	567	587	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53629	UniProtKB	Transmembrane	622	642	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53629	UniProtKB	Active site	579	579	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53629	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53629	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53629	UniProtKB	Sequence conflict	80	80	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53629	UniProtKB	Sequence conflict	184	184	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53629	UniProtKB	Sequence conflict	211	211	.	.	.	Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53629	UniProtKB	Sequence conflict	612	612	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P19146 1 181
+P19146	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+P19146	UniProtKB	Chain	2	181	.	.	.	ID=PRO_0000207419;Note=ADP-ribosylation factor 2	
+P19146	UniProtKB	Nucleotide binding	25	32	.	.	.	Note=GTP	
+P19146	UniProtKB	Nucleotide binding	126	129	.	.	.	Note=GTP	
+P19146	UniProtKB	Nucleotide binding	160	161	.	.	.	Note=GTP	
+P19146	UniProtKB	Binding site	48	48	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19146	UniProtKB	Binding site	70	70	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19146	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19146	UniProtKB	Cross-link	127	127	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11076	
+P19146	UniProtKB	Helix	10	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Beta strand	18	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Helix	30	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Beta strand	43	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Beta strand	51	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Beta strand	61	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Helix	76	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Beta strand	86	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Helix	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Helix	100	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Beta strand	120	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Helix	136	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Helix	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Beta strand	153	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Turn	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+P19146	UniProtKB	Helix	166	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3	
+##sequence-region P14843 1 370
+P14843	UniProtKB	Chain	1	370	.	.	.	ID=PRO_0000140849;Note=Phospho-2-dehydro-3-deoxyheptonate aldolase%2C phenylalanine-inhibited	
+##sequence-region P32448 1 525
+P32448	UniProtKB	Chain	1	525	.	.	.	ID=PRO_0000064696;Note=Anti-silencing protein 2	
+##sequence-region P53895 1 289
+P53895	UniProtKB	Chain	1	289	.	.	.	ID=PRO_0000203414;Note=Protein ASI2	
+P53895	UniProtKB	Topological domain	1	222	.	.	.	Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53895	UniProtKB	Transmembrane	223	243	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53895	UniProtKB	Topological domain	244	247	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53895	UniProtKB	Transmembrane	248	268	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53895	UniProtKB	Topological domain	269	289	.	.	.	Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04489 1 525
+Q04489	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04489	UniProtKB	Chain	2	525	.	.	.	ID=PRO_0000056940;Note=Asparagine synthetase domain-containing protein YML096W	
+Q04489	UniProtKB	Domain	2	209	.	.	.	Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609	
+Q04489	UniProtKB	Domain	210	523	.	.	.	Note=Asparagine synthetase	
+Q04489	UniProtKB	Active site	2	2	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P49089 1 572
+P49089	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49089	UniProtKB	Chain	2	572	.	.	.	ID=PRO_0000056917;Note=Asparagine synthetase [glutamine-hydrolyzing] 1	
+P49089	UniProtKB	Domain	2	186	.	.	.	Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609	
+P49089	UniProtKB	Domain	194	546	.	.	.	Note=Asparagine synthetase	
+P49089	UniProtKB	Nucleotide binding	366	367	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49089	UniProtKB	Region	49	53	.	.	.	Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49089	UniProtKB	Region	74	76	.	.	.	Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49089	UniProtKB	Active site	2	2	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49089	UniProtKB	Binding site	97	97	.	.	.	Note=Glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49089	UniProtKB	Binding site	233	233	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49089	UniProtKB	Binding site	292	292	.	.	.	Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49089	UniProtKB	Site	368	368	.	.	.	Note=Important for beta-aspartyl-AMP intermediate formation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49089	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P49089	UniProtKB	Modified residue	509	509	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P49090 1 572
+P49090	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49090	UniProtKB	Chain	2	572	.	.	.	ID=PRO_0000056918;Note=Asparagine synthetase [glutamine-hydrolyzing] 2	
+P49090	UniProtKB	Domain	2	186	.	.	.	Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609	
+P49090	UniProtKB	Domain	194	545	.	.	.	Note=Asparagine synthetase	
+P49090	UniProtKB	Nucleotide binding	365	366	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49090	UniProtKB	Region	49	53	.	.	.	Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49090	UniProtKB	Region	74	76	.	.	.	Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49090	UniProtKB	Active site	2	2	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49090	UniProtKB	Binding site	97	97	.	.	.	Note=Glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49090	UniProtKB	Binding site	233	233	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49090	UniProtKB	Binding site	291	291	.	.	.	Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49090	UniProtKB	Site	367	367	.	.	.	Note=Important for beta-aspartyl-AMP intermediate formation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49090	UniProtKB	Sequence conflict	560	560	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43601 1 500
+P43601	UniProtKB	Chain	1	500	.	.	.	ID=PRO_0000050874;Note=Autophagy-related protein 18	
+P43601	UniProtKB	Repeat	243	283	.	.	.	Note=WD 1	
+P43601	UniProtKB	Repeat	288	327	.	.	.	Note=WD 2	
+P43601	UniProtKB	Region	284	287	.	.	.	Note=Necessary for proper localization to vacuole membrane	
+P43601	UniProtKB	Motif	284	288	.	.	.	Note=FRRGT-motif;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16876790;Dbxref=PMID:16876790	
+P43601	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43601	UniProtKB	Mutagenesis	73	76	.	.	.	Note=Slight reduction of PIP2 binding. RRLR->SSLS	
+P43601	UniProtKB	Mutagenesis	264	264	.	.	.	Note=Impairs membrane-association. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491	
+P43601	UniProtKB	Mutagenesis	268	268	.	.	.	Note=Impairs membrane-association. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491	
+P43601	UniProtKB	Mutagenesis	271	271	.	.	.	Note=Impairs membrane-association. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491	
+P43601	UniProtKB	Mutagenesis	285	286	.	.	.	Note=Loss of recruitment to vacuole membrane. RR->GG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491	
+P43601	UniProtKB	Mutagenesis	285	286	.	.	.	Note=40-fold decrease of affinity to PIP2. RR->TT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491	
+P43601	UniProtKB	Mutagenesis	285	285	.	.	.	Note=Impairs membrane-association. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491	
+P43601	UniProtKB	Mutagenesis	286	286	.	.	.	Note=Impairs membrane-association. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491	
+P43601	UniProtKB	Mutagenesis	311	311	.	.	.	Note=Impairs membrane-association. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491	
+P43601	UniProtKB	Mutagenesis	313	313	.	.	.	Note=Impairs membrane-association. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491	
+P43601	UniProtKB	Mutagenesis	315	315	.	.	.	Note=Impairs membrane-association. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491	
+##sequence-region Q02887 1 496
+Q02887	UniProtKB	Chain	1	496	.	.	.	ID=PRO_0000050882;Note=Autophagy-related protein 21	
+Q02887	UniProtKB	Repeat	294	334	.	.	.	Note=WD 1	
+Q02887	UniProtKB	Repeat	346	385	.	.	.	Note=WD 2	
+Q02887	UniProtKB	Repeat	448	488	.	.	.	Note=WD 3	
+Q02887	UniProtKB	Motif	342	346	.	.	.	Note=FRRGT-motif	
+Q02887	UniProtKB	Compositional bias	77	80	.	.	.	Note=Poly-Glu	
+Q02887	UniProtKB	Modified residue	213	213	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02887	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q02887	UniProtKB	Mutagenesis	343	344	.	.	.	Note=Loss of aminopeptidase I precursor maturation and no more association with vacuole and punctate structures. RR->KK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15155809;Dbxref=PMID:15155809	
+##sequence-region P25568 1 528
+P25568	UniProtKB	Chain	1	528	.	.	.	ID=PRO_0000207629;Note=Autophagy-related protein 22	
+P25568	UniProtKB	Topological domain	1	98	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Topological domain	120	130	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Topological domain	152	153	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Transmembrane	154	174	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Topological domain	175	210	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Transmembrane	211	231	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Topological domain	232	241	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Topological domain	263	318	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Transmembrane	319	339	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Topological domain	340	352	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Transmembrane	353	373	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Topological domain	374	388	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Transmembrane	389	409	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Topological domain	410	417	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Transmembrane	418	438	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Topological domain	439	485	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Transmembrane	486	506	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Topological domain	507	528	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25568	UniProtKB	Modified residue	278	278	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q06485 1 197
+Q06485	UniProtKB	Chain	1	197	.	.	.	ID=PRO_0000247213;Note=Autophagy-related protein 33	
+Q06485	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06485	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06485	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06485	UniProtKB	Transmembrane	172	192	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06485	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06485	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40344 1 310
+P40344	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000213586;Note=Autophagy-related protein 3	
+P40344	UniProtKB	Region	1	7	.	.	.	Note=PE-binding	
+P40344	UniProtKB	Region	83	163	.	.	.	Note=Flexible region	
+P40344	UniProtKB	Region	238	285	.	.	.	Note=Handle region	
+P40344	UniProtKB	Motif	270	273	.	.	.	Note=ATG8 interaction motif (AIM)	
+P40344	UniProtKB	Active site	234	234	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40344	UniProtKB	Modified residue	19	19	.	.	.	Note=N6-acetyllysine%3B by ESA1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22539722;Dbxref=PMID:22539722	
+P40344	UniProtKB	Modified residue	48	48	.	.	.	Note=N6-acetyllysine%3B by ESA1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22539722;Dbxref=PMID:22539722	
+P40344	UniProtKB	Mutagenesis	213	213	.	.	.	Note=Decreases ATG8-PE comjugation and autophagy. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23503366;Dbxref=PMID:23503366	
+P40344	UniProtKB	Mutagenesis	234	234	.	.	.	Note=Loss of interaction with ATG8 and defect in autophagy and Cvt pathway. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11100732,ECO:0000269|PubMed:15277523;Dbxref=PMID:11100732,PMID:15277523	
+P40344	UniProtKB	Mutagenesis	234	234	.	.	.	Note=Instead of the formation of an intermediate complex with a thiol ester bond between ATG3 (E2-like enzyme) and ATG8 (substrate)%2C a stable complex with an O-ester bond is formed. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11100732,ECO:0000269|PubMed:15277523;Dbxref=PMID:11100732,PMID:15277523	
+P40344	UniProtKB	Mutagenesis	270	270	.	.	.	Note=Decreases interaction with ATG8. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20615880;Dbxref=PMID:20615880	
+P40344	UniProtKB	Mutagenesis	272	272	.	.	.	Note=Decreases interaction with ATG8. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20615880;Dbxref=PMID:20615880	
+P40344	UniProtKB	Mutagenesis	273	273	.	.	.	Note=Decreases interaction with ATG8. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20615880;Dbxref=PMID:20615880	
+P40344	UniProtKB	Helix	22	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Helix	30	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSL	
+P40344	UniProtKB	Helix	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSL	
+P40344	UniProtKB	Beta strand	69	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Turn	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Helix	135	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7G	
+P40344	UniProtKB	Beta strand	167	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Turn	177	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Beta strand	181	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Helix	198	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Turn	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Helix	210	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Beta strand	214	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Beta strand	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Beta strand	227	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Beta strand	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Helix	239	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Helix	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+P40344	UniProtKB	Helix	286	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT	
+##sequence-region P32907 1 282
+P32907	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P32907	UniProtKB	Chain	2	282	.	.	.	ID=PRO_0000135701;Note=Ammonia transport outward protein 2	
+P32907	UniProtKB	Topological domain	2	86	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Transmembrane	87	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Topological domain	108	119	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Topological domain	141	150	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Transmembrane	151	171	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Topological domain	172	184	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Topological domain	206	207	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Topological domain	229	238	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Transmembrane	239	259	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Topological domain	260	282	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32907	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P32907	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P32907	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P32907	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P32907	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P32907	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P32907	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+##sequence-region Q12349 1 124
+Q12349	UniProtKB	Transit peptide	1	32	.	.	.	Note=Mitochondrion	
+Q12349	UniProtKB	Chain	33	124	.	.	.	ID=PRO_0000002525;Note=ATP synthase subunit H%2C mitochondrial	
+##sequence-region P32454 1 952
+P32454	UniProtKB	Transit peptide	1	52	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32454	UniProtKB	Chain	53	952	.	.	.	ID=PRO_0000095104;Note=Aminopeptidase 2%2C mitochondrial	
+P32454	UniProtKB	Region	360	364	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32454	UniProtKB	Active site	397	397	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P32454	UniProtKB	Metal binding	396	396	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P32454	UniProtKB	Metal binding	400	400	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P32454	UniProtKB	Metal binding	419	419	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P32454	UniProtKB	Binding site	228	228	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32454	UniProtKB	Site	482	482	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32454	UniProtKB	Glycosylation	381	381	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32454	UniProtKB	Glycosylation	713	713	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32454	UniProtKB	Sequence conflict	73	73	.	.	.	Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32454	UniProtKB	Sequence conflict	92	93	.	.	.	Note=LL->FI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32454	UniProtKB	Sequence conflict	255	255	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32454	UniProtKB	Sequence conflict	533	533	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P05085 1 880
+P05085	UniProtKB	Chain	1	880	.	.	.	ID=PRO_0000114937;Note=Arginine metabolism regulation protein II	
+P05085	UniProtKB	DNA binding	21	48	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P05085	UniProtKB	Sequence conflict	4	4	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05085	UniProtKB	Sequence conflict	129	129	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05085	UniProtKB	Sequence conflict	283	283	.	.	.	Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05085	UniProtKB	Sequence conflict	345	345	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05085	UniProtKB	Sequence conflict	366	366	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05085	UniProtKB	Sequence conflict	549	549	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05085	UniProtKB	Sequence conflict	597	597	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05085	UniProtKB	Sequence conflict	665	665	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05085	UniProtKB	Sequence conflict	869	869	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32381 1 391
+P32381	UniProtKB	Chain	1	391	.	.	.	ID=PRO_0000089077;Note=Actin-related protein 2	
+P32381	UniProtKB	Nucleotide binding	159	161	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32381	UniProtKB	Nucleotide binding	213	217	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32381	UniProtKB	Nucleotide binding	304	309	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32381	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P47117 1 449
+P47117	UniProtKB	Chain	1	449	.	.	.	ID=PRO_0000089090;Note=Actin-related protein 3	
+##sequence-region Q12509 1 438
+Q12509	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000089121;Note=Actin-like protein ARP6	
+##sequence-region P33204 1 171
+P33204	UniProtKB	Chain	1	171	.	.	.	ID=PRO_0000124053;Note=Actin-related protein 2/3 complex subunit 4	
+##sequence-region P53244 1 586
+P53244	UniProtKB	Chain	1	586	.	.	.	ID=PRO_0000202804;Note=Arrestin-related trafficking adapter 5	
+P53244	UniProtKB	Compositional bias	199	204	.	.	.	Note=Poly-Ser	
+P53244	UniProtKB	Cross-link	364	364	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P53983 1 676
+P53983	UniProtKB	Chain	1	676	.	.	.	ID=PRO_0000203467;Note=Protein ASI3	
+P53983	UniProtKB	Topological domain	1	78	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Transmembrane	79	99	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Topological domain	100	126	.	.	.	Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Transmembrane	127	147	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Topological domain	148	156	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Topological domain	178	181	.	.	.	Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Topological domain	203	277	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Transmembrane	278	298	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Topological domain	299	676	.	.	.	Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Zinc finger	624	664	.	.	.	Note=RING-type%3B atypical	
+P53983	UniProtKB	Glycosylation	24	24	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Glycosylation	34	34	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Glycosylation	46	46	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Glycosylation	66	66	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53983	UniProtKB	Sequence conflict	1	15	.	.	.	Note=MSTNILQHVKQLLHN->MLSNCSIT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53983	UniProtKB	Sequence conflict	1	15	.	.	.	Note=MSTNILQHVKQLLHN->MLSNCSIT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CZ17 1 362
+P0CZ17	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786	
+P0CZ17	UniProtKB	Chain	26	362	.	.	.	ID=PRO_0000002362;Note=L-asparaginase 2-1	
+P0CZ17	UniProtKB	Domain	33	359	.	.	.	Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068	
+P0CZ17	UniProtKB	Region	122	123	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CZ17	UniProtKB	Active site	43	43	.	.	.	Note=O-isoaspartyl threonine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10099,ECO:0000255|PROSITE-ProRule:PRU10100	
+P0CZ17	UniProtKB	Binding site	89	89	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CZ17	UniProtKB	Glycosylation	29	29	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CZ17	UniProtKB	Glycosylation	93	93	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CZ17	UniProtKB	Glycosylation	239	239	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CZ17	UniProtKB	Natural variant	26	55	.	.	.	Note=Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786	
+P0CZ17	UniProtKB	Sequence conflict	31	31	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38929 1 1173
+P38929	UniProtKB	Chain	1	1173	.	.	.	ID=PRO_0000046232;Note=Calcium-transporting ATPase 2	
+P38929	UniProtKB	Topological domain	1	114	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Transmembrane	115	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Topological domain	140	152	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Topological domain	174	349	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Transmembrane	350	368	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Topological domain	369	388	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Transmembrane	389	409	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Topological domain	410	899	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Transmembrane	900	922	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Topological domain	923	929	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Transmembrane	930	950	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Topological domain	951	976	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Transmembrane	977	998	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Topological domain	999	1010	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Transmembrane	1011	1029	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Topological domain	1030	1065	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Transmembrane	1066	1086	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Topological domain	1087	1099	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Transmembrane	1100	1120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Topological domain	1121	1173	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38929	UniProtKB	Active site	445	445	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P39524 1 1355
+P39524	UniProtKB	Chain	1	1355	.	.	.	ID=PRO_0000046233;Note=Probable phospholipid-transporting ATPase DRS2	
+P39524	UniProtKB	Topological domain	1	221	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Transmembrane	222	242	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Topological domain	243	246	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Transmembrane	247	267	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Topological domain	268	449	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Transmembrane	450	470	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Topological domain	471	490	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Transmembrane	491	511	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Topological domain	512	1012	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Transmembrane	1013	1033	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Topological domain	1034	1043	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Transmembrane	1044	1064	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Topological domain	1065	1094	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Transmembrane	1095	1115	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Topological domain	1116	1131	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Transmembrane	1132	1152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Topological domain	1153	1161	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Transmembrane	1162	1182	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Topological domain	1183	1202	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Transmembrane	1203	1223	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Topological domain	1224	1355	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39524	UniProtKB	Active site	560	560	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39524	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39524	UniProtKB	Sequence conflict	45	46	.	.	.	Note=AN->GY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39524	UniProtKB	Sequence conflict	45	46	.	.	.	Note=AN->GY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39524	UniProtKB	Sequence conflict	450	450	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39524	UniProtKB	Sequence conflict	450	450	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39524	UniProtKB	Sequence conflict	674	674	.	.	.	Note=P->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39524	UniProtKB	Sequence conflict	674	674	.	.	.	Note=P->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39524	UniProtKB	Sequence conflict	891	892	.	.	.	Note=NT->KS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39524	UniProtKB	Sequence conflict	891	892	.	.	.	Note=NT->KS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39524	UniProtKB	Sequence conflict	953	954	.	.	.	Note=GD->AS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39524	UniProtKB	Sequence conflict	953	954	.	.	.	Note=GD->AS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39524	UniProtKB	Sequence conflict	987	987	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39524	UniProtKB	Sequence conflict	987	987	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39986 1 1215
+P39986	UniProtKB	Chain	1	1215	.	.	.	ID=PRO_0000046349;Note=Manganese-transporting ATPase 1	
+P39986	UniProtKB	Topological domain	1	21	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	22	43	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	44	49	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	50	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	73	191	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	192	214	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	215	217	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	218	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	237	399	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	400	419	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	420	432	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	433	454	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	455	993	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	994	1013	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	1014	1020	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	1021	1037	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	1038	1055	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	1056	1079	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	1080	1099	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	1100	1122	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	1123	1133	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	1134	1153	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	1154	1170	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Transmembrane	1171	1193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Topological domain	1194	1215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39986	UniProtKB	Active site	487	487	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39986	UniProtKB	Metal binding	816	816	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39986	UniProtKB	Metal binding	820	820	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39986	UniProtKB	Modified residue	324	324	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39986	UniProtKB	Modified residue	936	936	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39986	UniProtKB	Mutagenesis	487	487	.	.	.	Note=Loss of ATPase activity and transport function. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24392018;Dbxref=PMID:24392018	
+##sequence-region Q01217 1 863
+Q01217	UniProtKB	Transit peptide	1	65	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01217	UniProtKB	Chain	66	532	.	.	.	ID=PRO_0000002073;Note=Acetylglutamate kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01217	UniProtKB	Chain	533	863	.	.	.	ID=PRO_0000002074;Note=N-acetyl-gamma-glutamyl-phosphate reductase;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01217	UniProtKB	Domain	353	505	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+Q01217	UniProtKB	Active site	675	675	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10010	
+Q01217	UniProtKB	Modified residue	359	359	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q01217	UniProtKB	Helix	68	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Helix	81	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	100	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Helix	106	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Helix	113	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	130	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Helix	137	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Helix	162	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	190	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	195	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Helix	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	209	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Helix	220	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	231	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZG	
+Q01217	UniProtKB	Beta strand	244	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Helix	250	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	264	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	271	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZF	
+Q01217	UniProtKB	Turn	278	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Helix	289	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZG	
+Q01217	UniProtKB	Helix	304	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	326	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Helix	331	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Helix	334	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Beta strand	345	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH	
+Q01217	UniProtKB	Beta strand	355	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Helix	360	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Helix	366	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Turn	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Beta strand	380	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Helix	386	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Beta strand	398	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Beta strand	407	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Beta strand	415	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Beta strand	420	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Helix	428	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Helix	435	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Beta strand	448	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Helix	461	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Beta strand	469	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Beta strand	477	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+Q01217	UniProtKB	Helix	487	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7	
+##sequence-region Q02804 1 198
+Q02804	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000207422;Note=ADP-ribosylation factor-like protein 3	
+Q02804	UniProtKB	Nucleotide binding	24	31	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02804	UniProtKB	Nucleotide binding	74	78	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02804	UniProtKB	Nucleotide binding	133	136	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02804	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15077113,ECO:0000269|PubMed:15077114;Dbxref=PMID:15077113,PMID:15077114	
+Q02804	UniProtKB	Cross-link	50	50	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P28777 1 376
+P28777	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P28777	UniProtKB	Chain	2	376	.	.	.	ID=PRO_0000140704;Note=Chorismate synthase	
+P28777	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P28777	UniProtKB	Beta strand	6	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Beta strand	18	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Beta strand	30	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R52	
+P28777	UniProtKB	Helix	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Helix	40	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R52	
+P28777	UniProtKB	Beta strand	67	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Beta strand	79	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Helix	130	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Beta strand	150	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Helix	170	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Helix	181	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Helix	195	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Beta strand	217	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Turn	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Helix	238	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Beta strand	254	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R52	
+P28777	UniProtKB	Turn	258	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Helix	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Helix	268	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Beta strand	293	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Beta strand	304	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Helix	342	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+P28777	UniProtKB	Helix	347	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53	
+##sequence-region P18634 1 518
+P18634	UniProtKB	Chain	1	518	.	.	.	ID=PRO_0000203235;Note=Arrestin-related trafficking adapter 10	
+P18634	UniProtKB	Cross-link	118	118	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P50275 1 885
+P50275	UniProtKB	Chain	1	885	.	.	.	ID=PRO_0000064694;Note=Anaphase spindle elongation protein	
+P50275	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P0CX77 1 362
+P0CX77	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786	
+P0CX77	UniProtKB	Chain	26	362	.	.	.	ID=PRO_0000410441;Note=L-asparaginase 2-2	
+P0CX77	UniProtKB	Domain	33	359	.	.	.	Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068	
+P0CX77	UniProtKB	Region	122	123	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX77	UniProtKB	Active site	43	43	.	.	.	Note=O-isoaspartyl threonine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10099,ECO:0000255|PROSITE-ProRule:PRU10100	
+P0CX77	UniProtKB	Binding site	89	89	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX77	UniProtKB	Glycosylation	29	29	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX77	UniProtKB	Glycosylation	93	93	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX77	UniProtKB	Glycosylation	239	239	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX77	UniProtKB	Natural variant	26	55	.	.	.	Note=Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786	
+P0CX77	UniProtKB	Sequence conflict	243	243	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CX78 1 362
+P0CX78	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786	
+P0CX78	UniProtKB	Chain	26	362	.	.	.	ID=PRO_0000410442;Note=L-asparaginase 2-3	
+P0CX78	UniProtKB	Domain	33	359	.	.	.	Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068	
+P0CX78	UniProtKB	Region	122	123	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX78	UniProtKB	Active site	43	43	.	.	.	Note=O-isoaspartyl threonine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10099,ECO:0000255|PROSITE-ProRule:PRU10100	
+P0CX78	UniProtKB	Binding site	89	89	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX78	UniProtKB	Glycosylation	29	29	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX78	UniProtKB	Glycosylation	93	93	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX78	UniProtKB	Glycosylation	239	239	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX78	UniProtKB	Natural variant	26	55	.	.	.	Note=Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786	
+##sequence-region P40416 1 690
+P40416	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40416	UniProtKB	Chain	27	690	.	.	.	ID=PRO_0000000258;Note=Iron-sulfur clusters transporter ATM1%2C mitochondrial	
+P40416	UniProtKB	Topological domain	27	110	.	.	.	Note=Mitochondrial matrix	
+P40416	UniProtKB	Transmembrane	111	132	.	.	.	Note=Helical	
+P40416	UniProtKB	Topological domain	133	155	.	.	.	Note=Mitochondrial intermembrane	
+P40416	UniProtKB	Transmembrane	156	179	.	.	.	Note=Helical	
+P40416	UniProtKB	Topological domain	180	228	.	.	.	Note=Mitochondrial matrix	
+P40416	UniProtKB	Transmembrane	229	252	.	.	.	Note=Helical	
+P40416	UniProtKB	Topological domain	253	253	.	.	.	Note=Mitochondrial intermembrane	
+P40416	UniProtKB	Transmembrane	254	274	.	.	.	Note=Helical	
+P40416	UniProtKB	Topological domain	275	340	.	.	.	Note=Mitochondrial matrix	
+P40416	UniProtKB	Transmembrane	341	359	.	.	.	Note=Helical	
+P40416	UniProtKB	Topological domain	360	374	.	.	.	Note=Mitochondrial intermembrane	
+P40416	UniProtKB	Transmembrane	375	396	.	.	.	Note=Helical	
+P40416	UniProtKB	Topological domain	397	690	.	.	.	Note=Mitochondrial matrix	
+P40416	UniProtKB	Domain	111	401	.	.	.	Note=ABC transmembrane type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P40416	UniProtKB	Domain	436	672	.	.	.	Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P40416	UniProtKB	Nucleotide binding	469	480	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P40416	UniProtKB	Region	280	284	.	.	.	Note=Glutathione binding	
+P40416	UniProtKB	Region	343	346	.	.	.	Note=Glutathione binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40416	UniProtKB	Binding site	393	393	.	.	.	Note=Glutathione%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40416	UniProtKB	Binding site	445	445	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40416	UniProtKB	Mutagenesis	475	475	.	.	.	Note=Loss of function%3B significant decrease in ATP-binding%3B no homodimerization. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15225610;Dbxref=PMID:15225610	
+P40416	UniProtKB	Mutagenesis	598	598	.	.	.	Note=Loss of function%3B slight decrease in ATP-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15225610;Dbxref=PMID:15225610	
+P40416	UniProtKB	Mutagenesis	666	690	.	.	.	Note=Impairs protein stability. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24604199;Dbxref=PMID:24604199	
+P40416	UniProtKB	Sequence conflict	23	23	.	.	.	Note=I->IRNHS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40416	UniProtKB	Beta strand	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYH	
+P40416	UniProtKB	Helix	106	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	110	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	128	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	152	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	203	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	212	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Turn	216	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	229	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	236	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	256	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	305	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	315	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	367	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYH	
+P40416	UniProtKB	Helix	373	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	383	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	387	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Turn	390	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	397	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Turn	412	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	430	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	436	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	451	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	464	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	475	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	478	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	489	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	500	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	505	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	512	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	523	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	526	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	531	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	539	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	552	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	561	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	565	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	575	589	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	592	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	605	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	620	623	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	625	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	633	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	640	646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Beta strand	649	654	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	656	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+P40416	UniProtKB	Helix	666	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC	
+##sequence-region P81450 1 59
+P81450	UniProtKB	Chain	1	59	.	.	.	ID=PRO_0000071697;Note=ATP synthase subunit J%2C mitochondrial	
+P81450	UniProtKB	Transmembrane	9	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06321 1 1198
+Q06321	UniProtKB	Chain	1	1198	.	.	.	ID=PRO_0000215616;Note=Sterol 3-beta-glucosyltransferase	
+Q06321	UniProtKB	Domain	187	236	.	.	.	Note=GRAM 1	
+Q06321	UniProtKB	Domain	238	336	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+Q06321	UniProtKB	Domain	570	636	.	.	.	Note=GRAM 2	
+Q06321	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06321	UniProtKB	Modified residue	693	693	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06321	UniProtKB	Beta strand	741	745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	750	765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	769	774	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	776	778	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	779	784	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	788	791	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	797	805	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	810	839	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	842	846	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	848	850	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	853	860	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	864	870	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	876	878	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	891	919	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	928	931	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	933	935	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	938	940	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Turn	944	946	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	957	959	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	975	986	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	990	995	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	998	1000	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	1004	1017	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	1020	1025	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	1028	1031	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	1048	1050	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	1056	1059	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	1060	1062	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	1063	1068	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	1072	1080	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	1085	1087	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	1093	1103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Beta strand	1106	1109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	1115	1127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	1129	1144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+Q06321	UniProtKB	Helix	1147	1169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5	
+##sequence-region Q12142 1 997
+Q12142	UniProtKB	Chain	1	997	.	.	.	ID=PRO_0000119839;Note=Autophagy-related protein 9	
+Q12142	UniProtKB	Topological domain	1	318	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12142	UniProtKB	Transmembrane	319	339	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12142	UniProtKB	Topological domain	340	376	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12142	UniProtKB	Transmembrane	377	397	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12142	UniProtKB	Topological domain	398	538	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12142	UniProtKB	Transmembrane	539	559	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12142	UniProtKB	Topological domain	560	620	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12142	UniProtKB	Transmembrane	621	641	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12142	UniProtKB	Topological domain	642	656	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12142	UniProtKB	Transmembrane	657	677	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12142	UniProtKB	Topological domain	678	723	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12142	UniProtKB	Transmembrane	724	744	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12142	UniProtKB	Topological domain	745	997	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12142	UniProtKB	Compositional bias	907	978	.	.	.	Note=Asn-rich	
+Q12142	UniProtKB	Modified residue	143	143	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12142	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12142	UniProtKB	Modified residue	787	787	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12142	UniProtKB	Mutagenesis	192	192	.	.	.	Note=Aboloshes interaction with ATG11 and disrupts Cvt%2C but not bulk autophagy. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17178909;Dbxref=PMID:17178909	
+##sequence-region P38110 1 2787
+P38110	UniProtKB	Chain	1	2787	.	.	.	ID=PRO_0000088839;Note=Serine/threonine-protein kinase TEL1	
+P38110	UniProtKB	Domain	1734	2326	.	.	.	Note=FAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534	
+P38110	UniProtKB	Domain	2461	2787	.	.	.	Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269	
+P38110	UniProtKB	Domain	2755	2787	.	.	.	Note=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535	
+P38110	UniProtKB	Mutagenesis	1319	1319	.	.	.	Note=In TEL1-11%3B short telomere phenotype and impairs DNA-damage checkpoint function at 37 degrees Celsius. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16228207;Dbxref=PMID:16228207	
+P38110	UniProtKB	Mutagenesis	2611	2612	.	.	.	Note=Short telomere phenotype in vivo and impairs kinase activity in vitro%3B when associated with K-2616 and E-2631. GD->DA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11095737,ECO:0000269|PubMed:7671310;Dbxref=PMID:11095737,PMID:7671310	
+P38110	UniProtKB	Mutagenesis	2616	2616	.	.	.	Note=Short telomere phenotype in vivo and impairs kinase activity in vitro%3B when associated with D-2611-2612-A and E-2631. N->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11095737,ECO:0000269|PubMed:7671310;Dbxref=PMID:11095737,PMID:7671310	
+P38110	UniProtKB	Mutagenesis	2631	2631	.	.	.	Note=Short telomere phenotype in vivo and impairs kinase activity in vitro%3B when associated with D-2611-2612-A and K-2616. D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11095737,ECO:0000269|PubMed:7671310;Dbxref=PMID:11095737,PMID:7671310	
+P38110	UniProtKB	Sequence conflict	64	64	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38110	UniProtKB	Sequence conflict	164	164	.	.	.	Note=C->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38110	UniProtKB	Sequence conflict	1190	1190	.	.	.	Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38110	UniProtKB	Sequence conflict	1412	1412	.	.	.	Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38110	UniProtKB	Sequence conflict	1412	1412	.	.	.	Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P13587 1 1091
+P13587	UniProtKB	Chain	1	1091	.	.	.	ID=PRO_0000046242;Note=Sodium transport ATPase 1	
+P13587	UniProtKB	Topological domain	1	63	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Topological domain	85	90	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Topological domain	112	282	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Transmembrane	283	303	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Topological domain	304	312	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Transmembrane	313	333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Topological domain	334	815	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Transmembrane	816	836	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Topological domain	837	848	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Transmembrane	849	869	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Topological domain	870	885	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Transmembrane	886	906	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Topological domain	907	943	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Transmembrane	944	964	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Topological domain	965	991	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Transmembrane	992	1012	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Topological domain	1013	1021	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Transmembrane	1022	1042	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Topological domain	1043	1091	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13587	UniProtKB	Active site	369	369	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12359 1 275
+Q12359	UniProtKB	Chain	1	275	.	.	.	ID=PRO_0000135707;Note=Ammonia transport outward protein 3	
+Q12359	UniProtKB	Topological domain	1	84	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12359	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12359	UniProtKB	Topological domain	106	120	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12359	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12359	UniProtKB	Topological domain	142	181	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12359	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12359	UniProtKB	Topological domain	203	207	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12359	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12359	UniProtKB	Topological domain	229	236	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12359	UniProtKB	Transmembrane	237	257	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12359	UniProtKB	Topological domain	258	275	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12359	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+##sequence-region P18496 1 279
+P18496	UniProtKB	Chain	1	279	.	.	.	ID=PRO_0000071727;Note=Mitochondrial ATPase complex subunit ATP10	
+P18496	UniProtKB	Sequence conflict	224	224	.	.	.	Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P81451 1 68
+P81451	UniProtKB	Chain	1	68	.	.	.	ID=PRO_0000071699;Note=ATP synthase subunit K%2C mitochondrial	
+P81451	UniProtKB	Transmembrane	15	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P61829 1 76
+P61829	UniProtKB	Chain	1	76	.	.	.	ID=PRO_0000112240;Note=ATP synthase subunit 9%2C mitochondrial	
+P61829	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P61829	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P61829	UniProtKB	Site	59	59	.	.	.	Note=Reversibly protonated during proton transport;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P61829	UniProtKB	Modified residue	1	1	.	.	.	Note=N-formylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2894987;Dbxref=PMID:2894987	
+P61829	UniProtKB	Natural variant	46	46	.	.	.	Note=In strain: DS400/A3 and KL14-4A. T->L	
+P61829	UniProtKB	Natural variant	53	53	.	.	.	Note=In strain: DS400/A3%2C DS401 and oligomycin-resistant mutant. L->F	
+P61829	UniProtKB	Natural variant	57	57	.	.	.	Note=In oligomycin-resistant mutant and cross-resistance to venturicidin. L->V	
+P61829	UniProtKB	Natural variant	65	65	.	.	.	Note=In oligomycin-resistant mutant. C->S	
+P61829	UniProtKB	Helix	2	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F4S	
+P61829	UniProtKB	Helix	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F4S	
+P61829	UniProtKB	Helix	19	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F4S	
+P61829	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F4S	
+P61829	UniProtKB	Helix	44	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F4S	
+##sequence-region P22035 1 811
+P22035	UniProtKB	Chain	1	811	.	.	.	ID=PRO_0000197085;Note=Myb-like DNA-binding protein BAS1	
+P22035	UniProtKB	Domain	34	110	.	.	.	Note=Myb-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133	
+P22035	UniProtKB	Domain	111	165	.	.	.	Note=HTH myb-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P22035	UniProtKB	Domain	166	218	.	.	.	Note=HTH myb-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P22035	UniProtKB	DNA binding	138	161	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P22035	UniProtKB	DNA binding	191	214	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+##sequence-region Q05029 1 724
+Q05029	UniProtKB	Chain	1	724	.	.	.	ID=PRO_0000203335;Note=Protein BCH1	
+Q05029	UniProtKB	Region	711	724	.	.	.	Note=CHS5-binding	
+Q05029	UniProtKB	Helix	18	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Beta strand	37	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Beta strand	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q66	
+Q05029	UniProtKB	Helix	102	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Beta strand	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q66	
+Q05029	UniProtKB	Beta strand	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Beta strand	136	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Turn	142	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Beta strand	146	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Beta strand	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Beta strand	159	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	190	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Turn	207	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Beta strand	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q66	
+Q05029	UniProtKB	Helix	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Beta strand	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	237	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	245	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	252	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Beta strand	266	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	270	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	285	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	303	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	316	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	341	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	366	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	384	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	400	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	463	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Turn	469	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	475	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	493	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	539	564	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	575	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	592	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	608	630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	638	665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	672	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	687	697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	700	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q05029	UniProtKB	Helix	711	716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+##sequence-region P35817 1 686
+P35817	UniProtKB	Chain	1	686	.	.	.	ID=PRO_0000211176;Note=Bromodomain-containing factor 1	
+P35817	UniProtKB	Domain	165	237	.	.	.	Note=Bromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+P35817	UniProtKB	Domain	332	404	.	.	.	Note=Bromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+P35817	UniProtKB	Domain	518	598	.	.	.	Note=NET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00857	
+P35817	UniProtKB	Coiled coil	460	499	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35817	UniProtKB	Modified residue	270	270	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P35817	UniProtKB	Modified residue	429	429	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P35817	UniProtKB	Modified residue	615	615	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P35817	UniProtKB	Modified residue	659	659	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P35817	UniProtKB	Mutagenesis	187	187	.	.	.	Note=Impairs interaction with histones H3 and H4%3B when associated with F-354. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12620225;Dbxref=PMID:12620225	
+P35817	UniProtKB	Mutagenesis	354	354	.	.	.	Note=Impairs interaction with histones H3 and H4%3B when associated with F-187. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12620225;Dbxref=PMID:12620225	
+P35817	UniProtKB	Sequence conflict	8	8	.	.	.	Note=Q->LC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35817	UniProtKB	Sequence conflict	93	94	.	.	.	Note=GA->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35817	UniProtKB	Sequence conflict	94	94	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35817	UniProtKB	Sequence conflict	282	282	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35817	UniProtKB	Sequence conflict	385	385	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35817	UniProtKB	Sequence conflict	493	493	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39714 1 382
+P39714	UniProtKB	Chain	1	382	.	.	.	ID=PRO_0000160788;Note=(R%2CR)-butanediol dehydrogenase	
+P39714	UniProtKB	Metal binding	39	39	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39714	UniProtKB	Metal binding	73	73	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39714	UniProtKB	Metal binding	103	103	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39714	UniProtKB	Metal binding	120	120	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39714	UniProtKB	Metal binding	123	123	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39714	UniProtKB	Metal binding	131	131	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39714	UniProtKB	Metal binding	173	173	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39714	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39714	UniProtKB	Sequence conflict	322	322	.	.	.	Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P50273 1 684
+P50273	UniProtKB	Transit peptide	1	56	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50273	UniProtKB	Chain	57	684	.	.	.	ID=PRO_0000072452;Note=Mitochondrial translation factor ATP22	
+##sequence-region P07251 1 545
+P07251	UniProtKB	Transit peptide	1	35	.	.	.	Note=Mitochondrion	
+P07251	UniProtKB	Chain	36	545	.	.	.	ID=PRO_0000002433;Note=ATP synthase subunit alpha%2C mitochondrial	
+P07251	UniProtKB	Nucleotide binding	206	213	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07251	UniProtKB	Site	407	407	.	.	.	Note=Required for activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07251	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P07251	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P07251	UniProtKB	Mutagenesis	291	291	.	.	.	Note=In ATP1-2%3B growth-defect. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10744740;Dbxref=PMID:10744740	
+P07251	UniProtKB	Mutagenesis	383	383	.	.	.	Note=In ATP1-1%3B growth-defect. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10744740;Dbxref=PMID:10744740	
+P07251	UniProtKB	Sequence conflict	311	313	.	.	.	Note=QAV->ASL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07251	UniProtKB	Sequence conflict	321	321	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07251	UniProtKB	Sequence conflict	340	340	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07251	UniProtKB	Sequence conflict	340	340	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07251	UniProtKB	Sequence conflict	385	385	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07251	UniProtKB	Sequence conflict	459	459	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07251	UniProtKB	Sequence conflict	479	483	.	.	.	Note=VPLIY->SMII;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07251	UniProtKB	Sequence conflict	490	493	.	.	.	Note=LDGI->SGWY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07251	UniProtKB	Turn	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	65	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	75	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	97	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	108	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	124	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	161	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	173	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEE	
+P07251	UniProtKB	Beta strand	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEE	
+P07251	UniProtKB	Helix	188	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	203	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	208	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPD	
+P07251	UniProtKB	Helix	212	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	224	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Turn	232	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	237	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	247	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Turn	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	263	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	266	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	277	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	300	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	308	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	328	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	335	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	347	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Turn	351	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	357	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	367	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	374	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	383	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	391	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Turn	404	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Beta strand	408	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	412	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	418	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	438	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	449	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	475	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Turn	488	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	495	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	498	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	514	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P07251	UniProtKB	Helix	528	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+##sequence-region P09457 1 212
+P09457	UniProtKB	Transit peptide	1	17	.	.	.	Note=Mitochondrion	
+P09457	UniProtKB	Chain	18	212	.	.	.	ID=PRO_0000002656;Note=ATP synthase subunit 5%2C mitochondrial	
+##sequence-region P13090 1 542
+P13090	UniProtKB	Chain	1	542	.	.	.	ID=PRO_0000173367;Note=Aminotriazole resistance protein	
+P13090	UniProtKB	Topological domain	1	108	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	130	136	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	137	157	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	158	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	194	198	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	220	231	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	253	262	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	263	283	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	284	295	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	296	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	317	333	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	334	354	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	355	371	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	393	399	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	400	420	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	421	429	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	430	450	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	451	505	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Transmembrane	506	526	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Topological domain	527	542	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Glycosylation	394	394	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Glycosylation	471	471	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13090	UniProtKB	Sequence conflict	531	542	.	.	.	Note=ARAAAEYDCTVA->QELLQNTIALWLSGKRY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12067 1 313
+Q12067	UniProtKB	Chain	1	313	.	.	.	ID=PRO_0000064758;Note=Metal homeostasis factor ATX2	
+Q12067	UniProtKB	Topological domain	1	2	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Topological domain	24	67	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Topological domain	89	103	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Topological domain	125	154	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Transmembrane	155	175	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Topological domain	176	183	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Transmembrane	184	204	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Topological domain	205	217	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Transmembrane	218	238	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Topological domain	239	251	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Transmembrane	252	272	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Topological domain	273	285	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Transmembrane	286	306	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12067	UniProtKB	Topological domain	307	313	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12128 1 409
+Q12128	UniProtKB	Chain	1	409	.	.	.	ID=PRO_0000064810;Note=Rho-GTPase-activating protein BAG7	
+Q12128	UniProtKB	Domain	76	235	.	.	.	Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172	
+Q12128	UniProtKB	Compositional bias	319	326	.	.	.	Note=Poly-His	
+##sequence-region Q01389 1 1478
+Q01389	UniProtKB	Chain	1	1478	.	.	.	ID=PRO_0000085662;Note=Serine/threonine-protein kinase BCK1/SLK1/SSP31	
+Q01389	UniProtKB	Domain	1175	1440	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q01389	UniProtKB	Nucleotide binding	1181	1189	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q01389	UniProtKB	Active site	1303	1303	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q01389	UniProtKB	Binding site	1204	1204	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q01389	UniProtKB	Modified residue	407	407	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q01389	UniProtKB	Modified residue	411	411	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q01389	UniProtKB	Modified residue	491	491	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q01389	UniProtKB	Modified residue	747	747	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q01389	UniProtKB	Modified residue	816	816	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q01389	UniProtKB	Modified residue	1058	1058	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q01389	UniProtKB	Modified residue	1061	1061	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q01389	UniProtKB	Modified residue	1134	1134	.	.	.	Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01389	UniProtKB	Mutagenesis	1119	1119	.	.	.	Note=In BCK1-19%3B Dominant active. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729597;Dbxref=PMID:1729597	
+Q01389	UniProtKB	Mutagenesis	1120	1120	.	.	.	Note=In BCK1-11%3B Dominant active. I->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729597;Dbxref=PMID:1729597	
+Q01389	UniProtKB	Mutagenesis	1120	1120	.	.	.	Note=In BCK1-16%3B Dominant active. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729597;Dbxref=PMID:1729597	
+Q01389	UniProtKB	Mutagenesis	1146	1146	.	.	.	Note=In BCK1-10%3B Dominant active. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729597;Dbxref=PMID:1729597	
+Q01389	UniProtKB	Mutagenesis	1174	1174	.	.	.	Note=In BCK1-20%3B Dominant active. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729597;Dbxref=PMID:1729597	
+Q01389	UniProtKB	Sequence conflict	59	59	.	.	.	Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01389	UniProtKB	Sequence conflict	79	79	.	.	.	Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01389	UniProtKB	Sequence conflict	264	264	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01389	UniProtKB	Sequence conflict	279	279	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01389	UniProtKB	Sequence conflict	703	714	.	.	.	Note=RYPQTPSYYYDR->STPKPRVITMTE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01389	UniProtKB	Sequence conflict	795	795	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01389	UniProtKB	Sequence conflict	802	802	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01389	UniProtKB	Sequence conflict	808	808	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01389	UniProtKB	Sequence conflict	903	903	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01389	UniProtKB	Sequence conflict	919	919	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01389	UniProtKB	Sequence conflict	960	960	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01389	UniProtKB	Sequence conflict	962	962	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32839 1 456
+P32839	UniProtKB	Chain	1	456	.	.	.	ID=PRO_0000084777;Note=Mitochondrial chaperone BCS1	
+P32839	UniProtKB	Topological domain	1	44	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8599931;Dbxref=PMID:8599931	
+P32839	UniProtKB	Transmembrane	45	68	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32839	UniProtKB	Topological domain	69	456	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8599931;Dbxref=PMID:8599931	
+P32839	UniProtKB	Nucleotide binding	267	274	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32839	UniProtKB	Motif	69	83	.	.	.	Note=Mitochondrial-targeting signal	
+P32839	UniProtKB	Sequence conflict	119	119	.	.	.	Note=N->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32839	UniProtKB	Sequence conflict	267	267	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32839	UniProtKB	Sequence conflict	349	349	.	.	.	Note=L->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32839	UniProtKB	Sequence conflict	351	351	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39713 1 417
+P39713	UniProtKB	Chain	1	417	.	.	.	ID=PRO_0000160897;Note=Probable diacetyl reductase [(R)-acetoin forming] 2	
+P39713	UniProtKB	Metal binding	39	39	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39713	UniProtKB	Metal binding	64	64	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39713	UniProtKB	Metal binding	120	120	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39713	UniProtKB	Metal binding	123	123	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39713	UniProtKB	Metal binding	131	131	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39713	UniProtKB	Metal binding	173	173	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39713	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P39714	
+##sequence-region Q08347 1 646
+Q08347	UniProtKB	Chain	1	646	.	.	.	ID=PRO_0000227682;Note=Alkyl/aryl-sulfatase BDS1	
+Q08347	UniProtKB	Metal binding	162	162	.	.	.	Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25910	
+Q08347	UniProtKB	Metal binding	164	164	.	.	.	Note=Zinc%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25910	
+Q08347	UniProtKB	Metal binding	166	166	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25910	
+Q08347	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P38077 1 311
+P38077	UniProtKB	Transit peptide	1	33	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7929329;Dbxref=PMID:7929329	
+P38077	UniProtKB	Chain	34	311	.	.	.	ID=PRO_0000002691;Note=ATP synthase subunit gamma%2C mitochondrial	
+P38077	UniProtKB	Natural variant	207	207	.	.	.	Note=In strain: D273-10B/A1. S->I	
+P38077	UniProtKB	Natural variant	308	308	.	.	.	Note=In allele ATP3a. S->F	
+P38077	UniProtKB	Mutagenesis	273	273	.	.	.	Note=Lower activity. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7929329;Dbxref=PMID:7929329	
+P38077	UniProtKB	Mutagenesis	297	297	.	.	.	Note=In ATP3-5%3B dominant suppressor of the slow-growth phenotype of yme1 strains lacking mitochondrial DNA. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7498726;Dbxref=PMID:7498726	
+P38077	UniProtKB	Mutagenesis	303	303	.	.	.	Note=In ATP3-1%3B dominant suppressor of the slow-growth phenotype of yme1 strains lacking mitochondrial DNA. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7498726;Dbxref=PMID:7498726	
+P38077	UniProtKB	Helix	36	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Helix	83	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Beta strand	105	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Helix	120	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Beta strand	139	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Helix	145	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Helix	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Beta strand	159	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Beta strand	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Helix	173	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Helix	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Beta strand	193	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Beta strand	203	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Beta strand	209	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Helix	218	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Helix	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Beta strand	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+P38077	UniProtKB	Helix	239	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA	
+##sequence-region P81449 1 96
+P81449	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9857174;Dbxref=PMID:9857174	
+P81449	UniProtKB	Chain	2	96	.	.	.	ID=PRO_0000071689;Note=ATP synthase subunit e%2C mitochondrial	
+P81449	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9857174;Dbxref=PMID:9857174	
+##sequence-region Q12226 1 474
+Q12226	UniProtKB	Chain	1	474	.	.	.	ID=PRO_0000076181;Note=Trichothecene 3-O-acetyltransferase	
+##sequence-region P41815 1 604
+P41815	UniProtKB	Chain	1	604	.	.	.	ID=PRO_0000054147;Note=Valine amino-acid permease	
+P41815	UniProtKB	Topological domain	1	95	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	96	116	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	117	119	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	141	169	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	170	190	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	191	206	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	207	227	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	228	238	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	239	259	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	260	284	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	285	305	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	306	323	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	324	344	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	345	377	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	378	398	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	399	423	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	424	444	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	445	449	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	450	470	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	471	502	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	503	523	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	524	531	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Transmembrane	532	552	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Topological domain	553	604	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41815	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38084	
+P41815	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38084	
+P41815	UniProtKB	Sequence conflict	573	575	.	.	.	Note=VYD->GLR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47068 1 1157
+P47068	UniProtKB	Chain	1	1157	.	.	.	ID=PRO_0000064839;Note=Myosin tail region-interacting protein MTI1	
+P47068	UniProtKB	Domain	5	69	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P47068	UniProtKB	Coiled coil	234	301	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47068	UniProtKB	Coiled coil	356	430	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47068	UniProtKB	Compositional bias	278	412	.	.	.	Note=Glu-rich	
+P47068	UniProtKB	Compositional bias	674	830	.	.	.	Note=Pro-rich	
+P47068	UniProtKB	Modified residue	103	103	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P47068	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P47068	UniProtKB	Modified residue	166	166	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47068	UniProtKB	Modified residue	565	565	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47068	UniProtKB	Modified residue	621	621	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47068	UniProtKB	Modified residue	631	631	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+P47068	UniProtKB	Modified residue	634	634	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47068	UniProtKB	Modified residue	636	636	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47068	UniProtKB	Modified residue	638	638	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+P47068	UniProtKB	Modified residue	647	647	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47068	UniProtKB	Modified residue	850	850	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47068	UniProtKB	Modified residue	889	889	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P47068	UniProtKB	Modified residue	894	894	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47068	UniProtKB	Modified residue	895	895	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47068	UniProtKB	Cross-link	1012	1012	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P47068	UniProtKB	Beta strand	6	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0	
+P47068	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WDX	
+P47068	UniProtKB	Beta strand	31	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0	
+P47068	UniProtKB	Beta strand	39	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0	
+P47068	UniProtKB	Beta strand	54	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0	
+P47068	UniProtKB	Helix	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0	
+P47068	UniProtKB	Beta strand	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0	
+##sequence-region Q08236 1 1176
+Q08236	UniProtKB	Chain	1	1176	.	.	.	ID=PRO_0000218771;Note=Target of rapamycin complex 2 subunit AVO1	
+Q08236	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08236	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08236	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08236	UniProtKB	Modified residue	400	400	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08236	UniProtKB	Modified residue	509	509	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08236	UniProtKB	Modified residue	510	510	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08236	UniProtKB	Modified residue	552	552	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08236	UniProtKB	Beta strand	1069	1090	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB	
+Q08236	UniProtKB	Beta strand	1093	1097	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB	
+Q08236	UniProtKB	Beta strand	1112	1115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB	
+Q08236	UniProtKB	Helix	1116	1118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB	
+Q08236	UniProtKB	Beta strand	1119	1124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB	
+Q08236	UniProtKB	Beta strand	1131	1136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB	
+Q08236	UniProtKB	Beta strand	1145	1153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB	
+Q08236	UniProtKB	Helix	1154	1173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB	
+##sequence-region P47082 1 602
+P47082	UniProtKB	Chain	1	602	.	.	.	ID=PRO_0000093834;Note=Vacuolar amino acid transporter 1	
+P47082	UniProtKB	Topological domain	1	208	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Transmembrane	209	231	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Topological domain	232	240	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Topological domain	262	286	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Transmembrane	287	307	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Topological domain	308	321	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Transmembrane	322	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Topological domain	343	344	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Transmembrane	345	365	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Topological domain	366	389	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Transmembrane	390	410	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Topological domain	411	429	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Transmembrane	430	450	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Topological domain	451	466	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Transmembrane	467	487	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Topological domain	488	517	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Transmembrane	518	538	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Topological domain	539	543	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Transmembrane	544	564	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Topological domain	565	580	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Transmembrane	581	601	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Topological domain	602	602	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47082	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47082	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47082	UniProtKB	Modified residue	35	35	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47082	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47082	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P38176 1 459
+P38176	UniProtKB	Chain	1	459	.	.	.	ID=PRO_0000093838;Note=Vacuolar amino acid transporter 5	
+P38176	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38176	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38176	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38176	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38176	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38176	UniProtKB	Transmembrane	206	226	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38176	UniProtKB	Transmembrane	240	260	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38176	UniProtKB	Transmembrane	278	298	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38176	UniProtKB	Transmembrane	364	384	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38176	UniProtKB	Transmembrane	386	406	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38176	UniProtKB	Transmembrane	434	454	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P50080 1 613
+P50080	UniProtKB	Chain	1	613	.	.	.	ID=PRO_0000173426;Note=Azole resistance protein 1	
+P50080	UniProtKB	Topological domain	1	70	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	92	102	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	103	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	124	134	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	135	155	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	156	163	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	185	189	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	190	210	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	211	221	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	222	242	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	243	298	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	299	319	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	320	329	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	330	350	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	351	375	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	376	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	397	414	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	415	435	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	436	443	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	444	464	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	465	472	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	473	493	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	494	581	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Transmembrane	582	602	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50080	UniProtKB	Topological domain	603	613	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38084 1 609
+P38084	UniProtKB	Chain	1	609	.	.	.	ID=PRO_0000054146;Note=Leu/Val/Ile amino-acid permease	
+P38084	UniProtKB	Topological domain	1	99	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	121	123	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	124	144	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	145	173	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	195	210	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	211	231	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	232	235	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	236	256	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	257	289	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	290	310	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	311	328	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	329	349	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	350	374	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	375	395	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	396	427	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	428	448	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	449	451	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	452	472	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	473	500	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	501	521	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	522	536	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Transmembrane	537	557	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Topological domain	558	609	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38084	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38084	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38084	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38084	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38084	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38084	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38084	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38084	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38084	UniProtKB	Sequence conflict	139	139	.	.	.	Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38084	UniProtKB	Sequence conflict	203	203	.	.	.	Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39960 1 2167
+P39960	UniProtKB	Chain	1	2167	.	.	.	ID=PRO_0000068858;Note=GTPase-activating protein BEM2/IPL2	
+P39960	UniProtKB	Domain	592	859	.	.	.	Note=Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00168	
+P39960	UniProtKB	Domain	1846	1948	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P39960	UniProtKB	Domain	1967	2165	.	.	.	Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172	
+P39960	UniProtKB	Compositional bias	16	25	.	.	.	Note=Poly-Ser	
+P39960	UniProtKB	Compositional bias	35	43	.	.	.	Note=Poly-Ser	
+P39960	UniProtKB	Compositional bias	58	63	.	.	.	Note=Poly-His	
+P39960	UniProtKB	Compositional bias	198	208	.	.	.	Note=Poly-Asn	
+P39960	UniProtKB	Compositional bias	253	260	.	.	.	Note=Poly-Ser	
+P39960	UniProtKB	Compositional bias	1161	1165	.	.	.	Note=Poly-Thr	
+P39960	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39960	UniProtKB	Modified residue	283	283	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39960	UniProtKB	Modified residue	1012	1012	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P39960	UniProtKB	Modified residue	1016	1016	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P39960	UniProtKB	Modified residue	1038	1038	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39960	UniProtKB	Modified residue	1046	1046	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P39960	UniProtKB	Modified residue	1054	1054	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39960	UniProtKB	Modified residue	1128	1128	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39960	UniProtKB	Cross-link	27	27	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P36149 1 193
+P36149	UniProtKB	Chain	1	193	.	.	.	ID=PRO_0000211578;Note=Trafficking protein particle complex subunit BET3	
+P36149	UniProtKB	Lipidation	80	80	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15692564;Dbxref=PMID:15692564	
+P36149	UniProtKB	Mutagenesis	80	80	.	.	.	Note=Loss of palmitoylation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15692564;Dbxref=PMID:15692564	
+##sequence-region P47134 1 954
+P47134	UniProtKB	Chain	1	954	.	.	.	ID=PRO_0000122388;Note=Protein BIR1	
+P47134	UniProtKB	Repeat	20	117	.	.	.	Note=BIR 1	
+P47134	UniProtKB	Repeat	153	241	.	.	.	Note=BIR 2	
+P47134	UniProtKB	Metal binding	208	208	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00029	
+P47134	UniProtKB	Metal binding	211	211	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00029	
+P47134	UniProtKB	Metal binding	228	228	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00029	
+P47134	UniProtKB	Metal binding	237	237	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00029	
+P47134	UniProtKB	Modified residue	477	477	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47134	UniProtKB	Modified residue	508	508	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P47134	UniProtKB	Modified residue	552	552	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47134	UniProtKB	Modified residue	587	587	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P47134	UniProtKB	Modified residue	751	751	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47134	UniProtKB	Modified residue	765	765	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P47041 1 543
+P47041	UniProtKB	Chain	1	543	.	.	.	ID=PRO_0000203060;Note=Target of rapamycin complex 2 subunit BIT61	
+P47041	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47041	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47041	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47041	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q99177 1 341
+Q99177	UniProtKB	Chain	1	341	.	.	.	ID=PRO_0000239636;Note=Pre-mRNA-splicing factor BRR1	
+##sequence-region P53062 1 197
+P53062	UniProtKB	Chain	1	197	.	.	.	ID=PRO_0000202707;Note=Nucleus export protein BRR6	
+P53062	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53062	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08235 1 291
+Q08235	UniProtKB	Chain	1	291	.	.	.	ID=PRO_0000120235;Note=Ribosome biogenesis protein BRX1	
+Q08235	UniProtKB	Domain	31	232	.	.	.	Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034	
+Q08235	UniProtKB	Modified residue	285	285	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08235	UniProtKB	Sequence conflict	161	161	.	.	.	Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08235	UniProtKB	Sequence conflict	161	161	.	.	.	Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05611 1 235
+Q05611	UniProtKB	Chain	1	235	.	.	.	ID=PRO_0000064993;Note=Bypass of stop codon protein 2	
+Q05611	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05611	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q08280 1 497
+Q08280	UniProtKB	Chain	1	497	.	.	.	ID=PRO_0000084864;Note=Bypass of stop codon protein 6	
+Q08280	UniProtKB	Topological domain	1	72	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Topological domain	94	144	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Topological domain	166	167	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Topological domain	189	205	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Transmembrane	206	226	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Topological domain	227	232	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Topological domain	254	300	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Transmembrane	301	321	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Topological domain	322	340	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Transmembrane	341	361	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Topological domain	362	373	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Transmembrane	374	394	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Topological domain	395	397	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Transmembrane	398	418	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Topological domain	419	439	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Transmembrane	440	460	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Topological domain	461	462	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Transmembrane	463	483	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Topological domain	484	497	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q08280	UniProtKB	Modified residue	41	41	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08280	UniProtKB	Glycosylation	49	49	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08280	UniProtKB	Sequence conflict	472	472	.	.	.	Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47176 1 376
+P47176	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000103302;Note=Branched-chain-amino-acid aminotransferase%2C cytosolic	
+P47176	UniProtKB	Modified residue	202	202	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47176	UniProtKB	Sequence conflict	148	149	.	.	.	Note=IG->MA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47176	UniProtKB	Sequence conflict	194	195	.	.	.	Note=WP->CA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47176	UniProtKB	Sequence conflict	224	224	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47176	UniProtKB	Sequence conflict	313	313	.	.	.	Note=F->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P15703 1 313
+P15703	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8935650,ECO:0000269|PubMed:9748433;Dbxref=PMID:8935650,PMID:9748433	
+P15703	UniProtKB	Chain	24	313	.	.	.	ID=PRO_0000011896;Note=Glucan 1%2C3-beta-glucosidase	
+P15703	UniProtKB	Active site	233	233	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15703	UniProtKB	Active site	292	292	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15703	UniProtKB	Glycosylation	202	202	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15703	UniProtKB	Glycosylation	284	284	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P50277 1 480
+P50277	UniProtKB	Chain	1	480	.	.	.	ID=PRO_0000120378;Note=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase	
+P50277	UniProtKB	Region	65	66	.	.	.	Note=7-keto-8-aminopelargonic acid binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50277	UniProtKB	Region	126	127	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50277	UniProtKB	Binding site	26	26	.	.	.	Note=7-keto-8-aminopelargonic acid;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50277	UniProtKB	Binding site	270	270	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50277	UniProtKB	Binding site	314	314	.	.	.	Note=7-keto-8-aminopelargonic acid;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50277	UniProtKB	Binding site	350	350	.	.	.	Note=7-keto-8-aminopelargonic acid%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50277	UniProtKB	Binding site	352	352	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50277	UniProtKB	Binding site	441	441	.	.	.	Note=7-keto-8-aminopelargonic acid;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50277	UniProtKB	Modified residue	314	314	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50277	UniProtKB	Natural variant	229	229	.	.	.	Note=In strain: ATCC 28383 and ATCC 204626. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16269718;Dbxref=PMID:16269718	
+P50277	UniProtKB	Natural variant	295	295	.	.	.	Note=In strain: ATCC 28383 and ATCC 204626. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16269718;Dbxref=PMID:16269718	
+P50277	UniProtKB	Natural variant	384	384	.	.	.	Note=In strain: ATCC 28383 and ATCC 204626. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16269718;Dbxref=PMID:16269718	
+P50277	UniProtKB	Sequence conflict	140	140	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08965 1 1183
+Q08965	UniProtKB	Chain	1	1183	.	.	.	ID=PRO_0000195006;Note=Ribosome biogenesis protein BMS1	
+Q08965	UniProtKB	Domain	68	234	.	.	.	Note=Bms1-type G	
+Q08965	UniProtKB	Nucleotide binding	76	83	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08965	UniProtKB	Modified residue	438	438	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08965	UniProtKB	Modified residue	478	478	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08965	UniProtKB	Modified residue	492	492	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08965	UniProtKB	Modified residue	504	504	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08965	UniProtKB	Modified residue	516	516	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08965	UniProtKB	Modified residue	518	518	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08965	UniProtKB	Modified residue	523	523	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08965	UniProtKB	Modified residue	574	574	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08965	UniProtKB	Modified residue	578	578	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q08965	UniProtKB	Helix	549	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08965	UniProtKB	Helix	560	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08965	UniProtKB	Helix	618	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08965	UniProtKB	Helix	629	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+##sequence-region P47039 1 444
+P47039	UniProtKB	Chain	1	444	.	.	.	ID=PRO_0000123930;Note=Probable kynurenine--oxoglutarate transaminase BNA3	
+P47039	UniProtKB	Modified residue	271	271	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47039	UniProtKB	Helix	24	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	34	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	70	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	83	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	95	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Turn	106	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Beta strand	118	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	123	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Beta strand	141	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	152	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Beta strand	162	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	172	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Beta strand	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	188	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Beta strand	199	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Turn	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	217	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Beta strand	233	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Turn	239	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	257	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Beta strand	263	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	269	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Beta strand	281	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	288	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	307	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	325	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Beta strand	355	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Beta strand	380	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	384	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	403	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	409	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Beta strand	418	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	427	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+P47039	UniProtKB	Helix	437	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46	
+##sequence-region P40450 1 1375
+P40450	UniProtKB	Chain	1	1375	.	.	.	ID=PRO_0000194900;Note=BNI1-related protein 1	
+P40450	UniProtKB	Domain	94	490	.	.	.	Note=GBD/FH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00579	
+P40450	UniProtKB	Domain	659	851	.	.	.	Note=FH1	
+P40450	UniProtKB	Domain	868	1290	.	.	.	Note=FH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00774	
+P40450	UniProtKB	Domain	1302	1336	.	.	.	Note=DAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00577	
+P40450	UniProtKB	Coiled coil	520	601	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40450	UniProtKB	Compositional bias	659	839	.	.	.	Note=Pro-rich	
+P40450	UniProtKB	Compositional bias	1332	1335	.	.	.	Note=Arg/Lys-rich (basic)	
+P40450	UniProtKB	Modified residue	621	621	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40450	UniProtKB	Modified residue	751	751	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q07457 1 700
+Q07457	UniProtKB	Chain	1	700	.	.	.	ID=PRO_0000055857;Note=E3 ubiquitin-protein ligase BRE1	
+Q07457	UniProtKB	Zinc finger	648	687	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q07457	UniProtKB	Coiled coil	126	406	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07457	UniProtKB	Coiled coil	555	620	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07457	UniProtKB	Mutagenesis	663	663	.	.	.	Note=Abolishes ability to monoubiquitinate histone H2B. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535539;Dbxref=PMID:12535539	
+Q07457	UniProtKB	Mutagenesis	665	665	.	.	.	Note=Abolishes ability to monoubiquitinate histone H2B. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535539;Dbxref=PMID:12535539	
+Q07457	UniProtKB	Helix	633	646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E	
+Q07457	UniProtKB	Turn	649	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E	
+Q07457	UniProtKB	Beta strand	652	655	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E	
+Q07457	UniProtKB	Beta strand	658	660	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E	
+Q07457	UniProtKB	Turn	661	663	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E	
+Q07457	UniProtKB	Helix	669	677	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E	
+Q07457	UniProtKB	Turn	684	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E	
+Q07457	UniProtKB	Helix	692	694	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E	
+Q07457	UniProtKB	Beta strand	695	697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E	
+##sequence-region Q07660 1 1125
+Q07660	UniProtKB	Chain	1	1125	.	.	.	ID=PRO_0000239634;Note=Protein BRE4	
+Q07660	UniProtKB	Topological domain	1	143	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Transmembrane	144	164	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Topological domain	165	176	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Transmembrane	177	194	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Topological domain	195	198	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Topological domain	220	227	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Transmembrane	228	248	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Topological domain	249	254	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Topological domain	276	284	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Transmembrane	285	305	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Topological domain	306	706	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Transmembrane	707	727	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Topological domain	728	750	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Transmembrane	751	771	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Topological domain	772	780	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Transmembrane	781	801	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Topological domain	802	843	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Transmembrane	844	864	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Topological domain	865	1125	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07660	UniProtKB	Glycosylation	830	830	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12140 1 328
+Q12140	UniProtKB	Chain	1	328	.	.	.	ID=PRO_0000064992;Note=Bypass of stop codon protein 1	
+Q12140	UniProtKB	Domain	1	155	.	.	.	Note=Flo11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01168	
+Q12140	UniProtKB	Compositional bias	161	317	.	.	.	Note=Ser/Thr-rich	
+##sequence-region P53755 1 489
+P53755	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000064995;Note=Bypass of stop codon protein 5	
+P53755	UniProtKB	Modified residue	111	111	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53755	UniProtKB	Modified residue	350	350	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53755	UniProtKB	Sequence conflict	209	209	.	.	.	Note=Y->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06604 1 576
+Q06604	UniProtKB	Chain	1	576	.	.	.	ID=PRO_0000228137;Note=Protein BSP1	
+Q06604	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q06604	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06604	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06604	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06604	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06604	UniProtKB	Modified residue	309	309	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q06604	UniProtKB	Modified residue	320	320	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P25627 1 275
+P25627	UniProtKB	Chain	1	275	.	.	.	ID=PRO_0000204459;Note=18S rRNA (guanine(1575)-N(7))-methyltransferase	
+P25627	UniProtKB	Motif	257	264	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25627	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Fails to ctalyze the N-7 methylation of the G1575 residue. G->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18332120,ECO:0000269|PubMed:23233232;Dbxref=PMID:18332120,PMID:23233232	
+P25627	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Can only partially restore the slow-growth phenotype and the random budding pattern of a null mutant. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18332120,ECO:0000269|PubMed:23233232;Dbxref=PMID:18332120,PMID:23233232	
+P25627	UniProtKB	Mutagenesis	77	77	.	.	.	Note=No effect on growth and budding pattern. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18332120,ECO:0000269|PubMed:23233232;Dbxref=PMID:18332120,PMID:23233232	
+P25627	UniProtKB	Mutagenesis	77	77	.	.	.	Note=Fails to ctalyze the N-7 methylation of the G1575 residue. D->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18332120,ECO:0000269|PubMed:23233232;Dbxref=PMID:18332120,PMID:23233232	
+P25627	UniProtKB	Helix	16	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTU	
+P25627	UniProtKB	Helix	25	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Beta strand	50	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Helix	60	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Beta strand	72	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Helix	80	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Turn	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Beta strand	92	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Helix	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Beta strand	111	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Helix	120	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Helix	133	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Beta strand	148	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Helix	163	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Beta strand	179	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Turn	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+P25627	UniProtKB	Beta strand	194	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT	
+##sequence-region P50944 1 713
+P50944	UniProtKB	Chain	1	713	.	.	.	ID=PRO_0000093837;Note=Vacuolar amino acid transporter 4	
+P50944	UniProtKB	Topological domain	1	242	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	264	301	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	302	322	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	323	326	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	327	347	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	348	373	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	374	394	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	395	410	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	411	431	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	432	438	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	439	459	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	460	483	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	484	504	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	505	515	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	516	536	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	537	561	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	562	582	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	583	621	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	622	642	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	643	648	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	649	669	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	670	692	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Transmembrane	693	711	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Topological domain	712	713	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50944	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50944	UniProtKB	Modified residue	130	130	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50944	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P40501 1 490
+P40501	UniProtKB	Chain	1	490	.	.	.	ID=PRO_0000093840;Note=Vacuolar amino acid transporter 7	
+P40501	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Topological domain	28	34	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Topological domain	56	84	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Topological domain	106	108	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Topological domain	130	143	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Transmembrane	144	164	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Topological domain	165	190	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Transmembrane	191	211	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Topological domain	212	221	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Transmembrane	222	242	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Topological domain	243	264	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Transmembrane	265	285	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Topological domain	286	397	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Transmembrane	398	418	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Topological domain	419	428	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Transmembrane	429	449	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Topological domain	450	463	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Transmembrane	464	484	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40501	UniProtKB	Topological domain	485	490	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P41696 1 914
+P41696	UniProtKB	Chain	1	914	.	.	.	ID=PRO_0000046802;Note=Asparagine-rich zinc finger protein AZF1	
+P41696	UniProtKB	Zinc finger	593	615	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P41696	UniProtKB	Zinc finger	621	643	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P41696	UniProtKB	Zinc finger	649	671	.	.	.	Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P41696	UniProtKB	Zinc finger	677	702	.	.	.	Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P41696	UniProtKB	Compositional bias	136	143	.	.	.	Note=Poly-Gln	
+P41696	UniProtKB	Compositional bias	146	154	.	.	.	Note=Poly-Gln	
+P41696	UniProtKB	Compositional bias	362	381	.	.	.	Note=Poly-Asn	
+P41696	UniProtKB	Compositional bias	856	860	.	.	.	Note=Poly-Ser	
+P41696	UniProtKB	Compositional bias	861	868	.	.	.	Note=Poly-Asn	
+P41696	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41696	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41696	UniProtKB	Modified residue	325	325	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q12365 1 385
+Q12365	UniProtKB	Chain	1	385	.	.	.	ID=PRO_0000064840;Note=Spindle pole component BBP1	
+Q12365	UniProtKB	Coiled coil	229	355	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12365	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12365	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12365	UniProtKB	Modified residue	115	115	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q3E793 1 110
+Q3E793	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000248409;Note=BolA-like protein 1	
+Q3E793	UniProtKB	Mutagenesis	56	56	.	.	.	Note=No effect. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773	
+Q3E793	UniProtKB	Mutagenesis	56	56	.	.	.	Note=Partial loss of function. H->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773	
+Q3E793	UniProtKB	Mutagenesis	93	93	.	.	.	Note=Loss of function. H->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773	
+##sequence-region P38928 1 823
+P38928	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Chain	23	823	.	.	.	ID=PRO_0000020773;Note=Axial budding pattern protein 2	
+P38928	UniProtKB	Topological domain	23	508	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Transmembrane	509	529	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Topological domain	530	823	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Modified residue	642	642	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38928	UniProtKB	Modified residue	673	673	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38928	UniProtKB	Modified residue	676	676	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38928	UniProtKB	Glycosylation	41	41	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	50	50	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	96	96	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	117	117	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	163	163	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	260	260	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	266	266	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	304	304	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	324	324	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	359	359	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	382	382	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	389	389	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	403	403	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	447	447	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	451	451	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38928	UniProtKB	Glycosylation	495	495	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36122 1 765
+P36122	UniProtKB	Chain	1	765	.	.	.	ID=PRO_0000203204;Note=Protein BCH2	
+P36122	UniProtKB	Region	735	765	.	.	.	Note=CHS5-binding	
+##sequence-region P33306 1 851
+P33306	UniProtKB	Chain	1	851	.	.	.	ID=PRO_0000064883;Note=Protein BCK2	
+P33306	UniProtKB	Modified residue	334	334	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P33306	UniProtKB	Modified residue	757	757	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P33306	UniProtKB	Modified residue	761	761	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33306	UniProtKB	Sequence conflict	4	5	.	.	.	Note=NS->HC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33306	UniProtKB	Sequence conflict	100	100	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33306	UniProtKB	Sequence conflict	167	167	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33306	UniProtKB	Sequence conflict	812	812	.	.	.	Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33306	UniProtKB	Sequence conflict	827	827	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07442 1 638
+Q07442	UniProtKB	Chain	1	638	.	.	.	ID=PRO_0000239629;Note=Bromodomain-containing factor 2	
+Q07442	UniProtKB	Domain	150	222	.	.	.	Note=Bromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+Q07442	UniProtKB	Domain	337	409	.	.	.	Note=Bromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+Q07442	UniProtKB	Domain	506	590	.	.	.	Note=NET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00857	
+Q07442	UniProtKB	Coiled coil	468	537	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07442	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P53858 1 892
+P53858	UniProtKB	Chain	1	892	.	.	.	ID=PRO_0000064959;Note=Protein BNI4	
+P53858	UniProtKB	Compositional bias	122	129	.	.	.	Note=Poly-Glu	
+P53858	UniProtKB	Compositional bias	290	293	.	.	.	Note=Poly-Lys	
+P53858	UniProtKB	Compositional bias	321	324	.	.	.	Note=Poly-Ser	
+P53858	UniProtKB	Compositional bias	344	349	.	.	.	Note=Poly-Ser	
+P53858	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53858	UniProtKB	Modified residue	133	133	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53858	UniProtKB	Modified residue	281	281	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53858	UniProtKB	Modified residue	364	364	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53858	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53858	UniProtKB	Modified residue	410	410	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53858	UniProtKB	Modified residue	476	476	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53858	UniProtKB	Modified residue	500	500	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53858	UniProtKB	Modified residue	503	503	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53858	UniProtKB	Modified residue	618	618	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53858	UniProtKB	Modified residue	703	703	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53858	UniProtKB	Modified residue	746	746	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53858	UniProtKB	Modified residue	825	825	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53958 1 396
+P53958	UniProtKB	Chain	1	396	.	.	.	ID=PRO_0000203456;Note=Protein BOP3	
+##sequence-region Q06338 1 283
+Q06338	UniProtKB	Chain	1	283	.	.	.	ID=PRO_0000239628;Note=Protein BCP1	
+Q06338	UniProtKB	Modified residue	205	205	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06338	UniProtKB	Modified residue	209	209	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P47113 1 574
+P47113	UniProtKB	Chain	1	574	.	.	.	ID=PRO_0000064913;Note=Mitotic check point protein BFA1	
+P47113	UniProtKB	Compositional bias	193	201	.	.	.	Note=Poly-Glu	
+P47113	UniProtKB	Compositional bias	265	268	.	.	.	Note=Poly-Ser	
+P47113	UniProtKB	Modified residue	317	317	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40013 1 344
+P40013	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40013	UniProtKB	Chain	2	344	.	.	.	ID=PRO_0000213432;Note=Protein BIM1	
+P40013	UniProtKB	Domain	8	107	.	.	.	Note=Calponin-homology (CH)	
+P40013	UniProtKB	Domain	188	281	.	.	.	Note=EB1 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00576	
+P40013	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40013	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P40013	UniProtKB	Helix	9	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX	
+P40013	UniProtKB	Helix	27	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX	
+P40013	UniProtKB	Helix	34	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX	
+P40013	UniProtKB	Helix	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX	
+P40013	UniProtKB	Helix	59	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX	
+P40013	UniProtKB	Helix	84	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX	
+P40013	UniProtKB	Turn	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX	
+P40013	UniProtKB	Helix	92	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX	
+P40013	UniProtKB	Helix	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX	
+P40013	UniProtKB	Turn	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX	
+P40013	UniProtKB	Helix	182	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E61	
+P40013	UniProtKB	Helix	260	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E61	
+##sequence-region P38346 1 545
+P38346	UniProtKB	Chain	1	545	.	.	.	ID=PRO_0000202530;Note=Probable target of rapamycin complex 2 subunit BIT2	
+P38346	UniProtKB	Sequence conflict	152	153	.	.	.	Note=SG->RA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35727 1 113
+P35727	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000203176;Note=Biogenesis of lysosome-related organelles complex 1 subunit BLI1	
+P35727	UniProtKB	Coiled coil	57	97	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40471 1 297
+P40471	UniProtKB	Chain	1	297	.	.	.	ID=PRO_0000054520;Note=NADPH-dependent 1-acyldihydroxyacetone phosphate reductase	
+P40471	UniProtKB	Nucleotide binding	13	37	.	.	.	Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40471	UniProtKB	Active site	157	157	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001	
+P40471	UniProtKB	Binding site	144	144	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P29366 1 551
+P29366	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000064908;Note=Bud emergence protein 1	
+P29366	UniProtKB	Domain	72	132	.	.	.	Note=SH3 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P29366	UniProtKB	Domain	155	217	.	.	.	Note=SH3 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P29366	UniProtKB	Domain	278	404	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
+P29366	UniProtKB	Domain	478	551	.	.	.	Note=PB1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01081	
+P29366	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P29366	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P29366	UniProtKB	Modified residue	255	255	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P29366	UniProtKB	Modified residue	258	258	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P29366	UniProtKB	Modified residue	458	458	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P29366	UniProtKB	Modified residue	461	461	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956	
+P29366	UniProtKB	Beta strand	160	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Beta strand	170	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Beta strand	178	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Turn	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Beta strand	192	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Beta strand	198	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Beta strand	205	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Beta strand	217	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Helix	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQW	
+P29366	UniProtKB	Helix	227	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Turn	232	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Helix	239	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Turn	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV	
+P29366	UniProtKB	Beta strand	283	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V	
+P29366	UniProtKB	Beta strand	297	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V	
+P29366	UniProtKB	Beta strand	311	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V	
+P29366	UniProtKB	Helix	318	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V	
+P29366	UniProtKB	Turn	333	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V	
+P29366	UniProtKB	Helix	363	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V	
+P29366	UniProtKB	Helix	385	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V	
+P29366	UniProtKB	Helix	391	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V	
+P29366	UniProtKB	Beta strand	401	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V	
+P29366	UniProtKB	Beta strand	406	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V	
+P29366	UniProtKB	Beta strand	479	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9	
+P29366	UniProtKB	Beta strand	490	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9	
+P29366	UniProtKB	Helix	500	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9	
+P29366	UniProtKB	Beta strand	516	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9	
+P29366	UniProtKB	Beta strand	523	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9	
+P29366	UniProtKB	Helix	533	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9	
+P29366	UniProtKB	Beta strand	546	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9	
+##sequence-region P39011 1 633
+P39011	UniProtKB	Chain	1	633	.	.	.	ID=PRO_0000064910;Note=Bud emergence protein 4	
+##sequence-region Q03630 1 159
+Q03630	UniProtKB	Chain	1	159	.	.	.	ID=PRO_0000211565;Note=Trafficking protein particle complex subunit BET5	
+##sequence-region P38813 1 335
+P38813	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38813	UniProtKB	Chain	18	335	.	.	.	ID=PRO_0000014327;Note=Protein BIG1	
+P38813	UniProtKB	Topological domain	20	275	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38813	UniProtKB	Transmembrane	276	296	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38813	UniProtKB	Topological domain	297	335	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38813	UniProtKB	Glycosylation	24	24	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38813	UniProtKB	Glycosylation	144	144	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53744 1 561
+P53744	UniProtKB	Chain	1	561	.	.	.	ID=PRO_0000054282;Note=7-keto 8-aminopelargonic acid transporter	
+P53744	UniProtKB	Topological domain	1	49	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	71	77	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	99	160	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	182	204	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	205	225	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	226	230	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	231	251	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	252	281	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	282	302	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	303	321	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	322	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	343	369	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	370	390	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	391	439	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	440	460	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	461	461	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	462	482	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	483	507	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	508	528	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	529	540	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Transmembrane	541	560	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53744	UniProtKB	Topological domain	561	561	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43583 1 2143
+P43583	UniProtKB	Chain	1	2143	.	.	.	ID=PRO_0000076182;Note=Proteasome activator BLM10	
+P43583	UniProtKB	Repeat	1316	1355	.	.	.	Note=HEAT 1	
+P43583	UniProtKB	Repeat	1779	1814	.	.	.	Note=HEAT 2	
+P43583	UniProtKB	Repeat	1902	1941	.	.	.	Note=HEAT 3	
+P43583	UniProtKB	Repeat	1985	2023	.	.	.	Note=HEAT 4	
+P43583	UniProtKB	Region	1648	1732	.	.	.	Note=Bromodomain-like (BRDL)	
+P43583	UniProtKB	Motif	2141	2143	.	.	.	Note=YYX motif	
+P43583	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43583	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P43583	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P43583	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P43583	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P43583	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43583	UniProtKB	Modified residue	1041	1041	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P43583	UniProtKB	Mutagenesis	1663	1664	.	.	.	Note=Abolihes binding to acetylated histones. YN->HD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23706739;Dbxref=PMID:23706739	
+P43583	UniProtKB	Mutagenesis	2139	2139	.	.	.	Note=Does not affect binding to the proteasome. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621	
+P43583	UniProtKB	Mutagenesis	2140	2140	.	.	.	Note=Abolishes binding to the proteasome. S->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621	
+P43583	UniProtKB	Mutagenesis	2141	2143	.	.	.	Note=Loss of function. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20227375;Dbxref=PMID:20227375	
+P43583	UniProtKB	Mutagenesis	2141	2141	.	.	.	Note=Does not affect viability in the presence of cycloheximide. Y->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621	
+P43583	UniProtKB	Mutagenesis	2142	2142	.	.	.	Note=Loss of function%3B abolishes binding to the proteasome. Y->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621	
+P43583	UniProtKB	Mutagenesis	2142	2142	.	.	.	Note=Abolishes binding to the proteasome. Y->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621	
+P43583	UniProtKB	Mutagenesis	2143	2143	.	.	.	Note=Does not affect viability in the presence of cycloheximide. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621	
+P43583	UniProtKB	Helix	81	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	97	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	122	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	133	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	240	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	249	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	257	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	280	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	300	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	313	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	329	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	339	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	342	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	364	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	367	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	375	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	380	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	383	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	405	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	408	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	415	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	422	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	444	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	465	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	488	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	505	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	508	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	531	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	553	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	563	565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	568	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	591	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	612	627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	628	633	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	635	646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	649	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	658	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	662	671	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	678	693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	709	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	714	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	730	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	739	747	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	748	750	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	751	765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	773	787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	791	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	813	815	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	819	831	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	833	835	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	836	852	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	853	856	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	861	863	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	866	868	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	869	882	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	883	885	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	886	890	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	893	905	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	910	916	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	919	928	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	937	941	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	953	956	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	957	960	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	962	964	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	974	997	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1009	1023	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1026	1029	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1032	1035	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	1158	1161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	1162	1165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1167	1193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1199	1211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	1215	1217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1231	1238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1249	1266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1276	1288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1293	1307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	1308	1310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1313	1330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1335	1343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1347	1352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1353	1355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1357	1369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	1374	1377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	1378	1380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1381	1390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1404	1406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1408	1410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1420	1427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1430	1451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1460	1471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1481	1488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1489	1493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1496	1506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1508	1519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1523	1526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	1527	1530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	1536	1541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	1544	1546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1547	1554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	1577	1582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1593	1603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1608	1620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	1621	1625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1630	1643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1652	1654	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1655	1661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1668	1681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	1690	1692	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1693	1708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1716	1730	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1733	1735	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1737	1743	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1764	1774	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1782	1787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1795	1810	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1820	1828	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	1831	1834	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1843	1856	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1858	1861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	1869	1873	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1875	1890	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1893	1895	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1896	1899	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1900	1902	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1903	1907	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	1908	1911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1919	1923	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1929	1934	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	1936	1938	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1942	1951	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	1955	1958	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	1961	1963	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1964	1978	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	1979	1981	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1986	1989	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	1991	1994	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	1995	1999	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	2004	2019	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	2024	2034	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Turn	2039	2041	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	2045	2054	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	2056	2069	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	2081	2090	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Beta strand	2093	2095	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	2099	2102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	2104	2113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	2118	2121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	2122	2124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+P43583	UniProtKB	Helix	2131	2133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O	
+##sequence-region P47040 1 408
+P47040	UniProtKB	Signal peptide	1	30	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47040	UniProtKB	Chain	31	408	.	.	.	ID=PRO_0000020836;Note=Protein BTN1	
+P47040	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47040	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47040	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47040	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47040	UniProtKB	Transmembrane	238	258	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47040	UniProtKB	Transmembrane	323	343	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47040	UniProtKB	Transmembrane	369	389	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47040	UniProtKB	Natural variant	181	181	.	.	.	Note=In strain: K289-3A. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9753630;Dbxref=PMID:9753630	
+P47040	UniProtKB	Natural variant	328	328	.	.	.	Note=In strain: K289-3A. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9753630;Dbxref=PMID:9753630	
+P47040	UniProtKB	Sequence conflict	162	162	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P41695 1 1021
+P41695	UniProtKB	Chain	1	1021	.	.	.	ID=PRO_0000085676;Note=Checkpoint serine/threonine-protein kinase BUB1	
+P41695	UniProtKB	Domain	47	212	.	.	.	Note=BUB1 N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00822	
+P41695	UniProtKB	Domain	705	1021	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P41695	UniProtKB	Nucleotide binding	711	719	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P41695	UniProtKB	Active site	833	833	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P41695	UniProtKB	Binding site	733	733	.	.	.	Note=ATP	
+P41695	UniProtKB	Mutagenesis	733	733	.	.	.	Note=Loss of activity. K->R	
+P41695	UniProtKB	Sequence conflict	531	531	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41695	UniProtKB	Beta strand	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BL0	
+P41695	UniProtKB	Beta strand	317	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S	
+P41695	UniProtKB	Helix	323	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S	
+P41695	UniProtKB	Beta strand	330	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BL0	
+P41695	UniProtKB	Helix	336	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S	
+##sequence-region P39988 1 312
+P39988	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000213348;Note=Putative pyridoxal kinase BUD16	
+P39988	UniProtKB	Nucleotide binding	183	184	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39988	UniProtKB	Nucleotide binding	211	223	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39988	UniProtKB	Binding site	9	9	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39988	UniProtKB	Binding site	44	44	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39988	UniProtKB	Binding site	122	122	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39988	UniProtKB	Binding site	224	224	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04347 1 519
+Q04347	UniProtKB	Chain	1	519	.	.	.	ID=PRO_0000065014;Note=Bud site selection protein 22	
+Q04347	UniProtKB	Coiled coil	426	470	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04347	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+Q04347	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q04347	UniProtKB	Modified residue	371	371	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q04347	UniProtKB	Modified residue	375	375	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q04347	UniProtKB	Sequence conflict	497	497	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P85052 1 153
+P85052	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000270625;Note=Bud site selection protein 25	
+##sequence-region P33314 1 1104
+P33314	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P33314	UniProtKB	Chain	2	1104	.	.	.	ID=PRO_0000056656;Note=Inhibitory regulator protein BUD2/CLA2	
+P33314	UniProtKB	Domain	322	425	.	.	.	Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+P33314	UniProtKB	Domain	505	721	.	.	.	Note=Ras-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00167	
+P33314	UniProtKB	Compositional bias	496	499	.	.	.	Note=Poly-Ser	
+P33314	UniProtKB	Compositional bias	1096	1099	.	.	.	Note=Poly-Lys	
+P33314	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P33314	UniProtKB	Modified residue	854	854	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P33314	UniProtKB	Sequence conflict	437	437	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47136 1 1447
+P47136	UniProtKB	Chain	1	1447	.	.	.	ID=PRO_0000065017;Note=Bud site selection protein 4	
+P47136	UniProtKB	Domain	1302	1413	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P47136	UniProtKB	Region	768	879	.	.	.	Note=Interaction with IQG1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12446742;Dbxref=PMID:12446742	
+P47136	UniProtKB	Compositional bias	181	189	.	.	.	Note=Asp/Glu-rich (acidic)	
+P47136	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47136	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47136	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47136	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47136	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47136	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47136	UniProtKB	Modified residue	365	365	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47136	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47136	UniProtKB	Modified residue	511	511	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47136	UniProtKB	Modified residue	616	616	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47136	UniProtKB	Modified residue	805	805	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47136	UniProtKB	Modified residue	811	811	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47136	UniProtKB	Sequence conflict	340	340	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P41697 1 788
+P41697	UniProtKB	Chain	1	788	.	.	.	ID=PRO_0000065018;Note=Bud site selection protein 6	
+P41697	UniProtKB	Coiled coil	573	628	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41697	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41697	UniProtKB	Modified residue	233	233	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P41697	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P41697	UniProtKB	Modified residue	342	342	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956	
+P41697	UniProtKB	Sequence conflict	376	376	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41697	UniProtKB	Sequence conflict	384	385	.	.	.	Note=NA->KP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41697	UniProtKB	Sequence conflict	434	434	.	.	.	Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41697	UniProtKB	Sequence conflict	441	441	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41697	UniProtKB	Sequence conflict	454	454	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41697	UniProtKB	Sequence conflict	565	568	.	.	.	Note=ELGD->SH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41697	UniProtKB	Sequence conflict	742	742	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41697	UniProtKB	Sequence conflict	764	788	.	.	.	Note=FEEVERIRKQKDEANLRAYFGPGFT->LKK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41697	UniProtKB	Helix	555	594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OKQ	
+P41697	UniProtKB	Helix	600	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OKQ	
+P41697	UniProtKB	Helix	701	713	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WYB	
+P41697	UniProtKB	Helix	719	733	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WYB	
+P41697	UniProtKB	Turn	734	737	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WYB	
+##sequence-region P38822 1 633
+P38822	UniProtKB	Chain	1	633	.	.	.	ID=PRO_0000065033;Note=Protein BZZ1	
+P38822	UniProtKB	Domain	5	271	.	.	.	Note=F-BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01077	
+P38822	UniProtKB	Domain	493	555	.	.	.	Note=SH3 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P38822	UniProtKB	Domain	577	633	.	.	.	Note=SH3 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P38822	UniProtKB	Coiled coil	138	210	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38822	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38822	UniProtKB	Modified residue	463	463	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38822	UniProtKB	Modified residue	472	472	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38822	UniProtKB	Modified residue	476	476	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38822	UniProtKB	Sequence conflict	196	196	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38822	UniProtKB	Beta strand	520	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUU	
+P38822	UniProtKB	Beta strand	527	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUU	
+P38822	UniProtKB	Turn	537	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUU	
+P38822	UniProtKB	Beta strand	541	546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUU	
+P38822	UniProtKB	Helix	547	549	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUU	
+P38822	UniProtKB	Beta strand	582	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A28	
+P38822	UniProtKB	Beta strand	603	608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A28	
+P38822	UniProtKB	Beta strand	612	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A28	
+P38822	UniProtKB	Beta strand	623	628	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A28	
+P38822	UniProtKB	Helix	629	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A28	
+##sequence-region Q04749 1 426
+Q04749	UniProtKB	Chain	1	426	.	.	.	ID=PRO_0000067247;Note=Target of rapamycin complex 2 subunit AVO2	
+Q04749	UniProtKB	Repeat	4	33	.	.	.	Note=ANK 1	
+Q04749	UniProtKB	Repeat	39	68	.	.	.	Note=ANK 2	
+Q04749	UniProtKB	Repeat	74	104	.	.	.	Note=ANK 3	
+Q04749	UniProtKB	Repeat	108	137	.	.	.	Note=ANK 4	
+Q04749	UniProtKB	Repeat	141	171	.	.	.	Note=ANK 5	
+Q04749	UniProtKB	Modified residue	315	315	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04749	UniProtKB	Modified residue	350	350	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P40074 1 448
+P40074	UniProtKB	Chain	1	448	.	.	.	ID=PRO_0000093839;Note=Vacuolar amino acid transporter 6	
+P40074	UniProtKB	Topological domain	1	7	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Topological domain	29	32	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Topological domain	54	80	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Topological domain	102	125	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Transmembrane	126	146	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Topological domain	147	150	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Transmembrane	151	171	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Topological domain	172	195	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Transmembrane	196	216	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Topological domain	217	229	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Transmembrane	230	250	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Topological domain	251	267	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Transmembrane	268	288	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Topological domain	289	357	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Transmembrane	358	378	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Topological domain	379	381	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Transmembrane	382	402	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Topological domain	403	424	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Transmembrane	425	445	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Topological domain	446	448	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40074	UniProtKB	Modified residue	344	344	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P12630 1 587
+P12630	UniProtKB	Signal peptide	1	24	.	.	.	.	
+P12630	UniProtKB	Chain	25	587	.	.	.	ID=PRO_0000025834;Note=Barrierpepsin	
+P12630	UniProtKB	Domain	45	393	.	.	.	Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
+P12630	UniProtKB	Active site	63	63	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P12630	UniProtKB	Active site	287	287	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P12630	UniProtKB	Glycosylation	84	84	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12630	UniProtKB	Glycosylation	90	90	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12630	UniProtKB	Glycosylation	268	268	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12630	UniProtKB	Glycosylation	308	308	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12630	UniProtKB	Glycosylation	366	366	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12630	UniProtKB	Glycosylation	398	398	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12630	UniProtKB	Glycosylation	468	468	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12630	UniProtKB	Glycosylation	503	503	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12630	UniProtKB	Glycosylation	551	551	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12630	UniProtKB	Disulfide bond	322	358	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12186 1 476
+Q12186	UniProtKB	Chain	1	476	.	.	.	ID=PRO_0000234564;Note=Branchpoint-bridging protein	
+Q12186	UniProtKB	Domain	153	219	.	.	.	Note=KH	
+Q12186	UniProtKB	Zinc finger	271	288	.	.	.	Note=CCHC-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+Q12186	UniProtKB	Zinc finger	297	314	.	.	.	Note=CCHC-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+Q12186	UniProtKB	Compositional bias	363	474	.	.	.	Note=Pro-rich	
+Q12186	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12186	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12186	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12186	UniProtKB	Modified residue	382	382	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12186	UniProtKB	Mutagenesis	60	60	.	.	.	Note=In MSL5-2%3B temperature-sensitive%3B growth defect%3B when associated with N-72 and S-155. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10775271;Dbxref=PMID:10775271	
+Q12186	UniProtKB	Mutagenesis	72	72	.	.	.	Note=In MSL5-2%3B temperature-sensitive%3B growth defect%3B when associated with G-60 and S-155. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10775271;Dbxref=PMID:10775271	
+Q12186	UniProtKB	Mutagenesis	155	155	.	.	.	Note=In MSL5-2%3B temperature-sensitive%3B growth defect%3B when associated with G-60 and N-72. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10775271;Dbxref=PMID:10775271	
+Q12186	UniProtKB	Mutagenesis	195	195	.	.	.	Note=In MSL5-5%3B cold-sensitive%3B growth defect%3B when associated with V-258. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10775271;Dbxref=PMID:10775271	
+Q12186	UniProtKB	Mutagenesis	230	230	.	.	.	Note=In msl-5%3B loss of function. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9150140;Dbxref=PMID:9150140	
+Q12186	UniProtKB	Mutagenesis	258	258	.	.	.	Note=In MSL5-5%3B cold-sensitive%3B growth defect%3B when associated with D-195. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10775271;Dbxref=PMID:10775271	
+Q12186	UniProtKB	Beta strand	148	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN	
+Q12186	UniProtKB	Turn	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN	
+Q12186	UniProtKB	Helix	164	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN	
+Q12186	UniProtKB	Helix	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN	
+Q12186	UniProtKB	Helix	174	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN	
+Q12186	UniProtKB	Beta strand	186	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN	
+Q12186	UniProtKB	Helix	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN	
+Q12186	UniProtKB	Turn	206	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN	
+Q12186	UniProtKB	Beta strand	212	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN	
+Q12186	UniProtKB	Helix	224	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN	
+Q12186	UniProtKB	Helix	250	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN	
+##sequence-region P38891 1 393
+P38891	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38891	UniProtKB	Chain	17	393	.	.	.	ID=PRO_0000001281;Note=Branched-chain-amino-acid aminotransferase%2C mitochondrial	
+P38891	UniProtKB	Modified residue	219	219	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38891	UniProtKB	Modified residue	315	315	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38772 1 366
+P38772	UniProtKB	Chain	1	366	.	.	.	ID=PRO_0000173558;Note=Box C/D snoRNA protein 1	
+P38772	UniProtKB	Zinc finger	5	39	.	.	.	Note=HIT-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00453	
+P38772	UniProtKB	Modified residue	330	330	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38772	UniProtKB	Beta strand	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N94	
+P38772	UniProtKB	Turn	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N94	
+P38772	UniProtKB	Helix	27	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N94	
+P38772	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N94	
+##sequence-region P32873 1 1128
+P32873	UniProtKB	Chain	1	1128	.	.	.	ID=PRO_0000056728;Note=GTPase-activating protein BEM3	
+P32873	UniProtKB	Domain	634	741	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P32873	UniProtKB	Domain	913	1128	.	.	.	Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172	
+P32873	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P22804 1 142
+P22804	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000206892;Note=Protein transport protein BET1	
+P22804	UniProtKB	Topological domain	1	117	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22804	UniProtKB	Transmembrane	118	141	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22804	UniProtKB	Topological domain	142	142	.	.	.	Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22804	UniProtKB	Domain	52	114	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+P22804	UniProtKB	Helix	52	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+##sequence-region Q06631 1 534
+Q06631	UniProtKB	Chain	1	534	.	.	.	ID=PRO_0000056634;Note=Protein BFR2	
+Q06631	UniProtKB	Coiled coil	86	161	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06631	UniProtKB	Modified residue	41	41	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06631	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06631	UniProtKB	Modified residue	366	366	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06631	UniProtKB	Modified residue	372	372	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06631	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06631	UniProtKB	Sequence conflict	451	451	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11709 1 440
+P11709	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000083513;Note=Nuclear fusion protein BIK1	
+P11709	UniProtKB	Domain	26	69	.	.	.	Note=CAP-Gly;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00045	
+P11709	UniProtKB	Coiled coil	190	397	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P11709	UniProtKB	Motif	416	429	.	.	.	Note=CCHC-box	
+P11709	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P11709	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region P32451 1 375
+P32451	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32451	UniProtKB	Chain	17	375	.	.	.	ID=PRO_0000185567;Note=Biotin synthase%2C mitochondrial	
+P32451	UniProtKB	Metal binding	99	99	.	.	.	Note=Iron-sulfur 1 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32451	UniProtKB	Metal binding	103	103	.	.	.	Note=Iron-sulfur 1 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32451	UniProtKB	Metal binding	106	106	.	.	.	Note=Iron-sulfur 1 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32451	UniProtKB	Metal binding	143	143	.	.	.	Note=Iron-sulfur 2 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32451	UniProtKB	Metal binding	176	176	.	.	.	Note=Iron-sulfur 2 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32451	UniProtKB	Metal binding	236	236	.	.	.	Note=Iron-sulfur 2 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32451	UniProtKB	Metal binding	314	314	.	.	.	Note=Iron-sulfur 2 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32451	UniProtKB	Sequence conflict	348	349	.	.	.	Note=MC->IY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40493 1 336
+P40493	UniProtKB	Chain	1	336	.	.	.	ID=PRO_0000202971;Note=25S rRNA (uridine(2634)-N(3))-methyltransferase	
+P40493	UniProtKB	Mutagenesis	182	182	.	.	.	Note=Abolishes methyltransferase activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24335083;Dbxref=PMID:24335083	
+##sequence-region P39724 1 118
+P39724	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000201239;Note=BolA-like protein 3	
+P39724	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Partial loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773	
+P39724	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Loss of function. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773	
+P39724	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Dominant negative mutant%3B displays respiratory defects that are higher than the BOL1 BOL3 double mutant. H->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773	
+##sequence-region P26449 1 341
+P26449	UniProtKB	Chain	1	341	.	.	.	ID=PRO_0000050890;Note=Cell cycle arrest protein BUB3	
+P26449	UniProtKB	Repeat	9	48	.	.	.	Note=WD 1	
+P26449	UniProtKB	Repeat	54	96	.	.	.	Note=WD 2	
+P26449	UniProtKB	Repeat	97	137	.	.	.	Note=WD 3	
+P26449	UniProtKB	Repeat	144	185	.	.	.	Note=WD 4	
+P26449	UniProtKB	Repeat	191	233	.	.	.	Note=WD 5	
+P26449	UniProtKB	Repeat	249	288	.	.	.	Note=WD 6	
+P26449	UniProtKB	Repeat	292	329	.	.	.	Note=WD 7	
+P26449	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Abolishes checkpoint function. Benomyl-sensitive phenotype. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329	
+P26449	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Abolishes checkpoint function and interaction with MAD2%2C MAD3 and CDC20. Benomyl-sensitive phenotype. W->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11726501;Dbxref=PMID:11726501	
+P26449	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Abolishes checkpoint function and interaction with MAD2%2C MAD3 and CDC20. Benomyl-sensitive phenotype. W->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11726501;Dbxref=PMID:11726501	
+P26449	UniProtKB	Mutagenesis	188	188	.	.	.	Note=Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329	
+P26449	UniProtKB	Mutagenesis	191	191	.	.	.	Note=Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329	
+P26449	UniProtKB	Mutagenesis	192	192	.	.	.	Note=Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329	
+P26449	UniProtKB	Mutagenesis	193	193	.	.	.	Note=Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329	
+P26449	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Abolishes checkpoint function. Benomyl-sensitive phenotype. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329	
+P26449	UniProtKB	Mutagenesis	226	226	.	.	.	Note=Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329	
+P26449	UniProtKB	Mutagenesis	242	242	.	.	.	Note=Abolishes checkpoint function. Benomyl-sensitive phenotype. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329	
+P26449	UniProtKB	Mutagenesis	276	276	.	.	.	Note=Abolishes checkpoint function. Lowers interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329	
+P26449	UniProtKB	Mutagenesis	278	278	.	.	.	Note=Abolishes checkpoint function. No effect on interaction with BUB1. Lowers interaction with MAD3. Benomyl-sensitive phenotype. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329	
+P26449	UniProtKB	Beta strand	2	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	14	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Helix	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	25	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	33	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Turn	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	46	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	59	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	81	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	86	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	104	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Turn	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	114	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	122	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Helix	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S	
+P26449	UniProtKB	Beta strand	137	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	144	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	153	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	160	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	171	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3T	
+P26449	UniProtKB	Beta strand	186	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	196	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Helix	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	208	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	216	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	236	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S	
+P26449	UniProtKB	Beta strand	249	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S	
+P26449	UniProtKB	Beta strand	254	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Turn	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	266	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	275	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Turn	280	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	284	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	293	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	304	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Helix	315	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+P26449	UniProtKB	Beta strand	332	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ	
+##sequence-region Q08492 1 214
+Q08492	UniProtKB	Chain	1	214	.	.	.	ID=PRO_0000065013;Note=Bud site selection protein 21	
+Q08492	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08492	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q08492	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08492	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q05949 1 395
+Q05949	UniProtKB	Chain	1	395	.	.	.	ID=PRO_0000076186;Note=Protein BUR2	
+Q05949	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P40580 1 263
+P40580	UniProtKB	Chain	1	263	.	.	.	ID=PRO_0000054871;Note=Benzil reductase ((S)-benzoin forming) IRC24	
+P40580	UniProtKB	Nucleotide binding	6	30	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40580	UniProtKB	Active site	157	157	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001	
+P40580	UniProtKB	Binding site	144	144	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P09440 1 975
+P09440	UniProtKB	Transit peptide	1	34	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3528153;Dbxref=PMID:3528153	
+P09440	UniProtKB	Chain	35	975	.	.	.	ID=PRO_0000034052;Note=C-1-tetrahydrofolate synthase%2C mitochondrial	
+P09440	UniProtKB	Nucleotide binding	201	203	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09440	UniProtKB	Nucleotide binding	408	415	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09440	UniProtKB	Region	35	343	.	.	.	Note=Methylenetetrahydrofolate dehydrogenase and cyclohydrolase	
+P09440	UniProtKB	Region	83	87	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09440	UniProtKB	Region	130	132	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09440	UniProtKB	Region	301	305	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09440	UniProtKB	Region	344	975	.	.	.	Note=Formyltetrahydrofolate synthetase	
+P09440	UniProtKB	Binding site	226	226	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P43569 1 289
+P43569	UniProtKB	Chain	1	289	.	.	.	ID=PRO_0000093464;Note=CCR4-associated factor 16	
+P43569	UniProtKB	Domain	7	249	.	.	.	Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P43569	UniProtKB	Nucleotide binding	41	48	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+##sequence-region P53615 1 221
+P53615	UniProtKB	Chain	1	221	.	.	.	ID=PRO_0000077468;Note=Carbonic anhydrase	
+P53615	UniProtKB	Metal binding	57	57	.	.	.	Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3EYX,ECO:0000269|PubMed:19852838;Dbxref=PMID:19852838	
+P53615	UniProtKB	Metal binding	59	59	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61517	
+P53615	UniProtKB	Metal binding	112	112	.	.	.	Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3EYX,ECO:0000269|PubMed:19852838;Dbxref=PMID:19852838	
+P53615	UniProtKB	Metal binding	115	115	.	.	.	Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3EYX,ECO:0000269|PubMed:19852838;Dbxref=PMID:19852838	
+P53615	UniProtKB	Sequence conflict	39	39	.	.	.	Note=L->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53615	UniProtKB	Helix	18	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Beta strand	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Beta strand	73	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	89	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Beta strand	105	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	116	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	135	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	142	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	152	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	161	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Helix	184	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Beta strand	196	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Turn	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Beta strand	209	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+P53615	UniProtKB	Beta strand	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX	
+##sequence-region P07252 1 654
+P07252	UniProtKB	Chain	1	654	.	.	.	ID=PRO_0000089378;Note=Cytochrome B pre-mRNA-processing protein 1	
+##sequence-region P0C155 1 581
+P0C155	UniProtKB	Chain	1	581	.	.	.	ID=PRO_0000226147;Note=Putative carboxypeptidase YOL153C	
+P0C155	UniProtKB	Topological domain	1	29	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C155	UniProtKB	Transmembrane	30	46	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C155	UniProtKB	Topological domain	47	581	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C155	UniProtKB	Active site	172	172	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C155	UniProtKB	Active site	241	241	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C155	UniProtKB	Metal binding	170	170	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C155	UniProtKB	Metal binding	207	207	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C155	UniProtKB	Metal binding	207	207	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C155	UniProtKB	Metal binding	242	242	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C155	UniProtKB	Metal binding	270	270	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C155	UniProtKB	Metal binding	550	550	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0C155	UniProtKB	Glycosylation	54	54	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C155	UniProtKB	Glycosylation	76	76	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C155	UniProtKB	Glycosylation	335	335	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C155	UniProtKB	Glycosylation	428	428	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0C155	UniProtKB	Cross-link	17	17	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27614	
+##sequence-region P27614 1 576
+P27614	UniProtKB	Chain	1	576	.	.	.	ID=PRO_0000185271;Note=Carboxypeptidase S	
+P27614	UniProtKB	Topological domain	1	19	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27614	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27614	UniProtKB	Topological domain	41	576	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27614	UniProtKB	Active site	170	170	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27614	UniProtKB	Active site	239	239	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27614	UniProtKB	Metal binding	168	168	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27614	UniProtKB	Metal binding	205	205	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27614	UniProtKB	Metal binding	205	205	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27614	UniProtKB	Metal binding	240	240	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27614	UniProtKB	Metal binding	268	268	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27614	UniProtKB	Metal binding	547	547	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27614	UniProtKB	Glycosylation	88	88	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27614	UniProtKB	Glycosylation	176	176	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27614	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27614	UniProtKB	Glycosylation	381	381	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27614	UniProtKB	Glycosylation	525	525	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27614	UniProtKB	Cross-link	8	8	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P27614	UniProtKB	Sequence conflict	387	387	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00729 1 532
+P00729	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00729	UniProtKB	Propeptide	21	111	.	.	.	ID=PRO_0000004293;Note=Mediates translocation across the endoplasmic reticulum%2C renders the enzyme inactive during transit%2C and targets the molecule to the vacuole;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|Ref.4,ECO:0000305|PubMed:3028649;Dbxref=PMID:3028649	
+P00729	UniProtKB	Chain	112	532	.	.	.	ID=PRO_0000004294;Note=Carboxypeptidase Y	
+P00729	UniProtKB	Motif	24	27	.	.	.	Note=Vacuolar targeting signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3028649;Dbxref=PMID:3028649	
+P00729	UniProtKB	Active site	257	257	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7727362,ECO:0000269|Ref.5;Dbxref=PMID:7727362	
+P00729	UniProtKB	Active site	449	449	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7727362;Dbxref=PMID:7727362	
+P00729	UniProtKB	Active site	508	508	.	.	.	Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:2639680,ECO:0000305|PubMed:7727362;Dbxref=PMID:2639680,PMID:7727362	
+P00729	UniProtKB	Binding site	452	452	.	.	.	Note=Substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|Ref.5	
+P00729	UniProtKB	Binding site	509	509	.	.	.	Note=Substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|Ref.5	
+P00729	UniProtKB	Glycosylation	124	124	.	.	.	Note=N-linked (GlcNAc...) (high mannose) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28189789;Dbxref=PMID:28189789	
+P00729	UniProtKB	Glycosylation	198	198	.	.	.	Note=N-linked (GlcNAc...) (high mannose) asparagine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:28189789,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:28189789,PMID:7727362	
+P00729	UniProtKB	Glycosylation	279	279	.	.	.	Note=N-linked (GlcNAc...) (high mannose) asparagine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:28189789,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:28189789,PMID:7727362	
+P00729	UniProtKB	Glycosylation	479	479	.	.	.	Note=N-linked (GlcNAc...) (high mannose) asparagine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:28189789,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:28189789,PMID:7727362	
+P00729	UniProtKB	Disulfide bond	167	409	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:7727362	
+P00729	UniProtKB	Disulfide bond	304	318	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:7727362	
+P00729	UniProtKB	Disulfide bond	328	351	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:7727362	
+P00729	UniProtKB	Disulfide bond	335	344	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:7727362	
+P00729	UniProtKB	Disulfide bond	373	379	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:7727362	
+P00729	UniProtKB	Mutagenesis	508	508	.	.	.	Note=Inactivates enzyme. H->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7904479;Dbxref=PMID:7904479	
+P00729	UniProtKB	Sequence conflict	260	261	.	.	.	Note=GH->HG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00729	UniProtKB	Sequence conflict	389	389	.	.	.	Note=Y->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00729	UniProtKB	Sequence conflict	529	529	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00729	UniProtKB	Helix	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	129	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Turn	135	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	139	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Turn	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	157	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Turn	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	170	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Turn	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	178	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Turn	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	187	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	195	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	199	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	214	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	224	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	242	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YSC	
+P00729	UniProtKB	Turn	245	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	251	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	259	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	282	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	292	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	299	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	315	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	341	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	357	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	368	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	375	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	382	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	393	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	403	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P00729	UniProtKB	Helix	411	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Turn	419	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	422	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	428	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	441	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	454	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	469	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	478	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Turn	483	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	487	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Beta strand	498	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	510	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Helix	515	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+P00729	UniProtKB	Turn	527	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY	
+##sequence-region P14905 1 389
+P14905	UniProtKB	Chain	1	389	.	.	.	ID=PRO_0000089382;Note=Cytochrome B translational activator protein CBS2	
+##sequence-region P34730 1 273
+P34730	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P34730	UniProtKB	Chain	2	273	.	.	.	ID=PRO_0000058716;Note=Protein BMH2	
+P34730	UniProtKB	Compositional bias	245	261	.	.	.	Note=Poly-Gln	
+P34730	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P34730	UniProtKB	Sequence conflict	119	119	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P34730	UniProtKB	Sequence conflict	174	174	.	.	.	Note=G->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38041 1 980
+P38041	UniProtKB	Chain	1	980	.	.	.	ID=PRO_0000064968;Note=Protein BOB1	
+P38041	UniProtKB	Domain	13	77	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P38041	UniProtKB	Domain	228	292	.	.	.	Note=SAM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00184	
+P38041	UniProtKB	Domain	776	895	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P38041	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38041	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38041	UniProtKB	Modified residue	128	128	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38041	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38041	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38041	UniProtKB	Modified residue	209	209	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+P38041	UniProtKB	Modified residue	393	393	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38041	UniProtKB	Modified residue	412	412	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38041	UniProtKB	Modified residue	525	525	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38041	UniProtKB	Modified residue	528	528	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38041	UniProtKB	Modified residue	589	589	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38041	UniProtKB	Modified residue	590	590	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38041	UniProtKB	Modified residue	593	593	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38041	UniProtKB	Modified residue	644	644	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38041	UniProtKB	Modified residue	655	655	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38041	UniProtKB	Modified residue	735	735	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38041	UniProtKB	Modified residue	919	919	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P48558 1 297
+P48558	UniProtKB	Chain	1	297	.	.	.	ID=PRO_0000203369;Note=Bax inhibitor 1	
+P48558	UniProtKB	Topological domain	1	53	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Topological domain	75	85	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Topological domain	107	146	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Topological domain	168	171	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Transmembrane	172	192	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Topological domain	193	208	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Topological domain	230	239	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Transmembrane	240	260	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Topological domain	261	270	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Transmembrane	271	291	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Topological domain	292	297	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48558	UniProtKB	Sequence conflict	84	84	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53836 1 1060
+P53836	UniProtKB	Chain	1	1060	.	.	.	ID=PRO_0000203378;Note=CCR4-NOT transcriptional complex subunit CAF120	
+P53836	UniProtKB	Domain	75	204	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P53836	UniProtKB	Compositional bias	886	1030	.	.	.	Note=Pro-rich	
+P53836	UniProtKB	Modified residue	491	491	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53836	UniProtKB	Modified residue	510	510	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53836	UniProtKB	Modified residue	518	518	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53836	UniProtKB	Modified residue	538	538	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53836	UniProtKB	Modified residue	556	556	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P53836	UniProtKB	Modified residue	871	871	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53836	UniProtKB	Modified residue	885	885	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P39101 1 391
+P39101	UniProtKB	Chain	1	391	.	.	.	ID=PRO_0000071119;Note=Protein CAJ1	
+P39101	UniProtKB	Domain	4	73	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P39101	UniProtKB	Cross-link	132	132	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P17555 1 526
+P17555	UniProtKB	Chain	1	526	.	.	.	ID=PRO_0000205706;Note=Adenylyl cyclase-associated protein	
+P17555	UniProtKB	Domain	369	504	.	.	.	Note=C-CAP/cofactor C-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00659	
+P17555	UniProtKB	Region	1	168	.	.	.	Note=Adenyl cyclase-binding	
+P17555	UniProtKB	Region	354	361	.	.	.	Note=Interaction with SH3 domain of ABP1	
+P17555	UniProtKB	Region	370	526	.	.	.	Note=Dimerization and actin-binding	
+P17555	UniProtKB	Motif	169	369	.	.	.	Note=SH3-binding	
+P17555	UniProtKB	Compositional bias	262	300	.	.	.	Note=Ala/Pro/Ser-rich	
+P17555	UniProtKB	Compositional bias	277	282	.	.	.	Note=Poly-Pro	
+P17555	UniProtKB	Modified residue	454	454	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P17555	UniProtKB	Beta strand	371	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	378	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	391	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	400	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	417	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	435	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	439	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	456	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	464	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Turn	473	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	478	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	485	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Helix	495	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	500	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	508	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+P17555	UniProtKB	Beta strand	516	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z	
+##sequence-region P06787 1 147
+P06787	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000198328;Note=Calmodulin	
+P06787	UniProtKB	Domain	8	43	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P06787	UniProtKB	Domain	44	79	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P06787	UniProtKB	Domain	81	116	.	.	.	Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P06787	UniProtKB	Domain	117	147	.	.	.	Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P06787	UniProtKB	Calcium binding	21	32	.	.	.	Note=1	
+P06787	UniProtKB	Calcium binding	57	68	.	.	.	Note=2	
+P06787	UniProtKB	Calcium binding	94	105	.	.	.	Note=3	
+P06787	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06787	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P06787	UniProtKB	Mutagenesis	21	21	.	.	.	Note=Highly reduced affinity for Ca(2+). D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154	
+P06787	UniProtKB	Mutagenesis	32	32	.	.	.	Note=Highly reduced affinity for Ca(2+). E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154	
+P06787	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Highly reduced affinity for Ca(2+). D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154	
+P06787	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Highly reduced affinity for Ca(2+). E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154	
+P06787	UniProtKB	Mutagenesis	94	94	.	.	.	Note=Highly reduced affinity for Ca(2+). D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154	
+P06787	UniProtKB	Mutagenesis	105	105	.	.	.	Note=Highly reduced affinity for Ca(2+). E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154	
+P06787	UniProtKB	Helix	7	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54	
+P06787	UniProtKB	Beta strand	25	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54	
+P06787	UniProtKB	Helix	30	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54	
+P06787	UniProtKB	Helix	46	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54	
+P06787	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ	
+P06787	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54	
+P06787	UniProtKB	Helix	66	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54	
+P06787	UniProtKB	Helix	82	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ	
+P06787	UniProtKB	Beta strand	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ	
+P06787	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ	
+P06787	UniProtKB	Helix	103	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ	
+P06787	UniProtKB	Helix	119	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ	
+P06787	UniProtKB	Beta strand	132	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ	
+P06787	UniProtKB	Helix	138	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ	
+##sequence-region P27825 1 502
+P27825	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27825	UniProtKB	Chain	20	502	.	.	.	ID=PRO_0000004208;Note=Calnexin homolog	
+P27825	UniProtKB	Topological domain	20	481	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27825	UniProtKB	Transmembrane	482	502	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27825	UniProtKB	Repeat	250	261	.	.	.	Note=1-1	
+P27825	UniProtKB	Repeat	267	278	.	.	.	Note=1-2	
+P27825	UniProtKB	Repeat	286	297	.	.	.	Note=1-3	
+P27825	UniProtKB	Repeat	305	316	.	.	.	Note=1-4	
+P27825	UniProtKB	Repeat	320	330	.	.	.	Note=2-1	
+P27825	UniProtKB	Repeat	339	349	.	.	.	Note=2-2	
+P27825	UniProtKB	Repeat	353	363	.	.	.	Note=2-3	
+P27825	UniProtKB	Repeat	367	377	.	.	.	Note=2-4	
+P27825	UniProtKB	Region	248	381	.	.	.	Note=P domain (Extended arm);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27825	UniProtKB	Region	250	316	.	.	.	Note=4 X approximate repeats	
+P27825	UniProtKB	Region	320	377	.	.	.	Note=4 X approximate repeats	
+P27825	UniProtKB	Binding site	131	131	.	.	.	Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27825	UniProtKB	Glycosylation	25	25	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27825	UniProtKB	Glycosylation	104	104	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27825	UniProtKB	Glycosylation	296	296	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27825	UniProtKB	Glycosylation	416	416	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27825	UniProtKB	Glycosylation	425	425	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27825	UniProtKB	Disulfide bond	125	161	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27825	UniProtKB	Disulfide bond	332	338	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P04817 1 590
+P04817	UniProtKB	Chain	1	590	.	.	.	ID=PRO_0000054148;Note=Arginine permease CAN1	
+P04817	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Transmembrane	172	192	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Transmembrane	235	255	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Transmembrane	283	303	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Transmembrane	324	344	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Transmembrane	377	397	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Transmembrane	420	440	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Transmembrane	449	469	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Transmembrane	498	518	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Transmembrane	524	544	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04817	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32487	
+P04817	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32487	
+P04817	UniProtKB	Mutagenesis	113	113	.	.	.	Note=In CAN1-343%3B confers citrulline transport activity in GAP1-deleted cells. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	148	148	.	.	.	Note=In CAN1-337%3B confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate%2C alpha-aminoisobutyrate%2C 3-chloro-L-alanine%2C L-ethionine%2C L-allylglycine%2C and D-histidine%2C but not sensitivity to L-aspartic acid alpha-hydroxamate or p-fluoro-L-phenylalanine. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	149	149	.	.	.	Note=In CAN1-315%3B confers citrulline transport activity in GAP1-deleted cells. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	152	152	.	.	.	Note=In CAN1-342%3B confers citrulline transport activity in GAP1-deleted cells. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	173	173	.	.	.	Note=In CAN1-306%3B confers citrulline transport activity in GAP1-deleted cells. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	173	173	.	.	.	Note=In CAN1-327%3B confers citrulline transport activity in GAP1-deleted cells. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	308	308	.	.	.	Note=In CAN1-341%3B confers citrulline transport activity in GAP1-deleted cells. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	313	313	.	.	.	Note=In CAN1-329%3B confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate%2C alpha-aminoisobutyrate%2C 3-chloro-L-alanine%2C L-ethionine%2C L-allylglycine%2C and D-histidine%2C L-aspartic acid alpha-hydroxamate and p-fluoro-L-phenylalanine. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	354	355	.	.	.	Note=In CAN1-318%3B confers citrulline transport activity in GAP1-deleted cells. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	356	356	.	.	.	Note=In CAN1-340%3B confers citrulline transport activity in GAP1-deleted cells. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	356	356	.	.	.	Note=In CAN1-339%3B confers citrulline transport activity in GAP1-deleted cells. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	451	451	.	.	.	Note=In CAN1-328%3B confers citrulline transport activity in GAP1-deleted cells. W->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	451	451	.	.	.	Note=In CAN1-316%3B confers citrulline transport activity in GAP1-deleted cells. W->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	451	451	.	.	.	Note=In CAN1-335%3B confers citrulline transport activity in GAP1-deleted cells. W->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Mutagenesis	461	461	.	.	.	Note=In CAN1-307%3B confers citrulline transport activity in GAP1-deleted cells. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604	
+P04817	UniProtKB	Sequence conflict	534	534	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P28495 1 268
+P28495	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P28495	UniProtKB	Chain	2	268	.	.	.	ID=PRO_0000208646;Note=F-actin-capping protein subunit alpha	
+P28495	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P28495	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P34237 1 679
+P34237	UniProtKB	Chain	1	679	.	.	.	ID=PRO_0000071795;Note=Protein CASP	
+P34237	UniProtKB	Topological domain	1	614	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34237	UniProtKB	Transmembrane	615	635	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34237	UniProtKB	Topological domain	636	679	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34237	UniProtKB	Coiled coil	14	90	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34237	UniProtKB	Coiled coil	178	341	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34237	UniProtKB	Coiled coil	385	444	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34237	UniProtKB	Coiled coil	492	540	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34237	UniProtKB	Modified residue	364	364	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P34237	UniProtKB	Modified residue	450	450	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34237	UniProtKB	Modified residue	453	453	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34237	UniProtKB	Modified residue	555	555	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34237	UniProtKB	Mutagenesis	619	619	.	.	.	Note=Retained in the endoplasmic reticulum. Y->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12429822;Dbxref=PMID:12429822	
+P34237	UniProtKB	Mutagenesis	624	624	.	.	.	Note=No effect on subcellular location. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12429822;Dbxref=PMID:12429822	
+##sequence-region P15202 1 515
+P15202	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P15202	UniProtKB	Chain	2	515	.	.	.	ID=PRO_0000084928;Note=Peroxisomal catalase A	
+P15202	UniProtKB	Motif	513	515	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15202	UniProtKB	Active site	70	70	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9931255;Dbxref=PMID:9931255	
+P15202	UniProtKB	Active site	143	143	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9931255;Dbxref=PMID:9931255	
+P15202	UniProtKB	Metal binding	355	355	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9931255;Dbxref=PMID:9931255	
+P15202	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P15202	UniProtKB	Sequence conflict	131	131	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15202	UniProtKB	Beta strand	31	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Turn	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	50	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	72	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	101	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	119	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	126	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	136	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	155	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Turn	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	174	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	184	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	190	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	217	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	226	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	244	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	257	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	273	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	283	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Turn	302	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	308	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	322	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Turn	326	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	346	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	367	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	371	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Turn	395	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	425	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	429	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Beta strand	438	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	441	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	459	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	476	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+P15202	UniProtKB	Helix	491	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E	
+##sequence-region P53630 1 237
+P53630	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000188006;Note=Dethiobiotin synthetase	
+P53630	UniProtKB	Nucleotide binding	18	26	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q06071 1 122
+Q06071	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000247218;Note=Biogenesis of lysosome-related organelles complex 1 subunit BLS1	
+Q06071	UniProtKB	Modified residue	33	33	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q01532 1 483
+Q01532	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01532	UniProtKB	Chain	31	482	.	.	.	ID=PRO_0000050554;Note=Cysteine proteinase 1%2C mitochondrial	
+Q01532	UniProtKB	Propeptide	483	483	.	.	.	ID=PRO_0000292865;Note=Removed in mature form%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7638617;Dbxref=PMID:7638617	
+Q01532	UniProtKB	Active site	102	102	.	.	.	.	
+Q01532	UniProtKB	Active site	398	398	.	.	.	.	
+Q01532	UniProtKB	Active site	421	421	.	.	.	.	
+Q01532	UniProtKB	Alternative sequence	1	29	.	.	.	ID=VSP_026453;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01532	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Abolishes peptidase activity%2C which also hinders autocatalytic processing of the enzyme to the mature form. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9374524;Dbxref=PMID:9374524	
+Q01532	UniProtKB	Mutagenesis	271	274	.	.	.	Note=In GAL6DB%3B disrupts nucleic acid-binding activity%2C but retains normal peptidase activity. KDKK->ADAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9374524;Dbxref=PMID:9374524	
+Q01532	UniProtKB	Mutagenesis	398	398	.	.	.	Note=Abolishes Hcy-thiolactonase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16769724;Dbxref=PMID:16769724	
+Q01532	UniProtKB	Mutagenesis	479	479	.	.	.	Note=Results in the abnormal cleavage of 3 C-terminal residues instead of only 1 during autocatalytic processing. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9546396;Dbxref=PMID:9546396	
+Q01532	UniProtKB	Sequence conflict	187	187	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01532	UniProtKB	Helix	36	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	50	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	64	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	71	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GCB	
+Q01532	UniProtKB	Helix	102	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	128	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Turn	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	158	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	174	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	203	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A6R	
+Q01532	UniProtKB	Helix	232	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	264	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	275	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	282	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	296	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	311	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	326	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	333	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	350	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Turn	356	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Turn	362	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	374	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	385	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	398	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Turn	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	414	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Turn	425	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E03	
+Q01532	UniProtKB	Beta strand	432	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	437	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	444	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	451	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	456	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Beta strand	470	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01	
+Q01532	UniProtKB	Helix	477	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A6R	
+##sequence-region P29311 1 267
+P29311	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P29311	UniProtKB	Chain	2	267	.	.	.	ID=PRO_0000058715;Note=Protein BMH1	
+P29311	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P29311	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P29311	UniProtKB	Cross-link	76	76	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P29311	UniProtKB	Sequence conflict	197	197	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29311	UniProtKB	Sequence conflict	197	197	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29311	UniProtKB	Sequence conflict	263	267	.	.	.	Note=GEAPK->VKHQSKYSDKSKEKLLKKRKKKERGCNNL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P48445 1 690
+P48445	UniProtKB	Chain	1	690	.	.	.	ID=PRO_0000064981;Note=Biotin--protein ligase	
+P48445	UniProtKB	Domain	378	606	.	.	.	Note=BPL/LPL catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01067	
+##sequence-region P48582 1 844
+P48582	UniProtKB	Chain	1	844	.	.	.	ID=PRO_0000218872;Note=Vacuolar-sorting protein BRO1	
+P48582	UniProtKB	Domain	4	400	.	.	.	Note=BRO1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00526	
+P48582	UniProtKB	Coiled coil	547	583	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48582	UniProtKB	Modified residue	740	740	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P48582	UniProtKB	Sequence conflict	359	359	.	.	.	Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48582	UniProtKB	Helix	18	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Turn	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	41	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	60	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	82	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Beta strand	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Beta strand	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	113	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Turn	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Beta strand	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	141	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	171	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	203	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Turn	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Beta strand	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	239	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	270	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Turn	290	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	298	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Beta strand	318	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	330	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+P48582	UniProtKB	Helix	344	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1	
+##sequence-region P32639 1 2163
+P32639	UniProtKB	Chain	1	2163	.	.	.	ID=PRO_0000102086;Note=Pre-mRNA-splicing helicase BRR2	
+P32639	UniProtKB	Domain	508	692	.	.	.	Note=Helicase ATP-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32639	UniProtKB	Domain	718	921	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P32639	UniProtKB	Domain	998	1308	.	.	.	Note=SEC63 1	
+P32639	UniProtKB	Domain	1357	1533	.	.	.	Note=Helicase ATP-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32639	UniProtKB	Domain	1846	2160	.	.	.	Note=SEC63 2	
+P32639	UniProtKB	Nucleotide binding	521	528	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32639	UniProtKB	Nucleotide binding	1370	1377	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32639	UniProtKB	Motif	634	637	.	.	.	Note=DEIH box	
+P32639	UniProtKB	Motif	1474	1477	.	.	.	Note=DDAH box	
+P32639	UniProtKB	Compositional bias	1570	1575	.	.	.	Note=Poly-Ala	
+P32639	UniProtKB	Modified residue	403	403	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32639	UniProtKB	Mutagenesis	858	858	.	.	.	Note=Reduces spliceosomal pre-mRNA splicing. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23124065;Dbxref=PMID:23124065	
+P32639	UniProtKB	Mutagenesis	938	938	.	.	.	Note=Strongly reduced unwinding of U4/U6 snRNA. W->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19716790;Dbxref=PMID:19716790	
+P32639	UniProtKB	Mutagenesis	1107	1107	.	.	.	Note=Reduced ATP-dependent RNA helicase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19525970;Dbxref=PMID:19525970	
+P32639	UniProtKB	Mutagenesis	1110	1110	.	.	.	Note=Abolishes unwinding of U4/U6 snRNA. R->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19716790;Dbxref=PMID:19716790	
+P32639	UniProtKB	Helix	114	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	137	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	164	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	176	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	263	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	267	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52	
+P32639	UniProtKB	Turn	285	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	292	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	306	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	320	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	330	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	340	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52	
+P32639	UniProtKB	Turn	344	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	347	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	353	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	370	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	382	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	388	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	429	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	453	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	458	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	480	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	485	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	493	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	501	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	517	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	523	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD	
+P32639	UniProtKB	Helix	527	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	545	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	556	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	564	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	579	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	585	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	591	593	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	596	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	603	607	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	609	617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	619	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	622	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	628	633	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	636	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	644	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	659	662	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	666	673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	677	683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	688	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	691	693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	696	698	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	699	701	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD	
+P32639	UniProtKB	Beta strand	703	710	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	715	735	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	740	743	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	747	762	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	767	770	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	776	785	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	791	798	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	801	804	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	806	808	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD	
+P32639	UniProtKB	Helix	810	821	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	826	830	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	833	836	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	842	848	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	851	854	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	855	857	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	859	862	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	865	873	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	874	876	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD	
+P32639	UniProtKB	Turn	878	880	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	882	891	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	892	894	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	895	901	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	902	904	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	912	915	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	916	925	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	932	939	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	943	950	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	952	956	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	960	963	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	964	966	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	967	983	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	986	990	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	991	994	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	995	999	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1000	1008	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1012	1021	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1028	1036	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1039	1041	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	1048	1050	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1051	1059	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1069	1071	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD	
+P32639	UniProtKB	Helix	1072	1084	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1092	1119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1122	1137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1141	1143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD	
+P32639	UniProtKB	Helix	1145	1148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1154	1163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1168	1171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1178	1182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	1186	1190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1191	1196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1202	1224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1230	1233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1237	1244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1246	1248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1250	1259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1261	1263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1266	1275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1278	1282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1286	1297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1301	1307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1331	1333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1337	1340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1344	1347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52	
+P32639	UniProtKB	Helix	1350	1354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1356	1360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1366	1369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1372	1375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52	
+P32639	UniProtKB	Helix	1376	1389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1395	1398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1402	1416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	1417	1421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1424	1426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1432	1441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1443	1447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1449	1455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1456	1461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1463	1466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1470	1474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1476	1480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1482	1502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1507	1513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1519	1525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1529	1531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1532	1534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1537	1539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD	
+P32639	UniProtKB	Beta strand	1544	1553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1555	1558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52	
+P32639	UniProtKB	Helix	1561	1576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1581	1587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1588	1603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	1604	1606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1614	1622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1627	1629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1630	1634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1637	1640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1642	1644	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1646	1657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1660	1667	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1668	1670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1671	1673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1677	1683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1686	1689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Turn	1690	1693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1694	1697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1700	1707	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1714	1716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1718	1725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1726	1737	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1746	1749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1750	1759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1766	1773	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1777	1782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1786	1789	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Helix	1796	1816	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1819	1823	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1843	1846	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1847	1849	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	1860	1869	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	1876	1884	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	1887	1891	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	1898	1906	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Beta strand	1909	1911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Beta strand	1915	1917	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P32639	UniProtKB	Beta strand	1919	1921	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	1922	1935	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	1941	1967	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	1973	1985	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Beta strand	1989	1991	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD	
+P32639	UniProtKB	Helix	1993	1996	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	2002	2010	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	2016	2021	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	2024	2030	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	2035	2047	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Beta strand	2051	2057	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	2060	2062	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Beta strand	2067	2079	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Beta strand	2099	2105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Helix	2106	2108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Beta strand	2110	2117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Beta strand	2121	2131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Beta strand	2135	2148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+P32639	UniProtKB	Beta strand	2154	2163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1	
+##sequence-region O13558 1 102
+O13558	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000299769;Note=Putative uncharacterized protein BSC3	
+##sequence-region Q07992 1 125
+Q07992	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07992	UniProtKB	Chain	20	125	.	.	.	ID=PRO_0000299772;Note=Putative uncharacterized protein BUD28	
+##sequence-region Q12064 1 193
+Q12064	UniProtKB	Signal peptide	1	14	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12064	UniProtKB	Chain	15	193	.	.	.	ID=PRO_0000299773;Note=Putative uncharacterized protein BUD30	
+Q12064	UniProtKB	Compositional bias	2	58	.	.	.	Note=Ser-rich	
+##sequence-region P25558 1 1636
+P25558	UniProtKB	Chain	1	1636	.	.	.	ID=PRO_0000065016;Note=Bud site selection protein 3	
+P25558	UniProtKB	Modified residue	766	766	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25558	UniProtKB	Modified residue	1045	1045	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25558	UniProtKB	Modified residue	1063	1063	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25558	UniProtKB	Modified residue	1075	1075	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25558	UniProtKB	Modified residue	1134	1134	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25558	UniProtKB	Modified residue	1149	1149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25558	UniProtKB	Modified residue	1157	1157	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25558	UniProtKB	Modified residue	1160	1160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25558	UniProtKB	Modified residue	1228	1228	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25558	UniProtKB	Modified residue	1254	1254	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25558	UniProtKB	Modified residue	1257	1257	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25558	UniProtKB	Modified residue	1390	1390	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25558	UniProtKB	Modified residue	1412	1412	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25558	UniProtKB	Modified residue	1429	1429	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25558	UniProtKB	Modified residue	1440	1440	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25558	UniProtKB	Modified residue	1443	1443	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25558	UniProtKB	Modified residue	1501	1501	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25558	UniProtKB	Modified residue	1549	1549	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25558	UniProtKB	Modified residue	1589	1589	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25558	UniProtKB	Modified residue	1614	1614	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25558	UniProtKB	Cross-link	792	792	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25558	UniProtKB	Cross-link	963	963	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q12191 1 341
+Q12191	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12191	UniProtKB	Chain	2	341	.	.	.	ID=PRO_0000270973;Note=Binder of USO1 and GRH1 protein 1	
+Q12191	UniProtKB	Coiled coil	2	41	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12191	UniProtKB	Coiled coil	188	272	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12191	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12191	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12191	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12191	UniProtKB	Modified residue	292	292	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q03758 1 920
+Q03758	UniProtKB	Chain	1	920	.	.	.	ID=PRO_0000203241;Note=Ubiquitin ligase-binding protein BUL2	
+Q03758	UniProtKB	Motif	129	133	.	.	.	Note=PY-motif	
+Q03758	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03758	UniProtKB	Modified residue	557	557	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P12962 1 161
+P12962	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000084163;Note=Cap-associated protein CAF20	
+P12962	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12962	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P12962	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12962	UniProtKB	Modified residue	101	101	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12962	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P12962	UniProtKB	Modified residue	154	154	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P12962	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Reduces interaction with eIF4E/TIF45. Prevents pseudohyphal growth. Further reduces interaction with eIF4E/TIF45%3B when associated with A-9. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17083129;Dbxref=PMID:17083129	
+P12962	UniProtKB	Mutagenesis	9	9	.	.	.	Note=Further reduces interaction with eIF4E/TIF45%3B when associated with A-4. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17083129;Dbxref=PMID:17083129	
+##sequence-region P03965 1 1118
+P03965	UniProtKB	Chain	1	1118	.	.	.	ID=PRO_0000145091;Note=Carbamoyl-phosphate synthase arginine-specific large chain	
+P03965	UniProtKB	Domain	154	346	.	.	.	Note=ATP-grasp 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P03965	UniProtKB	Domain	698	890	.	.	.	Note=ATP-grasp 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P03965	UniProtKB	Nucleotide binding	174	229	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P03965	UniProtKB	Nucleotide binding	321	371	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P03965	UniProtKB	Metal binding	303	303	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P03965	UniProtKB	Metal binding	317	317	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P03965	UniProtKB	Metal binding	317	317	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P03965	UniProtKB	Metal binding	319	319	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P03965	UniProtKB	Metal binding	848	848	.	.	.	Note=Manganese 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P03965	UniProtKB	Metal binding	861	861	.	.	.	Note=Manganese 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38278 1 337
+P38278	UniProtKB	Chain	1	337	.	.	.	ID=PRO_0000202494;Note=25S rRNA (adenine(2142)-N(1))-methyltransferase	
+P38278	UniProtKB	Mutagenesis	180	180	.	.	.	Note=Abolishes methyltransferase activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23558746;Dbxref=PMID:23558746	
+P38278	UniProtKB	Sequence conflict	312	312	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38278	UniProtKB	Sequence conflict	312	312	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12291 1 365
+Q12291	UniProtKB	Chain	1	365	.	.	.	ID=PRO_0000247230;Note=25S rRNA (uridine(2843)-N(3))-methyltransferase	
+Q12291	UniProtKB	Mutagenesis	294	294	.	.	.	Note=Abolishes methyltransferase activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24335083;Dbxref=PMID:24335083	
+##sequence-region P53890 1 448
+P53890	UniProtKB	Chain	1	448	.	.	.	ID=PRO_0000203411;Note=Bud neck protein 5	
+P53890	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53890	UniProtKB	Modified residue	179	179	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P53890	UniProtKB	Modified residue	194	194	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53890	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53890	UniProtKB	Modified residue	270	270	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53890	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53890	UniProtKB	Modified residue	274	274	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53890	UniProtKB	Modified residue	332	332	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53890	UniProtKB	Modified residue	340	340	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53890	UniProtKB	Modified residue	344	344	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53890	UniProtKB	Modified residue	346	346	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53890	UniProtKB	Modified residue	350	350	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P39969 1 1040
+P39969	UniProtKB	Chain	1	1040	.	.	.	ID=PRO_0000064970;Note=Protein BOI2	
+P39969	UniProtKB	Domain	43	107	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P39969	UniProtKB	Domain	266	330	.	.	.	Note=SAM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00184	
+P39969	UniProtKB	Domain	768	887	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P39969	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39969	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39969	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P39969	UniProtKB	Modified residue	450	450	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P39969	UniProtKB	Modified residue	519	519	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P39969	UniProtKB	Modified residue	523	523	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P39969	UniProtKB	Modified residue	546	546	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39969	UniProtKB	Modified residue	652	652	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P39969	UniProtKB	Sequence conflict	733	733	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43132 1 505
+P43132	UniProtKB	Chain	1	505	.	.	.	ID=PRO_0000064987;Note=COMPASS component BRE2	
+P43132	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43132	UniProtKB	Helix	483	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RT4	
+##sequence-region P53841 1 131
+P53841	UniProtKB	Chain	1	131	.	.	.	ID=PRO_0000064994;Note=Bypass of stop codon protein 4	
+P53841	UniProtKB	Natural variant	3	3	.	.	.	Note=In strain: XH1549. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065	
+P53841	UniProtKB	Natural variant	6	6	.	.	.	Note=In strain: AS2.101%2C AS2.1406%2C AS2.179%2C AS2.7%2C AS2.724%2C AS2.771%2C AS2.820 and AS2.93. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065	
+P53841	UniProtKB	Natural variant	9	10	.	.	.	Note=In strain: XH1549. NK->T	
+P53841	UniProtKB	Natural variant	16	16	.	.	.	Note=In strain: XH1549. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065	
+P53841	UniProtKB	Natural variant	19	19	.	.	.	Note=In strain: XH1549. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065	
+P53841	UniProtKB	Natural variant	22	22	.	.	.	Note=In strain: XH1549. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065	
+P53841	UniProtKB	Natural variant	32	32	.	.	.	Note=In strain: XH1549. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065	
+P53841	UniProtKB	Natural variant	42	42	.	.	.	Note=In strain: AS2.101%2C AS2.1406%2C AS2.179%2C AS2.7%2C AS2.724%2C AS2.771%2C AS2.820%2C AS2.93 and XH1549. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065	
+P53841	UniProtKB	Natural variant	92	92	.	.	.	Note=In strain: AS2.724 and AS2.820. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065	
+##sequence-region P38356 1 321
+P38356	UniProtKB	Chain	1	321	.	.	.	ID=PRO_0000064996;Note=Metal homeostatis protein BSD2	
+P38356	UniProtKB	Topological domain	1	178	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38356	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38356	UniProtKB	Topological domain	200	211	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38356	UniProtKB	Transmembrane	212	232	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38356	UniProtKB	Topological domain	233	280	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38356	UniProtKB	Transmembrane	281	301	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38356	UniProtKB	Topological domain	302	321	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38356	UniProtKB	Cross-link	312	312	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38356	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Reverses the aerobic defects of yeast strains lacking superoxide dismutase (SOD). Associated with elevated copper ion accumulation and increased sensitivity to the toxic effects of copper and cadmium. Exhibits no additional sensitivity to manganese. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7935419;Dbxref=PMID:7935419	
+##sequence-region O94143 1 102
+O94143	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000299770;Note=Putative uncharacterized protein BUD19	
+##sequence-region Q08004 1 166
+Q08004	UniProtKB	Chain	1	166	.	.	.	ID=PRO_0000046803;Note=Bud site selection protein 20	
+Q08004	UniProtKB	Zinc finger	49	73	.	.	.	Note=C2H2-type	
+##sequence-region Q03783 1 95
+Q03783	UniProtKB	Chain	1	95	.	.	.	ID=PRO_0000299771;Note=Putative uncharacterized protein BUD26	
+Q03783	UniProtKB	Transmembrane	21	43	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03783	UniProtKB	Transmembrane	68	87	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43573 1 796
+P43573	UniProtKB	Chain	1	796	.	.	.	ID=PRO_0000153693;Note=Bud site selection protein 27	
+P43573	UniProtKB	Coiled coil	81	121	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43573	UniProtKB	Modified residue	580	580	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P53323 1 261
+P53323	UniProtKB	Chain	1	261	.	.	.	ID=PRO_0000088189;Note=EKC/KEOPS complex subunit BUD32	
+P53323	UniProtKB	Domain	16	261	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53323	UniProtKB	Nucleotide binding	22	30	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53323	UniProtKB	Active site	161	161	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028	
+P53323	UniProtKB	Binding site	43	43	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53323	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12023889;Dbxref=PMID:12023889	
+P53323	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12023889;Dbxref=PMID:12023889	
+P53323	UniProtKB	Mutagenesis	187	187	.	.	.	Note=Reduced kinase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12023889;Dbxref=PMID:12023889	
+P53323	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Reduced kinase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12023889;Dbxref=PMID:12023889	
+P53323	UniProtKB	Helix	5	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Beta strand	20	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Beta strand	29	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Beta strand	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Beta strand	49	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Helix	73	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Beta strand	94	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Turn	99	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Beta strand	103	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Beta strand	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWA	
+P53323	UniProtKB	Helix	122	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Helix	136	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Beta strand	166	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Beta strand	175	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Helix	192	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Helix	214	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+P53323	UniProtKB	Helix	233	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+##sequence-region P41698 1 603
+P41698	UniProtKB	Chain	1	603	.	.	.	ID=PRO_0000065020;Note=Bud site selection protein 8	
+P41698	UniProtKB	Topological domain	1	515	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Transmembrane	516	536	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Topological domain	537	577	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Transmembrane	578	598	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Topological domain	599	603	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Compositional bias	84	95	.	.	.	Note=Poly-Ser	
+P41698	UniProtKB	Glycosylation	92	92	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Glycosylation	110	110	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Glycosylation	211	211	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Glycosylation	240	240	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Glycosylation	271	271	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Glycosylation	333	333	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Glycosylation	396	396	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Glycosylation	423	423	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41698	UniProtKB	Sequence conflict	140	140	.	.	.	Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41698	UniProtKB	Sequence conflict	145	145	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41698	UniProtKB	Sequence conflict	221	221	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41698	UniProtKB	Sequence conflict	350	350	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41698	UniProtKB	Sequence conflict	354	354	.	.	.	Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41698	UniProtKB	Sequence conflict	422	422	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41698	UniProtKB	Sequence conflict	602	602	.	.	.	Note=R->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53226 1 547
+P53226	UniProtKB	Chain	1	547	.	.	.	ID=PRO_0000065021;Note=Bud site selection protein 9	
+P53226	UniProtKB	Topological domain	1	460	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Transmembrane	461	481	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Topological domain	482	521	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Transmembrane	522	542	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Topological domain	543	547	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Modified residue	112	112	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53226	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53226	UniProtKB	Glycosylation	83	83	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Glycosylation	139	139	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Glycosylation	142	142	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Glycosylation	221	221	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Glycosylation	259	259	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Glycosylation	263	263	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Glycosylation	289	289	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Glycosylation	299	299	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Glycosylation	340	340	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53226	UniProtKB	Sequence conflict	16	16	.	.	.	Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53226	UniProtKB	Sequence conflict	27	27	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53226	UniProtKB	Sequence conflict	132	132	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53226	UniProtKB	Sequence conflict	249	249	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53226	UniProtKB	Sequence conflict	260	260	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53226	UniProtKB	Sequence conflict	298	298	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53226	UniProtKB	Sequence conflict	321	321	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53226	UniProtKB	Sequence conflict	345	345	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53226	UniProtKB	Sequence conflict	406	406	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53226	UniProtKB	Sequence conflict	451	451	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53226	UniProtKB	Sequence conflict	480	480	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53226	UniProtKB	Sequence conflict	545	545	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P48524 1 976
+P48524	UniProtKB	Chain	1	976	.	.	.	ID=PRO_0000065022;Note=Ubiquitin ligase-binding protein BUL1	
+P48524	UniProtKB	Motif	156	160	.	.	.	Note=PY-motif	
+P48524	UniProtKB	Compositional bias	631	640	.	.	.	Note=Poly-Ser	
+P48524	UniProtKB	Compositional bias	868	876	.	.	.	Note=Poly-Ser	
+P48524	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P48524	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P48524	UniProtKB	Mutagenesis	157	157	.	.	.	Note=Abolishes interaction with RSP5 and reduces HSE-mediated gene expression%3B when associated with A-158. P->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12821147,ECO:0000269|PubMed:9931424;Dbxref=PMID:12821147,PMID:9931424	
+P48524	UniProtKB	Mutagenesis	158	158	.	.	.	Note=Abolishes interaction with RSP5 and reduces HSE-mediated gene expression%3B when associated with Q-157. P->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12821147,ECO:0000269|PubMed:9931424;Dbxref=PMID:12821147,PMID:9931424	
+P48524	UniProtKB	Sequence conflict	35	35	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48524	UniProtKB	Sequence conflict	773	775	.	.	.	Note=YDD->ISN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48524	UniProtKB	Sequence conflict	963	963	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07245 1 946
+P07245	UniProtKB	Chain	1	946	.	.	.	ID=PRO_0000199326;Note=C-1-tetrahydrofolate synthase%2C cytoplasmic	
+P07245	UniProtKB	Nucleotide binding	169	171	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07245	UniProtKB	Nucleotide binding	384	391	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07245	UniProtKB	Region	1	319	.	.	.	Note=Methylenetetrahydrofolate dehydrogenase and cyclohydrolase	
+P07245	UniProtKB	Region	51	55	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07245	UniProtKB	Region	98	100	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07245	UniProtKB	Region	277	281	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07245	UniProtKB	Region	320	946	.	.	.	Note=Formyltetrahydrofolate synthetase	
+P07245	UniProtKB	Binding site	194	194	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07245	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P07245	UniProtKB	Modified residue	318	318	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07245	UniProtKB	Modified residue	322	322	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07245	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Almost no effect on activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2541774;Dbxref=PMID:2541774	
+P07245	UniProtKB	Mutagenesis	144	144	.	.	.	Note=Cyclohydrolase activity is reduced 20-fold. Dehydrogenase Km is increased 7-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2541774;Dbxref=PMID:2541774	
+P07245	UniProtKB	Mutagenesis	257	257	.	.	.	Note=Cyclohydrolase activity is increased 2-fold. Dehydrogenase Km is increased 2-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2541774;Dbxref=PMID:2541774	
+##sequence-region P36076 1 571
+P36076	UniProtKB	Chain	1	571	.	.	.	ID=PRO_0000182039;Note=Coenzyme A biosynthesis protein 3	
+P36076	UniProtKB	Compositional bias	508	570	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P36076	UniProtKB	Modified residue	42	42	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956	
+P36076	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36076	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36076	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P36076	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36076	UniProtKB	Mutagenesis	478	478	.	.	.	Note=Abolishes PPCDC activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19915539;Dbxref=PMID:19915539	
+##sequence-region Q03941 1 241
+Q03941	UniProtKB	Chain	1	241	.	.	.	ID=PRO_0000173043;Note=Dephospho-CoA kinase CAB5	
+Q03941	UniProtKB	Domain	3	211	.	.	.	Note=DPCK	
+Q03941	UniProtKB	Nucleotide binding	8	15	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P13517 1 287
+P13517	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P13517	UniProtKB	Chain	2	287	.	.	.	ID=PRO_0000204642;Note=F-actin-capping protein subunit beta	
+P13517	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P13517	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P13517	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13517	UniProtKB	Sequence conflict	140	140	.	.	.	Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13517	UniProtKB	Sequence conflict	146	147	.	.	.	Note=FK->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07258 1 411
+P07258	UniProtKB	Chain	1	411	.	.	.	ID=PRO_0000112372;Note=Carbamoyl-phosphate synthase arginine-specific small chain	
+P07258	UniProtKB	Domain	185	376	.	.	.	Note=Glutamine amidotransferase type-1	
+P07258	UniProtKB	Active site	264	264	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07258	UniProtKB	Active site	349	349	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07258	UniProtKB	Active site	351	351	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38995 1 1004
+P38995	UniProtKB	Chain	1	1004	.	.	.	ID=PRO_0000046318;Note=Copper-transporting ATPase	
+P38995	UniProtKB	Topological domain	1	262	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Transmembrane	263	283	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Topological domain	284	303	.	.	.	Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Transmembrane	304	324	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Topological domain	325	335	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Transmembrane	336	356	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Topological domain	357	370	.	.	.	Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Transmembrane	371	391	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Topological domain	392	528	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Transmembrane	529	549	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Topological domain	550	577	.	.	.	Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Transmembrane	578	598	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Topological domain	599	901	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Transmembrane	902	924	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Topological domain	925	927	.	.	.	Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Transmembrane	928	950	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Topological domain	951	1004	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38995	UniProtKB	Domain	3	68	.	.	.	Note=HMA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38995	UniProtKB	Domain	81	147	.	.	.	Note=HMA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38995	UniProtKB	Active site	627	627	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38995	UniProtKB	Metal binding	13	13	.	.	.	Note=Copper	
+P38995	UniProtKB	Metal binding	16	16	.	.	.	Note=Copper	
+P38995	UniProtKB	Metal binding	91	91	.	.	.	Note=Copper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38995	UniProtKB	Metal binding	94	94	.	.	.	Note=Copper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38995	UniProtKB	Metal binding	838	838	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38995	UniProtKB	Metal binding	842	842	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P38995	UniProtKB	Beta strand	2	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ	
+P38995	UniProtKB	Helix	14	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ	
+P38995	UniProtKB	Beta strand	27	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ	
+P38995	UniProtKB	Turn	37	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ	
+P38995	UniProtKB	Beta strand	41	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ	
+P38995	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVS	
+P38995	UniProtKB	Helix	52	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ	
+P38995	UniProtKB	Beta strand	66	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ	
+##sequence-region Q02948 1 557
+Q02948	UniProtKB	Chain	1	557	.	.	.	ID=PRO_0000218559;Note=Vacuolar protein sorting-associated protein 30	
+Q02948	UniProtKB	Region	320	539	.	.	.	Note=BARA	
+Q02948	UniProtKB	Region	515	540	.	.	.	Note=Required for membrane-association%2C autophagic function during starvation and normal autophagosome morphology;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23878393;Dbxref=PMID:23878393	
+Q02948	UniProtKB	Coiled coil	189	322	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02948	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q02948	UniProtKB	Turn	322	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+Q02948	UniProtKB	Beta strand	329	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+Q02948	UniProtKB	Beta strand	335	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+Q02948	UniProtKB	Beta strand	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+Q02948	UniProtKB	Helix	353	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+Q02948	UniProtKB	Beta strand	379	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+Q02948	UniProtKB	Helix	387	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+Q02948	UniProtKB	Beta strand	391	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+Q02948	UniProtKB	Beta strand	413	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+Q02948	UniProtKB	Helix	435	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+Q02948	UniProtKB	Beta strand	502	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+Q02948	UniProtKB	Helix	513	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7	
+##sequence-region P38934 1 470
+P38934	UniProtKB	Chain	1	470	.	.	.	ID=PRO_0000064919;Note=Nuclear segregation protein BFR1	
+P38934	UniProtKB	Coiled coil	17	178	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38934	UniProtKB	Coiled coil	237	281	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38934	UniProtKB	Coiled coil	398	469	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38934	UniProtKB	Modified residue	260	260	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38934	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P38934	UniProtKB	Modified residue	369	369	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q06333 1 122
+Q06333	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000253844;Note=Biogenesis of lysosome-related organelles complex 1 subunit CNL1	
+Q06333	UniProtKB	Coiled coil	63	95	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04199 1 468
+Q04199	UniProtKB	Chain	1	468	.	.	.	ID=PRO_0000050894;Note=Chromatin assembly factor 1 subunit p60	
+Q04199	UniProtKB	Repeat	11	52	.	.	.	Note=WD 1	
+Q04199	UniProtKB	Repeat	69	108	.	.	.	Note=WD 2	
+Q04199	UniProtKB	Repeat	143	182	.	.	.	Note=WD 3	
+Q04199	UniProtKB	Repeat	185	224	.	.	.	Note=WD 4	
+Q04199	UniProtKB	Repeat	371	413	.	.	.	Note=WD 5	
+##sequence-region Q06150 1 570
+Q06150	UniProtKB	Chain	1	570	.	.	.	ID=PRO_0000247176;Note=Protein BOP2	
+Q06150	UniProtKB	Modified residue	383	383	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P53741 1 515
+P53741	UniProtKB	Chain	1	515	.	.	.	ID=PRO_0000194803;Note=UBP3-associated protein BRE5	
+P53741	UniProtKB	Domain	8	140	.	.	.	Note=NTF2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00137	
+P53741	UniProtKB	Domain	418	494	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P53741	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53741	UniProtKB	Modified residue	282	282	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53741	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53741	UniProtKB	Modified residue	340	340	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53741	UniProtKB	Modified residue	398	398	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53741	UniProtKB	Helix	5	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+P53741	UniProtKB	Helix	24	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+P53741	UniProtKB	Beta strand	31	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+P53741	UniProtKB	Beta strand	56	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+P53741	UniProtKB	Helix	62	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+P53741	UniProtKB	Helix	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+P53741	UniProtKB	Beta strand	79	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+P53741	UniProtKB	Helix	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+P53741	UniProtKB	Beta strand	97	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+P53741	UniProtKB	Beta strand	114	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+P53741	UniProtKB	Beta strand	131	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY	
+##sequence-region P43571 1 1029
+P43571	UniProtKB	Chain	1	1029	.	.	.	ID=PRO_0000202676;Note=GPI inositol-deacylase	
+P43571	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Transmembrane	708	728	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Transmembrane	749	769	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Transmembrane	804	824	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Transmembrane	872	892	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Transmembrane	920	940	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Transmembrane	957	977	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Transmembrane	985	1005	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Transmembrane	1008	1028	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Active site	236	236	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43571	UniProtKB	Glycosylation	19	19	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Glycosylation	295	295	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Glycosylation	302	302	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Glycosylation	447	447	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Glycosylation	456	456	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Glycosylation	485	485	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Glycosylation	565	565	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Glycosylation	651	651	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Glycosylation	668	668	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Glycosylation	694	694	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43571	UniProtKB	Glycosylation	918	918	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36130 1 643
+P36130	UniProtKB	Chain	1	643	.	.	.	ID=PRO_0000051478;Note=CCR4-associated factor 4	
+P36130	UniProtKB	Repeat	317	357	.	.	.	Note=WD 1	
+P36130	UniProtKB	Repeat	360	400	.	.	.	Note=WD 2	
+P36130	UniProtKB	Repeat	422	461	.	.	.	Note=WD 3	
+P36130	UniProtKB	Repeat	479	526	.	.	.	Note=WD 4	
+P36130	UniProtKB	Repeat	527	566	.	.	.	Note=WD 5	
+P36130	UniProtKB	Repeat	568	603	.	.	.	Note=WD 6	
+P36130	UniProtKB	Repeat	614	643	.	.	.	Note=WD 7	
+P36130	UniProtKB	Region	1	274	.	.	.	Note=Required for interaction with FIS1 and MDV1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16009724;Dbxref=PMID:16009724	
+P36130	UniProtKB	Region	74	126	.	.	.	Note=Sufficient for interaction with FIS1	
+P36130	UniProtKB	Coiled coil	160	255	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36130	UniProtKB	Mutagenesis	85	86	.	.	.	Note=Abolishes interaction with FIS1. FR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17998537;Dbxref=PMID:17998537	
+P36130	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Abolishes interaction with FIS1. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17998537;Dbxref=PMID:17998537	
+P36130	UniProtKB	Mutagenesis	110	110	.	.	.	Note=Abolishes interaction with FIS1. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17998537;Dbxref=PMID:17998537	
+P36130	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Abolishes interaction with FIS1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17998537;Dbxref=PMID:17998537	
+P36130	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Abolishes interaction with FIS1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17998537;Dbxref=PMID:17998537	
+P36130	UniProtKB	Sequence conflict	94	95	.	.	.	Note=QR->HG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36130	UniProtKB	Helix	83	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PQR	
+P36130	UniProtKB	Turn	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PQR	
+P36130	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PQR	
+P36130	UniProtKB	Helix	110	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PQR	
+##sequence-region P41832 1 1953
+P41832	UniProtKB	Chain	1	1953	.	.	.	ID=PRO_0000194899;Note=Protein BNI1	
+P41832	UniProtKB	Domain	174	696	.	.	.	Note=GBD/FH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00579	
+P41832	UniProtKB	Domain	1053	1337	.	.	.	Note=FH1	
+P41832	UniProtKB	Domain	1348	1766	.	.	.	Note=FH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00774	
+P41832	UniProtKB	Domain	1792	1826	.	.	.	Note=DAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00577	
+P41832	UniProtKB	Coiled coil	712	807	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41832	UniProtKB	Coiled coil	864	894	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41832	UniProtKB	Coiled coil	928	981	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41832	UniProtKB	Coiled coil	1732	1811	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41832	UniProtKB	Compositional bias	64	67	.	.	.	Note=Poly-Ser	
+P41832	UniProtKB	Compositional bias	1053	1057	.	.	.	Note=Poly-Ser	
+P41832	UniProtKB	Compositional bias	1239	1250	.	.	.	Note=Poly-Pro	
+P41832	UniProtKB	Compositional bias	1278	1291	.	.	.	Note=Poly-Pro	
+P41832	UniProtKB	Compositional bias	1303	1309	.	.	.	Note=Poly-Pro	
+P41832	UniProtKB	Compositional bias	1751	1754	.	.	.	Note=Poly-Glu	
+P41832	UniProtKB	Modified residue	311	311	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P41832	UniProtKB	Modified residue	325	325	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41832	UniProtKB	Modified residue	1085	1085	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41832	UniProtKB	Modified residue	1170	1170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P41832	UniProtKB	Modified residue	1338	1338	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P41832	UniProtKB	Modified residue	1344	1344	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P41832	UniProtKB	Modified residue	1918	1918	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41832	UniProtKB	Sequence conflict	938	938	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41832	UniProtKB	Sequence conflict	938	938	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41832	UniProtKB	Sequence conflict	938	938	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41832	UniProtKB	Sequence conflict	1430	1430	.	.	.	Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41832	UniProtKB	Beta strand	1371	1373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1378	1388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1391	1398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Beta strand	1400	1402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1405	1413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Turn	1414	1416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1423	1432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1434	1436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1441	1449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Turn	1450	1452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1453	1456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1459	1464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1468	1471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1475	1480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1482	1484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1494	1496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1504	1506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y64	
+P41832	UniProtKB	Helix	1509	1516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Turn	1517	1524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1525	1535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1538	1560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1563	1579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1582	1584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1591	1596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Beta strand	1597	1599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Beta strand	1603	1608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX4	
+P41832	UniProtKB	Helix	1609	1620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1622	1626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1627	1630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1632	1637	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Helix	1642	1665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Turn	1667	1669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Turn	1671	1673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y64	
+P41832	UniProtKB	Helix	1680	1715	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+P41832	UniProtKB	Beta strand	1720	1722	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y64	
+P41832	UniProtKB	Helix	1723	1757	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5	
+##sequence-region P50084 1 137
+P50084	UniProtKB	Chain	1	137	.	.	.	ID=PRO_0000202851;Note=Protein BNS1	
+##sequence-region P53838 1 576
+P53838	UniProtKB	Chain	1	576	.	.	.	ID=PRO_0000079243;Note=Boron transporter 1	
+P53838	UniProtKB	Topological domain	1	84	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	106	116	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	117	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	135	140	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	141	160	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	161	165	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	166	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	187	192	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	193	213	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	214	235	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	236	256	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	257	274	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	275	295	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	296	329	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	330	350	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	351	373	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	374	394	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	395	438	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	439	459	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	460	495	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	496	516	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	517	518	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Transmembrane	519	539	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53838	UniProtKB	Topological domain	540	576	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25385 1 244
+P25385	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000207557;Note=Protein transport protein BOS1	
+P25385	UniProtKB	Topological domain	1	222	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25385	UniProtKB	Transmembrane	223	240	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25385	UniProtKB	Topological domain	241	244	.	.	.	Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25385	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P14772 1 1559
+P14772	UniProtKB	Chain	1	1559	.	.	.	ID=PRO_0000093448;Note=Bile pigment transporter 1	
+P14772	UniProtKB	Topological domain	1	29	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	30	50	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	51	84	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	106	110	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	111	127	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	128	139	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	161	178	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	200	283	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	284	304	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	305	333	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	334	354	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	355	410	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	411	431	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	432	434	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	435	455	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	456	518	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	519	539	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	540	560	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	561	581	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	582	972	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	973	993	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	994	1030	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	1031	1052	.	.	.	Note=Helical%3B Name%3D13;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	1053	1095	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	1096	1116	.	.	.	Note=Helical%3B Name%3D14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	1117	1117	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	1118	1138	.	.	.	Note=Helical%3B Name%3D15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	1139	1209	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	1210	1230	.	.	.	Note=Helical%3B Name%3D16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	1231	1235	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Transmembrane	1236	1256	.	.	.	Note=Helical%3B Name%3D17;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Topological domain	1257	1559	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14772	UniProtKB	Domain	292	578	.	.	.	Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Domain	639	871	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P14772	UniProtKB	Domain	980	1265	.	.	.	Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P14772	UniProtKB	Domain	1302	1553	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P14772	UniProtKB	Nucleotide binding	672	679	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P14772	UniProtKB	Nucleotide binding	1336	1343	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P14772	UniProtKB	Modified residue	645	645	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P14772	UniProtKB	Modified residue	885	885	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14772	UniProtKB	Modified residue	889	889	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14772	UniProtKB	Modified residue	893	893	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14772	UniProtKB	Modified residue	895	895	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14772	UniProtKB	Modified residue	916	916	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14772	UniProtKB	Modified residue	927	927	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P14772	UniProtKB	Modified residue	931	931	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P14772	UniProtKB	Modified residue	934	934	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P14772	UniProtKB	Glycosylation	1011	1011	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38770 1 471
+P38770	UniProtKB	Chain	1	471	.	.	.	ID=PRO_0000202892;Note=Nucleus export protein BRL1	
+P38770	UniProtKB	Topological domain	1	299	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38770	UniProtKB	Transmembrane	300	320	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38770	UniProtKB	Topological domain	321	407	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38770	UniProtKB	Transmembrane	408	428	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38770	UniProtKB	Topological domain	429	471	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53194 1 125
+P53194	UniProtKB	Chain	1	125	.	.	.	ID=PRO_0000202777;Note=Uncharacterized protein BRP1	
+##sequence-region P53286 1 410
+P53286	UniProtKB	Chain	1	410	.	.	.	ID=PRO_0000065007;Note=Protein BTN2	
+P53286	UniProtKB	Coiled coil	243	330	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53286	UniProtKB	Compositional bias	215	301	.	.	.	Note=Glu-rich	
+##sequence-region P53727 1 317
+P53727	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000213349;Note=Putative pyridoxal kinase BUD17	
+P53727	UniProtKB	Nucleotide binding	190	191	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53727	UniProtKB	Nucleotide binding	220	232	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53727	UniProtKB	Binding site	16	16	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53727	UniProtKB	Binding site	128	128	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53727	UniProtKB	Binding site	233	233	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53727	UniProtKB	Sequence conflict	93	93	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25337 1 157
+P25337	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000193902;Note=Pre-mRNA-splicing factor BUD31	
+P25337	UniProtKB	Motif	2	11	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25337	UniProtKB	Helix	16	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P25337	UniProtKB	Helix	42	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P25337	UniProtKB	Helix	75	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P25337	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MY1	
+P25337	UniProtKB	Helix	89	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P25337	UniProtKB	Turn	99	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P25337	UniProtKB	Turn	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P25337	UniProtKB	Beta strand	114	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P25337	UniProtKB	Helix	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P25337	UniProtKB	Helix	126	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P25337	UniProtKB	Turn	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P25300 1 642
+P25300	UniProtKB	Chain	1	642	.	.	.	ID=PRO_0000068859;Note=Bud site selection protein 5	
+P25300	UniProtKB	Domain	224	339	.	.	.	Note=N-terminal Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00135	
+P25300	UniProtKB	Domain	412	640	.	.	.	Note=Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00168	
+P25300	UniProtKB	Sequence conflict	110	110	.	.	.	Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25300	UniProtKB	Sequence conflict	111	111	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25300	UniProtKB	Sequence conflict	225	225	.	.	.	Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25300	UniProtKB	Sequence conflict	401	401	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25300	UniProtKB	Sequence conflict	401	401	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25300	UniProtKB	Sequence conflict	481	481	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25300	UniProtKB	Sequence conflict	481	481	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08754 1 746
+Q08754	UniProtKB	Chain	1	746	.	.	.	ID=PRO_0000065019;Note=Bud site selection protein 7	
+Q08754	UniProtKB	Region	733	746	.	.	.	Note=CHS5-binding	
+##sequence-region P23293 1 657
+P23293	UniProtKB	Chain	1	657	.	.	.	ID=PRO_0000085687;Note=Serine/threonine-protein kinase BUR1	
+P23293	UniProtKB	Domain	60	366	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23293	UniProtKB	Nucleotide binding	66	74	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23293	UniProtKB	Active site	195	195	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P23293	UniProtKB	Binding site	89	89	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23293	UniProtKB	Modified residue	240	240	.	.	.	Note=Phosphothreonine%3B by CAK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12215532;Dbxref=PMID:12215532	
+P23293	UniProtKB	Modified residue	400	400	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P23293	UniProtKB	Modified residue	405	405	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P23293	UniProtKB	Modified residue	417	417	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23293	UniProtKB	Modified residue	634	634	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P23293	UniProtKB	Mutagenesis	107	107	.	.	.	Note=Loss of kinase activity in vitro. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12972617;Dbxref=PMID:12972617	
+P23293	UniProtKB	Mutagenesis	213	213	.	.	.	Note=Loss of kinase activity in vitro. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12972617;Dbxref=PMID:12972617	
+P23293	UniProtKB	Mutagenesis	240	240	.	.	.	Note=No phosphorylation of SGV1. T->A%2CD%2CE;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12215532,ECO:0000269|PubMed:12972617;Dbxref=PMID:12215532,PMID:12972617	
+##sequence-region P36106 1 594
+P36106	UniProtKB	Chain	1	594	.	.	.	ID=PRO_0000203191;Note=Transcription factor BYE1	
+P36106	UniProtKB	Domain	254	365	.	.	.	Note=TFIIS central;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00651	
+P36106	UniProtKB	Zinc finger	72	134	.	.	.	Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+P36106	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36106	UniProtKB	Helix	234	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P36106	UniProtKB	Helix	254	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P36106	UniProtKB	Helix	272	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P36106	UniProtKB	Helix	285	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P36106	UniProtKB	Helix	302	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P36106	UniProtKB	Beta strand	317	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXX	
+P36106	UniProtKB	Helix	320	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P36106	UniProtKB	Helix	332	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P36106	UniProtKB	Helix	346	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P36106	UniProtKB	Turn	360	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+##sequence-region Q05791 1 360
+Q05791	UniProtKB	Chain	1	360	.	.	.	ID=PRO_0000227684;Note=Cell division cycle protein 123	
+Q05791	UniProtKB	Mutagenesis	274	274	.	.	.	Note=Reduces the interaction with DMA1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434	
+##sequence-region P32797 1 924
+P32797	UniProtKB	Chain	1	924	.	.	.	ID=PRO_0000089441;Note=Cell division control protein 13	
+P32797	UniProtKB	DNA binding	500	686	.	.	.	Note=OB	
+P32797	UniProtKB	Modified residue	306	306	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32797	UniProtKB	Modified residue	308	308	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32797	UniProtKB	Modified residue	333	333	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32797	UniProtKB	Mutagenesis	50	50	.	.	.	Note=Increase in length of X' and Y' telomeres. Disrupts interaction with POL1 but not FUN12. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792	
+P32797	UniProtKB	Mutagenesis	72	72	.	.	.	Note=Disrupts interaction with POL1 and FUN12. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792	
+P32797	UniProtKB	Mutagenesis	124	124	.	.	.	Note=Disrupts interaction with POL1 but not FUN12. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792	
+P32797	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Disrupts interaction with POL1 but not FUN12. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792	
+P32797	UniProtKB	Mutagenesis	228	228	.	.	.	Note=Disrupts interaction with POL1 but not FUN12. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792	
+P32797	UniProtKB	Mutagenesis	243	243	.	.	.	Note=Disrupts interaction with POL1 and FUN12. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792	
+P32797	UniProtKB	Mutagenesis	392	392	.	.	.	Note=Disrupts interaction with POL1 but not FUN12. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792	
+P32797	UniProtKB	Mutagenesis	523	523	.	.	.	Note=Increase in length of X' and Y' telomeres. Disrupts interaction with POL1 but not FUN12. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792	
+P32797	UniProtKB	Sequence conflict	40	40	.	.	.	Note=L->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32797	UniProtKB	Helix	21	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Beta strand	32	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Beta strand	48	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NWT	
+P32797	UniProtKB	Beta strand	70	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Helix	79	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Beta strand	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Beta strand	125	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Beta strand	138	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Helix	151	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Helix	178	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Beta strand	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Helix	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Helix	211	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P32797	UniProtKB	Helix	348	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Beta strand	359	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Helix	377	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Beta strand	381	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Beta strand	385	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Beta strand	394	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Turn	403	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Beta strand	406	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Helix	415	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Helix	424	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Helix	429	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Turn	437	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Beta strand	444	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Beta strand	463	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE	
+P32797	UniProtKB	Turn	510	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Beta strand	521	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Beta strand	531	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Beta strand	539	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Beta strand	565	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Turn	571	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Beta strand	575	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Helix	581	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Beta strand	595	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Helix	599	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Beta strand	617	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Beta strand	626	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Beta strand	631	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Beta strand	642	644	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Helix	645	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Helix	653	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Helix	670	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+P32797	UniProtKB	Helix	677	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL	
+##sequence-region P25656 1 391
+P25656	UniProtKB	Chain	1	391	.	.	.	ID=PRO_0000207670;Note=Cell division control protein 50	
+P25656	UniProtKB	Topological domain	1	44	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25656	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25656	UniProtKB	Topological domain	66	331	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25656	UniProtKB	Transmembrane	332	352	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25656	UniProtKB	Topological domain	353	391	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25656	UniProtKB	Glycosylation	199	199	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25656	UniProtKB	Glycosylation	216	216	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25656	UniProtKB	Glycosylation	237	237	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25656	UniProtKB	Glycosylation	288	288	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25656	UniProtKB	Glycosylation	329	329	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P09119 1 513
+P09119	UniProtKB	Chain	1	513	.	.	.	ID=PRO_0000150977;Note=Cell division control protein 6	
+P09119	UniProtKB	Nucleotide binding	108	115	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P09119	UniProtKB	Region	1	47	.	.	.	Note=Interaction with CDC4%3B required for degradation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9312054;Dbxref=PMID:9312054	
+P09119	UniProtKB	Motif	27	33	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8892760;Dbxref=PMID:8892760	
+P09119	UniProtKB	Modified residue	368	368	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P09119	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Impairs nuclear localization. K->R%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8892760;Dbxref=PMID:8892760	
+P09119	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Impairs ORC1-binding and leads to defective association with chromatin. K->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10075735,ECO:0000269|PubMed:9892652;Dbxref=PMID:10075735,PMID:9892652	
+P09119	UniProtKB	Sequence conflict	3	3	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09119	UniProtKB	Sequence conflict	202	202	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09119	UniProtKB	Sequence conflict	225	225	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09119	UniProtKB	Sequence conflict	272	272	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09119	UniProtKB	Sequence conflict	277	277	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09119	UniProtKB	Sequence conflict	339	339	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09119	UniProtKB	Sequence conflict	395	396	.	.	.	Note=SK->LQN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09119	UniProtKB	Sequence conflict	402	402	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09119	UniProtKB	Sequence conflict	410	410	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09119	UniProtKB	Sequence conflict	436	436	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53197 1 566
+P53197	UniProtKB	Chain	1	566	.	.	.	ID=PRO_0000050904;Note=APC/C activator protein CDH1	
+P53197	UniProtKB	Repeat	258	298	.	.	.	Note=WD 1	
+P53197	UniProtKB	Repeat	300	339	.	.	.	Note=WD 2	
+P53197	UniProtKB	Repeat	342	379	.	.	.	Note=WD 3	
+P53197	UniProtKB	Repeat	383	422	.	.	.	Note=WD 4	
+P53197	UniProtKB	Repeat	425	467	.	.	.	Note=WD 5	
+P53197	UniProtKB	Repeat	469	510	.	.	.	Note=WD 6	
+P53197	UniProtKB	Repeat	513	552	.	.	.	Note=WD 7	
+P53197	UniProtKB	Motif	55	61	.	.	.	Note=C-box	
+P53197	UniProtKB	Compositional bias	32	38	.	.	.	Note=Poly-Ser	
+P53197	UniProtKB	Modified residue	213	213	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53197	UniProtKB	Mutagenesis	12	12	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-16%3B A-42%3B A-157%3B A-169%3B A-173%3B A-176%3B A-227 and A-239. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566	
+P53197	UniProtKB	Mutagenesis	16	16	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-12%3B A-42%3B A-157%3B A-169%3B A-173%3B A-176%3B A-227 and A-239. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566	
+P53197	UniProtKB	Mutagenesis	42	42	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-157%3B A-169%3B A-173%3B A-176%3B A-227 and A-239. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566	
+P53197	UniProtKB	Mutagenesis	157	157	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-169%3B A-173%3B A-176%3B A-227 and A-239. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566	
+P53197	UniProtKB	Mutagenesis	169	169	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-157%3B A-173%3B A-176%3B A-227 and A-239. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566	
+P53197	UniProtKB	Mutagenesis	173	173	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-157%3B A-169%3B A-176%3B A-227 and A-239. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566	
+P53197	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-157%3B A-169%3B A-173%3B A-227 and A-239. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566	
+P53197	UniProtKB	Mutagenesis	227	227	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-157%3B A-169%3B A-173%3B A-176 and A-239. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566	
+P53197	UniProtKB	Mutagenesis	239	239	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-157%3B A-169%3B A-173%3B A-176 and A-227. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566	
+P53197	UniProtKB	Beta strand	252	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	269	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	275	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	284	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Turn	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	295	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	305	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	314	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	326	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Turn	331	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	335	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	347	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	356	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	366	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	373	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	378	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	388	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	395	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	399	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	409	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	420	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	430	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	437	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	442	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Turn	449	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	453	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Turn	459	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	463	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	474	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	481	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	486	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	497	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	502	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	507	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	518	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	527	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Turn	535	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+P53197	UniProtKB	Beta strand	538	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6	
+##sequence-region P47112 1 604
+P47112	UniProtKB	Chain	1	604	.	.	.	ID=PRO_0000203095;Note=Cell division cycle protein CDT1	
+P47112	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Turn	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Helix	26	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Beta strand	41	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Helix	51	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Turn	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Beta strand	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Beta strand	87	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Helix	109	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Beta strand	141	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5ME9	
+P47112	UniProtKB	Beta strand	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Beta strand	149	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Beta strand	194	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Beta strand	220	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Beta strand	227	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Helix	234	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Beta strand	249	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Helix	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5ME9	
+P47112	UniProtKB	Beta strand	258	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Helix	278	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Helix	291	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Helix	299	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC	
+P47112	UniProtKB	Beta strand	333	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Helix	340	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC	
+P47112	UniProtKB	Helix	357	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC	
+P47112	UniProtKB	Beta strand	370	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC	
+P47112	UniProtKB	Beta strand	381	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC	
+P47112	UniProtKB	Helix	391	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA	
+P47112	UniProtKB	Helix	399	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC	
+P47112	UniProtKB	Beta strand	417	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC	
+P47112	UniProtKB	Helix	495	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB	
+P47112	UniProtKB	Beta strand	525	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB	
+P47112	UniProtKB	Helix	531	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB	
+P47112	UniProtKB	Helix	551	564	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB	
+P47112	UniProtKB	Turn	566	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB	
+P47112	UniProtKB	Beta strand	569	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB	
+P47112	UniProtKB	Beta strand	580	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB	
+P47112	UniProtKB	Helix	588	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB	
+##sequence-region Q12453 1 761
+Q12453	UniProtKB	Chain	1	761	.	.	.	ID=PRO_0000237655;Note=Cytoplasmic export protein 1	
+Q12453	UniProtKB	Repeat	385	423	.	.	.	Note=HEAT 1	
+Q12453	UniProtKB	Repeat	498	534	.	.	.	Note=HEAT 2	
+Q12453	UniProtKB	Modified residue	754	754	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12453	UniProtKB	Turn	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Beta strand	16	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Beta strand	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Beta strand	28	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Turn	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Beta strand	43	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Turn	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	56	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Beta strand	77	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Beta strand	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	110	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Turn	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Beta strand	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Beta strand	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	164	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Turn	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	190	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Turn	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	213	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	226	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	237	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	243	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	253	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	259	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	277	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	287	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	292	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	325	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	346	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	359	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	378	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	386	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	392	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	398	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	412	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	417	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	423	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	437	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	451	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Beta strand	454	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	458	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	478	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	492	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	497	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	504	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	509	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+Q12453	UniProtKB	Helix	517	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA	
+##sequence-region Q06632 1 1357
+Q06632	UniProtKB	Chain	1	1357	.	.	.	ID=PRO_0000076203;Note=Protein CFT1	
+##sequence-region P13365 1 580
+P13365	UniProtKB	Chain	1	580	.	.	.	ID=PRO_0000080413;Note=G1/S-specific cyclin CLN3	
+P13365	UniProtKB	Sequence conflict	23	23	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53188 1 120
+P53188	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000202773;Note=rRNA-processing protein CGR1	
+P53188	UniProtKB	Coiled coil	47	106	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P07267 1 405
+P07267	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8840499;Dbxref=PMID:8840499	
+P07267	UniProtKB	Propeptide	23	76	.	.	.	ID=PRO_0000025873;Note=Activation peptide;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6	
+P07267	UniProtKB	Chain	77	405	.	.	.	ID=PRO_0000025874;Note=Saccharopepsin	
+P07267	UniProtKB	Domain	91	402	.	.	.	Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
+P07267	UniProtKB	Active site	109	109	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P07267	UniProtKB	Active site	294	294	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P07267	UniProtKB	Glycosylation	144	144	.	.	.	Note=N-linked (GlcNAc...) asparagine	
+P07267	UniProtKB	Glycosylation	345	345	.	.	.	Note=N-linked (GlcNAc...) asparagine	
+P07267	UniProtKB	Disulfide bond	122	127	.	.	.	.	
+P07267	UniProtKB	Disulfide bond	328	361	.	.	.	.	
+P07267	UniProtKB	Mutagenesis	294	294	.	.	.	Note=Inactivation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1959673;Dbxref=PMID:1959673	
+P07267	UniProtKB	Beta strand	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	90	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Turn	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	102	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	115	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Helix	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Helix	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	142	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	155	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	171	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Helix	186	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	195	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Helix	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Helix	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Helix	213	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	224	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Helix	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	240	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Helix	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	255	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Turn	267	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	271	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	282	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	290	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Helix	304	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	317	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FQ8	
+P07267	UniProtKB	Beta strand	322	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Helix	328	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	337	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	344	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Turn	350	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	353	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	360	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Turn	372	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	376	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Helix	382	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	388	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Turn	394	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+P07267	UniProtKB	Beta strand	398	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+##sequence-region P39113 1 1433
+P39113	UniProtKB	Chain	1	1433	.	.	.	ID=PRO_0000114940;Note=Regulatory protein CAT8	
+P39113	UniProtKB	DNA binding	70	97	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P39113	UniProtKB	Compositional bias	208	212	.	.	.	Note=Poly-Pro	
+P39113	UniProtKB	Compositional bias	972	976	.	.	.	Note=Poly-Asn	
+P39113	UniProtKB	Sequence conflict	303	303	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	747	747	.	.	.	Note=K->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	768	768	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	999	1002	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	1008	1008	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	1016	1016	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	1019	1019	.	.	.	Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	1061	1061	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	1072	1074	.	.	.	Note=TDA->ADS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	1092	1092	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	1100	1100	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	1120	1120	.	.	.	Note=M->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39113	UniProtKB	Sequence conflict	1162	1162	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35203 1 478
+P35203	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7957085;Dbxref=PMID:7957085	
+P35203	UniProtKB	Chain	2	478	.	.	.	ID=PRO_0000089370;Note=Centromere DNA-binding protein complex CBF3 subunit C	
+P35203	UniProtKB	Compositional bias	198	222	.	.	.	Note=Asp/Glu-rich (acidic)	
+P35203	UniProtKB	Compositional bias	216	229	.	.	.	Note=Ser-rich	
+##sequence-region P32582 1 507
+P32582	UniProtKB	Chain	1	507	.	.	.	ID=PRO_0000167135;Note=Cystathionine beta-synthase	
+P32582	UniProtKB	Domain	373	432	.	.	.	Note=CBS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P32582	UniProtKB	Region	196	200	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32582	UniProtKB	Binding site	84	84	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32582	UniProtKB	Binding site	289	289	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32582	UniProtKB	Modified residue	53	53	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32582	UniProtKB	Modified residue	134	134	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32582	UniProtKB	Modified residue	350	350	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32582	UniProtKB	Modified residue	424	424	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32582	UniProtKB	Natural variant	504	504	.	.	.	Note=In strain: UCD932. S->N	
+P32582	UniProtKB	Sequence conflict	2	2	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32582	UniProtKB	Sequence conflict	8	8	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32582	UniProtKB	Sequence conflict	63	63	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32582	UniProtKB	Sequence conflict	104	104	.	.	.	Note=L->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32582	UniProtKB	Sequence conflict	129	129	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32582	UniProtKB	Sequence conflict	163	163	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32582	UniProtKB	Sequence conflict	407	407	.	.	.	Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32582	UniProtKB	Sequence conflict	436	437	.	.	.	Note=GK->VE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32582	UniProtKB	Sequence conflict	441	441	.	.	.	Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32582	UniProtKB	Sequence conflict	481	481	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P21269 1 546
+P21269	UniProtKB	Alternative sequence	1	17	.	.	.	ID=VSP_018699;Note=In isoform Cytoplasmic+nuclear 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21269	UniProtKB	Alternative sequence	1	9	.	.	.	ID=VSP_018698;Note=In isoform Cytoplasmic+nuclear 1. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06703 1 312
+Q06703	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06703	UniProtKB	Chain	26	312	.	.	.	ID=PRO_0000024827;Note=Chitin deacetylase 2	
+Q06703	UniProtKB	Domain	118	307	.	.	.	Note=NodB homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01014	
+Q06703	UniProtKB	Glycosylation	142	142	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06703	UniProtKB	Glycosylation	181	181	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06703	UniProtKB	Glycosylation	199	199	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06703	UniProtKB	Glycosylation	246	246	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06703	UniProtKB	Glycosylation	263	263	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P27636 1 974
+P27636	UniProtKB	Chain	1	974	.	.	.	ID=PRO_0000085717;Note=Cell division control protein 15	
+P27636	UniProtKB	Domain	25	272	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P27636	UniProtKB	Nucleotide binding	31	39	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P27636	UniProtKB	Region	360	702	.	.	.	Note=Self association domain	
+P27636	UniProtKB	Region	751	974	.	.	.	Note=Auto-inhibitory domain	
+P27636	UniProtKB	Active site	146	146	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P27636	UniProtKB	Binding site	54	54	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P27636	UniProtKB	Modified residue	561	561	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22031224;Dbxref=PMID:22031224	
+P27636	UniProtKB	Modified residue	567	567	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:22031224;Dbxref=PMID:19779198,PMID:22031224	
+P27636	UniProtKB	Modified residue	870	870	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22031224;Dbxref=PMID:22031224	
+P27636	UniProtKB	Sequence conflict	316	316	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27636	UniProtKB	Sequence conflict	316	316	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27636	UniProtKB	Sequence conflict	316	316	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27636	UniProtKB	Sequence conflict	316	316	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27636	UniProtKB	Sequence conflict	321	321	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27636	UniProtKB	Sequence conflict	321	321	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27636	UniProtKB	Sequence conflict	321	321	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27636	UniProtKB	Sequence conflict	321	321	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27636	UniProtKB	Sequence conflict	900	902	.	.	.	Note=KDV->NGC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27636	UniProtKB	Sequence conflict	900	902	.	.	.	Note=KDV->NGC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40986 1 491
+P40986	UniProtKB	Chain	1	491	.	.	.	ID=PRO_0000089444;Note=Cell division control protein 1	
+P40986	UniProtKB	Topological domain	1	39	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40986	UniProtKB	Transmembrane	40	60	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40986	UniProtKB	Topological domain	61	391	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40986	UniProtKB	Transmembrane	392	412	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40986	UniProtKB	Topological domain	413	465	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40986	UniProtKB	Transmembrane	466	486	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40986	UniProtKB	Topological domain	487	491	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40986	UniProtKB	Compositional bias	8	38	.	.	.	Note=Lys-rich	
+P40986	UniProtKB	Metal binding	95	95	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40986	UniProtKB	Metal binding	144	144	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40986	UniProtKB	Metal binding	144	144	.	.	.	Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40986	UniProtKB	Metal binding	183	183	.	.	.	Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40986	UniProtKB	Metal binding	323	323	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40986	UniProtKB	Sequence conflict	439	439	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40986	UniProtKB	Sequence conflict	478	478	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P04821 1 1589
+P04821	UniProtKB	Chain	1	1589	.	.	.	ID=PRO_0000068863;Note=Cell division control protein 25	
+P04821	UniProtKB	Transmembrane	1452	1473	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04821	UniProtKB	Domain	58	128	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P04821	UniProtKB	Domain	1117	1247	.	.	.	Note=N-terminal Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00135	
+P04821	UniProtKB	Domain	1305	1542	.	.	.	Note=Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00168	
+P04821	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04821	UniProtKB	Modified residue	154	154	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04821	UniProtKB	Modified residue	423	423	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04821	UniProtKB	Modified residue	580	580	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04821	UniProtKB	Modified residue	596	596	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04821	UniProtKB	Modified residue	632	632	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04821	UniProtKB	Modified residue	635	635	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04821	UniProtKB	Modified residue	649	649	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04821	UniProtKB	Sequence conflict	497	497	.	.	.	Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04821	UniProtKB	Sequence conflict	954	963	.	.	.	Note=PVGHHEPFKN->LSVIMNLSR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25694 1 835
+P25694	UniProtKB	Chain	1	835	.	.	.	ID=PRO_0000084587;Note=Cell division control protein 48	
+P25694	UniProtKB	Nucleotide binding	257	263	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072	
+P25694	UniProtKB	Binding site	358	358	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072	
+P25694	UniProtKB	Binding site	394	394	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072	
+P25694	UniProtKB	Modified residue	472	472	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25694	UniProtKB	Modified residue	519	519	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25694	UniProtKB	Modified residue	735	735	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25694	UniProtKB	Modified residue	770	770	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P25694	UniProtKB	Cross-link	305	305	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25694	UniProtKB	Cross-link	322	322	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25694	UniProtKB	Cross-link	346	346	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25694	UniProtKB	Cross-link	522	522	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25694	UniProtKB	Cross-link	539	539	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25694	UniProtKB	Cross-link	594	594	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P25694	UniProtKB	Cross-link	673	673	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region P06243 1 507
+P06243	UniProtKB	Chain	1	507	.	.	.	ID=PRO_0000085766;Note=Cell division control protein 7	
+P06243	UniProtKB	Domain	33	469	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06243	UniProtKB	Nucleotide binding	39	47	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06243	UniProtKB	Active site	163	163	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P06243	UniProtKB	Binding site	76	76	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region P53829 1 373
+P53829	UniProtKB	Chain	1	373	.	.	.	ID=PRO_0000203375;Note=Protein CAF40	
+##sequence-region P43568 1 368
+P43568	UniProtKB	Chain	1	368	.	.	.	ID=PRO_0000085690;Note=Serine/threonine-protein kinase CAK1	
+P43568	UniProtKB	Domain	1	368	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P43568	UniProtKB	Active site	156	156	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+##sequence-region P53223 1 239
+P53223	UniProtKB	Chain	1	239	.	.	.	ID=PRO_0000215629;Note=Dolichyldiphosphatase	
+P53223	UniProtKB	Topological domain	1	34	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53223	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53223	UniProtKB	Topological domain	56	131	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53223	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53223	UniProtKB	Topological domain	153	164	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53223	UniProtKB	Transmembrane	165	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53223	UniProtKB	Topological domain	186	239	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40969 1 608
+P40969	UniProtKB	Chain	1	608	.	.	.	ID=PRO_0000114941;Note=Centromere DNA-binding protein complex CBF3 subunit B	
+P40969	UniProtKB	DNA binding	14	42	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P40969	UniProtKB	Modified residue	575	575	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40969	UniProtKB	Helix	58	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Turn	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	75	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Turn	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	96	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	108	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	134	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	154	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	176	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	186	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	204	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Turn	223	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	231	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Turn	241	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	245	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	250	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	280	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	313	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QUQ	
+P40969	UniProtKB	Helix	338	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Turn	357	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	367	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	394	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	427	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	444	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Turn	447	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	451	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	457	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	480	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	498	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	501	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Beta strand	530	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	536	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	555	562	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	589	600	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+P40969	UniProtKB	Helix	603	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ	
+##sequence-region P53894 1 756
+P53894	UniProtKB	Chain	1	756	.	.	.	ID=PRO_0000085697;Note=Serine/threonine-protein kinase CBK1	
+P53894	UniProtKB	Domain	352	672	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53894	UniProtKB	Domain	673	754	.	.	.	Note=AGC-kinase C-terminal	
+P53894	UniProtKB	Nucleotide binding	358	366	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53894	UniProtKB	Compositional bias	23	34	.	.	.	Note=Poly-Gln	
+P53894	UniProtKB	Compositional bias	160	164	.	.	.	Note=Poly-Ser	
+P53894	UniProtKB	Compositional bias	214	232	.	.	.	Note=Poly-Gln	
+P53894	UniProtKB	Compositional bias	235	250	.	.	.	Note=Poly-Gln	
+P53894	UniProtKB	Active site	475	475	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P53894	UniProtKB	Binding site	381	381	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53894	UniProtKB	Modified residue	109	109	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53894	UniProtKB	Helix	299	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Beta strand	349	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Beta strand	366	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Turn	372	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Beta strand	378	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Beta strand	385	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Beta strand	415	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Beta strand	425	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Helix	437	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Helix	450	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Helix	458	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Beta strand	478	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Helix	557	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Helix	561	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Beta strand	582	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Helix	591	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Turn	619	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Helix	622	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Helix	640	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Beta strand	656	658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Beta strand	663	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P53894	UniProtKB	Helix	679	681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+##sequence-region P03874 1 630
+P03874	UniProtKB	Chain	1	630	.	.	.	ID=PRO_0000089380;Note=Cytochrome B pre-mRNA-processing protein 2	
+P03874	UniProtKB	Sequence conflict	490	490	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11433 1 854
+P11433	UniProtKB	Chain	1	854	.	.	.	ID=PRO_0000080934;Note=Cell division control protein 24	
+P11433	UniProtKB	Domain	278	454	.	.	.	Note=DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00062	
+P11433	UniProtKB	Domain	478	668	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P11433	UniProtKB	Domain	761	854	.	.	.	Note=PB1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01081	
+P11433	UniProtKB	Compositional bias	494	600	.	.	.	Note=Ser/Thr-rich	
+P11433	UniProtKB	Compositional bias	681	778	.	.	.	Note=Ser/Thr-rich	
+P11433	UniProtKB	Beta strand	762	768	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1O	
+P11433	UniProtKB	Beta strand	780	784	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS	
+P11433	UniProtKB	Helix	792	801	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS	
+P11433	UniProtKB	Turn	802	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS	
+P11433	UniProtKB	Beta strand	817	820	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS	
+P11433	UniProtKB	Turn	821	823	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS	
+P11433	UniProtKB	Beta strand	824	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS	
+P11433	UniProtKB	Helix	833	844	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS	
+P11433	UniProtKB	Beta strand	848	852	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS	
+##sequence-region P38042 1 758
+P38042	UniProtKB	Chain	1	758	.	.	.	ID=PRO_0000106274;Note=Anaphase-promoting complex subunit CDC27	
+P38042	UniProtKB	Repeat	154	187	.	.	.	Note=TPR 1	
+P38042	UniProtKB	Repeat	472	505	.	.	.	Note=TPR 2	
+P38042	UniProtKB	Repeat	540	573	.	.	.	Note=TPR 3	
+P38042	UniProtKB	Repeat	574	607	.	.	.	Note=TPR 4	
+P38042	UniProtKB	Repeat	608	641	.	.	.	Note=TPR 5	
+P38042	UniProtKB	Repeat	642	675	.	.	.	Note=TPR 6	
+P38042	UniProtKB	Repeat	676	709	.	.	.	Note=TPR 7	
+P38042	UniProtKB	Repeat	710	743	.	.	.	Note=TPR 8	
+P38042	UniProtKB	Compositional bias	365	388	.	.	.	Note=Poly-Asn	
+P38042	UniProtKB	Mutagenesis	267	267	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-304%3B A-328%3B A-351 and A-397. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279	
+P38042	UniProtKB	Mutagenesis	304	304	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-267%3B A-304%3B A-351 and A-397. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279	
+P38042	UniProtKB	Mutagenesis	328	328	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-267%3B A-304%3B A-328 and A-397. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279	
+P38042	UniProtKB	Mutagenesis	351	351	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-267%3B A-304%3B A-328 and A-304. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279	
+P38042	UniProtKB	Mutagenesis	397	397	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-304%3B A-328%3B A-351 and A-397. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279	
+P38042	UniProtKB	Mutagenesis	613	613	.	.	.	Note=In CDC27-633%3B G2/M cell cycle arrest at 35 degrees Celsius. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1819514;Dbxref=PMID:1819514	
+P38042	UniProtKB	Mutagenesis	614	614	.	.	.	Note=Abolishes interaction with CDC23. L->GL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7925276;Dbxref=PMID:7925276	
+P38042	UniProtKB	Sequence conflict	430	430	.	.	.	Note=S->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38042	UniProtKB	Sequence conflict	430	430	.	.	.	Note=S->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06549 1 142
+Q06549	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000171685;Note=Cytidine deaminase	
+Q06549	UniProtKB	Domain	9	139	.	.	.	Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083	
+Q06549	UniProtKB	Region	50	52	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06549	UniProtKB	Active site	63	63	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06549	UniProtKB	Metal binding	61	61	.	.	.	Note=Zinc%3B catalytic	
+Q06549	UniProtKB	Metal binding	96	96	.	.	.	Note=Zinc%3B catalytic	
+Q06549	UniProtKB	Metal binding	99	99	.	.	.	Note=Zinc%3B catalytic	
+Q06549	UniProtKB	Helix	8	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Helix	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Turn	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Beta strand	34	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Beta strand	45	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Helix	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Helix	62	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Beta strand	81	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Beta strand	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Helix	97	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Beta strand	112	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Beta strand	118	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Helix	128	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+Q06549	UniProtKB	Helix	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T	
+##sequence-region P20438 1 545
+P20438	UniProtKB	Chain	1	545	.	.	.	ID=PRO_0000080412;Note=G1/S-specific cyclin CLN2	
+P20438	UniProtKB	Sequence conflict	440	440	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P24869 1 491
+P24869	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P24869	UniProtKB	Chain	2	491	.	.	.	ID=PRO_0000080404;Note=G2/mitotic-specific cyclin-2	
+P24869	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P80235 1 687
+P80235	UniProtKB	Chain	1	687	.	.	.	ID=PRO_0000210175;Note=Putative mitochondrial carnitine O-acetyltransferase	
+P80235	UniProtKB	Region	446	459	.	.	.	Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P80235	UniProtKB	Active site	346	346	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P80235	UniProtKB	Binding site	481	481	.	.	.	Note=Carnitine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P80235	UniProtKB	Binding site	494	494	.	.	.	Note=Carnitine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P80235	UniProtKB	Modified residue	517	517	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P80235	UniProtKB	Sequence conflict	25	25	.	.	.	Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P80235	UniProtKB	Sequence conflict	392	392	.	.	.	Note=S->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P80235	UniProtKB	Sequence conflict	595	596	.	.	.	Note=SF->AS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P80235	UniProtKB	Sequence conflict	653	653	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P80235	UniProtKB	Sequence conflict	660	660	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32796 1 670
+P32796	UniProtKB	Region	465	472	.	.	.	Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32796	UniProtKB	Motif	668	670	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32796	UniProtKB	Active site	378	378	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32796	UniProtKB	Binding site	461	461	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32796	UniProtKB	Binding site	494	494	.	.	.	Note=Carnitine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32796	UniProtKB	Binding site	498	498	.	.	.	Note=Coenzyme A%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32796	UniProtKB	Binding site	507	507	.	.	.	Note=Carnitine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32796	UniProtKB	Binding site	597	597	.	.	.	Note=Coenzyme A%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32796	UniProtKB	Alternative sequence	1	22	.	.	.	ID=VSP_018690;Note=In isoform Peroxisomal. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32796	UniProtKB	Sequence conflict	263	263	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32796	UniProtKB	Sequence conflict	308	308	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25296 1 175
+P25296	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+P25296	UniProtKB	Chain	2	175	.	.	.	ID=PRO_0000073498;Note=Calcineurin subunit B	
+P25296	UniProtKB	Domain	21	56	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P25296	UniProtKB	Domain	53	88	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P25296	UniProtKB	Domain	90	125	.	.	.	Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P25296	UniProtKB	Domain	131	166	.	.	.	Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P25296	UniProtKB	Calcium binding	34	45	.	.	.	Note=1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P25296	UniProtKB	Calcium binding	66	77	.	.	.	Note=2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P25296	UniProtKB	Calcium binding	103	114	.	.	.	Note=3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P25296	UniProtKB	Calcium binding	144	155	.	.	.	Note=4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P25296	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1321337;Dbxref=PMID:1321337	
+##sequence-region P07253 1 162
+P07253	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07253	UniProtKB	Chain	2	162	.	.	.	ID=PRO_0000089381;Note=Cytochrome B pre-mRNA-processing protein 6	
+P07253	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07253	UniProtKB	Modified residue	97	97	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P07253	UniProtKB	Sequence conflict	2	2	.	.	.	Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36038 1 271
+P36038	UniProtKB	Chain	1	271	.	.	.	ID=PRO_0000203131;Note=Cytochrome b termination protein 1	
+P36038	UniProtKB	Sequence conflict	270	270	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P37366 1 393
+P37366	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000080504;Note=Cyclin CCL1	
+##sequence-region P37267 1 147
+P37267	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000020845;Note=Assembly factor CBP4	
+P37267	UniProtKB	Transmembrane	5	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37267	UniProtKB	Sequence conflict	42	42	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P48237 1 864
+P48237	UniProtKB	Repeat	319	355	.	.	.	Note=PPR 1	
+P48237	UniProtKB	Repeat	356	390	.	.	.	Note=PPR 2	
+##sequence-region P31384 1 837
+P31384	UniProtKB	Chain	1	837	.	.	.	ID=PRO_0000218577;Note=Glucose-repressible alcohol dehydrogenase transcriptional effector	
+P31384	UniProtKB	Repeat	334	356	.	.	.	Note=LRR 1	
+P31384	UniProtKB	Repeat	358	379	.	.	.	Note=LRR 2	
+P31384	UniProtKB	Repeat	381	402	.	.	.	Note=LRR 3	
+P31384	UniProtKB	Repeat	404	426	.	.	.	Note=LRR 4	
+P31384	UniProtKB	Repeat	427	447	.	.	.	Note=LRR 5	
+P31384	UniProtKB	Compositional bias	15	24	.	.	.	Note=Poly-Gln	
+P31384	UniProtKB	Compositional bias	77	103	.	.	.	Note=Asn-rich	
+P31384	UniProtKB	Compositional bias	89	103	.	.	.	Note=Poly-Asn	
+P31384	UniProtKB	Compositional bias	190	206	.	.	.	Note=Gln-rich	
+P31384	UniProtKB	Metal binding	556	556	.	.	.	Note=Magnesium	
+P31384	UniProtKB	Modified residue	33	33	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P31384	UniProtKB	Modified residue	278	278	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P31384	UniProtKB	Modified residue	285	285	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P31384	UniProtKB	Mutagenesis	556	556	.	.	.	Note=Loss of activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11889047;Dbxref=PMID:11889047	
+P31384	UniProtKB	Mutagenesis	713	713	.	.	.	Note=Strongly reduces activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11889047;Dbxref=PMID:11889047	
+P31384	UniProtKB	Mutagenesis	780	780	.	.	.	Note=Reduces activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11889047;Dbxref=PMID:11889047	
+P31384	UniProtKB	Mutagenesis	818	818	.	.	.	Note=Loss of activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11889047;Dbxref=PMID:11889047	
+P31384	UniProtKB	Sequence conflict	544	544	.	.	.	Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31384	UniProtKB	Sequence conflict	803	803	.	.	.	Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31384	UniProtKB	Turn	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	155	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	176	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	245	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Beta strand	338	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	351	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	374	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Beta strand	384	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	399	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Beta strand	406	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	441	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	515	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Turn	520	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	528	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	533	546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Beta strand	550	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	559	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Turn	564	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Beta strand	600	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Helix	800	803	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Beta strand	807	811	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P31384	UniProtKB	Beta strand	816	818	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+##sequence-region Q12127 1 133
+Q12127	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10322008;Dbxref=PMID:10322008	
+Q12127	UniProtKB	Chain	19	112	.	.	.	ID=PRO_0000020879;Note=Covalently-linked cell wall protein 12	
+Q12127	UniProtKB	Propeptide	113	133	.	.	.	ID=PRO_0000020880;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12127	UniProtKB	Repeat	75	88	.	.	.	Note=1	
+Q12127	UniProtKB	Repeat	91	103	.	.	.	Note=2	
+Q12127	UniProtKB	Lipidation	112	112	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12127	UniProtKB	Glycosylation	21	21	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17315267;Dbxref=PMID:17315267	
+Q12127	UniProtKB	Glycosylation	23	23	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	24	24	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	26	26	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	28	28	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	31	31	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	32	32	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	33	33	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	36	36	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	38	38	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	39	39	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	46	46	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	48	48	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243	
+Q12127	UniProtKB	Glycosylation	81	81	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17315267;Dbxref=PMID:17315267	
+Q12127	UniProtKB	Glycosylation	97	97	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17315267;Dbxref=PMID:17315267	
+Q12127	UniProtKB	Cross-link	80	80	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P32457 1 520
+P32457	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P32457	UniProtKB	Chain	2	520	.	.	.	ID=PRO_0000173496;Note=Cell division control protein 3	
+P32457	UniProtKB	Domain	116	411	.	.	.	Note=Septin-type G	
+P32457	UniProtKB	Nucleotide binding	126	133	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32457	UniProtKB	Nucleotide binding	287	295	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32457	UniProtKB	Coiled coil	427	508	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32457	UniProtKB	Binding site	207	207	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32457	UniProtKB	Binding site	344	344	.	.	.	Note=GTP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32457	UniProtKB	Binding site	360	360	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32457	UniProtKB	Site	415	415	.	.	.	Note=Not sumoylated	
+P32457	UniProtKB	Site	443	443	.	.	.	Note=Not sumoylated	
+P32457	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P32457	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P32457	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P32457	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32457	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32457	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32457	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32457	UniProtKB	Modified residue	468	468	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32457	UniProtKB	Modified residue	509	509	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32457	UniProtKB	Cross-link	4	4	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
+P32457	UniProtKB	Cross-link	11	11	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
+P32457	UniProtKB	Cross-link	30	30	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
+P32457	UniProtKB	Cross-link	63	63	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15166219,ECO:0000269|PubMed:15542864;Dbxref=PMID:15166219,PMID:15542864	
+P32457	UniProtKB	Cross-link	287	287	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
+P32457	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Abolishes sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719	
+P32457	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Abolishes sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719	
+P32457	UniProtKB	Mutagenesis	287	287	.	.	.	Note=Abolishes sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719	
+P32457	UniProtKB	Mutagenesis	415	415	.	.	.	Note=No effect on sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719	
+P32457	UniProtKB	Mutagenesis	443	443	.	.	.	Note=No effect on sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719	
+P32457	UniProtKB	Sequence conflict	431	431	.	.	.	Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06697 1 393
+Q06697	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000238580;Note=Cell division control protein 73	
+Q06697	UniProtKB	Modified residue	114	114	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06697	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06697	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Beta strand	248	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DM4	
+Q06697	UniProtKB	Turn	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Helix	255	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Helix	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Beta strand	276	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Beta strand	287	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Beta strand	291	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Helix	305	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Beta strand	311	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Helix	320	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Beta strand	326	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Helix	331	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Beta strand	338	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Helix	352	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Beta strand	357	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+Q06697	UniProtKB	Helix	369	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DM4	
+Q06697	UniProtKB	Helix	372	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46	
+##sequence-region P41733 1 394
+P41733	UniProtKB	Chain	1	394	.	.	.	ID=PRO_0000121398;Note=GPI transamidase component GAB1	
+P41733	UniProtKB	Topological domain	1	135	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Topological domain	157	160	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Topological domain	182	190	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Transmembrane	191	211	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Topological domain	212	224	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Transmembrane	225	245	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Topological domain	246	250	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Transmembrane	251	271	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Topological domain	272	297	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Transmembrane	298	318	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Topological domain	319	324	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Transmembrane	325	345	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Topological domain	346	351	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Transmembrane	352	372	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Topological domain	373	394	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41733	UniProtKB	Region	235	255	.	.	.	Note=May be involved in recognition of long-chain fatty acids in GPI;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P17106 1 351
+P17106	UniProtKB	Chain	1	351	.	.	.	ID=PRO_0000127161;Note=Centromere-binding protein 1	
+P17106	UniProtKB	Domain	222	270	.	.	.	Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981	
+P17106	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P17106	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P17106	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P17106	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P17106	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P17106	UniProtKB	Sequence conflict	144	144	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17106	UniProtKB	Sequence conflict	168	168	.	.	.	Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17106	UniProtKB	Sequence conflict	262	262	.	.	.	Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17106	UniProtKB	Sequence conflict	262	262	.	.	.	Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17106	UniProtKB	Sequence conflict	262	262	.	.	.	Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03702 1 353
+Q03702	UniProtKB	Metal binding	293	293	.	.	.	Note=Magnesium	
+Q03702	UniProtKB	Metal binding	294	294	.	.	.	Note=Magnesium	
+Q03702	UniProtKB	Mutagenesis	79	79	.	.	.	Note=>200-fold decrease in activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168	
+Q03702	UniProtKB	Mutagenesis	145	145	.	.	.	Note=>200-fold decrease in activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168	
+Q03702	UniProtKB	Mutagenesis	146	146	.	.	.	Note=100-fold decrease in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168	
+Q03702	UniProtKB	Mutagenesis	147	147	.	.	.	Note=70-fold decrease in activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168	
+Q03702	UniProtKB	Mutagenesis	150	150	.	.	.	Note=4-fold decrease in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168	
+Q03702	UniProtKB	Mutagenesis	231	231	.	.	.	Note=>200-fold decrease in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168	
+Q03702	UniProtKB	Mutagenesis	231	231	.	.	.	Note=47-fold decrease in activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168	
+Q03702	UniProtKB	Mutagenesis	291	291	.	.	.	Note=>200-fold decrease in activity. K->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168	
+Q03702	UniProtKB	Mutagenesis	292	292	.	.	.	Note=80-fold decrease in activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168	
+Q03702	UniProtKB	Mutagenesis	293	293	.	.	.	Note=>200-fold decrease in activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168	
+Q03702	UniProtKB	Mutagenesis	294	294	.	.	.	Note=>200-fold decrease in activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168	
+##sequence-region P38273 1 704
+P38273	UniProtKB	Chain	1	704	.	.	.	ID=PRO_0000202491;Note=Vacuolar fusion protein CCZ1	
+##sequence-region Q06702 1 301
+Q06702	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06702	UniProtKB	Chain	25	301	.	.	.	ID=PRO_0000024826;Note=Chitin deacetylase 1	
+Q06702	UniProtKB	Domain	108	288	.	.	.	Note=NodB homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01014	
+Q06702	UniProtKB	Glycosylation	26	26	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06702	UniProtKB	Glycosylation	50	50	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06702	UniProtKB	Glycosylation	68	68	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06702	UniProtKB	Glycosylation	189	189	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25342 1 322
+P25342	UniProtKB	Chain	1	322	.	.	.	ID=PRO_0000173498;Note=Cell division control protein 10	
+P25342	UniProtKB	Domain	29	302	.	.	.	Note=Septin-type G	
+P25342	UniProtKB	Nucleotide binding	39	46	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25342	UniProtKB	Nucleotide binding	180	188	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25342	UniProtKB	Binding site	74	74	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25342	UniProtKB	Binding site	100	100	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25342	UniProtKB	Binding site	236	236	.	.	.	Note=GTP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25342	UniProtKB	Binding site	251	251	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25342	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25342	UniProtKB	Modified residue	216	216	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region P32468 1 407
+P32468	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32468	UniProtKB	Chain	2	407	.	.	.	ID=PRO_0000173500;Note=Cell division control protein 12	
+P32468	UniProtKB	Domain	31	314	.	.	.	Note=Septin-type G	
+P32468	UniProtKB	Nucleotide binding	41	48	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32468	UniProtKB	Nucleotide binding	180	188	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32468	UniProtKB	Coiled coil	344	406	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32468	UniProtKB	Binding site	75	75	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32468	UniProtKB	Binding site	101	101	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32468	UniProtKB	Binding site	247	247	.	.	.	Note=GTP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32468	UniProtKB	Binding site	263	263	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32468	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P09798 1 840
+P09798	UniProtKB	Chain	1	840	.	.	.	ID=PRO_0000106269;Note=Anaphase-promoting complex subunit CDC16	
+P09798	UniProtKB	Repeat	229	260	.	.	.	Note=TPR 1	
+P09798	UniProtKB	Repeat	263	288	.	.	.	Note=TPR 2	
+P09798	UniProtKB	Repeat	296	319	.	.	.	Note=TPR 3	
+P09798	UniProtKB	Repeat	357	388	.	.	.	Note=TPR 4	
+P09798	UniProtKB	Repeat	393	416	.	.	.	Note=TPR 5	
+P09798	UniProtKB	Repeat	426	454	.	.	.	Note=TPR 6	
+P09798	UniProtKB	Repeat	464	492	.	.	.	Note=TPR 7	
+P09798	UniProtKB	Repeat	499	526	.	.	.	Note=TPR 8	
+P09798	UniProtKB	Repeat	531	560	.	.	.	Note=TPR 9	
+P09798	UniProtKB	Repeat	565	593	.	.	.	Note=TPR 10	
+P09798	UniProtKB	Repeat	600	628	.	.	.	Note=TPR 11	
+P09798	UniProtKB	Repeat	633	665	.	.	.	Note=TPR 12	
+P09798	UniProtKB	Repeat	671	703	.	.	.	Note=TPR 13	
+P09798	UniProtKB	Repeat	708	737	.	.	.	Note=TPR 14	
+P09798	UniProtKB	Compositional bias	209	220	.	.	.	Note=Poly-Thr	
+P09798	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-59%3B A-95%3B A-103%3B A-115 and A-406. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279	
+P09798	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-44%3B A-95%3B A-103%3B A-115 and A-406. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279	
+P09798	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-44%3B A-59%3B A-103%3B A-115 and A-406. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279	
+P09798	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-44%3B A-59%3B A-95%3B A-115 and A-406. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279	
+P09798	UniProtKB	Mutagenesis	115	115	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-44%3B A-59%3B A-95%3B A-103 and A-406. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279	
+P09798	UniProtKB	Mutagenesis	406	406	.	.	.	Note=Abolishes phosphorylation%3B when associated with A-44%3B A-59%3B A-95%3B A-103 and A-115. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279	
+P09798	UniProtKB	Mutagenesis	482	482	.	.	.	Note=In CDC16-264%3B G2/M cell cycle arrest at 36 degrees Celsius. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9660930;Dbxref=PMID:9660930	
+P09798	UniProtKB	Mutagenesis	530	530	.	.	.	Note=In CDC16-183%3B G2/M cell cycle arrest at 37 degrees Celsius. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12928868;Dbxref=PMID:12928868	
+P09798	UniProtKB	Mutagenesis	557	557	.	.	.	Note=In CDC16-1%3B G2/M cell cycle arrest at 36 degrees Celsius. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9660930;Dbxref=PMID:9660930	
+##sequence-region P16522 1 626
+P16522	UniProtKB	Chain	1	626	.	.	.	ID=PRO_0000106272;Note=Anaphase-promoting complex subunit CDC23	
+P16522	UniProtKB	Repeat	215	248	.	.	.	Note=TPR 1	
+P16522	UniProtKB	Repeat	295	328	.	.	.	Note=TPR 2	
+P16522	UniProtKB	Repeat	329	362	.	.	.	Note=TPR 3	
+P16522	UniProtKB	Repeat	363	396	.	.	.	Note=TPR 4	
+P16522	UniProtKB	Repeat	397	430	.	.	.	Note=TPR 5	
+P16522	UniProtKB	Repeat	431	464	.	.	.	Note=TPR 6	
+P16522	UniProtKB	Repeat	465	498	.	.	.	Note=TPR 7	
+P16522	UniProtKB	Repeat	499	532	.	.	.	Note=TPR 8	
+P16522	UniProtKB	Repeat	536	569	.	.	.	Note=TPR 9	
+P16522	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:10871279;Dbxref=PMID:18407956,PMID:10871279	
+P16522	UniProtKB	Mutagenesis	39	39	.	.	.	Note=In CDC23-50%3B G2/M cell cycle arrest at 37 degrees Celsius. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	42	42	.	.	.	Note=In CDC23-54%3B G2/M cell cycle arrest at 37 degrees Celsius. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	80	80	.	.	.	Note=In CDC23-44%3B G2/M cell cycle arrest at 37 degrees Celsius. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	85	85	.	.	.	Note=In CDC23-51%3B G2/M cell cycle arrest at 37 degrees Celsius. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	93	93	.	.	.	Note=In CDC23-52%3B G2/M cell cycle arrest at 37 degrees Celsius. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	94	94	.	.	.	Note=In CDC23-4%3B G2/M cell cycle arrest at 36 degrees Celsius. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	103	103	.	.	.	Note=In CDC23-40%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with V-573. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	114	114	.	.	.	Note=In CDC23-53%3B G2/M cell cycle arrest at 37 degrees Celsius. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	114	114	.	.	.	Note=In CDC23-41%3B G2/M cell cycle arrest at 37 degrees Celsius. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	123	123	.	.	.	Note=In CDC23-6%3B G2/M cell cycle arrest at 36 degrees Celsius. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	213	213	.	.	.	Note=In CDC23-47%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with W-583. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	306	306	.	.	.	Note=In CDC23-49%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with P-326. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	326	326	.	.	.	Note=In CDC23-49%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with E-306. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	398	398	.	.	.	Note=In CDC23-37%3B G2/M cell cycle arrest at 30 degrees Celsius. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	404	404	.	.	.	Note=In CDC23-39%3B G2/M cell cycle arrest at 37 degrees Celsius. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	439	439	.	.	.	Note=In CDC23-2%3B G2/M cell cycle arrest at 36 degrees Celsius. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	472	472	.	.	.	Note=In CDC23-1%3B G2/M cell cycle arrest at 36 degrees Celsius. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	485	485	.	.	.	Note=In CDC23-56%3B G2/M cell cycle arrest at 37 degrees Celsius. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	573	573	.	.	.	Note=In CDC23-40%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with R-103. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787	
+P16522	UniProtKB	Mutagenesis	583	626	.	.	.	Note=In CDC23-47%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with G-213. Missing	
+##sequence-region P06704 1 161
+P06704	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000073577;Note=Cell division control protein 31	
+P06704	UniProtKB	Domain	20	55	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P06704	UniProtKB	Domain	56	91	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P06704	UniProtKB	Domain	93	128	.	.	.	Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P06704	UniProtKB	Domain	129	161	.	.	.	Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P06704	UniProtKB	Calcium binding	33	44	.	.	.	Note=1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P06704	UniProtKB	Calcium binding	142	153	.	.	.	Note=2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P06704	UniProtKB	Modified residue	130	130	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P06704	UniProtKB	Sequence conflict	77	77	.	.	.	Note=K->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06704	UniProtKB	Sequence conflict	110	110	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06704	UniProtKB	Turn	10	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Helix	19	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Beta strand	36	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Helix	42	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Helix	58	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Helix	78	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Helix	94	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Beta strand	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Helix	115	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Helix	131	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Beta strand	143	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+P06704	UniProtKB	Helix	151	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+##sequence-region P53082 1 120
+P53082	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000201232;Note=BolA-like protein 2	
+##sequence-region P25356 1 2167
+P25356	UniProtKB	Chain	1	2167	.	.	.	ID=PRO_0000050887;Note=Beige protein homolog 1	
+P25356	UniProtKB	Domain	1368	1499	.	.	.	Note=BEACH-type PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01119	
+P25356	UniProtKB	Domain	1545	1839	.	.	.	Note=BEACH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00026	
+P25356	UniProtKB	Repeat	1927	1965	.	.	.	Note=WD 1	
+P25356	UniProtKB	Repeat	1976	2015	.	.	.	Note=WD 2	
+P25356	UniProtKB	Repeat	2017	2054	.	.	.	Note=WD 3	
+P25356	UniProtKB	Repeat	2072	2111	.	.	.	Note=WD 4	
+P25356	UniProtKB	Repeat	2129	2167	.	.	.	Note=WD 5	
+P25356	UniProtKB	Cross-link	1667	1667	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25356	UniProtKB	Sequence conflict	1893	1893	.	.	.	Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P26448 1 306
+P26448	UniProtKB	Chain	1	306	.	.	.	ID=PRO_0000208008;Note=Mitotic check point protein BUB2	
+P26448	UniProtKB	Domain	37	235	.	.	.	Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163	
+##sequence-region P27637 1 709
+P27637	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P27637	UniProtKB	Chain	2	707	.	.	.	ID=PRO_0000065012;Note=Bud site selection protein 14	
+P27637	UniProtKB	Domain	259	320	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P27637	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P27637	UniProtKB	Modified residue	159	159	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27637	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P27637	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27637	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27637	UniProtKB	Modified residue	212	212	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P27637	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P27637	UniProtKB	Modified residue	376	376	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P27637	UniProtKB	Modified residue	378	378	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P27637	UniProtKB	Modified residue	401	401	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27637	UniProtKB	Modified residue	507	507	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27637	UniProtKB	Modified residue	655	655	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27637	UniProtKB	Modified residue	658	658	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P27637	UniProtKB	Modified residue	670	670	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27637	UniProtKB	Sequence conflict	439	439	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27637	UniProtKB	Sequence conflict	439	439	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27637	UniProtKB	Sequence conflict	573	595	.	.	.	Note=KDISQYIHAKSKIEETTNVENTE->RTFTYIMQNRKLRDNKRGKHR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27637	UniProtKB	Sequence conflict	573	595	.	.	.	Note=KDISQYIHAKSKIEETTNVENTE->RTFTYIMQNRKLRDNKRGKHR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27637	UniProtKB	Sequence conflict	609	609	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27637	UniProtKB	Sequence conflict	609	609	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47158 1 497
+P47158	UniProtKB	Transit peptide	1	27	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47158	UniProtKB	Chain	28	497	.	.	.	ID=PRO_0000203117;Note=Putative transferase CAF17%2C mitochondrial	
+##sequence-region P53934 1 400
+P53934	UniProtKB	Chain	1	400	.	.	.	ID=PRO_0000203441;Note=Carnosine N-methyltransferase	
+P53934	UniProtKB	Natural variant	42	42	.	.	.	Note=In strain: SK1. A->E	
+P53934	UniProtKB	Natural variant	154	154	.	.	.	Note=In strain: SK1. V->M	
+P53934	UniProtKB	Natural variant	317	317	.	.	.	Note=In strain: SK1. E->D	
+##sequence-region P06115 1 562
+P06115	UniProtKB	Chain	1	562	.	.	.	ID=PRO_0000084929;Note=Catalase T	
+P06115	UniProtKB	Active site	64	64	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10013	
+P06115	UniProtKB	Active site	137	137	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10013	
+P06115	UniProtKB	Metal binding	351	351	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06115	UniProtKB	Sequence conflict	429	429	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06115	UniProtKB	Sequence conflict	539	539	.	.	.	Note=C->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32504 1 956
+P32504	UniProtKB	Chain	1	956	.	.	.	ID=PRO_0000089369;Note=Centromere DNA-binding protein complex CBF3 subunit A	
+P32504	UniProtKB	Modified residue	566	566	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32504	UniProtKB	Modified residue	706	706	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32504	UniProtKB	Sequence conflict	418	418	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32504	UniProtKB	Sequence conflict	774	774	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32504	UniProtKB	Helix	45	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Turn	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	82	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Turn	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	108	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	148	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	184	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Turn	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Turn	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	208	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	228	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Beta strand	249	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Beta strand	266	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	278	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	282	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Turn	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	309	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Turn	314	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	318	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Beta strand	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	335	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	356	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Beta strand	368	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	371	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	380	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	390	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	396	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	401	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	429	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	438	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	447	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	452	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	483	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	488	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	493	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	504	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Turn	518	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	521	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+P32504	UniProtKB	Helix	527	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO	
+##sequence-region P33322 1 483
+P33322	UniProtKB	Chain	1	483	.	.	.	ID=PRO_0000121982;Note=H/ACA ribonucleoprotein complex subunit 4	
+P33322	UniProtKB	Domain	266	341	.	.	.	Note=PUA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00161	
+P33322	UniProtKB	Repeat	434	436	.	.	.	Note=1	
+P33322	UniProtKB	Repeat	437	439	.	.	.	Note=2	
+P33322	UniProtKB	Repeat	440	442	.	.	.	Note=3	
+P33322	UniProtKB	Repeat	443	445	.	.	.	Note=4	
+P33322	UniProtKB	Repeat	446	448	.	.	.	Note=5	
+P33322	UniProtKB	Repeat	449	451	.	.	.	Note=6	
+P33322	UniProtKB	Repeat	452	454	.	.	.	Note=7	
+P33322	UniProtKB	Repeat	455	457	.	.	.	Note=8	
+P33322	UniProtKB	Repeat	458	460	.	.	.	Note=9	
+P33322	UniProtKB	Repeat	461	463	.	.	.	Note=10	
+P33322	UniProtKB	Region	434	463	.	.	.	Note=10 X 3 AA tandem repeats of K-K-[DE]	
+P33322	UniProtKB	Active site	95	95	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33322	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33322	UniProtKB	Modified residue	378	378	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P33322	UniProtKB	Cross-link	9	9	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P33322	UniProtKB	Cross-link	267	267	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P33322	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Reduced pseudouridylation of rRNA and reduced snoRNA levels. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523634;Dbxref=PMID:10523634	
+P33322	UniProtKB	Mutagenesis	94	94	.	.	.	Note=Reduced pseudouridylation of rRNA. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523634;Dbxref=PMID:10523634	
+P33322	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Reduced pseudouridylation of rRNA. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523634;Dbxref=PMID:10523634	
+P33322	UniProtKB	Helix	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	32	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	53	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	60	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	72	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	94	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UAI	
+P33322	UniProtKB	Beta strand	99	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	107	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	113	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	121	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	138	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	148	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	165	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Turn	179	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	183	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	196	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	211	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	233	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	250	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UAI	
+P33322	UniProtKB	Helix	259	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	268	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	276	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	283	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	287	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	290	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	302	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	312	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	322	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Beta strand	329	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P33322	UniProtKB	Helix	355	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZV0	
+##sequence-region P14066 1 229
+P14066	UniProtKB	Transit peptide	1	25	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1657414;Dbxref=PMID:1657414	
+P14066	UniProtKB	Chain	26	229	.	.	.	ID=PRO_0000020850;Note=Cytochrome b translational activator protein CBS1%2C mitochondrial	
+P14066	UniProtKB	Mutagenesis	98	98	.	.	.	Note=Loss of function%2C causes respiratory deficiency. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669873;Dbxref=PMID:10669873	
+P14066	UniProtKB	Mutagenesis	100	100	.	.	.	Note=In CBS1-1%2C which is respiratory deficient. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669873;Dbxref=PMID:10669873	
+P14066	UniProtKB	Mutagenesis	124	124	.	.	.	Note=Loss of function%2C causes respiratory deficiency. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669873;Dbxref=PMID:10669873	
+P14066	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Loss of function%2C causes respiratory deficiency. F->S%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669873;Dbxref=PMID:10669873	
+##sequence-region P50077 1 2039
+P50077	UniProtKB	Chain	1	2039	.	.	.	ID=PRO_0000054106;Note=Calcium-channel protein CCH1	
+P50077	UniProtKB	Transmembrane	346	366	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	384	404	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	563	583	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	658	678	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	691	711	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	766	786	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	809	829	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	841	861	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	904	924	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	942	962	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	978	998	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1207	1227	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1247	1267	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1277	1297	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1340	1360	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1408	1428	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1452	1472	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1529	1549	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1554	1574	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1596	1616	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1618	1638	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1654	1674	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Transmembrane	1748	1768	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50077	UniProtKB	Domain	1787	1822	.	.	.	Note=EF-hand;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P50077	UniProtKB	Modified residue	284	284	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P50077	UniProtKB	Sequence conflict	1185	1185	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50077	UniProtKB	Sequence conflict	1203	1203	.	.	.	Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00431 1 361
+P00431	UniProtKB	Transit peptide	1	67	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6257176;Dbxref=PMID:6257176	
+P00431	UniProtKB	Chain	68	361	.	.	.	ID=PRO_0000023634;Note=Cytochrome c peroxidase%2C mitochondrial	
+P00431	UniProtKB	Active site	119	119	.	.	.	Note=Proton acceptor	
+P00431	UniProtKB	Active site	258	258	.	.	.	Note=Tryptophan radical intermediate	
+P00431	UniProtKB	Metal binding	242	242	.	.	.	Note=Iron (heme axial ligand)	
+P00431	UniProtKB	Site	115	115	.	.	.	Note=Transition state stabilizer	
+P00431	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00431	UniProtKB	Natural variant	33	33	.	.	.	Note=In allele 2. A->AA	
+P00431	UniProtKB	Natural variant	120	120	.	.	.	Note=In allele 2. T->I	
+P00431	UniProtKB	Natural variant	219	219	.	.	.	Note=In allele 2. D->G	
+P00431	UniProtKB	Mutagenesis	258	258	.	.	.	Note=Substantially diminished activity. W->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2851317;Dbxref=PMID:2851317	
+P00431	UniProtKB	Sequence conflict	41	41	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00431	UniProtKB	Sequence conflict	62	62	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00431	UniProtKB	Sequence conflict	145	146	.	.	.	Note=ND->DN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00431	UniProtKB	Sequence conflict	231	231	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00431	UniProtKB	Sequence conflict	273	273	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00431	UniProtKB	Helix	83	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Turn	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IA8	
+P00431	UniProtKB	Helix	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Helix	110	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Turn	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Beta strand	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Helix	141	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Helix	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Turn	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Helix	153	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Beta strand	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B0Z	
+P00431	UniProtKB	Helix	171	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Helix	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Turn	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MKR	
+P00431	UniProtKB	Helix	218	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Turn	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Helix	232	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Helix	240	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Beta strand	244	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Helix	249	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Beta strand	256	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Beta strand	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M23	
+P00431	UniProtKB	Helix	268	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Beta strand	278	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Beta strand	284	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PCC	
+P00431	UniProtKB	Beta strand	288	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Turn	293	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMT	
+P00431	UniProtKB	Beta strand	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMT	
+P00431	UniProtKB	Helix	300	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Helix	309	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Helix	322	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+P00431	UniProtKB	Beta strand	345	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCN	
+P00431	UniProtKB	Helix	356	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O	
+##sequence-region Q7LHD1 1 136
+Q7LHD1	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q7LHD1	UniProtKB	Chain	19	115	.	.	.	ID=PRO_0000226148;Note=Putative covalently bound cell wall protein 22	
+Q7LHD1	UniProtKB	Propeptide	116	136	.	.	.	ID=PRO_0000226149;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q7LHD1	UniProtKB	Compositional bias	23	114	.	.	.	Note=Thr-rich	
+Q7LHD1	UniProtKB	Lipidation	115	115	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q7LHD1	UniProtKB	Glycosylation	21	21	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q7LHD1	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P21560 1 335
+P21560	UniProtKB	Transit peptide	1	38	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21560	UniProtKB	Chain	39	335	.	.	.	ID=PRO_0000004775;Note=Protein CBP3%2C mitochondrial	
+P21560	UniProtKB	Transmembrane	152	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P19073 1 191
+P19073	UniProtKB	Chain	1	188	.	.	.	ID=PRO_0000198955;Note=Cell division control protein 42	
+P19073	UniProtKB	Propeptide	189	191	.	.	.	ID=PRO_0000281285;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19073	UniProtKB	Nucleotide binding	10	17	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19073	UniProtKB	Nucleotide binding	57	61	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19073	UniProtKB	Nucleotide binding	115	118	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19073	UniProtKB	Motif	32	40	.	.	.	Note=Effector region;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19073	UniProtKB	Modified residue	188	188	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19073	UniProtKB	Lipidation	188	188	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19073	UniProtKB	Mutagenesis	12	12	.	.	.	Note=Enhances interaction with RGA1. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507	
+P19073	UniProtKB	Mutagenesis	58	58	.	.	.	Note=Temperature-sensitive mutant. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507	
+P19073	UniProtKB	Mutagenesis	61	61	.	.	.	Note=Enhances interaction with RGA1. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507	
+P19073	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Temperature-sensitive mutant. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507	
+P19073	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Temperature-sensitive mutant. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507	
+P19073	UniProtKB	Mutagenesis	118	118	.	.	.	Note=Dramatically reduces interaction with RGA1. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507	
+P19073	UniProtKB	Mutagenesis	142	142	.	.	.	Note=In CDC42-1%3B temperature-sensitive mutant. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507	
+P19073	UniProtKB	Mutagenesis	188	188	.	.	.	Note=Enhances interaction with RGA1. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507	
+P19073	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32458 1 415
+P32458	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P32458	UniProtKB	Chain	2	415	.	.	.	ID=PRO_0000173499;Note=Cell division control protein 11	
+P32458	UniProtKB	Domain	19	298	.	.	.	Note=Septin-type G	
+P32458	UniProtKB	Nucleotide binding	29	36	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32458	UniProtKB	Nucleotide binding	172	180	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32458	UniProtKB	Coiled coil	354	414	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32458	UniProtKB	Motif	12	19	.	.	.	Note=Basic motif	
+P32458	UniProtKB	Binding site	92	92	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32458	UniProtKB	Binding site	230	230	.	.	.	Note=GTP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32458	UniProtKB	Binding site	247	247	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32458	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P32458	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P32458	UniProtKB	Modified residue	305	305	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32458	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P32458	UniProtKB	Cross-link	412	412	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
+P32458	UniProtKB	Mutagenesis	12	16	.	.	.	Note=Loss of function%3B abolishes association with PI(4)P and PI(5)P. RKRKH->QQEQQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577	
+P32458	UniProtKB	Mutagenesis	12	16	.	.	.	Note=Loss of function%3B strongly decreases association with PI(4)P and PI(5)P. RKRKH->QQQQQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577	
+P32458	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Abolishes GTP-binding%3B no strong effect in vivo. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577	
+P32458	UniProtKB	Mutagenesis	32	32	.	.	.	Note=Abolishes GTP-binding%3B no strong effect in vivo. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577	
+P32458	UniProtKB	Mutagenesis	34	34	.	.	.	Note=Abolishes GTP-binding%3B no strong effect in vivo. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577	
+P32458	UniProtKB	Mutagenesis	35	35	.	.	.	Note=Abolishes GTP-binding%3B no strong effect in vivo. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577	
+P32458	UniProtKB	Mutagenesis	40	40	.	.	.	Note=Temperature-sensitive%3B no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius%3B abolishes interaction with itself. N->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577	
+P32458	UniProtKB	Mutagenesis	230	230	.	.	.	Note=Temperature-sensitive%3B no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577	
+P32458	UniProtKB	Mutagenesis	412	412	.	.	.	Note=Abolishes sumoylation in vitro. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719	
+P32458	UniProtKB	Beta strand	23	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Beta strand	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Turn	36	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Beta strand	69	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Beta strand	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Beta strand	85	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Helix	104	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Beta strand	137	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Beta strand	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Helix	151	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Turn	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Beta strand	166	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Helix	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Helix	178	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Beta strand	206	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Helix	213	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Beta strand	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Beta strand	263	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Helix	269	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+P32458	UniProtKB	Helix	287	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1	
+##sequence-region P14724 1 124
+P14724	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000089446;Note=Anaphase-promoting complex subunit CDC26	
+P14724	UniProtKB	Compositional bias	53	77	.	.	.	Note=Asp-rich	
+P14724	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14724	UniProtKB	Sequence conflict	50	50	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14724	UniProtKB	Sequence conflict	121	124	.	.	.	Note=IREE->TARNNSISAYAHAHAHAHASTFTFTYKISSL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P06101 1 506
+P06101	UniProtKB	Chain	1	506	.	.	.	ID=PRO_0000195067;Note=Hsp90 co-chaperone Cdc37	
+P06101	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:17220467;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198,PMID:17220467	
+P06101	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P06101	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P06101	UniProtKB	Modified residue	466	466	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P06101	UniProtKB	Modified residue	484	484	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P06101	UniProtKB	Mutagenesis	14	14	.	.	.	Note=Leads to osmosensitivity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17220467;Dbxref=PMID:17220467	
+P06101	UniProtKB	Sequence conflict	169	169	.	.	.	Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12018 1 815
+Q12018	UniProtKB	Chain	1	815	.	.	.	ID=PRO_0000119805;Note=Cell division control protein 53	
+Q12018	UniProtKB	Region	9	280	.	.	.	Note=Required for interaction with SKP1/CBF3D and F-box protein	
+Q12018	UniProtKB	Region	448	748	.	.	.	Note=Required for interaction with CDC34/UBC3	
+Q12018	UniProtKB	Cross-link	760	760	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13616	
+Q12018	UniProtKB	Mutagenesis	488	488	.	.	.	Note=Prevents CDC34/UBC3 interaction. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9499404;Dbxref=PMID:9499404	
+Q12018	UniProtKB	Helix	735	762	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P	
+Q12018	UniProtKB	Beta strand	763	766	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P	
+Q12018	UniProtKB	Helix	767	778	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P	
+Q12018	UniProtKB	Turn	779	781	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P	
+Q12018	UniProtKB	Helix	786	798	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P	
+Q12018	UniProtKB	Beta strand	801	804	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P	
+Q12018	UniProtKB	Beta strand	808	813	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P	
+##sequence-region P38910 1 106
+P38910	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38910	UniProtKB	Chain	2	106	.	.	.	ID=PRO_0000174922;Note=10 kDa heat shock protein%2C mitochondrial	
+P38910	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38910	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38910	UniProtKB	Sequence conflict	82	82	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47818 1 322
+P47818	UniProtKB	Chain	1	322	.	.	.	ID=PRO_0000089394;Note=Protein CCC1	
+P47818	UniProtKB	Topological domain	1	99	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47818	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47818	UniProtKB	Topological domain	121	129	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47818	UniProtKB	Transmembrane	130	150	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47818	UniProtKB	Topological domain	151	236	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47818	UniProtKB	Transmembrane	237	257	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47818	UniProtKB	Topological domain	258	259	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47818	UniProtKB	Transmembrane	260	280	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47818	UniProtKB	Topological domain	281	300	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47818	UniProtKB	Transmembrane	301	321	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47818	UniProtKB	Topological domain	322	322	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47818	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47818	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47818	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47818	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47818	UniProtKB	Modified residue	83	83	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P06182 1 269
+P06182	UniProtKB	Chain	1	269	.	.	.	ID=PRO_0000121718;Note=Cytochrome c heme lyase	
+P06182	UniProtKB	Repeat	25	30	.	.	.	Note=HRM 1	
+P06182	UniProtKB	Repeat	41	46	.	.	.	Note=HRM 2	
+##sequence-region P40202 1 249
+P40202	UniProtKB	Chain	1	249	.	.	.	ID=PRO_0000213542;Note=Superoxide dismutase 1 copper chaperone	
+P40202	UniProtKB	Domain	7	70	.	.	.	Note=HMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P40202	UniProtKB	Metal binding	16	16	.	.	.	Note=Zinc%3B shared with apo-SOD1;Ontology_term=ECO:0000244,ECO:0000255,ECO:0000269;evidence=ECO:0000244|PDB:1JK9,ECO:0000255|PROSITE-ProRule:PRU00280,ECO:0000269|PubMed:11524675;Dbxref=PMID:11524675	
+P40202	UniProtKB	Metal binding	17	17	.	.	.	Note=Copper 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P40202	UniProtKB	Metal binding	20	20	.	.	.	Note=Copper 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P40202	UniProtKB	Metal binding	229	229	.	.	.	Note=Copper 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P40202	UniProtKB	Metal binding	231	231	.	.	.	Note=Copper 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280	
+P40202	UniProtKB	Disulfide bond	27	64	.	.	.	Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1QUP,ECO:0000269|PubMed:7557423;Dbxref=PMID:7557423	
+P40202	UniProtKB	Disulfide bond	229	229	.	.	.	Note=Interchain (with C-58 in apo-SOD1);Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1JK9,ECO:0000269|PubMed:24374639;Dbxref=PMID:24374639	
+P40202	UniProtKB	Helix	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP	
+P40202	UniProtKB	Beta strand	7	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP	
+P40202	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK9	
+P40202	UniProtKB	Helix	20	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP	
+P40202	UniProtKB	Beta strand	34	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP	
+P40202	UniProtKB	Turn	41	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP	
+P40202	UniProtKB	Beta strand	45	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP	
+P40202	UniProtKB	Helix	54	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP	
+P40202	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP	
+P40202	UniProtKB	Beta strand	79	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Beta strand	100	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Beta strand	113	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Beta strand	127	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Helix	142	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Beta strand	148	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Beta strand	161	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Turn	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Beta strand	169	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Helix	182	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Turn	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Beta strand	188	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Helix	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Beta strand	202	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK9	
+P40202	UniProtKB	Beta strand	208	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8	
+P40202	UniProtKB	Beta strand	216	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP	
+P40202	UniProtKB	Helix	236	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK9	
+##sequence-region O13547 1 238
+O13547	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10322008;Dbxref=PMID:10322008	
+O13547	UniProtKB	Chain	23	217	.	.	.	ID=PRO_0000020881;Note=Covalently-linked cell wall protein 14	
+O13547	UniProtKB	Propeptide	218	238	.	.	.	ID=PRO_0000020882;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13547	UniProtKB	Compositional bias	77	215	.	.	.	Note=Ser-rich	
+O13547	UniProtKB	Lipidation	217	217	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13547	UniProtKB	Glycosylation	87	87	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13547	UniProtKB	Cross-link	161	161	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q00684 1 551
+Q00684	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000094875;Note=Tyrosine-protein phosphatase CDC14	
+Q00684	UniProtKB	Active site	283	283	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10044	
+Q00684	UniProtKB	Modified residue	467	467	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q00684	UniProtKB	Mutagenesis	253	253	.	.	.	Note=Inactivates catalytic activity and leads to substrate retention. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21127052;Dbxref=PMID:21127052	
+Q00684	UniProtKB	Mutagenesis	280	280	.	.	.	Note=Leads to temperature sensitivity. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21784165;Dbxref=PMID:21784165	
+Q00684	UniProtKB	Mutagenesis	283	283	.	.	.	Note=Inactivates catalytic activity and leads to substrate retention. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21127052;Dbxref=PMID:21127052	
+Q00684	UniProtKB	Sequence conflict	118	118	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P26309 1 610
+P26309	UniProtKB	Chain	1	610	.	.	.	ID=PRO_0000050903;Note=APC/C activator protein CDC20	
+P26309	UniProtKB	Repeat	257	296	.	.	.	Note=WD 1	
+P26309	UniProtKB	Repeat	299	338	.	.	.	Note=WD 2	
+P26309	UniProtKB	Repeat	342	379	.	.	.	Note=WD 3	
+P26309	UniProtKB	Repeat	383	422	.	.	.	Note=WD 4	
+P26309	UniProtKB	Repeat	425	467	.	.	.	Note=WD 5	
+P26309	UniProtKB	Repeat	469	519	.	.	.	Note=WD 6	
+P26309	UniProtKB	Repeat	523	562	.	.	.	Note=WD 7	
+P26309	UniProtKB	Motif	17	25	.	.	.	Note=D-box	
+P26309	UniProtKB	Motif	85	101	.	.	.	Note=Bipartite nuclear localization signal	
+P26309	UniProtKB	Motif	144	150	.	.	.	Note=C-box	
+P26309	UniProtKB	Motif	586	592	.	.	.	Note=KEN box;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P26309	UniProtKB	Mutagenesis	205	205	.	.	.	Note=Confers spindle checkpoint resistance and diminishes binding to MAD2 and MAD3. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461437;Dbxref=PMID:9461437	
+P26309	UniProtKB	Mutagenesis	209	209	.	.	.	Note=Confers spindle checkpoint resistance and diminishes binding to MAD2 and MAD3. P->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461437;Dbxref=PMID:9461437	
+P26309	UniProtKB	Mutagenesis	210	210	.	.	.	Note=Confers spindle checkpoint resistance and diminishes binding to MAD2 and MAD3. P->L%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461437;Dbxref=PMID:9461437	
+P26309	UniProtKB	Sequence conflict	318	319	.	.	.	Note=IG->MA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region O13297 1 549
+O13297	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+O13297	UniProtKB	Chain	2	549	.	.	.	ID=PRO_0000210119;Note=mRNA-capping enzyme subunit beta	
+O13297	UniProtKB	Active site	223	223	.	.	.	Note=N6-GMP-lysine intermediate	
+O13297	UniProtKB	Site	280	280	.	.	.	Note=Essential for dimer formation	
+O13297	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+O13297	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+O13297	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+O13297	UniProtKB	Mutagenesis	280	280	.	.	.	Note=Significant growth defects. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788946;Dbxref=PMID:12788946	
+O13297	UniProtKB	Mutagenesis	520	520	.	.	.	Note=No growth. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788946;Dbxref=PMID:12788946	
+O13297	UniProtKB	Mutagenesis	523	523	.	.	.	Note=Temperature sensitive growth phenotype. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788946;Dbxref=PMID:12788946	
+O13297	UniProtKB	Mutagenesis	524	524	.	.	.	Note=Temperature sensitive growth phenotype. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788946;Dbxref=PMID:12788946	
+O13297	UniProtKB	Sequence conflict	242	242	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+O13297	UniProtKB	Helix	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Turn	254	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+O13297	UniProtKB	Beta strand	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Helix	280	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Turn	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Helix	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	304	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	319	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	330	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	338	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Helix	345	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Helix	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Turn	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	368	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	391	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	405	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	425	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	437	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+O13297	UniProtKB	Helix	441	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	446	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8I	
+O13297	UniProtKB	Beta strand	453	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Helix	464	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	468	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Beta strand	488	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Helix	499	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Turn	508	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+O13297	UniProtKB	Helix	514	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H	
+##sequence-region P20437 1 546
+P20437	UniProtKB	Chain	1	546	.	.	.	ID=PRO_0000080411;Note=G1/S-specific cyclin CLN1	
+##sequence-region P29029 1 562
+P29029	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1918080,ECO:0000269|PubMed:9748433;Dbxref=PMID:1918080,PMID:9748433	
+P29029	UniProtKB	Chain	21	562	.	.	.	ID=PRO_0000011936;Note=Endochitinase	
+P29029	UniProtKB	Region	21	327	.	.	.	Note=Catalytic	
+P29029	UniProtKB	Region	481	562	.	.	.	Note=Chitin-binding%2C high affinity	
+P29029	UniProtKB	Compositional bias	328	480	.	.	.	Note=Ser/Thr-rich	
+P29029	UniProtKB	Active site	157	157	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10053	
+P29029	UniProtKB	Glycosylation	553	553	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29029	UniProtKB	Natural variant	16	16	.	.	.	Note=In strain: DBY939. L->P	
+P29029	UniProtKB	Natural variant	23	23	.	.	.	Note=In strain: DBY939 and SEY6210. R->S	
+P29029	UniProtKB	Natural variant	321	321	.	.	.	Note=In strain: DBY939. T->S	
+P29029	UniProtKB	Natural variant	336	340	.	.	.	Note=In strain: DBY939. Missing	
+P29029	UniProtKB	Natural variant	399	399	.	.	.	Note=In strain: DBY939. S->A	
+P29029	UniProtKB	Natural variant	433	434	.	.	.	Note=In strain: DBY939. PI->SL	
+P29029	UniProtKB	Natural variant	461	461	.	.	.	Note=In strain: DBY939. T->K	
+P29029	UniProtKB	Natural variant	477	481	.	.	.	Note=In strain: DBY939. Missing	
+P29029	UniProtKB	Sequence conflict	168	168	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29029	UniProtKB	Sequence conflict	168	168	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29029	UniProtKB	Beta strand	28	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Helix	44	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	54	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Turn	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Helix	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Helix	87	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	102	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	110	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY4	
+P29029	UniProtKB	Helix	119	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Turn	143	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	150	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Helix	164	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	189	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Turn	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Helix	198	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	207	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	219	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY5	
+P29029	UniProtKB	Helix	226	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	243	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	254	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Helix	263	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	279	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Helix	287	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+P29029	UniProtKB	Beta strand	294	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TXE	
+P29029	UniProtKB	Helix	300	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2	
+##sequence-region P32178 1 256
+P32178	UniProtKB	Chain	1	256	.	.	.	ID=PRO_0000119204;Note=Chorismate mutase	
+P32178	UniProtKB	Domain	3	255	.	.	.	Note=Chorismate mutase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00516	
+P32178	UniProtKB	Mutagenesis	226	226	.	.	.	Note=Constitutively activated and feedback-resistant. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2646272;Dbxref=PMID:2646272	
+P32178	UniProtKB	Helix	6	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	12	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CSM	
+P32178	UniProtKB	Helix	59	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	114	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	126	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Beta strand	130	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CSM	
+P32178	UniProtKB	Helix	140	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	161	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	173	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	185	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	195	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Beta strand	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CSM	
+P32178	UniProtKB	Helix	227	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Helix	238	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM	
+P32178	UniProtKB	Turn	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CSM	
+##sequence-region Q12114 1 671
+Q12114	UniProtKB	Chain	1	671	.	.	.	ID=PRO_0000089661;Note=Chitin biosynthesis protein CHS5	
+Q12114	UniProtKB	Domain	78	168	.	.	.	Note=Fibronectin type-III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316	
+Q12114	UniProtKB	Domain	166	262	.	.	.	Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+Q12114	UniProtKB	Compositional bias	279	635	.	.	.	Note=Glu-rich	
+Q12114	UniProtKB	Compositional bias	645	671	.	.	.	Note=Lys-rich	
+Q12114	UniProtKB	Modified residue	305	305	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12114	UniProtKB	Modified residue	338	338	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12114	UniProtKB	Modified residue	362	362	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12114	UniProtKB	Modified residue	365	365	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12114	UniProtKB	Modified residue	383	383	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12114	UniProtKB	Modified residue	384	384	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12114	UniProtKB	Modified residue	573	573	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12114	UniProtKB	Modified residue	579	579	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12114	UniProtKB	Modified residue	590	590	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12114	UniProtKB	Cross-link	584	584	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q12114	UniProtKB	Beta strand	4	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q12114	UniProtKB	Beta strand	19	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+Q12114	UniProtKB	Beta strand	27	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q12114	UniProtKB	Turn	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+Q12114	UniProtKB	Beta strand	44	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3	
+Q12114	UniProtKB	Helix	57	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+Q12114	UniProtKB	Beta strand	84	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Beta strand	94	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Beta strand	108	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Turn	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Beta strand	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Beta strand	142	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Beta strand	154	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Beta strand	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Helix	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Helix	189	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Beta strand	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Beta strand	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Helix	227	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Helix	243	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Helix	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Helix	266	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+Q12114	UniProtKB	Helix	279	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+##sequence-region P38843 1 316
+P38843	UniProtKB	Chain	1	316	.	.	.	ID=PRO_0000202922;Note=Chitin synthase export chaperone	
+P38843	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38843	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38843	UniProtKB	Transmembrane	130	150	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38843	UniProtKB	Transmembrane	170	190	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38843	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38843	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38843	UniProtKB	Transmembrane	266	286	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P35190 1 452
+P35190	UniProtKB	Chain	1	452	.	.	.	ID=PRO_0000080503;Note=PHO85 cyclin CLG1	
+P35190	UniProtKB	Compositional bias	395	401	.	.	.	Note=Poly-Gln	
+##sequence-region Q03654 1 590
+Q03654	UniProtKB	Chain	1	590	.	.	.	ID=PRO_0000197107;Note=Pre-mRNA-splicing factor CEF1	
+Q03654	UniProtKB	Domain	1	60	.	.	.	Note=HTH myb-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+Q03654	UniProtKB	Domain	63	110	.	.	.	Note=HTH myb-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+Q03654	UniProtKB	DNA binding	33	56	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+Q03654	UniProtKB	DNA binding	84	106	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+Q03654	UniProtKB	Region	460	490	.	.	.	Note=Interaction with PRP19 and self-interaction	
+Q03654	UniProtKB	Compositional bias	238	321	.	.	.	Note=Lys-rich	
+Q03654	UniProtKB	Mutagenesis	33	33	.	.	.	Note=No effect. Slower growth and thermosensitivity%3B when associated with G-84. Complete loss of function%3B when associated with G-52 and G-84. Complete loss of function%3B when associated with G-52%3B G-84 and G-102. W->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632794;Dbxref=PMID:9632794	
+Q03654	UniProtKB	Mutagenesis	52	52	.	.	.	Note=No effect. Slower growth and thermosensitivity%3B when associated with G-84. Complete loss of function%3B when associated with G-33 and G-84. Complete loss of function%3B when associated with G-33%3B G-84 and G-102. W->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11784857,ECO:0000269|PubMed:9632794;Dbxref=PMID:11784857,PMID:9632794	
+Q03654	UniProtKB	Mutagenesis	84	84	.	.	.	Note=No effect. Slower growth and thermosensitivity%3B when associated with G-33 or G-52. Complete loss of function%3B when associated with G-33 and G-52 or G-52 and Y-102. Complete loss of function%3B when associated with G-33%3B G-52 and G-102. W->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11784857,ECO:0000269|PubMed:9632794;Dbxref=PMID:11784857,PMID:9632794	
+Q03654	UniProtKB	Mutagenesis	102	102	.	.	.	Note=No effect. Slower growth and thermosensitivity%3B when associated with G-52 or G-84. Complete loss of function%3B when associated with G-33%3B G-52 and G-84. Y->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632794;Dbxref=PMID:9632794	
+Q03654	UniProtKB	Sequence conflict	11	11	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03654	UniProtKB	Sequence conflict	192	192	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03654	UniProtKB	Helix	15	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Helix	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Helix	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Helix	45	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Helix	67	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Beta strand	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Helix	86	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Helix	95	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Helix	146	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Helix	165	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Turn	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Helix	233	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Helix	483	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03654	UniProtKB	Helix	583	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region Q12102 1 859
+Q12102	UniProtKB	Chain	1	859	.	.	.	ID=PRO_0000076204;Note=Cleavage factor two protein 2	
+Q12102	UniProtKB	Beta strand	3	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	10	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	18	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	25	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Turn	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	40	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	70	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	78	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	86	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	91	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	110	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	121	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Turn	143	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	149	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	163	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	173	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	208	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	223	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	243	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Turn	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	253	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	279	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Turn	284	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	288	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	302	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	310	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Turn	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	323	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	328	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	338	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	346	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	362	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	375	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	405	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	631	633	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	640	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	653	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	666	672	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	673	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	679	683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	687	689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Helix	692	700	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	704	707	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+Q12102	UniProtKB	Beta strand	714	716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X	
+##sequence-region P24868 1 471
+P24868	UniProtKB	Chain	1	471	.	.	.	ID=PRO_0000080403;Note=G2/mitotic-specific cyclin-1	
+##sequence-region P24870 1 427
+P24870	UniProtKB	Chain	1	427	.	.	.	ID=PRO_0000080405;Note=G2/mitotic-specific cyclin-3	
+P24870	UniProtKB	Sequence conflict	48	48	.	.	.	Note=D->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P30283 1 435
+P30283	UniProtKB	Chain	1	435	.	.	.	ID=PRO_0000080408;Note=S-phase entry cyclin-5	
+##sequence-region P43634 1 648
+P43634	UniProtKB	Chain	1	648	.	.	.	ID=PRO_0000114942;Note=Activatory protein CHA4	
+P43634	UniProtKB	DNA binding	44	70	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P43634	UniProtKB	Compositional bias	32	35	.	.	.	Note=Poly-Asn	
+P43634	UniProtKB	Compositional bias	48	52	.	.	.	Note=Poly-Arg	
+P43634	UniProtKB	Compositional bias	105	109	.	.	.	Note=Poly-Ser	
+P43634	UniProtKB	Compositional bias	195	198	.	.	.	Note=Poly-Gln	
+P43634	UniProtKB	Compositional bias	302	306	.	.	.	Note=Poly-Ser	
+P43634	UniProtKB	Modified residue	164	164	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P43634	UniProtKB	Modified residue	166	166	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P22516 1 861
+P22516	UniProtKB	Chain	1	861	.	.	.	ID=PRO_0000055138;Note=ATP-dependent DNA helicase CHL1	
+P22516	UniProtKB	Domain	6	458	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P22516	UniProtKB	Nucleotide binding	42	49	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P22516	UniProtKB	Motif	393	396	.	.	.	Note=DEAH box	
+P22516	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22516	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22516	UniProtKB	Mutagenesis	47	47	.	.	.	Note=No ATPase activity%3B increase in chromosome missegregation. G->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931920;Dbxref=PMID:10931920	
+P22516	UniProtKB	Mutagenesis	48	48	.	.	.	Note=No ATPase activity%3B increase in chromosome missegregation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931920;Dbxref=PMID:10931920	
+##sequence-region Q08032 1 650
+Q08032	UniProtKB	Chain	1	650	.	.	.	ID=PRO_0000192819;Note=Cell division control protein 45	
+Q08032	UniProtKB	Modified residue	453	453	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08032	UniProtKB	Sequence conflict	576	576	.	.	.	Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07834 1 779
+P07834	UniProtKB	Chain	1	779	.	.	.	ID=PRO_0000050899;Note=Cell division control protein 4	
+P07834	UniProtKB	Domain	272	319	.	.	.	Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080	
+P07834	UniProtKB	Repeat	380	408	.	.	.	Note=WD 1	
+P07834	UniProtKB	Repeat	420	449	.	.	.	Note=WD 2	
+P07834	UniProtKB	Repeat	461	493	.	.	.	Note=WD 3	
+P07834	UniProtKB	Repeat	528	556	.	.	.	Note=WD 4	
+P07834	UniProtKB	Repeat	568	598	.	.	.	Note=WD 5	
+P07834	UniProtKB	Repeat	630	658	.	.	.	Note=WD 6	
+P07834	UniProtKB	Repeat	669	698	.	.	.	Note=WD 7	
+P07834	UniProtKB	Motif	82	85	.	.	.	Note=Nuclear localization signal	
+P07834	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07834	UniProtKB	Mutagenesis	82	82	.	.	.	Note=Prevents nuclear localization%3B when associated with A-83 and A-85. K->A	
+P07834	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Prevents nuclear localization%3B when associated with A-82 and A-85. R->A	
+P07834	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Prevents nuclear localization. R->G	
+P07834	UniProtKB	Mutagenesis	85	85	.	.	.	Note=Prevents nuclear localization%3B when associated with A-82 and A-83. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11080155;Dbxref=PMID:11080155	
+P07834	UniProtKB	Sequence conflict	460	460	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07834	UniProtKB	Helix	228	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P63	
+P07834	UniProtKB	Helix	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P63	
+P07834	UniProtKB	Helix	242	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P63	
+P07834	UniProtKB	Helix	256	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P63	
+P07834	UniProtKB	Helix	274	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Helix	280	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Helix	292	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Helix	303	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Helix	313	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Turn	328	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Helix	331	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Helix	347	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	373	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	381	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	385	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	394	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	404	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Turn	409	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	413	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	425	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Turn	432	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKS	
+P07834	UniProtKB	Beta strand	435	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	445	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Turn	450	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	454	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	466	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	478	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	489	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	509	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Helix	516	518	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	522	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	533	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	542	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	552	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Turn	557	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	561	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	573	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Turn	580	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	584	589	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	594	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	624	628	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	635	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	642	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	652	658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Turn	659	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	664	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	676	681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	683	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	693	698	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Turn	699	701	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	704	707	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Turn	709	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	714	722	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	725	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P07834	UniProtKB	Beta strand	735	742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+##sequence-region P32562 1 705
+P32562	UniProtKB	Chain	1	705	.	.	.	ID=PRO_0000085762;Note=Cell cycle serine/threonine-protein kinase CDC5/MSD2	
+P32562	UniProtKB	Domain	82	337	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32562	UniProtKB	Domain	520	587	.	.	.	Note=POLO box 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00154	
+P32562	UniProtKB	Domain	619	692	.	.	.	Note=POLO box 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00154	
+P32562	UniProtKB	Nucleotide binding	88	96	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32562	UniProtKB	Active site	204	204	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P32562	UniProtKB	Binding site	110	110	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32562	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32562	UniProtKB	Modified residue	419	419	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P36012 1 229
+P36012	UniProtKB	Chain	1	229	.	.	.	ID=PRO_0000221376;Note=Histone H3-like centromeric protein CSE4	
+P36012	UniProtKB	Region	132	229	.	.	.	Note=H3-like	
+P36012	UniProtKB	Motif	115	132	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36012	UniProtKB	Compositional bias	1	66	.	.	.	Note=Ser-rich	
+P36012	UniProtKB	Mutagenesis	176	176	.	.	.	Note=In CSE4-102%3B impairs nuclear division by disrupting the core centromere structure%3B when associated with T-218. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891506;Dbxref=PMID:10891506	
+P36012	UniProtKB	Mutagenesis	194	194	.	.	.	Note=In CSE4-111%3B impairs nuclear division by disrupting the core centromere structure. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891506;Dbxref=PMID:10891506	
+P36012	UniProtKB	Mutagenesis	197	197	.	.	.	Note=In CSE4-110%3B impairs nuclear division by disrupting the core centromere structure. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891506;Dbxref=PMID:10891506	
+P36012	UniProtKB	Mutagenesis	218	218	.	.	.	Note=In CSE4-102%3B impairs nuclear division by disrupting the core centromere structure%3B when associated with S-176. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891506;Dbxref=PMID:10891506	
+P36012	UniProtKB	Helix	157	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LY8	
+P36012	UniProtKB	Helix	180	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LY8	
+P36012	UniProtKB	Turn	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LY8	
+P36012	UniProtKB	Helix	214	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LY8	
+##sequence-region Q03705 1 181
+Q03705	UniProtKB	Chain	1	181	.	.	.	ID=PRO_0000203259;Note=EKC/KEOPS complex subunit CGI121	
+Q03705	UniProtKB	Beta strand	2	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Beta strand	9	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Helix	25	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Turn	31	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW5	
+Q03705	UniProtKB	Turn	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XAH	
+Q03705	UniProtKB	Beta strand	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Helix	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Helix	50	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Beta strand	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Helix	74	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Beta strand	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Helix	88	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Beta strand	104	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Beta strand	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW9	
+Q03705	UniProtKB	Helix	118	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Beta strand	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Helix	138	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Helix	147	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+Q03705	UniProtKB	Helix	165	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7	
+##sequence-region P24871 1 460
+P24871	UniProtKB	Chain	1	460	.	.	.	ID=PRO_0000080406;Note=G2/mitotic-specific cyclin-4	
+P24871	UniProtKB	Sequence conflict	255	255	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24871	UniProtKB	Sequence conflict	318	318	.	.	.	Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24871	UniProtKB	Sequence conflict	328	328	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38221 1 457
+P38221	UniProtKB	Chain	1	457	.	.	.	ID=PRO_0000090722;Note=Phosphatidate cytidylyltransferase	
+P38221	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38221	UniProtKB	Transmembrane	154	174	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38221	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38221	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38221	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38221	UniProtKB	Transmembrane	330	350	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38221	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Reduced enzyme level. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8910557;Dbxref=PMID:8910557	
+##sequence-region P39525 1 442
+P39525	UniProtKB	Chain	1	442	.	.	.	ID=PRO_0000180356;Note=3-oxoacyl-[acyl-carrier-protein] synthase homolog	
+P39525	UniProtKB	Active site	187	187	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10022	
+##sequence-region P40558 1 293
+P40558	UniProtKB	Chain	1	293	.	.	.	ID=PRO_0000184952;Note=Cytosolic Fe-S cluster assembly factor CFD1	
+P40558	UniProtKB	Nucleotide binding	25	32	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03039	
+P40558	UniProtKB	Metal binding	201	201	.	.	.	Note=Iron-sulfur (4Fe-4S)%3B shared with dimeric partner	
+P40558	UniProtKB	Metal binding	204	204	.	.	.	Note=Iron-sulfur (4Fe-4S)%3B shared with dimeric partner	
+P40558	UniProtKB	Modified residue	291	291	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40558	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Loss of function. K->A	
+P40558	UniProtKB	Mutagenesis	86	86	.	.	.	Note=Loss of function. T->A	
+P40558	UniProtKB	Mutagenesis	182	182	.	.	.	Note=Does not impair function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766	
+P40558	UniProtKB	Mutagenesis	201	201	.	.	.	Note=Loss of function and disrupts heterotetramer formation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766	
+P40558	UniProtKB	Mutagenesis	204	204	.	.	.	Note=Loss of function and disrupts heterotetramer formation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766	
+P40558	UniProtKB	Mutagenesis	207	207	.	.	.	Note=Does not impair function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766	
+##sequence-region P32656 1 232
+P32656	UniProtKB	Chain	1	232	.	.	.	ID=PRO_0000202657;Note=Glutathione-specific gamma-glutamylcyclotransferase	
+P32656	UniProtKB	Region	10	15	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75223	
+P32656	UniProtKB	Active site	115	115	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75223	
+P32656	UniProtKB	Mutagenesis	115	115	.	.	.	Note=Loss of catalytic activity against glutathione. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23070364;Dbxref=PMID:23070364	
+P32656	UniProtKB	Beta strand	8	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Helix	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Beta strand	25	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Beta strand	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Beta strand	54	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Helix	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Helix	69	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Helix	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Beta strand	91	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Helix	101	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Turn	115	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWI	
+P32656	UniProtKB	Beta strand	119	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Helix	135	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Turn	149	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWI	
+P32656	UniProtKB	Beta strand	154	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Helix	176	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Helix	193	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+P32656	UniProtKB	Helix	219	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK	
+##sequence-region Q05583 1 330
+Q05583	UniProtKB	Chain	1	330	.	.	.	ID=PRO_0000253806;Note=Cytosolic iron-sulfur protein assembly protein 1	
+Q05583	UniProtKB	Repeat	12	53	.	.	.	Note=WD 1	
+Q05583	UniProtKB	Repeat	56	95	.	.	.	Note=WD 2	
+Q05583	UniProtKB	Repeat	105	144	.	.	.	Note=WD 3	
+Q05583	UniProtKB	Repeat	151	190	.	.	.	Note=WD 4	
+Q05583	UniProtKB	Repeat	195	236	.	.	.	Note=WD 5	
+Q05583	UniProtKB	Repeat	248	286	.	.	.	Note=WD 6	
+Q05583	UniProtKB	Repeat	292	330	.	.	.	Note=WD 7	
+Q05583	UniProtKB	Mutagenesis	127	127	.	.	.	Note=Impaired in cytosolic Fe/S protein assembly. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17937914;Dbxref=PMID:17937914	
+Q05583	UniProtKB	Beta strand	5	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	17	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	26	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	36	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	47	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	61	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	70	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	82	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	98	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	110	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	121	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	131	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	144	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	156	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	163	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	177	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	186	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	200	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	208	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	213	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	223	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	237	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	253	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	264	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	273	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	282	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Turn	292	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	298	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	312	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+Q05583	UniProtKB	Beta strand	319	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES	
+##sequence-region P53280 1 1122
+P53280	UniProtKB	Chain	1	1122	.	.	.	ID=PRO_0000202824;Note=Protein CAF130	
+P53280	UniProtKB	Modified residue	1042	1042	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32943 1 380
+P32943	UniProtKB	Chain	1	380	.	.	.	ID=PRO_0000080409;Note=S-phase entry cyclin-6	
+P32943	UniProtKB	Sequence conflict	77	77	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32943	UniProtKB	Sequence conflict	92	92	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32943	UniProtKB	Sequence conflict	109	109	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32943	UniProtKB	Sequence conflict	223	223	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P08004 1 1131
+P08004	UniProtKB	Chain	1	1131	.	.	.	ID=PRO_0000193727;Note=Chitin synthase 1	
+P08004	UniProtKB	Transmembrane	795	815	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08004	UniProtKB	Transmembrane	833	853	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08004	UniProtKB	Transmembrane	866	886	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08004	UniProtKB	Transmembrane	914	934	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08004	UniProtKB	Transmembrane	942	962	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08004	UniProtKB	Transmembrane	1042	1062	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08004	UniProtKB	Transmembrane	1101	1121	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08004	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P08004	UniProtKB	Modified residue	35	35	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08004	UniProtKB	Modified residue	270	270	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P08004	UniProtKB	Modified residue	299	299	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P08004	UniProtKB	Modified residue	318	318	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P08004	UniProtKB	Modified residue	328	328	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P08004	UniProtKB	Modified residue	358	358	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P08004	UniProtKB	Sequence conflict	815	815	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08004	UniProtKB	Sequence conflict	815	815	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P14180 1 963
+P14180	UniProtKB	Chain	1	963	.	.	.	ID=PRO_0000193728;Note=Chitin synthase 2	
+P14180	UniProtKB	Topological domain	1	643	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Transmembrane	644	664	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Topological domain	665	677	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Transmembrane	678	698	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Topological domain	699	711	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Transmembrane	712	732	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Topological domain	733	743	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Transmembrane	744	764	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Topological domain	765	775	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Transmembrane	776	796	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Topological domain	797	875	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Transmembrane	876	896	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Topological domain	897	905	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Transmembrane	906	926	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Topological domain	927	963	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14180	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14180	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14180	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14180	UniProtKB	Modified residue	133	133	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14180	UniProtKB	Modified residue	217	217	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P14180	UniProtKB	Glycosylation	22	22	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Glycosylation	197	197	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Glycosylation	447	447	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14180	UniProtKB	Mutagenesis	197	197	.	.	.	Note=30%25 decrease of activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	312	312	.	.	.	Note=20%25 increase of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	355	355	.	.	.	Note=10%25 decrease of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	393	393	.	.	.	Note=5%25 decrease of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	441	441	.	.	.	Note=Loss of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	441	441	.	.	.	Note=Loss of activity. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	447	447	.	.	.	Note=80%25 decrease of activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	490	490	.	.	.	Note=70%25 decrease of activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	492	492	.	.	.	Note=80%25 decrease of activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	493	493	.	.	.	Note=90%25 decrease of activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	494	494	.	.	.	Note=95%25 decrease of activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	497	497	.	.	.	Note=95%25 decrease of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	502	502	.	.	.	Note=90%25 decrease of activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	505	505	.	.	.	Note=80%25 decrease of activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	506	506	.	.	.	Note=20%25 increase of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	508	508	.	.	.	Note=60%25 decrease of activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	509	509	.	.	.	Note=70%25 decrease of activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	514	514	.	.	.	Note=80%25 decrease of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	515	515	.	.	.	Note=90%25 decrease of activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	516	516	.	.	.	Note=95%25 decrease of activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	521	521	.	.	.	Note=Loss of activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	522	522	.	.	.	Note=60%25 decrease of activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	537	537	.	.	.	Note=No change in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	550	550	.	.	.	Note=85%25 decrease of activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	556	556	.	.	.	Note=95%25 decrease of activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	559	559	.	.	.	Note=95%25 decrease of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	561	561	.	.	.	Note=Loss of activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	561	561	.	.	.	Note=65%25 decrease of activity. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	561	561	.	.	.	Note=Loss of activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	562	562	.	.	.	Note=Loss of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	562	562	.	.	.	Note=Loss of activity. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	562	562	.	.	.	Note=Loss of activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	563	563	.	.	.	Note=Loss of activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	563	563	.	.	.	Note=94%25 decrease of activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	565	565	.	.	.	Note=95%25 decrease of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	589	589	.	.	.	Note=70%25 decrease of activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	592	592	.	.	.	Note=70%25 decrease of activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	601	601	.	.	.	Note=Loss of activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	601	601	.	.	.	Note=Loss of activity. Q->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	602	603	.	.	.	Note=Loss of activity. RR->KK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	602	602	.	.	.	Note=Loss of activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	602	602	.	.	.	Note=95%25 decrease of activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	603	603	.	.	.	Note=Loss of activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	603	603	.	.	.	Note=57%25 decrease of activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	604	604	.	.	.	Note=Loss of activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	604	604	.	.	.	Note=Loss of activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	605	605	.	.	.	Note=Loss of activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	605	605	.	.	.	Note=Loss of activity. W->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+P14180	UniProtKB	Mutagenesis	607	607	.	.	.	Note=95%25 decrease of activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457	
+##sequence-region P38147 1 527
+P38147	UniProtKB	Chain	1	527	.	.	.	ID=PRO_0000085857;Note=Serine/threonine-protein kinase CHK1	
+P38147	UniProtKB	Domain	15	281	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38147	UniProtKB	Nucleotide binding	21	29	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38147	UniProtKB	Active site	142	142	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P38147	UniProtKB	Binding site	45	45	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region P38907 1 458
+P38907	UniProtKB	Chain	1	458	.	.	.	ID=PRO_0000089646;Note=Central kinetochore subunit CHL4	
+P38907	UniProtKB	Beta strand	383	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38907	UniProtKB	Beta strand	396	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38907	UniProtKB	Helix	409	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38907	UniProtKB	Helix	424	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38907	UniProtKB	Turn	429	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38907	UniProtKB	Beta strand	440	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38907	UniProtKB	Beta strand	446	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+##sequence-region P40955 1 746
+P40955	UniProtKB	Chain	1	746	.	.	.	ID=PRO_0000089662;Note=Chitin biosynthesis protein CHS6	
+P40955	UniProtKB	Region	734	746	.	.	.	Note=CHS5-binding	
+P40955	UniProtKB	Helix	32	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	53	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	77	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	91	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	107	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	131	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Turn	139	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	143	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	155	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	173	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	212	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	227	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Turn	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	245	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	249	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	265	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	283	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	301	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	315	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	319	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	327	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	353	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	371	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	387	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Turn	424	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	435	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	450	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	459	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	473	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Turn	477	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	489	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Turn	495	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	500	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	509	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	517	519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	522	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	585	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	605	608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8	
+P40955	UniProtKB	Helix	613	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	629	642	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	646	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Beta strand	663	665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	671	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	694	707	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	709	718	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+P40955	UniProtKB	Helix	724	740	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+##sequence-region P20486 1 150
+P20486	UniProtKB	Chain	1	150	.	.	.	ID=PRO_0000206245;Note=Cyclin-dependent kinases regulatory subunit	
+P20486	UniProtKB	Compositional bias	118	133	.	.	.	Note=Poly-Gln	
+P20486	UniProtKB	Helix	15	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2	
+P20486	UniProtKB	Helix	23	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2	
+P20486	UniProtKB	Beta strand	37	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2	
+P20486	UniProtKB	Helix	48	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2	
+P20486	UniProtKB	Helix	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2	
+P20486	UniProtKB	Turn	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2	
+P20486	UniProtKB	Beta strand	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2	
+P20486	UniProtKB	Helix	71	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2	
+P20486	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2	
+P20486	UniProtKB	Beta strand	97	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2	
+P20486	UniProtKB	Turn	106	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2	
+##sequence-region P53264 1 445
+P53264	UniProtKB	Transit peptide	1	39	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53264	UniProtKB	Chain	40	445	.	.	.	ID=PRO_0000202813;Note=Cardiolipin-specific deacylase 1%2C mitochondrial	
+P53264	UniProtKB	Domain	142	430	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53264	UniProtKB	Motif	424	429	.	.	.	Note=HXXXXD motif	
+##sequence-region P38323 1 520
+P38323	UniProtKB	Transit peptide	1	13	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38323	UniProtKB	Chain	14	520	.	.	.	ID=PRO_0000160569;Note=ATP-dependent clpX-like chaperone%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38323	UniProtKB	Nucleotide binding	140	147	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00499	
+P38323	UniProtKB	Mutagenesis	174	174	.	.	.	Note=Abrogates unfolding activity of unfoldase. Mildly increased ATPase activity. Reduces ALA synthesis. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25957689;Dbxref=PMID:25957689	
+P38323	UniProtKB	Mutagenesis	206	206	.	.	.	Note=Blocks ATP hydrolysis. E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:25957689;Dbxref=PMID:25957689	
+##sequence-region P33313 1 385
+P33313	UniProtKB	Chain	1	385	.	.	.	ID=PRO_0000106279;Note=Hsp70/Hsp90 co-chaperone CNS1	
+P33313	UniProtKB	Repeat	83	116	.	.	.	Note=TPR 1	
+P33313	UniProtKB	Repeat	121	154	.	.	.	Note=TPR 2	
+P33313	UniProtKB	Repeat	155	189	.	.	.	Note=TPR 3	
+P33313	UniProtKB	Mutagenesis	90	90	.	.	.	Note=In CNS1-1%3B disrupts interaction with Hsp90%2C temperature-sensitive defect impairing Hsp90-dependent function. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788914;Dbxref=PMID:12788914	
+P33313	UniProtKB	Mutagenesis	140	140	.	.	.	Note=In CNS1-2%3B disrupts interaction with Hsp90%2C temperature-sensitive defect impairing Hsp90-dependent function. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788914;Dbxref=PMID:12788914	
+P33313	UniProtKB	Mutagenesis	260	260	.	.	.	Note=In CNS1-3%3B temperature-sensitive defect impairing Hsp90-dependent function%3B when associated with G-324 and S-330. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788914;Dbxref=PMID:12788914	
+P33313	UniProtKB	Mutagenesis	324	324	.	.	.	Note=In CNS1-3%3B temperature-sensitive defect impairing Hsp90-dependent function%3B when associated with G-260 and S-330. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788914;Dbxref=PMID:12788914	
+P33313	UniProtKB	Mutagenesis	330	330	.	.	.	Note=In CNS1-3%3B temperature-sensitive defect impairing Hsp90-dependent function%3B when associated with G-260 and G-324. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788914;Dbxref=PMID:12788914	
+P33313	UniProtKB	Sequence conflict	6	13	.	.	.	Note=ANGGYTKP->RQMEDIPNQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q3E823 1 68
+Q3E823	UniProtKB	Chain	1	68	.	.	.	ID=PRO_0000238657;Note=Cytochrome c oxidase assembly factor 2	
+##sequence-region Q3E7B2 1 85
+Q3E7B2	UniProtKB	Chain	1	85	.	.	.	ID=PRO_0000245412;Note=Cytochrome c oxidase assembly factor 3%2C mitochondrial	
+Q3E7B2	UniProtKB	Topological domain	1	26	.	.	.	Note=Mitochondrial matrix	
+Q3E7B2	UniProtKB	Transmembrane	27	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E7B2	UniProtKB	Topological domain	50	85	.	.	.	Note=Mitochondrial intermembrane	
+##sequence-region Q3E846 1 104
+Q3E846	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000247793;Note=Cytochrome c oxidase assembly factor 6	
+Q3E846	UniProtKB	Domain	22	76	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E846	UniProtKB	Motif	25	35	.	.	.	Note=Cx9C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E846	UniProtKB	Motif	57	68	.	.	.	Note=Cx10C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E846	UniProtKB	Disulfide bond	25	68	.	.	.	Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000305|PubMed:20922212;Dbxref=PMID:20922212	
+Q3E846	UniProtKB	Disulfide bond	35	57	.	.	.	Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000305|PubMed:20922212;Dbxref=PMID:20922212	
+Q3E846	UniProtKB	Mutagenesis	25	25	.	.	.	Note=Loss of function. Localizes correctly to the mitochondrion%2C but reduces the steady-state level of the protein in the mitochondrial fraction. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24549041;Dbxref=PMID:24549041	
+Q3E846	UniProtKB	Mutagenesis	26	26	.	.	.	Note=Loss of function. Localizes correctly to the mitochondrion%2C but severely reduces the steady-state level of the protein in the mitochondrial fraction. W->C	
+Q3E846	UniProtKB	Mutagenesis	35	35	.	.	.	Note=Loss of function. Localizes correctly to the mitochondrion%2C but reduces the steady-state level of the protein in the mitochondrial fraction. C->A	
+Q3E846	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Loss of function. Localizes correctly to the mitochondrion%2C but reduces the steady-state level of the protein in the mitochondrial fraction. C->A	
+Q3E846	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Loss of function. Localizes correctly to the mitochondrion%2C but severely reduces the steady-state level of the protein in the mitochondrial fraction. C->A	
+##sequence-region Q12309 1 687
+Q12309	UniProtKB	Chain	1	687	.	.	.	ID=PRO_0000205753;Note=Pre-mRNA-splicing factor CLF1	
+Q12309	UniProtKB	Repeat	45	77	.	.	.	Note=HAT 1	
+Q12309	UniProtKB	Repeat	79	111	.	.	.	Note=HAT 2	
+Q12309	UniProtKB	Repeat	113	145	.	.	.	Note=HAT 3	
+Q12309	UniProtKB	Repeat	147	178	.	.	.	Note=HAT 4	
+Q12309	UniProtKB	Repeat	180	211	.	.	.	Note=HAT 5	
+Q12309	UniProtKB	Repeat	213	247	.	.	.	Note=HAT 6	
+Q12309	UniProtKB	Repeat	251	283	.	.	.	Note=HAT 7	
+Q12309	UniProtKB	Repeat	300	332	.	.	.	Note=HAT 8	
+Q12309	UniProtKB	Repeat	337	369	.	.	.	Note=HAT 9	
+Q12309	UniProtKB	Repeat	383	416	.	.	.	Note=HAT 10	
+Q12309	UniProtKB	Repeat	451	483	.	.	.	Note=HAT 11	
+Q12309	UniProtKB	Repeat	525	557	.	.	.	Note=HAT 12	
+Q12309	UniProtKB	Repeat	629	661	.	.	.	Note=HAT 13	
+Q12309	UniProtKB	Helix	40	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	65	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	81	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	99	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	115	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	133	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Turn	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	149	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	166	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	182	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	199	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	215	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	240	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12309	UniProtKB	Helix	260	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region Q08685 1 445
+Q08685	UniProtKB	Chain	1	445	.	.	.	ID=PRO_0000076211;Note=mRNA cleavage and polyadenylation factor CLP1	
+Q08685	UniProtKB	Nucleotide binding	133	138	.	.	.	Note=ATP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03035,ECO:0000269|PubMed:17151076;Dbxref=PMID:17151076	
+Q08685	UniProtKB	Binding site	33	33	.	.	.	Note=ATP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03035,ECO:0000269|PubMed:17151076;Dbxref=PMID:17151076	
+Q08685	UniProtKB	Binding site	72	72	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03035,ECO:0000269|PubMed:17151076;Dbxref=PMID:17151076	
+Q08685	UniProtKB	Mutagenesis	136	136	.	.	.	Note=Completely abolishes interaction with PCF11. No effect on growth%3B when associated with A-137. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22216186;Dbxref=PMID:22216186	
+Q08685	UniProtKB	Mutagenesis	137	137	.	.	.	Note=Completely abolishes interaction with PCF11. No effect on growth%3B when associated with A-136. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22216186;Dbxref=PMID:22216186	
+Q08685	UniProtKB	Mutagenesis	161	161	.	.	.	Note=Compromises interaction with PCF11. No effect on growth. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18648070,ECO:0000269|PubMed:22216186;Dbxref=PMID:18648070,PMID:22216186	
+Q08685	UniProtKB	Beta strand	24	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	43	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	65	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	72	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	81	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Turn	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	96	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	103	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	125	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	136	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NPI	
+Q08685	UniProtKB	Beta strand	156	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	172	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	206	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	219	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	241	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	248	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	255	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	263	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	276	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	286	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	304	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	318	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Turn	337	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NPI	
+Q08685	UniProtKB	Beta strand	344	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	350	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	355	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	361	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	371	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	378	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	384	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Helix	397	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	405	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Turn	416	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	420	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+Q08685	UniProtKB	Beta strand	434	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+##sequence-region P32657 1 1468
+P32657	UniProtKB	Chain	1	1468	.	.	.	ID=PRO_0000080237;Note=Chromo domain-containing protein 1	
+P32657	UniProtKB	Domain	195	257	.	.	.	Note=Chromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00053	
+P32657	UniProtKB	Domain	285	350	.	.	.	Note=Chromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00053	
+P32657	UniProtKB	Domain	388	562	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32657	UniProtKB	Domain	699	860	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P32657	UniProtKB	Nucleotide binding	401	408	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32657	UniProtKB	Motif	513	516	.	.	.	Note=DEAH box	
+P32657	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32657	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32657	UniProtKB	Modified residue	987	987	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32657	UniProtKB	Modified residue	989	989	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32657	UniProtKB	Modified residue	1336	1336	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32657	UniProtKB	Modified residue	1364	1364	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32657	UniProtKB	Modified residue	1372	1372	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32657	UniProtKB	Cross-link	1144	1144	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P32657	UniProtKB	Mutagenesis	220	220	.	.	.	Note=No interaction with methylated histone H3 'K-4'. E->L%2CW;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15647753,ECO:0000269|PubMed:17433364;Dbxref=PMID:15647753,PMID:17433364	
+P32657	UniProtKB	Mutagenesis	222	222	.	.	.	Note=Confers interaction with methylated histone H3 'K-4'. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15647753;Dbxref=PMID:15647753	
+P32657	UniProtKB	Mutagenesis	314	314	.	.	.	Note=No effect on interaction with methylated histone H3 'K-4'. L->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15647753;Dbxref=PMID:15647753	
+P32657	UniProtKB	Mutagenesis	316	316	.	.	.	Note=Disrupts interaction with methylated histone H3 'K-4'%3B abrogates histone acetylation activity of SLIK. Y->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15647753;Dbxref=PMID:15647753	
+P32657	UniProtKB	Beta strand	179	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Turn	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DY7	
+P32657	UniProtKB	Helix	193	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Helix	204	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Beta strand	211	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Helix	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Beta strand	226	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Helix	230	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Beta strand	234	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DY7	
+P32657	UniProtKB	Helix	239	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Helix	251	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Helix	264	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Beta strand	286	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Beta strand	299	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DY8	
+P32657	UniProtKB	Beta strand	303	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Beta strand	320	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Helix	324	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Helix	332	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E	
+P32657	UniProtKB	Helix	1012	1025	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Helix	1029	1031	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TED	
+P32657	UniProtKB	Helix	1032	1037	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Helix	1046	1091	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Beta strand	1092	1094	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Beta strand	1096	1098	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TED	
+P32657	UniProtKB	Beta strand	1101	1103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TED	
+P32657	UniProtKB	Helix	1104	1112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Beta strand	1119	1122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TED	
+P32657	UniProtKB	Beta strand	1125	1129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TED	
+P32657	UniProtKB	Helix	1130	1150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Helix	1155	1157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Beta strand	1171	1173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Helix	1177	1190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Helix	1195	1200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Turn	1202	1204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Helix	1207	1209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Helix	1250	1264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+P32657	UniProtKB	Turn	1265	1268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0	
+##sequence-region Q06350 1 511
+Q06350	UniProtKB	Signal peptide	1	34	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06350	UniProtKB	Chain	35	511	.	.	.	ID=PRO_0000011937;Note=Sporulation-specific chitinase 2	
+Q06350	UniProtKB	Active site	223	223	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10053	
+Q06350	UniProtKB	Glycosylation	147	147	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06350	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06350	UniProtKB	Glycosylation	456	456	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06350	UniProtKB	Glycosylation	472	472	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P05374 1 869
+P05374	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P05374	UniProtKB	Chain	2	869	.	.	.	ID=PRO_0000058304;Note=Phosphatidylethanolamine N-methyltransferase	
+P05374	UniProtKB	Topological domain	2	55	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217	
+P05374	UniProtKB	Topological domain	77	86	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Transmembrane	87	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217	
+P05374	UniProtKB	Topological domain	108	187	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217	
+P05374	UniProtKB	Topological domain	209	212	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Transmembrane	213	233	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217	
+P05374	UniProtKB	Topological domain	234	258	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Transmembrane	259	279	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217	
+P05374	UniProtKB	Topological domain	280	291	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Transmembrane	292	310	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217	
+P05374	UniProtKB	Topological domain	311	362	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Transmembrane	363	383	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217	
+P05374	UniProtKB	Topological domain	384	389	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Transmembrane	390	410	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217	
+P05374	UniProtKB	Topological domain	411	439	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Transmembrane	440	460	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217	
+P05374	UniProtKB	Topological domain	461	463	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Transmembrane	464	484	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217	
+P05374	UniProtKB	Topological domain	485	534	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Transmembrane	535	555	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217	
+P05374	UniProtKB	Topological domain	556	869	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P05374	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P29465 1 1165
+P29465	UniProtKB	Chain	1	1165	.	.	.	ID=PRO_0000193729;Note=Chitin synthase 3	
+P29465	UniProtKB	Topological domain	1	170	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P29465	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29465	UniProtKB	Topological domain	192	202	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P29465	UniProtKB	Transmembrane	203	223	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29465	UniProtKB	Topological domain	224	452	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P29465	UniProtKB	Transmembrane	453	473	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29465	UniProtKB	Topological domain	474	1006	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P29465	UniProtKB	Transmembrane	1007	1027	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29465	UniProtKB	Topological domain	1028	1029	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P29465	UniProtKB	Transmembrane	1030	1050	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29465	UniProtKB	Topological domain	1051	1055	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P29465	UniProtKB	Transmembrane	1056	1076	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29465	UniProtKB	Topological domain	1077	1080	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P29465	UniProtKB	Transmembrane	1081	1101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29465	UniProtKB	Topological domain	1102	1165	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P29465	UniProtKB	Modified residue	537	537	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P29465	UniProtKB	Modified residue	538	538	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P29465	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P29465	UniProtKB	Glycosylation	114	114	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P29465	UniProtKB	Glycosylation	152	152	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P29465	UniProtKB	Glycosylation	163	163	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P29465	UniProtKB	Glycosylation	303	303	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P29465	UniProtKB	Glycosylation	332	332	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P29465	UniProtKB	Glycosylation	371	371	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P29465	UniProtKB	Cross-link	136	136	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P29465	UniProtKB	Mutagenesis	991	991	.	.	.	Note=Reduces catalytic activity by 67%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183	
+P29465	UniProtKB	Mutagenesis	993	993	.	.	.	Note=Reduces catalytic activity by 89%25. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183	
+P29465	UniProtKB	Mutagenesis	994	994	.	.	.	Note=Completely abolishes catalytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183	
+P29465	UniProtKB	Mutagenesis	995	995	.	.	.	Note=Reduces catalytic activity by 87%25. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183	
+P29465	UniProtKB	Mutagenesis	999	999	.	.	.	Note=Reduces catalytic activity by 59%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183	
+P29465	UniProtKB	Sequence conflict	1163	1163	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29465	UniProtKB	Helix	13	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW	
+##sequence-region P40019 1 153
+P40019	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40019	UniProtKB	Chain	2	153	.	.	.	ID=PRO_0000202623;Note=Histone H2A.Z-specific chaperone CHZ1	
+P40019	UniProtKB	Region	87	108	.	.	.	Note=Important for H2A.Z-H2B binding	
+P40019	UniProtKB	Compositional bias	32	36	.	.	.	Note=Poly-Arg	
+P40019	UniProtKB	Compositional bias	84	89	.	.	.	Note=Poly-Glu	
+P40019	UniProtKB	Compositional bias	138	150	.	.	.	Note=Asp/Glu-rich (acidic)	
+P40019	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40019	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40019	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40019	UniProtKB	Helix	75	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JSS	
+P40019	UniProtKB	Helix	86	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JSS	
+P40019	UniProtKB	Helix	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JSS	
+P40019	UniProtKB	Turn	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JSS	
+P40019	UniProtKB	Helix	116	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JSS	
+##sequence-region P43635 1 486
+P43635	UniProtKB	Transit peptide	1	23	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43635	UniProtKB	Chain	24	486	.	.	.	ID=PRO_0000169985;Note=Citrate synthase 3%2C mitochondrial	
+P43635	UniProtKB	Motif	484	486	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43635	UniProtKB	Active site	315	315	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117	
+P43635	UniProtKB	Active site	361	361	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117	
+P43635	UniProtKB	Active site	419	419	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117	
+##sequence-region Q07897 1 291
+Q07897	UniProtKB	Chain	1	291	.	.	.	ID=PRO_0000247153;Note=Protein CMS1	
+Q07897	UniProtKB	Compositional bias	43	51	.	.	.	Note=Poly-Asp	
+Q07897	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q01649 1 594
+Q01649	UniProtKB	Chain	1	594	.	.	.	ID=PRO_0000089750;Note=Spindle pole body-associated protein CIK1	
+Q01649	UniProtKB	Coiled coil	81	360	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40987 1 1014
+P40987	UniProtKB	Chain	1	1014	.	.	.	ID=PRO_0000089761;Note=Chromosome instability protein 1	
+##sequence-region P27895 1 1000
+P27895	UniProtKB	Chain	1	1000	.	.	.	ID=PRO_0000125367;Note=Kinesin-like protein CIN8	
+P27895	UniProtKB	Domain	36	477	.	.	.	Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P27895	UniProtKB	Nucleotide binding	128	135	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P27895	UniProtKB	Coiled coil	518	615	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27895	UniProtKB	Coiled coil	860	904	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27895	UniProtKB	Modified residue	972	972	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P27895	UniProtKB	Sequence conflict	216	216	.	.	.	Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27895	UniProtKB	Sequence conflict	216	216	.	.	.	Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27895	UniProtKB	Sequence conflict	793	793	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27895	UniProtKB	Sequence conflict	793	793	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P48562 1 842
+P48562	UniProtKB	Chain	1	842	.	.	.	ID=PRO_0000085865;Note=Serine/threonine-protein kinase CLA4	
+P48562	UniProtKB	Domain	61	179	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P48562	UniProtKB	Domain	184	197	.	.	.	Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057	
+P48562	UniProtKB	Domain	546	825	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P48562	UniProtKB	Nucleotide binding	552	560	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P48562	UniProtKB	Compositional bias	136	144	.	.	.	Note=Poly-Ser	
+P48562	UniProtKB	Compositional bias	372	387	.	.	.	Note=Poly-Gln	
+P48562	UniProtKB	Active site	693	693	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P48562	UniProtKB	Binding site	594	594	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P48562	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48562	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P48562	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P48562	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48562	UniProtKB	Modified residue	425	425	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P48562	UniProtKB	Sequence conflict	390	390	.	.	.	Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P22137 1 1653
+P22137	UniProtKB	Chain	1	1653	.	.	.	ID=PRO_0000205785;Note=Clathrin heavy chain	
+P22137	UniProtKB	Repeat	543	689	.	.	.	Note=CHCR 1	
+P22137	UniProtKB	Repeat	692	834	.	.	.	Note=CHCR 2	
+P22137	UniProtKB	Repeat	839	978	.	.	.	Note=CHCR 3	
+P22137	UniProtKB	Repeat	985	1130	.	.	.	Note=CHCR 4	
+P22137	UniProtKB	Repeat	1134	1275	.	.	.	Note=CHCR 5	
+P22137	UniProtKB	Repeat	1280	1426	.	.	.	Note=CHCR 6	
+P22137	UniProtKB	Repeat	1429	1572	.	.	.	Note=CHCR 7	
+P22137	UniProtKB	Region	1	483	.	.	.	Note=Globular terminal domain	
+P22137	UniProtKB	Region	23	66	.	.	.	Note=WD40-like repeat 1	
+P22137	UniProtKB	Region	67	107	.	.	.	Note=WD40-like repeat 2	
+P22137	UniProtKB	Region	108	152	.	.	.	Note=WD40-like repeat 3	
+P22137	UniProtKB	Region	153	198	.	.	.	Note=WD40-like repeat 4	
+P22137	UniProtKB	Region	199	263	.	.	.	Note=WD40-like repeat 5	
+P22137	UniProtKB	Region	264	307	.	.	.	Note=WD40-like repeat 6	
+P22137	UniProtKB	Region	308	336	.	.	.	Note=WD40-like repeat 7	
+P22137	UniProtKB	Region	453	469	.	.	.	Note=Binding site for the uncoating ATPase%2C involved in lattice disassembly;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22137	UniProtKB	Region	484	527	.	.	.	Note=Flexible linker	
+P22137	UniProtKB	Region	528	1653	.	.	.	Note=Heavy chain arm	
+P22137	UniProtKB	Region	1219	1528	.	.	.	Note=Involved in binding clathrin light chain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22137	UniProtKB	Cross-link	1107	1107	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region D6W196 1 494
+D6W196	UniProtKB	Chain	1	494	.	.	.	ID=PRO_0000402277;Note=Truncated non-functional calcium-binding mitochondrial carrier SAL1-1	
+D6W196	UniProtKB	Transmembrane	231	248	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6W196	UniProtKB	Transmembrane	307	326	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6W196	UniProtKB	Transmembrane	355	368	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6W196	UniProtKB	Transmembrane	409	428	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6W196	UniProtKB	Transmembrane	458	475	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6W196	UniProtKB	Domain	11	46	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+D6W196	UniProtKB	Domain	80	115	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+D6W196	UniProtKB	Domain	120	155	.	.	.	Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+D6W196	UniProtKB	Domain	156	191	.	.	.	Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+D6W196	UniProtKB	Repeat	225	332	.	.	.	Note=Solcar 1	
+D6W196	UniProtKB	Repeat	345	434	.	.	.	Note=Solcar 2	
+D6W196	UniProtKB	Repeat	452	494	.	.	.	Note=Solcar 3%3B truncated	
+D6W196	UniProtKB	Calcium binding	59	70	.	.	.	Note=1	
+D6W196	UniProtKB	Calcium binding	93	104	.	.	.	Note=2	
+D6W196	UniProtKB	Calcium binding	155	166	.	.	.	Note=3	
+D6W196	UniProtKB	Sequence conflict	131	131	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08058 1 207
+Q08058	UniProtKB	Transit peptide	1	39	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08058	UniProtKB	Chain	40	207	.	.	.	ID=PRO_0000227688;Note=Coenzyme Q-binding protein COQ10%2C mitochondrial	
+##sequence-region P53318 1 479
+P53318	UniProtKB	Transit peptide	1	17	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03193	
+P53318	UniProtKB	Chain	18	479	.	.	.	ID=PRO_0000207581;Note=Ubiquinone biosynthesis monooxygenase COQ6%2C mitochondrial	
+P53318	UniProtKB	Mutagenesis	202	202	.	.	.	Note=Accumulates ubiquinone biosynthesis intermediates lacking the C5-ring hydroxyl. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21944752;Dbxref=PMID:21944752	
+P53318	UniProtKB	Mutagenesis	386	386	.	.	.	Note=Accumulates ubiquinone biosynthesis intermediates lacking the C5-ring hydroxyl%3B when associated with D-388. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21944752;Dbxref=PMID:21944752	
+P53318	UniProtKB	Mutagenesis	388	388	.	.	.	Note=Accumulates ubiquinone biosynthesis intermediates lacking the C5-ring hydroxyl%3B when associated with A-386. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21944752;Dbxref=PMID:21944752	
+P53318	UniProtKB	Sequence conflict	60	60	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53318	UniProtKB	Sequence conflict	68	68	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53318	UniProtKB	Sequence conflict	313	313	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05779 1 260
+Q05779	UniProtKB	Region	189	192	.	.	.	Note=Lipid binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75208	
+Q05779	UniProtKB	Mutagenesis	135	135	.	.	.	Note=Inability to grow on nonfermentable carbon sources. L->E%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443	
+Q05779	UniProtKB	Mutagenesis	174	174	.	.	.	Note=Impaired ability to grow on nonfermentable carbon sources. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443	
+Q05779	UniProtKB	Mutagenesis	185	185	.	.	.	Note=Inability to grow on nonfermentable carbon sources. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443	
+Q05779	UniProtKB	Mutagenesis	188	188	.	.	.	Note=Inability to grow on nonfermentable carbon sources. W->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443	
+Q05779	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Impaired ability to grow on nonfermentable carbon sources. Y->D%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443	
+Q05779	UniProtKB	Mutagenesis	204	204	.	.	.	Note=Impaired ability to grow on nonfermentable carbon sources. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443	
+##sequence-region Q06156 1 1176
+Q06156	UniProtKB	Chain	1	1176	.	.	.	ID=PRO_0000095046;Note=Condensin complex subunit 1	
+Q06156	UniProtKB	Modified residue	464	464	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06156	UniProtKB	Modified residue	475	475	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53079 1 417
+P53079	UniProtKB	Chain	1	417	.	.	.	ID=PRO_0000213494;Note=Conserved oligomeric Golgi complex subunit 1	
+P53079	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53079	UniProtKB	Modified residue	305	305	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38779 1 376
+P38779	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000202895;Note=Proteasome-interacting protein CIC1	
+P38779	UniProtKB	Region	310	376	.	.	.	Note=Required for interaction with CDC4	
+##sequence-region P00890 1 479
+P00890	UniProtKB	Transit peptide	1	37	.	.	.	Note=Mitochondrion	
+P00890	UniProtKB	Chain	38	479	.	.	.	ID=PRO_0000005479;Note=Citrate synthase%2C mitochondrial	
+P00890	UniProtKB	Active site	312	312	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117	
+P00890	UniProtKB	Active site	358	358	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117	
+P00890	UniProtKB	Active site	413	413	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117	
+P00890	UniProtKB	Sequence conflict	58	58	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00890	UniProtKB	Sequence conflict	78	78	.	.	.	Note=E->EE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q3E7A9 1 73
+Q3E7A9	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000247790;Note=Cx9C motif-containing protein 4%2C mitochondrial	
+Q3E7A9	UniProtKB	Domain	2	44	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E7A9	UniProtKB	Motif	5	15	.	.	.	Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E7A9	UniProtKB	Motif	26	36	.	.	.	Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E7A9	UniProtKB	Disulfide bond	5	36	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E7A9	UniProtKB	Disulfide bond	15	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+##sequence-region Q12510 1 522
+Q12510	UniProtKB	Chain	1	522	.	.	.	ID=PRO_0000240874;Note=DNA damage-binding protein CMR1	
+Q12510	UniProtKB	Repeat	183	224	.	.	.	Note=WD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12510	UniProtKB	Repeat	239	281	.	.	.	Note=WD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12510	UniProtKB	Repeat	287	327	.	.	.	Note=WD 3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12510	UniProtKB	Repeat	331	371	.	.	.	Note=WD 4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12510	UniProtKB	Repeat	388	427	.	.	.	Note=WD 5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12510	UniProtKB	Repeat	442	481	.	.	.	Note=WD 6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12510	UniProtKB	Repeat	482	521	.	.	.	Note=WD 7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12510	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12510	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q12510	UniProtKB	Modified residue	224	224	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q06680 1 1035
+Q06680	UniProtKB	Chain	1	1035	.	.	.	ID=PRO_0000095048;Note=Condensin complex subunit 3	
+Q06680	UniProtKB	Repeat	113	150	.	.	.	Note=HEAT 1	
+Q06680	UniProtKB	Repeat	153	191	.	.	.	Note=HEAT 2	
+Q06680	UniProtKB	Repeat	201	239	.	.	.	Note=HEAT 3	
+Q06680	UniProtKB	Repeat	597	635	.	.	.	Note=HEAT 4	
+Q06680	UniProtKB	Repeat	827	864	.	.	.	Note=HEAT 5	
+Q06680	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06680	UniProtKB	Modified residue	933	933	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06680	UniProtKB	Modified residue	981	981	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q06680	UniProtKB	Modified residue	1008	1008	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P39110 1 191
+P39110	UniProtKB	Chain	1	191	.	.	.	ID=PRO_0000122464;Note=GTP-binding protein CIN4	
+P39110	UniProtKB	Nucleotide binding	23	30	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39110	UniProtKB	Nucleotide binding	69	73	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39110	UniProtKB	Nucleotide binding	131	134	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P47001 1 227
+P47001	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10438739;Dbxref=PMID:10438739	
+P47001	UniProtKB	Propeptide	22	64	.	.	.	ID=PRO_0000033258;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10438739,ECO:0000269|PubMed:12776183,ECO:0000269|PubMed:12898712,ECO:0000269|PubMed:16495216,ECO:0000269|PubMed:9301021,ECO:0000269|PubMed:9748433;Dbxref=PMID:10438739,PMID:12776183,PMID:12898712,PMID:16495216,PMID:9301021,PMID:9748433	
+P47001	UniProtKB	Chain	65	227	.	.	.	ID=PRO_0000033259;Note=Cell wall mannoprotein CIS3	
+P47001	UniProtKB	Repeat	65	78	.	.	.	Note=PIR1/2/3	
+P47001	UniProtKB	Site	64	65	.	.	.	Note=Cleavage%3B by KEX2	
+P47001	UniProtKB	Site	74	74	.	.	.	Note=Covalent attachment to cell wall glycan	
+P47001	UniProtKB	Glycosylation	68	68	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216	
+P47001	UniProtKB	Glycosylation	78	78	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216	
+P47001	UniProtKB	Glycosylation	105	105	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183	
+P47001	UniProtKB	Glycosylation	106	106	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183	
+P47001	UniProtKB	Glycosylation	107	107	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183	
+P47001	UniProtKB	Glycosylation	109	109	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183	
+P47001	UniProtKB	Glycosylation	111	111	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183	
+P47001	UniProtKB	Glycosylation	112	112	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183	
+P47001	UniProtKB	Glycosylation	113	113	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183	
+P47001	UniProtKB	Glycosylation	114	114	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47001	UniProtKB	Glycosylation	116	116	.	.	.	Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183	
+P47001	UniProtKB	Glycosylation	117	117	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183	
+P47001	UniProtKB	Glycosylation	118	118	.	.	.	Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183	
+P47001	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Does not affect cell wall incorporation. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216	
+P47001	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Does not affect cell wall incorporation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216	
+P47001	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Results in complete loss of cell wall incorporation. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216	
+P47001	UniProtKB	Mutagenesis	72	72	.	.	.	Note=Results in complete loss of cell wall incorporation. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216	
+P47001	UniProtKB	Mutagenesis	74	74	.	.	.	Note=Results in complete loss of cell wall incorporation. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216	
+P47001	UniProtKB	Mutagenesis	76	76	.	.	.	Note=Results in complete loss of cell wall incorporation. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216	
+P47001	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Does not affect cell wall incorporation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216	
+P47001	UniProtKB	Mutagenesis	79	79	.	.	.	Note=Does not affect cell wall incorporation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216	
+P47001	UniProtKB	Mutagenesis	82	82	.	.	.	Note=Does not affect cell wall incorporation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216	
+P47001	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Does not affect cell wall incorporation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12898712;Dbxref=PMID:12898712	
+P47001	UniProtKB	Mutagenesis	197	197	.	.	.	Note=Results in the incorporation of KEX2-unprocessed precursor protein into the cell wall. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12898712;Dbxref=PMID:12898712	
+P47001	UniProtKB	Mutagenesis	208	227	.	.	.	Note=In PIR4t18%3B destabilizes the protein. QNVAEQCSAIHLEAVSLVDC->LDC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12898712;Dbxref=PMID:12898712	
+P47001	UniProtKB	Mutagenesis	227	227	.	.	.	Note=Does not affect cell wall incorporation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12898712;Dbxref=PMID:12898712	
+P47001	UniProtKB	Sequence conflict	43	44	.	.	.	Note=AA->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47001	UniProtKB	Sequence conflict	68	68	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47001	UniProtKB	Sequence conflict	88	88	.	.	.	Note=S->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03690 1 1277
+Q03690	UniProtKB	Chain	1	1277	.	.	.	ID=PRO_0000123557;Note=Clustered mitochondria protein 1	
+Q03690	UniProtKB	Domain	339	596	.	.	.	Note=Clu;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01167	
+Q03690	UniProtKB	Repeat	704	738	.	.	.	Note=TPR 1	
+Q03690	UniProtKB	Repeat	1020	1053	.	.	.	Note=TPR 2	
+Q03690	UniProtKB	Repeat	1148	1181	.	.	.	Note=TPR 3	
+Q03690	UniProtKB	Modified residue	1247	1247	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P53865 1 581
+P53865	UniProtKB	Chain	1	581	.	.	.	ID=PRO_0000089973;Note=Chaotic nuclear migration protein 67	
+P53865	UniProtKB	Coiled coil	179	252	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53865	UniProtKB	Coiled coil	306	363	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53865	UniProtKB	Coiled coil	373	451	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53865	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53865	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53865	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53865	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53865	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53865	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53865	UniProtKB	Helix	429	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7	
+P53865	UniProtKB	Helix	449	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7	
+P53865	UniProtKB	Helix	455	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7	
+P53865	UniProtKB	Helix	467	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7	
+P53865	UniProtKB	Helix	475	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7	
+P53865	UniProtKB	Helix	483	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7	
+P53865	UniProtKB	Helix	501	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7	
+P53865	UniProtKB	Helix	504	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7	
+P53865	UniProtKB	Helix	518	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7	
+P53865	UniProtKB	Helix	540	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7	
+P53865	UniProtKB	Helix	563	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7	
+##sequence-region P41810 1 973
+P41810	UniProtKB	Chain	1	973	.	.	.	ID=PRO_0000193839;Note=Coatomer subunit beta	
+P41810	UniProtKB	Repeat	98	133	.	.	.	Note=HEAT 1	
+P41810	UniProtKB	Repeat	134	170	.	.	.	Note=HEAT 2	
+P41810	UniProtKB	Repeat	279	317	.	.	.	Note=HEAT 3	
+P41810	UniProtKB	Repeat	318	354	.	.	.	Note=HEAT 4	
+P41810	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P41810	UniProtKB	Modified residue	540	540	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P41810	UniProtKB	Mutagenesis	334	336	.	.	.	Note=Loses ability to recognize arginine (R)-based ER localization signals in proteins. Recognition of C-terminal di-lysine signals present in proteins is unimpaired. DLD->NAN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17954604;Dbxref=PMID:17954604	
+P41810	UniProtKB	Sequence conflict	412	412	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40509 1 296
+P40509	UniProtKB	Chain	1	296	.	.	.	ID=PRO_0000193856;Note=Coatomer subunit epsilon	
+P40509	UniProtKB	Helix	4	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Turn	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	31	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Beta strand	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	57	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	73	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Turn	78	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	86	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	102	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Turn	114	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3	
+P40509	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3	
+P40509	UniProtKB	Helix	121	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	138	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	154	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Turn	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	182	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	197	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	213	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	226	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Turn	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Beta strand	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	240	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	259	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P40509	UniProtKB	Helix	273	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+##sequence-region O13525 1 335
+O13525	UniProtKB	Transit peptide	1	10	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03111	
+O13525	UniProtKB	Chain	11	335	.	.	.	ID=PRO_0000006035;Note=Ubiquinone biosynthesis protein COQ4%2C mitochondrial	
+O13525	UniProtKB	Mutagenesis	120	120	.	.	.	Note=In COQ4-3%3B abolishes coenzyme Q biosynthesis%2C but does not affect stability of other COQ polypeptides. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19022396;Dbxref=PMID:19022396	
+O13525	UniProtKB	Mutagenesis	121	121	.	.	.	Note=In COQ4-2%3B abolishes coenzyme Q biosynthesis%2C but does not affect stability of other COQ polypeptides. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19022396;Dbxref=PMID:19022396	
+O13525	UniProtKB	Mutagenesis	226	226	.	.	.	Note=In COQ4-1%3B abolishes coenzyme Q biosynthesis%2C but does not affect stability of other COQ polypeptides. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11469793,ECO:0000269|PubMed:19022396;Dbxref=PMID:11469793,PMID:19022396	
+##sequence-region P41735 1 233
+P41735	UniProtKB	Transit peptide	1	15	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194	
+P41735	UniProtKB	Chain	16	233	.	.	.	ID=PRO_0000089330;Note=5-demethoxyubiquinone hydroxylase%2C mitochondrial	
+P41735	UniProtKB	Metal binding	63	63	.	.	.	Note=Iron 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194	
+P41735	UniProtKB	Metal binding	95	95	.	.	.	Note=Iron 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194	
+P41735	UniProtKB	Metal binding	95	95	.	.	.	Note=Iron 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194	
+P41735	UniProtKB	Metal binding	98	98	.	.	.	Note=Iron 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194	
+P41735	UniProtKB	Metal binding	147	147	.	.	.	Note=Iron 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194	
+P41735	UniProtKB	Metal binding	194	194	.	.	.	Note=Iron 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194	
+P41735	UniProtKB	Metal binding	194	194	.	.	.	Note=Iron 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194	
+P41735	UniProtKB	Metal binding	197	197	.	.	.	Note=Iron 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194	
+P41735	UniProtKB	Mutagenesis	194	194	.	.	.	Note=Lacks ubiquinone and accumulates the intermediate DMQH2%2C causing respiratory deficiency. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624818;Dbxref=PMID:16624818	
+##sequence-region Q01519 1 83
+Q01519	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1331057,ECO:0000269|PubMed:1331058;Dbxref=PMID:1331057,PMID:1331058	
+Q01519	UniProtKB	Chain	2	83	.	.	.	ID=PRO_0000194925;Note=Cytochrome c oxidase subunit 6B	
+Q01519	UniProtKB	Domain	24	67	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q01519	UniProtKB	Motif	27	37	.	.	.	Note=Cx9C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q01519	UniProtKB	Motif	48	59	.	.	.	Note=Cx10C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q01519	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+Q01519	UniProtKB	Disulfide bond	27	59	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q01519	UniProtKB	Disulfide bond	37	48	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+##sequence-region Q03048 1 143
+Q03048	UniProtKB	Chain	1	143	.	.	.	ID=PRO_0000214915;Note=Cofilin	
+Q03048	UniProtKB	Domain	5	137	.	.	.	Note=ADF-H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00599	
+Q03048	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03048	UniProtKB	Mutagenesis	105	106	.	.	.	Note=Reduced interaction with PIP2. KD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11747431;Dbxref=PMID:11747431	
+Q03048	UniProtKB	Mutagenesis	109	110	.	.	.	Note=Defects in actin monomer interaction. RR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11747431;Dbxref=PMID:11747431	
+Q03048	UniProtKB	Sequence conflict	1	5	.	.	.	Note=MSRSG->MWGKKFIRSQENVKFLCS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03048	UniProtKB	Helix	10	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF	
+Q03048	UniProtKB	Beta strand	26	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF	
+Q03048	UniProtKB	Beta strand	36	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF	
+Q03048	UniProtKB	Helix	50	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF	
+Q03048	UniProtKB	Beta strand	63	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF	
+Q03048	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CFY	
+Q03048	UniProtKB	Beta strand	80	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF	
+Q03048	UniProtKB	Beta strand	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPV	
+Q03048	UniProtKB	Helix	95	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF	
+Q03048	UniProtKB	Beta strand	117	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF	
+Q03048	UniProtKB	Helix	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF	
+Q03048	UniProtKB	Helix	129	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF	
+##sequence-region P53622 1 1201
+P53622	UniProtKB	Chain	1	1201	.	.	.	ID=PRO_0000050910;Note=Coatomer subunit alpha	
+P53622	UniProtKB	Repeat	9	39	.	.	.	Note=WD 1	
+P53622	UniProtKB	Repeat	51	81	.	.	.	Note=WD 2	
+P53622	UniProtKB	Repeat	93	123	.	.	.	Note=WD 3	
+P53622	UniProtKB	Repeat	135	165	.	.	.	Note=WD 4	
+P53622	UniProtKB	Repeat	207	237	.	.	.	Note=WD 5	
+P53622	UniProtKB	Repeat	251	281	.	.	.	Note=WD 6	
+P53622	UniProtKB	Sequence conflict	753	753	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53622	UniProtKB	Sequence conflict	753	753	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53622	UniProtKB	Sequence conflict	905	905	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53622	UniProtKB	Sequence conflict	905	905	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53622	UniProtKB	Sequence conflict	1006	1006	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53622	UniProtKB	Sequence conflict	1006	1006	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53622	UniProtKB	Sequence conflict	1027	1028	.	.	.	Note=DA->NT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53622	UniProtKB	Sequence conflict	1027	1028	.	.	.	Note=DA->NT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53622	UniProtKB	Helix	649	658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ	
+P53622	UniProtKB	Helix	662	672	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ	
+P53622	UniProtKB	Helix	675	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ	
+P53622	UniProtKB	Helix	691	700	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ	
+P53622	UniProtKB	Helix	704	714	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ	
+P53622	UniProtKB	Helix	717	729	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ	
+P53622	UniProtKB	Helix	733	743	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ	
+P53622	UniProtKB	Helix	746	755	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ	
+P53622	UniProtKB	Helix	759	768	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ	
+P53622	UniProtKB	Helix	772	781	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ	
+P53622	UniProtKB	Helix	786	788	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ	
+P53622	UniProtKB	Helix	900	907	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	911	916	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	920	931	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	937	939	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	940	949	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Beta strand	951	954	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Beta strand	957	961	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3	
+P53622	UniProtKB	Beta strand	964	967	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Beta strand	969	971	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Beta strand	973	975	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	977	979	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	987	1002	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	1006	1021	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Beta strand	1025	1027	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3	
+P53622	UniProtKB	Helix	1029	1055	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Turn	1059	1061	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3	
+P53622	UniProtKB	Helix	1062	1071	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	1072	1074	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	1079	1095	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	1099	1110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	1117	1130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Beta strand	1147	1149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Turn	1151	1153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Beta strand	1156	1161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Beta strand	1163	1165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Turn	1167	1169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Beta strand	1172	1174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Helix	1175	1177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Beta strand	1179	1181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3	
+P53622	UniProtKB	Beta strand	1183	1186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2	
+P53622	UniProtKB	Beta strand	1188	1191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3	
+##sequence-region P00401 1 534
+P00401	UniProtKB	Chain	1	534	.	.	.	ID=PRO_0000183432;Note=Cytochrome c oxidase subunit 1	
+P00401	UniProtKB	Transmembrane	16	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Transmembrane	58	80	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Transmembrane	101	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Transmembrane	148	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Transmembrane	183	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Transmembrane	237	259	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Transmembrane	266	288	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Transmembrane	303	325	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Transmembrane	337	359	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Transmembrane	374	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Transmembrane	409	431	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Transmembrane	451	473	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00401	UniProtKB	Metal binding	62	62	.	.	.	Note=Iron (heme A axial ligand);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Metal binding	241	241	.	.	.	Note=Copper B;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Metal binding	245	245	.	.	.	Note=Copper B;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Metal binding	290	290	.	.	.	Note=Copper B;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Metal binding	291	291	.	.	.	Note=Copper B;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Metal binding	376	376	.	.	.	Note=Iron (heme A3 axial ligand);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Metal binding	378	378	.	.	.	Note=Iron (heme A axial ligand);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Cross-link	241	245	.	.	.	Note=1'-histidyl-3'-tyrosine (His-Tyr);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00401	UniProtKB	Sequence conflict	57	57	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Sequence conflict	69	69	.	.	.	Note=F->CT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Sequence conflict	224	224	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Sequence conflict	328	328	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Sequence conflict	378	378	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Sequence conflict	479	485	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Sequence conflict	492	492	.	.	.	Note=N->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00401	UniProtKB	Sequence conflict	496	510	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32344 1 111
+P32344	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000097136;Note=Mitochondrial mRNA-processing protein COX24	
+P32344	UniProtKB	Compositional bias	82	111	.	.	.	Note=Arg/Lys-rich (basic)	
+##sequence-region P38287 1 376
+P38287	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000079395;Note=Mannosyl phosphorylinositol ceramide synthase CSH1	
+P38287	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38287	UniProtKB	Transmembrane	274	294	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38287	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P43639 1 278
+P43639	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P43639	UniProtKB	Chain	2	278	.	.	.	ID=PRO_0000068257;Note=Casein kinase II subunit beta	
+P43639	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P43639	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+##sequence-region P46946 1 345
+P46946	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000097565;Note=DNA endonuclease SAE2	
+P46946	UniProtKB	Region	21	172	.	.	.	Note=DNA-binding	
+P46946	UniProtKB	Modified residue	143	143	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46946	UniProtKB	Modified residue	267	267	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18716619,ECO:0000269|PubMed:20150422;Dbxref=PMID:18716619,PMID:20150422	
+P46946	UniProtKB	Mutagenesis	72	72	.	.	.	Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-73%2C A-75%2C A-76 and A-90. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15121837;Dbxref=PMID:15121837	
+P46946	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-73%2C A-75%2C A-76 and A-90. Abolishes DNA damage-induced phosphorylation and function in DNA repair%3B when associated with A-90%2C A-249%2C A-279 and A-289. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15121837,ECO:0000269|PubMed:16861895,ECO:0000269|PubMed:18670132;Dbxref=PMID:15121837,PMID:16861895,PMID:18670132	
+P46946	UniProtKB	Mutagenesis	75	75	.	.	.	Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-72%2C A-75%2C A-76 and A-90. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15121837;Dbxref=PMID:15121837	
+P46946	UniProtKB	Mutagenesis	76	76	.	.	.	Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-72%2C A-73%2C A-75 and A-90. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15121837;Dbxref=PMID:15121837	
+P46946	UniProtKB	Mutagenesis	90	90	.	.	.	Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-72%2C A-73%2C A-75 and A-76. Abolishes DNA damage-induced phosphorylation and function in DNA repair%3B when associated with A-73%2C A-249%2C A-279 and A-289. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15121837,ECO:0000269|PubMed:16861895,ECO:0000269|PubMed:18670132;Dbxref=PMID:15121837,PMID:16861895,PMID:18670132	
+P46946	UniProtKB	Mutagenesis	223	223	.	.	.	Note=Leads to camptothecin hypersensitivity and loss of function%3B when associated with A-225. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18716619;Dbxref=PMID:18716619	
+P46946	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Leads to camptothecin hypersensitivity and loss of function%3B when associated with A-223. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18716619;Dbxref=PMID:18716619	
+P46946	UniProtKB	Mutagenesis	249	249	.	.	.	Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-278%2C A-279%2C and A-289. Abolishes DNA damage-induced phosphorylation and function in DNA repair%3B when associated with A-73%2C A-90%2C A-279 and A-289. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15121837,ECO:0000269|PubMed:16861895,ECO:0000269|PubMed:18670132;Dbxref=PMID:15121837,PMID:16861895,PMID:18670132	
+P46946	UniProtKB	Mutagenesis	267	267	.	.	.	Note=Leads to camptothecin hypersensitivity and loss of function. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18716619,ECO:0000269|PubMed:20150422;Dbxref=PMID:18716619,PMID:20150422	
+P46946	UniProtKB	Mutagenesis	267	267	.	.	.	Note=Leads to constitutive activation of the DNA repair function. S->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18716619,ECO:0000269|PubMed:20150422;Dbxref=PMID:18716619,PMID:20150422	
+P46946	UniProtKB	Mutagenesis	270	270	.	.	.	Note=Abolishes DNA-binding and endonuclease activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18042458;Dbxref=PMID:18042458	
+P46946	UniProtKB	Mutagenesis	278	278	.	.	.	Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-249%2C A-279%2C and A-289. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15121837;Dbxref=PMID:15121837	
+P46946	UniProtKB	Mutagenesis	279	279	.	.	.	Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-249%2C A-278%2C and A-289. Abolishes DNA damage-induced phosphorylation and function in DNA repair%3B when associated with A-73%2C A-90%2C A-249 and A-289. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15121837,ECO:0000269|PubMed:16861895,ECO:0000269|PubMed:18670132;Dbxref=PMID:15121837,PMID:16861895,PMID:18670132	
+P46946	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-249%2C A-278%2C and A-279. Abolishes DNA damage-induced phosphorylation and function in DNA repair%3B when associated with A-73%2C A-90%2C A-249 and A-279. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15121837,ECO:0000269|PubMed:16861895,ECO:0000269|PubMed:18670132;Dbxref=PMID:15121837,PMID:16861895,PMID:18670132	
+##sequence-region P32074 1 935
+P32074	UniProtKB	Chain	1	935	.	.	.	ID=PRO_0000193861;Note=Coatomer subunit gamma	
+P32074	UniProtKB	Repeat	258	296	.	.	.	Note=HEAT 1	
+P32074	UniProtKB	Repeat	337	372	.	.	.	Note=HEAT 2	
+P32074	UniProtKB	Repeat	373	410	.	.	.	Note=HEAT 3	
+P32074	UniProtKB	Repeat	412	449	.	.	.	Note=HEAT 4	
+P32074	UniProtKB	Repeat	524	562	.	.	.	Note=HEAT 5	
+P32074	UniProtKB	Modified residue	638	638	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32074	UniProtKB	Modified residue	643	643	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32074	UniProtKB	Modified residue	653	653	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32074	UniProtKB	Cross-link	647	647	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32074	UniProtKB	Sequence conflict	353	353	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05892 1 277
+Q05892	UniProtKB	Chain	1	277	.	.	.	ID=PRO_0000268626;Note=MIOREX complex component 2	
+##sequence-region P18900 1 473
+P18900	UniProtKB	Metal binding	193	193	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Metal binding	193	193	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Metal binding	197	197	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Metal binding	197	197	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Metal binding	364	364	.	.	.	Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Binding site	84	84	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Binding site	87	87	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Binding site	186	186	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Binding site	202	202	.	.	.	Note=Polyprenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Binding site	203	203	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Binding site	323	323	.	.	.	Note=Polyprenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Binding site	324	324	.	.	.	Note=Polyprenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Binding site	361	361	.	.	.	Note=Polyprenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18900	UniProtKB	Binding site	378	378	.	.	.	Note=Polyprenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P27697 1 501
+P27697	UniProtKB	Transit peptide	1	29	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27697	UniProtKB	Chain	30	501	.	.	.	ID=PRO_0000000260;Note=Atypical kinase COQ8%2C mitochondrial	
+P27697	UniProtKB	Domain	188	501	.	.	.	Note=Protein kinase	
+P27697	UniProtKB	Nucleotide binding	303	306	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60	
+P27697	UniProtKB	Motif	134	137	.	.	.	Note=KxGQ motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60	
+P27697	UniProtKB	Motif	195	198	.	.	.	Note=AAAS motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60	
+P27697	UniProtKB	Active site	346	346	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60	
+P27697	UniProtKB	Binding site	198	198	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60	
+P27697	UniProtKB	Binding site	216	216	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60	
+P27697	UniProtKB	Binding site	351	351	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60	
+P27697	UniProtKB	Binding site	365	365	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60	
+P27697	UniProtKB	Mutagenesis	89	89	.	.	.	Note=In coq8-2%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186	
+P27697	UniProtKB	Mutagenesis	130	130	.	.	.	Note=In coq8-5%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. Impairs coenzyme Q6 biosynthesis. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186	
+P27697	UniProtKB	Mutagenesis	134	134	.	.	.	Note=Abolishes coenzyme Q biosynthesis. Able to autophosphorylate in cis. K->A%2CH%2CR%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25498144,ECO:0000269|PubMed:27499294;Dbxref=PMID:25498144,PMID:27499294	
+P27697	UniProtKB	Mutagenesis	137	137	.	.	.	Note=Abolishes coenzyme Q biosynthesis. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144	
+P27697	UniProtKB	Mutagenesis	197	197	.	.	.	Note=Abolishes coenzyme Q biosynthesis. Able to autophosphorylate in cis. A->G%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25498144,ECO:0000269|PubMed:27499294;Dbxref=PMID:25498144,PMID:27499294	
+P27697	UniProtKB	Mutagenesis	197	197	.	.	.	Note=In coq8-3%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. Impairs coenzyme Q6 biosynthesis. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186	
+P27697	UniProtKB	Mutagenesis	198	198	.	.	.	Note=Decreased coenzyme Q biosynthesis. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144	
+P27697	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Impairs coenzyme Q biosynthesis. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186	
+P27697	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Abolishes coenzyme Q biosynthesis. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144	
+P27697	UniProtKB	Mutagenesis	229	229	.	.	.	Note=In coq8-6%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186	
+P27697	UniProtKB	Mutagenesis	269	269	.	.	.	Note=Abolishes coenzyme Q biosynthesis. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144	
+P27697	UniProtKB	Mutagenesis	346	346	.	.	.	Note=Abolishes coenzyme Q biosynthesis. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144	
+P27697	UniProtKB	Mutagenesis	346	346	.	.	.	Note=In coq8-2%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186	
+P27697	UniProtKB	Mutagenesis	348	348	.	.	.	Note=In coq8-4%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. N->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186	
+P27697	UniProtKB	Mutagenesis	351	351	.	.	.	Note=Abolishes coenzyme Q biosynthesis. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144	
+P27697	UniProtKB	Mutagenesis	365	365	.	.	.	Note=Abolishes coenzyme Q biosynthesis. Enhanced autophosphorylation in cis. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25498144,ECO:0000269|PubMed:27499294;Dbxref=PMID:25498144,PMID:27499294	
+P27697	UniProtKB	Mutagenesis	471	471	.	.	.	Note=Abolishes coenzyme Q biosynthesis. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144	
+P27697	UniProtKB	Mutagenesis	475	475	.	.	.	Note=In coq8-8%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. G->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186	
+##sequence-region P52924 1 374
+P52924	UniProtKB	Chain	1	374	.	.	.	ID=PRO_0000207521;Note=Protein COS10	
+P52924	UniProtKB	Topological domain	1	36	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52924	UniProtKB	Transmembrane	37	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52924	UniProtKB	Topological domain	60	62	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52924	UniProtKB	Transmembrane	63	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52924	UniProtKB	Topological domain	86	374	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43542 1 379
+P43542	UniProtKB	Chain	1	379	.	.	.	ID=PRO_0000207515;Note=Protein COS4	
+P43542	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43542	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43542	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43542	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53344 1 381
+P53344	UniProtKB	Chain	1	381	.	.	.	ID=PRO_0000207517;Note=Protein COS6	
+P53344	UniProtKB	Topological domain	1	42	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53344	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53344	UniProtKB	Topological domain	64	69	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53344	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53344	UniProtKB	Topological domain	91	381	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32798 1 439
+P32798	UniProtKB	Chain	1	439	.	.	.	ID=PRO_0000206102;Note=Cobalt uptake protein COT1	
+P32798	UniProtKB	Transmembrane	10	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32798	UniProtKB	Transmembrane	43	60	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32798	UniProtKB	Transmembrane	78	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32798	UniProtKB	Transmembrane	114	133	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32798	UniProtKB	Transmembrane	244	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32798	UniProtKB	Transmembrane	279	295	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32798	UniProtKB	Compositional bias	140	148	.	.	.	Note=His-rich (could be involved in coordination of cobalt ions)	
+P32798	UniProtKB	Compositional bias	163	169	.	.	.	Note=His-rich (could be involved in coordination of cobalt ions)	
+P32798	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32798	UniProtKB	Cross-link	301	301	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538	
+P32798	UniProtKB	Sequence conflict	227	227	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32798	UniProtKB	Sequence conflict	333	334	.	.	.	Note=HI->RV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32798	UniProtKB	Sequence conflict	424	424	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47081 1 118
+P47081	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12287 1 69
+Q12287	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9407107;Dbxref=PMID:9407107	
+Q12287	UniProtKB	Chain	2	69	.	.	.	ID=PRO_0000213541;Note=Cytochrome c oxidase copper chaperone	
+Q12287	UniProtKB	Domain	23	65	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q12287	UniProtKB	Motif	26	36	.	.	.	Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q12287	UniProtKB	Motif	47	57	.	.	.	Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q12287	UniProtKB	Metal binding	23	23	.	.	.	Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14061	
+Q12287	UniProtKB	Metal binding	24	24	.	.	.	Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14061	
+Q12287	UniProtKB	Disulfide bond	26	57	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q12287	UniProtKB	Disulfide bond	36	47	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q12287	UniProtKB	Beta strand	3	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U97	
+Q12287	UniProtKB	Beta strand	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U96	
+Q12287	UniProtKB	Beta strand	23	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z2G	
+Q12287	UniProtKB	Helix	28	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U96	
+Q12287	UniProtKB	Helix	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U96	
+Q12287	UniProtKB	Helix	48	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U96	
+Q12287	UniProtKB	Turn	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U96	
+##sequence-region P04037 1 155
+P04037	UniProtKB	Transit peptide	1	25	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6327686;Dbxref=PMID:6327686	
+P04037	UniProtKB	Chain	26	155	.	.	.	ID=PRO_0000006114;Note=Cytochrome c oxidase subunit 4%2C mitochondrial	
+P04037	UniProtKB	Metal binding	111	111	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00692	
+P04037	UniProtKB	Metal binding	134	134	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00692	
+P04037	UniProtKB	Metal binding	137	137	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00692	
+P04037	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P04037	UniProtKB	Sequence conflict	26	26	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04037	UniProtKB	Sequence conflict	73	73	.	.	.	Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04037	UniProtKB	Beta strand	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR8	
+P04037	UniProtKB	Beta strand	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX	
+P04037	UniProtKB	Beta strand	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX	
+P04037	UniProtKB	Beta strand	109	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX	
+P04037	UniProtKB	Beta strand	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX	
+P04037	UniProtKB	Beta strand	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX	
+P04037	UniProtKB	Beta strand	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX	
+P04037	UniProtKB	Beta strand	140	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX	
+##sequence-region P00424 1 153
+P00424	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6300105,ECO:0000269|PubMed:6327686;Dbxref=PMID:6300105,PMID:6327686	
+P00424	UniProtKB	Chain	21	153	.	.	.	ID=PRO_0000006097;Note=Cytochrome c oxidase polypeptide 5A%2C mitochondrial	
+P00424	UniProtKB	Sequence conflict	51	51	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00425 1 151
+P00425	UniProtKB	Transit peptide	1	17	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00425	UniProtKB	Chain	18	151	.	.	.	ID=PRO_0000006098;Note=Cytochrome c oxidase polypeptide 5B%2C mitochondrial	
+##sequence-region P04039 1 78
+P04039	UniProtKB	Transit peptide	1	27	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6327685,ECO:0000269|PubMed:7851399;Dbxref=PMID:6327685,PMID:7851399	
+P04039	UniProtKB	Chain	28	74	.	.	.	ID=PRO_0000006173;Note=Cytochrome c oxidase polypeptide VIII%2C mitochondrial	
+P04039	UniProtKB	Propeptide	75	78	.	.	.	ID=PRO_0000006174	
+P04039	UniProtKB	Sequence conflict	47	47	.	.	.	Note=T->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04039	UniProtKB	Sequence conflict	68	68	.	.	.	Note=C->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P10614 1 530
+P10614	UniProtKB	Chain	1	530	.	.	.	ID=PRO_0000052012;Note=Lanosterol 14-alpha demethylase	
+P10614	UniProtKB	Topological domain	1	20	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10614	UniProtKB	Transmembrane	21	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10614	UniProtKB	Topological domain	42	530	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10614	UniProtKB	Metal binding	470	470	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P10614	UniProtKB	Modified residue	458	458	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P10614	UniProtKB	Cross-link	116	116	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P10614	UniProtKB	Cross-link	353	353	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P10614	UniProtKB	Cross-link	454	454	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P10614	UniProtKB	Sequence conflict	433	433	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10614	UniProtKB	Sequence conflict	433	433	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10614	UniProtKB	Helix	9	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	27	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Turn	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	69	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	76	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	89	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	98	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	105	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Turn	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	122	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	144	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	160	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Turn	182	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Turn	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	190	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	196	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	215	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	225	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	238	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	249	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	283	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	301	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	334	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	349	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	357	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	364	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	383	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	405	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	410	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Turn	417	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Turn	421	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	428	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	444	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	451	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	466	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Helix	473	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	491	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	507	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+P10614	UniProtKB	Beta strand	518	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ	
+##sequence-region P17898 1 393
+P17898	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000056808;Note=Cholinephosphotransferase 1	
+P17898	UniProtKB	Topological domain	1	40	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Transmembrane	41	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Topological domain	62	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Topological domain	194	210	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Transmembrane	211	231	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Topological domain	232	263	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Transmembrane	264	284	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Topological domain	285	285	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Transmembrane	286	306	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Topological domain	307	320	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Transmembrane	321	341	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Topological domain	342	348	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Transmembrane	349	369	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17898	UniProtKB	Topological domain	370	393	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P08679 1 460
+P08679	UniProtKB	Chain	1	460	.	.	.	ID=PRO_0000169984;Note=Citrate synthase%2C peroxisomal	
+P08679	UniProtKB	Motif	458	460	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08679	UniProtKB	Active site	293	293	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117	
+P08679	UniProtKB	Active site	339	339	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117	
+P08679	UniProtKB	Active site	394	394	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117	
+P08679	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08679	UniProtKB	Cross-link	218	218	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P08679	UniProtKB	Cross-link	239	239	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P08679	UniProtKB	Cross-link	354	354	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P08679	UniProtKB	Cross-link	385	385	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region P17891 1 233
+P17891	UniProtKB	Chain	1	233	.	.	.	ID=PRO_0000205776;Note=Clathrin light chain	
+P17891	UniProtKB	Region	144	204	.	.	.	Note=Involved in binding clathrin heavy chain;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17891	UniProtKB	Coiled coil	125	186	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17891	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P17891	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region P53332 1 305
+P53332	UniProtKB	Chain	1	305	.	.	.	ID=PRO_0000202870;Note=Phosphopantetheine adenylyltransferase	
+##sequence-region P43618 1 361
+P43618	UniProtKB	Chain	1	361	.	.	.	ID=PRO_0000202697;Note=Kinetochore-associated protein CNN1	
+P43618	UniProtKB	Sequence conflict	8	8	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43618	UniProtKB	Helix	63	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GEQ	
+##sequence-region P40452 1 197
+P40452	UniProtKB	Chain	1	197	.	.	.	ID=PRO_0000202954;Note=Cytochrome c oxidase assembly factor 1	
+P40452	UniProtKB	Topological domain	1	73	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40452	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40452	UniProtKB	Topological domain	95	197	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05809 1 96
+Q05809	UniProtKB	Chain	1	96	.	.	.	ID=PRO_0000247207;Note=Cytochrome oxidase assembly factor 4	
+Q05809	UniProtKB	Domain	36	77	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q05809	UniProtKB	Motif	39	49	.	.	.	Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q05809	UniProtKB	Motif	59	69	.	.	.	Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q05809	UniProtKB	Disulfide bond	39	69	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q05809	UniProtKB	Disulfide bond	49	59	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+##sequence-region P53600 1 189
+P53600	UniProtKB	Chain	1	189	.	.	.	ID=PRO_0000193830;Note=Coatomer subunit zeta	
+##sequence-region P53239 1 316
+P53239	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53239	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53239	UniProtKB	Transmembrane	275	295	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E731 1 98
+Q3E731	UniProtKB	Chain	1	98	.	.	.	ID=PRO_0000122292;Note=Cytochrome c oxidase assembly protein COX19	
+Q3E731	UniProtKB	Domain	27	70	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E731	UniProtKB	Motif	30	40	.	.	.	Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E731	UniProtKB	Motif	52	62	.	.	.	Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E731	UniProtKB	Disulfide bond	30	62	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E731	UniProtKB	Disulfide bond	40	52	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E731	UniProtKB	Mutagenesis	63	63	.	.	.	Note=In COX19-1%3B causes a respiratory-deficient phenotype because of lack of cytochrome c activity. R->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12171940;Dbxref=PMID:12171940	
+##sequence-region P00410 1 251
+P00410	UniProtKB	Propeptide	1	15	.	.	.	ID=PRO_0000419180;Note=Removed in mature form	
+P00410	UniProtKB	Chain	16	251	.	.	.	ID=PRO_0000006048;Note=Cytochrome c oxidase subunit 2	
+P00410	UniProtKB	Topological domain	16	42	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00410	UniProtKB	Transmembrane	43	64	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00410	UniProtKB	Topological domain	65	82	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00410	UniProtKB	Transmembrane	83	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00410	UniProtKB	Topological domain	108	251	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00410	UniProtKB	Metal binding	186	186	.	.	.	Note=Copper A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00410	UniProtKB	Metal binding	221	221	.	.	.	Note=Copper A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00410	UniProtKB	Metal binding	225	225	.	.	.	Note=Copper A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00410	UniProtKB	Metal binding	229	229	.	.	.	Note=Copper A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00410	UniProtKB	Site	15	16	.	.	.	Note=Cleavage%3B by IMP1	
+P00410	UniProtKB	Sequence conflict	59	59	.	.	.	Note=Y->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00420 1 269
+P00420	UniProtKB	Chain	1	269	.	.	.	ID=PRO_0000183874;Note=Cytochrome c oxidase subunit 3	
+P00420	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00420	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00420	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00420	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00420	UniProtKB	Transmembrane	167	187	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00420	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00420	UniProtKB	Transmembrane	247	267	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00420	UniProtKB	Sequence conflict	263	263	.	.	.	Note=V->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00420	UniProtKB	Sequence conflict	263	263	.	.	.	Note=V->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P41811 1 889
+P41811	UniProtKB	Chain	1	889	.	.	.	ID=PRO_0000050918;Note=Coatomer subunit beta'	
+P41811	UniProtKB	Repeat	11	41	.	.	.	Note=WD 1	
+P41811	UniProtKB	Repeat	53	83	.	.	.	Note=WD 2	
+P41811	UniProtKB	Repeat	95	125	.	.	.	Note=WD 3	
+P41811	UniProtKB	Repeat	138	169	.	.	.	Note=WD 4	
+P41811	UniProtKB	Repeat	182	214	.	.	.	Note=WD 5	
+P41811	UniProtKB	Repeat	226	256	.	.	.	Note=WD 6	
+P41811	UniProtKB	Modified residue	326	326	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41811	UniProtKB	Beta strand	6	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	16	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	23	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	35	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Turn	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	46	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	58	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Helix	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	69	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Turn	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	89	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	100	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	107	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	121	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Turn	126	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	132	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	143	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	155	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	163	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	176	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	189	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	200	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	208	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Turn	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	220	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	231	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	238	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	252	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Turn	257	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	262	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	269	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Helix	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J82	
+P41811	UniProtKB	Beta strand	287	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	294	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73	
+P41811	UniProtKB	Beta strand	313	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	327	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	350	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	360	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	368	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	378	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Turn	384	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	389	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	396	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	404	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	416	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	423	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	438	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	442	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	453	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Turn	458	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	463	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	471	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	480	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Turn	490	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	496	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Helix	504	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	518	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Helix	523	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	526	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	537	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	545	549	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	554	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	563	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	573	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Turn	580	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	584	589	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+P41811	UniProtKB	Beta strand	594	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP	
+##sequence-region P27680 1 312
+P27680	UniProtKB	Transit peptide	1	32	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03190	
+P27680	UniProtKB	Chain	33	312	.	.	.	ID=PRO_0000035932;Note=Ubiquinone biosynthesis O-methyltransferase%2C mitochondrial	
+P27680	UniProtKB	Binding site	68	68	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03190	
+P27680	UniProtKB	Binding site	130	130	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03190	
+P27680	UniProtKB	Binding site	153	153	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03190	
+P27680	UniProtKB	Binding site	196	196	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03190	
+##sequence-region P49017 1 307
+P49017	UniProtKB	Transit peptide	1	19	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03191	
+P49017	UniProtKB	Chain	20	307	.	.	.	ID=PRO_0000193361;Note=2-methoxy-6-polyprenyl-1%2C4-benzoquinol methylase%2C mitochondrial	
+P49017	UniProtKB	Region	179	180	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03191,ECO:0000269|PubMed:25084328;Dbxref=PMID:25084328	
+P49017	UniProtKB	Binding site	122	122	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03191,ECO:0000269|PubMed:25084328;Dbxref=PMID:25084328	
+P49017	UniProtKB	Binding site	148	148	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03191,ECO:0000269|PubMed:25084328;Dbxref=PMID:25084328	
+P49017	UniProtKB	Binding site	197	197	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03191,ECO:0000269|PubMed:25084328;Dbxref=PMID:25084328	
+P49017	UniProtKB	Helix	74	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Helix	90	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Beta strand	114	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Helix	124	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Beta strand	143	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Helix	151	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Beta strand	166	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBW	
+P49017	UniProtKB	Beta strand	173	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Turn	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Beta strand	191	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Helix	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Helix	206	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Beta strand	217	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Helix	234	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Helix	258	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Helix	274	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Beta strand	286	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Helix	295	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+P49017	UniProtKB	Beta strand	299	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX	
+##sequence-region P53053 1 380
+P53053	UniProtKB	Chain	1	380	.	.	.	ID=PRO_0000207522;Note=Protein COS12	
+P53053	UniProtKB	Topological domain	1	70	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53053	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53053	UniProtKB	Topological domain	92	231	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53053	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53053	UniProtKB	Topological domain	253	257	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53053	UniProtKB	Transmembrane	258	278	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53053	UniProtKB	Topological domain	279	380	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX13 1 379
+P0CX13	UniProtKB	Chain	1	379	.	.	.	ID=PRO_0000409750;Note=Protein COS3	
+P0CX13	UniProtKB	Topological domain	1	72	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX13	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX13	UniProtKB	Topological domain	94	254	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX13	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX13	UniProtKB	Topological domain	276	379	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07788 1 383
+Q07788	UniProtKB	Chain	1	383	.	.	.	ID=PRO_0000207518;Note=Protein COS7	
+Q07788	UniProtKB	Topological domain	1	42	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07788	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07788	UniProtKB	Topological domain	64	72	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07788	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07788	UniProtKB	Topological domain	94	232	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07788	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07788	UniProtKB	Topological domain	254	254	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07788	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07788	UniProtKB	Topological domain	276	383	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39103 1 70
+P39103	UniProtKB	Chain	1	70	.	.	.	ID=PRO_0000183930;Note=Cytochrome c oxidase assembly protein COX14	
+P39103	UniProtKB	Transmembrane	17	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38170 1 754
+P38170	UniProtKB	Chain	1	754	.	.	.	ID=PRO_0000095047;Note=Condensin complex subunit 2	
+P38170	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38170	UniProtKB	Modified residue	548	548	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38170	UniProtKB	Sequence conflict	517	517	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38170	UniProtKB	Sequence conflict	517	517	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06096 1 861
+Q06096	UniProtKB	Chain	1	861	.	.	.	ID=PRO_0000213508;Note=Conserved oligomeric Golgi complex subunit 4	
+##sequence-region P53195 1 279
+P53195	UniProtKB	Chain	1	279	.	.	.	ID=PRO_0000213520;Note=Conserved oligomeric Golgi complex subunit 7	
+P53195	UniProtKB	Sequence conflict	12	12	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04935 1 205
+Q04935	UniProtKB	Transmembrane	91	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04935	UniProtKB	Transmembrane	116	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E7A4 1 109
+Q3E7A4	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000248414;Note=COX assembly mitochondrial protein 2	
+Q3E7A4	UniProtKB	Domain	10	54	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E7A4	UniProtKB	Motif	13	23	.	.	.	Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E7A4	UniProtKB	Motif	36	46	.	.	.	Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E7A4	UniProtKB	Disulfide bond	13	46	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q3E7A4	UniProtKB	Disulfide bond	23	36	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+##sequence-region P53951 1 403
+P53951	UniProtKB	Chain	1	403	.	.	.	ID=PRO_0000213512;Note=Conserved oligomeric Golgi complex subunit 5	
+##sequence-region P43621 1 546
+P43621	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8617224;Dbxref=PMID:8617224	
+P43621	UniProtKB	Chain	2	546	.	.	.	ID=PRO_0000193848;Note=Coatomer subunit delta	
+P43621	UniProtKB	Domain	288	546	.	.	.	Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404	
+P43621	UniProtKB	Region	190	440	.	.	.	Note=Interaction with DSL1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14504276;Dbxref=PMID:14504276	
+P43621	UniProtKB	Modified residue	277	277	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43621	UniProtKB	Beta strand	289	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	309	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Helix	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	328	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Helix	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Helix	355	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	366	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	380	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	398	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	409	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	428	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Helix	447	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Turn	451	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJX	
+P43621	UniProtKB	Beta strand	456	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	463	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	478	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Helix	490	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	495	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	501	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	517	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+P43621	UniProtKB	Beta strand	525	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJX	
+P43621	UniProtKB	Beta strand	533	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ	
+##sequence-region P32378 1 372
+P32378	UniProtKB	Transit peptide	1	42	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189	
+P32378	UniProtKB	Chain	43	372	.	.	.	ID=PRO_0000035921;Note=4-hydroxybenzoate polyprenyltransferase%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189	
+P32378	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189	
+P32378	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189	
+P32378	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189	
+P32378	UniProtKB	Transmembrane	193	213	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189	
+P32378	UniProtKB	Transmembrane	229	249	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189	
+P32378	UniProtKB	Transmembrane	298	318	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189	
+P32378	UniProtKB	Transmembrane	352	372	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189	
+P32378	UniProtKB	Region	134	156	.	.	.	Note=Allylic polyprenyl diphosphate-binding site;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03189,ECO:0000305|PubMed:1740455;Dbxref=PMID:1740455	
+P32378	UniProtKB	Compositional bias	29	49	.	.	.	Note=Ser-rich	
+P32378	UniProtKB	Sequence conflict	273	273	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00427 1 148
+P00427	UniProtKB	Transit peptide	1	40	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6290493;Dbxref=PMID:6290493	
+P00427	UniProtKB	Chain	41	148	.	.	.	ID=PRO_0000006108;Note=Cytochrome c oxidase subunit 6%2C mitochondrial	
+##sequence-region P21595 1 489
+P21595	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000052042;Note=Cytochrome P450-DIT2	
+P21595	UniProtKB	Metal binding	435	435	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21595	UniProtKB	Sequence conflict	445	445	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38930 1 258
+P38930	UniProtKB	Chain	1	258	.	.	.	ID=PRO_0000068258;Note=Casein kinase II subunit beta'	
+##sequence-region P40465 1 213
+P40465	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000202960;Note=Chromosome segregation in meiosis protein 2	
+P40465	UniProtKB	Sequence conflict	18	18	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40465	UniProtKB	Helix	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQ6	
+P40465	UniProtKB	Beta strand	8	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Helix	17	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Beta strand	33	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Helix	48	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Helix	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Helix	63	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Beta strand	69	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Helix	77	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Beta strand	110	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Helix	119	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Helix	132	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Beta strand	155	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Helix	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Helix	171	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Beta strand	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Helix	199	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+P40465	UniProtKB	Beta strand	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+##sequence-region Q06705 1 408
+Q06705	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q06705	UniProtKB	Chain	2	408	.	.	.	ID=PRO_0000228155;Note=Phosphatidylinositol transfer protein CSR1	
+Q06705	UniProtKB	Domain	157	317	.	.	.	Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056	
+Q06705	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q06705	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q06705	UniProtKB	Sequence conflict	6	6	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47976 1 325
+P47976	UniProtKB	Chain	1	325	.	.	.	ID=PRO_0000089173;Note=mRNA decay factor CTH1	
+P47976	UniProtKB	Zinc finger	204	232	.	.	.	Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+P47976	UniProtKB	Zinc finger	242	270	.	.	.	Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+P47976	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Abolishes mRNA binding. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18522836;Dbxref=PMID:18522836	
+P47976	UniProtKB	Sequence conflict	142	143	.	.	.	Note=EI->RV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03957 1 528
+Q03957	UniProtKB	Chain	1	528	.	.	.	ID=PRO_0000085906;Note=CTD kinase subunit alpha	
+Q03957	UniProtKB	Domain	183	469	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03957	UniProtKB	Nucleotide binding	189	197	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03957	UniProtKB	Motif	37	44	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03957	UniProtKB	Compositional bias	506	528	.	.	.	Note=Asn/Asp-rich	
+Q03957	UniProtKB	Active site	306	306	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q03957	UniProtKB	Binding site	212	212	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03957	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03957	UniProtKB	Modified residue	338	338	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15870265;Dbxref=PMID:15870265	
+Q03957	UniProtKB	Mutagenesis	324	324	.	.	.	Note=Cold-sensitive. Sensitive to hydroxyurea and UV irradiation. Interferes with ATP-binding. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12684377,ECO:0000269|PubMed:15870265;Dbxref=PMID:12684377,PMID:15870265	
+Q03957	UniProtKB	Mutagenesis	338	338	.	.	.	Note=Cold-sensitive. Abolishes kinase activity. Delayed growth at early stationary phase. Shows no increase in CTD Ser-2 phosphorylation in the transition from rapid growth to stationary phase. Has compromised transcriptional activation of two stationary-phase genes CTT1 and SPI1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15870265;Dbxref=PMID:15870265	
+##sequence-region P38428 1 203
+P38428	UniProtKB	Chain	1	203	.	.	.	ID=PRO_0000203346;Note=Coupling of ubiquitin conjugation to ER degradation protein 1	
+P38428	UniProtKB	Topological domain	1	6	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9388185;Dbxref=PMID:9388185	
+P38428	UniProtKB	Transmembrane	7	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38428	UniProtKB	Topological domain	24	203	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9388185;Dbxref=PMID:9388185	
+P38428	UniProtKB	Domain	65	107	.	.	.	Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468	
+P38428	UniProtKB	Sequence conflict	48	48	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38428	UniProtKB	Helix	67	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MYX	
+P38428	UniProtKB	Helix	82	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MYX	
+P38428	UniProtKB	Helix	95	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MYX	
+P38428	UniProtKB	Turn	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MYX	
+P38428	UniProtKB	Helix	151	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+P38428	UniProtKB	Helix	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+P38428	UniProtKB	Helix	173	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+P38428	UniProtKB	Helix	196	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU	
+##sequence-region P40094 1 801
+P40094	UniProtKB	Chain	1	801	.	.	.	ID=PRO_0000213503;Note=Conserved oligomeric Golgi complex subunit 3	
+P40094	UniProtKB	Modified residue	507	507	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40094	UniProtKB	Modified residue	647	647	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P53959 1 839
+P53959	UniProtKB	Chain	1	839	.	.	.	ID=PRO_0000213517;Note=Conserved oligomeric Golgi complex subunit 6	
+##sequence-region Q06440 1 651
+Q06440	UniProtKB	Chain	1	651	.	.	.	ID=PRO_0000050940;Note=Coronin-like protein	
+Q06440	UniProtKB	Repeat	79	110	.	.	.	Note=WD 1	
+Q06440	UniProtKB	Repeat	138	169	.	.	.	Note=WD 2	
+Q06440	UniProtKB	Repeat	180	210	.	.	.	Note=WD 3	
+Q06440	UniProtKB	Repeat	226	257	.	.	.	Note=WD 4	
+Q06440	UniProtKB	Coiled coil	618	650	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06440	UniProtKB	Modified residue	441	441	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q06440	UniProtKB	Modified residue	454	454	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+Q06440	UniProtKB	Modified residue	456	456	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06440	UniProtKB	Modified residue	517	517	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q06440	UniProtKB	Modified residue	529	529	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q06440	UniProtKB	Modified residue	573	573	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06440	UniProtKB	Modified residue	579	579	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53822 1 381
+P53822	UniProtKB	Chain	1	381	.	.	.	ID=PRO_0000207513;Note=Protein COS1	
+P53822	UniProtKB	Topological domain	1	42	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53822	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53822	UniProtKB	Topological domain	64	72	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53822	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53822	UniProtKB	Topological domain	94	231	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53822	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53822	UniProtKB	Topological domain	253	254	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53822	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53822	UniProtKB	Topological domain	276	381	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47187 1 383
+P47187	UniProtKB	Chain	1	383	.	.	.	ID=PRO_0000207516;Note=Protein COS5	
+P47187	UniProtKB	Topological domain	1	42	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47187	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47187	UniProtKB	Topological domain	64	72	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47187	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47187	UniProtKB	Topological domain	94	232	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47187	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47187	UniProtKB	Topological domain	254	254	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47187	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47187	UniProtKB	Topological domain	276	383	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38723 1 381
+P38723	UniProtKB	Chain	1	381	.	.	.	ID=PRO_0000207519;Note=Protein COS8	
+P38723	UniProtKB	Topological domain	1	42	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38723	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38723	UniProtKB	Topological domain	64	72	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38723	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38723	UniProtKB	Topological domain	94	237	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38723	UniProtKB	Transmembrane	238	258	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38723	UniProtKB	Topological domain	259	381	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P21592 1 462
+P21592	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21592	UniProtKB	Chain	31	462	.	.	.	ID=PRO_0000035925;Note=Protoheme IX farnesyltransferase%2C mitochondrial	
+P21592	UniProtKB	Transmembrane	141	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21592	UniProtKB	Transmembrane	180	198	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21592	UniProtKB	Transmembrane	221	239	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21592	UniProtKB	Transmembrane	250	268	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21592	UniProtKB	Transmembrane	338	356	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21592	UniProtKB	Transmembrane	369	386	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21592	UniProtKB	Transmembrane	429	453	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40086 1 486
+P40086	UniProtKB	Chain	1	486	.	.	.	ID=PRO_0000183933;Note=Cytochrome c oxidase assembly protein COX15	
+P40086	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40086	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40086	UniProtKB	Transmembrane	201	221	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40086	UniProtKB	Transmembrane	244	264	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40086	UniProtKB	Transmembrane	294	314	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40086	UniProtKB	Transmembrane	403	423	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40086	UniProtKB	Transmembrane	425	445	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P10174 1 60
+P10174	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3013877;Dbxref=PMID:3013877	
+P10174	UniProtKB	Chain	2	60	.	.	.	ID=PRO_0000183907;Note=Cytochrome c oxidase subunit 7	
+P10174	UniProtKB	Transmembrane	31	51	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12150 1 2958
+Q12150	UniProtKB	Chain	1	2958	.	.	.	ID=PRO_0000228143;Note=Protein CSF1	
+Q12150	UniProtKB	Topological domain	1	17	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Transmembrane	18	38	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Topological domain	39	2958	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	117	117	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	144	144	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	271	271	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	478	478	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	530	530	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	816	816	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	821	821	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	839	839	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	892	892	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	1309	1309	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	1368	1368	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	1453	1453	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	1785	1785	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	1921	1921	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	2130	2130	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	2146	2146	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	2280	2280	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	2337	2337	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	2520	2520	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	2578	2578	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	2719	2719	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12150	UniProtKB	Glycosylation	2869	2869	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P15790 1 372
+P15790	UniProtKB	Chain	1	372	.	.	.	ID=PRO_0000085889;Note=Casein kinase II subunit alpha	
+P15790	UniProtKB	Domain	40	363	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P15790	UniProtKB	Nucleotide binding	46	54	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P15790	UniProtKB	Active site	195	195	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P15790	UniProtKB	Binding site	69	69	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P15790	UniProtKB	Beta strand	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FI1	
+P15790	UniProtKB	Beta strand	37	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Beta strand	53	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Turn	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Beta strand	65	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	76	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	112	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Beta strand	136	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Turn	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Beta strand	148	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	169	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Beta strand	201	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Beta strand	209	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	239	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	251	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Beta strand	269	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	277	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	290	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LFI	
+P15790	UniProtKB	Helix	319	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Turn	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	328	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	334	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	348	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	354	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	361	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+P15790	UniProtKB	Helix	364	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7	
+##sequence-region P19454 1 339
+P19454	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3468112;Dbxref=PMID:3468112	
+P19454	UniProtKB	Chain	2	339	.	.	.	ID=PRO_0000085896;Note=Casein kinase II subunit alpha'	
+P19454	UniProtKB	Domain	50	334	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P19454	UniProtKB	Nucleotide binding	56	64	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P19454	UniProtKB	Active site	167	167	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P19454	UniProtKB	Binding site	79	79	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region Q12748 1 733
+Q12748	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12748	UniProtKB	Chain	2	733	.	.	.	ID=PRO_0000079493;Note=Central kinetochore subunit CTF3	
+Q12748	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P47977 1 285
+P47977	UniProtKB	Chain	1	285	.	.	.	ID=PRO_0000089174;Note=mRNA decay factor CTH2	
+P47977	UniProtKB	Zinc finger	169	197	.	.	.	Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+P47977	UniProtKB	Zinc finger	207	235	.	.	.	Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+P47977	UniProtKB	Region	37	55	.	.	.	Note=Required for mRNA decay activity	
+P47977	UniProtKB	Mutagenesis	190	190	.	.	.	Note=Abolishes mRNA binding. C->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652485;Dbxref=PMID:15652485	
+P47977	UniProtKB	Mutagenesis	213	213	.	.	.	Note=Abolishes mRNA binding. C->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652485;Dbxref=PMID:15652485	
+##sequence-region Q08923 1 506
+Q08923	UniProtKB	Chain	1	506	.	.	.	ID=PRO_0000234079;Note=Histone deacetylase complex subunit CTI6	
+Q08923	UniProtKB	Zinc finger	72	123	.	.	.	Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+Q08923	UniProtKB	Modified residue	174	174	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08923	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08923	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08923	UniProtKB	Modified residue	216	216	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08923	UniProtKB	Modified residue	267	267	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08923	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Impairs growth under iron-limiting conditions. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15133041;Dbxref=PMID:15133041	
+Q08923	UniProtKB	Mutagenesis	100	100	.	.	.	Note=Impairs growth under iron-limiting conditions. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15133041;Dbxref=PMID:15133041	
+Q08923	UniProtKB	Sequence conflict	342	342	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12734 1 1121
+Q12734	UniProtKB	Chain	1	1121	.	.	.	ID=PRO_0000228156;Note=Transcription factor CSR2	
+Q12734	UniProtKB	Compositional bias	304	346	.	.	.	Note=Asn-rich	
+Q12734	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12734	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12734	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12734	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12734	UniProtKB	Modified residue	987	987	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12734	UniProtKB	Cross-link	841	841	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region Q06032 1 482
+Q06032	UniProtKB	Chain	1	482	.	.	.	ID=PRO_0000232995;Note=Chromosome stability protein 9	
+Q06032	UniProtKB	Compositional bias	333	445	.	.	.	Note=Ser-rich	
+##sequence-region Q02732 1 369
+Q02732	UniProtKB	Chain	1	369	.	.	.	ID=PRO_0000079492;Note=Central kinetochore subunit CTF19	
+Q02732	UniProtKB	Coiled coil	51	87	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46962 1 323
+P46962	UniProtKB	Chain	1	323	.	.	.	ID=PRO_0000080507;Note=CTD kinase subunit beta	
+##sequence-region Q03220 1 320
+Q03220	UniProtKB	Chain	1	320	.	.	.	ID=PRO_0000210120;Note=Polynucleotide 5'-triphosphatase	
+##sequence-region P38818 1 585
+P38818	UniProtKB	Chain	1	585	.	.	.	ID=PRO_0000202911;Note=Cytochrome c lysine N-methyltransferase 1	
+P38818	UniProtKB	Domain	18	273	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+P38818	UniProtKB	Region	186	288	.	.	.	Note=SET-like	
+P38818	UniProtKB	Sequence conflict	256	256	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P41817 1 306
+P41817	UniProtKB	Chain	1	306	.	.	.	ID=PRO_0000048859;Note=Homeobox protein CUP9	
+P41817	UniProtKB	DNA binding	162	224	.	.	.	Note=Homeobox%3B TALE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108	
+##sequence-region P53333 1 577
+P53333	UniProtKB	Chain	1	577	.	.	.	ID=PRO_0000215678;Note=Pre-mRNA-splicing factor CWC22	
+P53333	UniProtKB	Domain	22	204	.	.	.	Note=MIF4G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00698	
+P53333	UniProtKB	Domain	290	407	.	.	.	Note=MI;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00698	
+P53333	UniProtKB	Compositional bias	533	577	.	.	.	Note=Arg-rich	
+P53333	UniProtKB	Helix	9	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Turn	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	37	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Turn	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	53	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	73	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	88	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	111	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	132	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	148	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	167	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	188	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Turn	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	237	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	286	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Beta strand	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Turn	304	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	308	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Turn	319	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	324	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Beta strand	336	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	341	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	355	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	380	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	399	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Beta strand	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	414	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	434	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Beta strand	447	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	455	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53333	UniProtKB	Helix	475	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P25603 1 130
+P25603	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000079617;Note=Putative uncharacterized protein CWH36	
+##sequence-region P25618 1 953
+P25618	UniProtKB	Chain	1	953	.	.	.	ID=PRO_0000021052;Note=Protein CWH43	
+P25618	UniProtKB	Topological domain	1	7	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	29	64	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	86	91	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	113	117	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	139	149	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	171	175	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	176	196	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	197	278	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	279	299	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	300	307	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	308	328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	329	330	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	331	351	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	352	352	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	353	368	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	369	380	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	381	401	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	402	420	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	421	441	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	442	450	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	451	471	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	472	495	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	496	516	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	517	517	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	518	538	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	539	547	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	548	568	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	569	585	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	586	606	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	607	613	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	614	634	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	635	642	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Transmembrane	643	663	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Topological domain	664	953	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Region	1	229	.	.	.	Note=PGAP2-like	
+P25618	UniProtKB	Region	230	953	.	.	.	Note=PGAP2IP-like	
+P25618	UniProtKB	Region	862	882	.	.	.	Note=Required for function in lipid remodeling	
+P25618	UniProtKB	Active site	802	802	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25618	UniProtKB	Glycosylation	419	419	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Glycosylation	490	490	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Glycosylation	767	767	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Glycosylation	792	792	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Glycosylation	825	825	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25618	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Causes destabilization of the protein and induces the release of cell wall proteins in the culture medium. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11427965,ECO:0000269|PubMed:17761529;Dbxref=PMID:11427965,PMID:17761529	
+P25618	UniProtKB	Mutagenesis	472	472	.	.	.	Note=No effect on introduction of ceramides into the GPI anchor. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529	
+P25618	UniProtKB	Mutagenesis	693	693	.	.	.	Note=No effect on introduction of ceramides into the GPI anchor. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529	
+P25618	UniProtKB	Mutagenesis	713	713	.	.	.	Note=Impairs the introduction of ceramides into the GPI anchor. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17714445;Dbxref=PMID:17714445	
+P25618	UniProtKB	Mutagenesis	770	770	.	.	.	Note=No effect on introduction of ceramides into the GPI anchor. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529	
+P25618	UniProtKB	Mutagenesis	771	771	.	.	.	Note=No effect on introduction of ceramides into the GPI anchor. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529	
+P25618	UniProtKB	Mutagenesis	802	802	.	.	.	Note=Abrogates the introduction of ceramides into the GPI anchor. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17714445;Dbxref=PMID:17714445	
+P25618	UniProtKB	Mutagenesis	807	807	.	.	.	Note=No effect on introduction of ceramides into the GPI anchor. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529	
+P25618	UniProtKB	Mutagenesis	862	862	.	.	.	Note=Impairs the introduction of ceramides into the GPI anchor. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529	
+P25618	UniProtKB	Mutagenesis	882	882	.	.	.	Note=Abrogates the introduction of ceramides into the GPI anchor. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529	
+##sequence-region P53271 1 262
+P53271	UniProtKB	Chain	1	262	.	.	.	ID=PRO_0000213499;Note=Conserved oligomeric Golgi complex subunit 2	
+P53271	UniProtKB	Helix	110	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ	
+P53271	UniProtKB	Helix	133	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ	
+P53271	UniProtKB	Beta strand	154	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ	
+P53271	UniProtKB	Helix	158	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ	
+P53271	UniProtKB	Helix	184	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ	
+P53271	UniProtKB	Helix	214	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ	
+P53271	UniProtKB	Turn	245	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ	
+P53271	UniProtKB	Helix	249	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ	
+##sequence-region Q04632 1 607
+Q04632	UniProtKB	Chain	1	607	.	.	.	ID=PRO_0000213525;Note=Conserved oligomeric Golgi complex subunit 8	
+Q04632	UniProtKB	Modified residue	410	410	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P07255 1 59
+P07255	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3013877;Dbxref=PMID:3013877	
+P07255	UniProtKB	Chain	2	56	.	.	.	ID=PRO_0000006076;Note=Cytochrome c oxidase subunit 7A	
+P07255	UniProtKB	Propeptide	57	59	.	.	.	ID=PRO_0000006077;Note=Removed in mature form	
+P07255	UniProtKB	Transmembrane	16	34	.	.	.	Note=Helical	
+##sequence-region P36064 1 111
+P36064	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000203147;Note=COX assembly mitochondrial protein	
+P36064	UniProtKB	Domain	39	82	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+P36064	UniProtKB	Motif	42	52	.	.	.	Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+P36064	UniProtKB	Motif	64	74	.	.	.	Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+P36064	UniProtKB	Disulfide bond	42	74	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+P36064	UniProtKB	Disulfide bond	52	64	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+##sequence-region P38845 1 465
+P38845	UniProtKB	Chain	1	465	.	.	.	ID=PRO_0000202923;Note=Cruciform DNA-recognizing protein 1	
+P38845	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000409594;Note=CRP1 short N-terminal subpeptide	
+P38845	UniProtKB	Chain	161	465	.	.	.	ID=PRO_0000409595;Note=CRP1 short C-terminal subpeptide	
+P38845	UniProtKB	Region	160	161	.	.	.	Note=X-DNA-binding	
+P38845	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38845	UniProtKB	Modified residue	156	156	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38845	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38845	UniProtKB	Modified residue	271	271	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38845	UniProtKB	Modified residue	295	295	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38845	UniProtKB	Modified residue	319	319	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38845	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38845	UniProtKB	Modified residue	366	366	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38845	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38845	UniProtKB	Modified residue	440	440	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P41902 1 69
+P41902	UniProtKB	Chain	1	69	.	.	.	ID=PRO_0000197370;Note=Metallothionein-like protein CRS5	
+##sequence-region P33307 1 960
+P33307	UniProtKB	Chain	1	960	.	.	.	ID=PRO_0000117293;Note=Importin alpha re-exporter	
+P33307	UniProtKB	Repeat	1	33	.	.	.	Note=HEAT 1	
+P33307	UniProtKB	Domain	23	96	.	.	.	Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115	
+P33307	UniProtKB	Repeat	34	73	.	.	.	Note=HEAT 2	
+P33307	UniProtKB	Repeat	74	120	.	.	.	Note=HEAT 3	
+P33307	UniProtKB	Repeat	121	157	.	.	.	Note=HEAT 4	
+P33307	UniProtKB	Repeat	158	220	.	.	.	Note=HEAT 5	
+P33307	UniProtKB	Repeat	221	278	.	.	.	Note=HEAT 6	
+P33307	UniProtKB	Repeat	279	323	.	.	.	Note=HEAT 7	
+P33307	UniProtKB	Repeat	324	392	.	.	.	Note=HEAT 8	
+P33307	UniProtKB	Repeat	393	445	.	.	.	Note=HEAT 9	
+P33307	UniProtKB	Repeat	446	489	.	.	.	Note=HEAT 10	
+P33307	UniProtKB	Repeat	490	528	.	.	.	Note=HEAT 11	
+P33307	UniProtKB	Repeat	529	586	.	.	.	Note=HEAT 12	
+P33307	UniProtKB	Repeat	587	630	.	.	.	Note=HEAT 13	
+P33307	UniProtKB	Repeat	631	674	.	.	.	Note=HEAT 14	
+P33307	UniProtKB	Repeat	675	716	.	.	.	Note=HEAT 15	
+P33307	UniProtKB	Repeat	717	751	.	.	.	Note=HEAT 16	
+P33307	UniProtKB	Repeat	752	794	.	.	.	Note=HEAT 17	
+P33307	UniProtKB	Repeat	795	826	.	.	.	Note=HEAT 18	
+P33307	UniProtKB	Repeat	827	928	.	.	.	Note=HEAT 19%3B with insert	
+P33307	UniProtKB	Repeat	929	960	.	.	.	Note=HEAT 20	
+P33307	UniProtKB	Motif	366	381	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33307	UniProtKB	Sequence conflict	515	515	.	.	.	Note=Y->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33307	UniProtKB	Helix	3	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	20	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	36	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	51	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Beta strand	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	80	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	99	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Turn	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	124	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	139	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	161	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	197	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	223	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	229	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	245	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H	
+P33307	UniProtKB	Beta strand	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H	
+P33307	UniProtKB	Helix	258	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	278	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H	
+P33307	UniProtKB	Helix	306	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	323	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	327	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	332	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	343	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	351	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Turn	354	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	361	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	377	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	393	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Turn	415	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H	
+P33307	UniProtKB	Helix	419	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Beta strand	434	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	452	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	461	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	472	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	486	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	491	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	510	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Beta strand	530	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Beta strand	535	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	539	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Turn	542	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	546	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	564	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	571	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Turn	585	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	589	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	592	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	613	628	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	632	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	635	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Turn	655	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	658	671	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Beta strand	672	674	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H	
+P33307	UniProtKB	Turn	677	679	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	680	682	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	683	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	689	692	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Turn	695	697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	698	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	713	715	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	720	730	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Turn	733	735	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	736	749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	752	755	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	756	758	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	759	768	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	769	771	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	776	793	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	795	803	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	809	816	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	818	821	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	822	824	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	828	843	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	846	851	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	853	855	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	856	868	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	894	896	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H	
+P33307	UniProtKB	Helix	899	901	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Turn	914	916	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	917	932	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Beta strand	934	936	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H	
+P33307	UniProtKB	Helix	937	941	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	942	944	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+P33307	UniProtKB	Helix	947	957	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+##sequence-region P43497 1 92
+P43497	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7768807;Dbxref=PMID:7768807	
+P43497	UniProtKB	Chain	21	71	.	.	.	ID=PRO_0000033252;Note=Cell wall protein CWP2	
+P43497	UniProtKB	Propeptide	72	92	.	.	.	ID=PRO_0000033253;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43497	UniProtKB	Repeat	24	37	.	.	.	Note=PIR1/2/3	
+P43497	UniProtKB	Site	33	33	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43497	UniProtKB	Lipidation	71	71	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX12 1 379
+P0CX12	UniProtKB	Chain	1	379	.	.	.	ID=PRO_0000207514;Note=Protein COS2	
+P0CX12	UniProtKB	Topological domain	1	72	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX12	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX12	UniProtKB	Topological domain	94	254	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX12	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX12	UniProtKB	Topological domain	276	379	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36034 1 407
+P36034	UniProtKB	Chain	1	407	.	.	.	ID=PRO_0000207520;Note=Protein COS9	
+P36034	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36034	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36034	UniProtKB	Transmembrane	261	281	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P19516 1 300
+P19516	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19516	UniProtKB	Topological domain	106	300	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19516	UniProtKB	Sequence conflict	24	31	.	.	.	Note=WLAPHALA->MVGTSCAS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19516	UniProtKB	Sequence conflict	146	146	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19516	UniProtKB	Sequence conflict	146	146	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32799 1 129
+P32799	UniProtKB	Transit peptide	1	9	.	.	.	Note=Mitochondrion	
+P32799	UniProtKB	Chain	10	129	.	.	.	ID=PRO_0000006127;Note=Cytochrome c oxidase subunit 6A%2C mitochondrial	
+##sequence-region P38824 1 151
+P38824	UniProtKB	Transit peptide	1	10	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38824	UniProtKB	Chain	11	151	.	.	.	ID=PRO_0000202912;Note=Cytochrome c oxidase-assembly factor COX23%2C mitochondrial	
+P38824	UniProtKB	Domain	101	143	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+P38824	UniProtKB	Motif	104	114	.	.	.	Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+P38824	UniProtKB	Motif	125	135	.	.	.	Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+P38824	UniProtKB	Disulfide bond	104	135	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+P38824	UniProtKB	Disulfide bond	114	125	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+##sequence-region P53314 1 239
+P53314	UniProtKB	Chain	1	239	.	.	.	ID=PRO_0000202859;Note=2'%2C3'-cyclic-nucleotide 3'-phosphodiesterase	
+P53314	UniProtKB	Active site	39	39	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53314	UniProtKB	Active site	150	150	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53314	UniProtKB	Binding site	41	41	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53314	UniProtKB	Binding site	152	152	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53314	UniProtKB	Binding site	155	155	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53314	UniProtKB	Mutagenesis	39	39	.	.	.	Note=Abolishes cyclic nucleotide phosphodiesterase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10734185;Dbxref=PMID:10734185	
+P53314	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Reduces strongly cyclic nucleotide phosphodiesterase activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10734185;Dbxref=PMID:10734185	
+P53314	UniProtKB	Mutagenesis	150	150	.	.	.	Note=Abolishes cyclic nucleotide phosphodiesterase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10734185;Dbxref=PMID:10734185	
+P53314	UniProtKB	Mutagenesis	152	152	.	.	.	Note=Reduces strongly cyclic nucleotide phosphodiesterase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10734185;Dbxref=PMID:10734185	
+##sequence-region Q12289 1 327
+Q12289	UniProtKB	Chain	1	327	.	.	.	ID=PRO_0000090681;Note=Mitochondrial carnitine carrier	
+Q12289	UniProtKB	Transmembrane	33	49	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12289	UniProtKB	Transmembrane	107	123	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12289	UniProtKB	Transmembrane	141	162	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12289	UniProtKB	Transmembrane	196	212	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12289	UniProtKB	Transmembrane	244	260	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12289	UniProtKB	Transmembrane	293	313	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12289	UniProtKB	Repeat	33	126	.	.	.	Note=Solcar 1	
+Q12289	UniProtKB	Repeat	139	221	.	.	.	Note=Solcar 2	
+Q12289	UniProtKB	Repeat	237	321	.	.	.	Note=Solcar 3	
+##sequence-region P38892 1 291
+P38892	UniProtKB	Chain	1	291	.	.	.	ID=PRO_0000202943;Note=Probable S-adenosylmethionine-dependent methyltransferase CRG1	
+P38892	UniProtKB	Sequence conflict	23	23	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53968 1 678
+P53968	UniProtKB	Chain	1	678	.	.	.	ID=PRO_0000046804;Note=Transcriptional regulator CRZ1	
+P53968	UniProtKB	Zinc finger	569	591	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P53968	UniProtKB	Zinc finger	597	619	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P53968	UniProtKB	Compositional bias	115	140	.	.	.	Note=Poly-Gln	
+P53968	UniProtKB	Compositional bias	367	370	.	.	.	Note=Poly-Asn	
+P53968	UniProtKB	Compositional bias	483	487	.	.	.	Note=Poly-Asn	
+P53968	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53968	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53968	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53968	UniProtKB	Modified residue	385	385	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q08054 1 341
+Q08054	UniProtKB	Chain	1	341	.	.	.	ID=PRO_0000079399;Note=Chitin synthase 3 complex protein CSI2	
+Q08054	UniProtKB	Compositional bias	33	112	.	.	.	Note=Poly-Ser	
+##sequence-region Q12348 1 645
+Q12348	UniProtKB	Chain	1	645	.	.	.	ID=PRO_0000121024;Note=COP9 signalosome complex subunit 10	
+Q12348	UniProtKB	Domain	430	540	.	.	.	Note=PCI	
+##sequence-region P14306 1 219
+P14306	UniProtKB	Chain	1	219	.	.	.	ID=PRO_0000204753;Note=Carboxypeptidase Y inhibitor	
+P14306	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12473200;Dbxref=PMID:12473200	
+P14306	UniProtKB	Sequence conflict	56	56	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14306	UniProtKB	Sequence conflict	165	165	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14306	UniProtKB	Sequence conflict	211	219	.	.	.	Note=SNFFYAETK->VQFLLCGNEIGIYIYICICIYFLDFSAFHLTFYYFCFIYVFVTNGQMFVGTNVYVKQNT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14306	UniProtKB	Helix	2	4	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Helix	7	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Helix	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Beta strand	33	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Helix	54	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Beta strand	62	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Beta strand	89	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Beta strand	108	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Beta strand	133	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Beta strand	144	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Beta strand	161	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Helix	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Helix	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Beta strand	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Helix	197	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Turn	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+P14306	UniProtKB	Beta strand	207	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX	
+##sequence-region P53301 1 507
+P53301	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53301	UniProtKB	Chain	23	482	.	.	.	ID=PRO_0000045430;Note=Probable glycosidase CRH1	
+P53301	UniProtKB	Propeptide	483	507	.	.	.	ID=PRO_0000045431;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53301	UniProtKB	Domain	34	260	.	.	.	Note=GH16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01098	
+P53301	UniProtKB	Compositional bias	63	66	.	.	.	Note=Poly-Ser	
+P53301	UniProtKB	Compositional bias	301	481	.	.	.	Note=Ser-rich	
+P53301	UniProtKB	Compositional bias	301	310	.	.	.	Note=Poly-Ser	
+P53301	UniProtKB	Compositional bias	345	357	.	.	.	Note=Poly-Ser	
+P53301	UniProtKB	Compositional bias	387	391	.	.	.	Note=Poly-Ser	
+P53301	UniProtKB	Compositional bias	467	470	.	.	.	Note=Poly-Ser	
+P53301	UniProtKB	Active site	134	134	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53301	UniProtKB	Active site	138	138	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53301	UniProtKB	Lipidation	482	482	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53301	UniProtKB	Glycosylation	117	117	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53301	UniProtKB	Glycosylation	177	177	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53301	UniProtKB	Glycosylation	201	201	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06538 1 782
+Q06538	UniProtKB	Chain	1	782	.	.	.	ID=PRO_0000247173;Note=Calcium permeable stress-gated cation channel 1	
+Q06538	UniProtKB	Topological domain	1	34	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Topological domain	56	116	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Transmembrane	117	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Topological domain	140	181	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Topological domain	203	440	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Transmembrane	441	461	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Topological domain	462	485	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Transmembrane	486	506	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Topological domain	507	530	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Transmembrane	531	551	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Topological domain	552	578	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Transmembrane	579	599	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Topological domain	600	621	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Transmembrane	622	642	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Topological domain	643	648	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Transmembrane	649	669	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Topological domain	670	681	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Transmembrane	682	702	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Topological domain	703	709	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Transmembrane	710	730	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Topological domain	731	782	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06538	UniProtKB	Glycosylation	171	171	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P35206 1 410
+P35206	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Chain	18	410	.	.	.	ID=PRO_0000021012;Note=Mannosyl phosphorylinositol ceramide synthase regulatory protein CSG2	
+P35206	UniProtKB	Topological domain	18	50	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Topological domain	72	141	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Transmembrane	142	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Topological domain	162	167	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Transmembrane	168	187	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Topological domain	188	197	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Transmembrane	198	217	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Topological domain	218	245	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Transmembrane	246	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Topological domain	266	285	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Transmembrane	286	305	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Topological domain	306	324	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Transmembrane	325	344	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Topological domain	345	355	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Transmembrane	356	374	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Topological domain	375	385	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Transmembrane	386	404	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Topological domain	405	410	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Glycosylation	35	35	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Glycosylation	49	49	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35206	UniProtKB	Sequence conflict	68	68	.	.	.	Note=L->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25651 1 190
+P25651	UniProtKB	Chain	1	190	.	.	.	ID=PRO_0000202577;Note=Monopolin complex subunit CSM1	
+P25651	UniProtKB	Coiled coil	31	70	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25651	UniProtKB	Helix	11	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4X	
+P25651	UniProtKB	Helix	71	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S	
+P25651	UniProtKB	Beta strand	83	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S	
+P25651	UniProtKB	Beta strand	96	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S	
+P25651	UniProtKB	Beta strand	116	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S	
+P25651	UniProtKB	Turn	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S	
+P25651	UniProtKB	Beta strand	131	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S	
+P25651	UniProtKB	Helix	143	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S	
+P25651	UniProtKB	Helix	155	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S	
+P25651	UniProtKB	Beta strand	161	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S	
+P25651	UniProtKB	Helix	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S	
+P25651	UniProtKB	Helix	168	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S	
+##sequence-region Q08955 1 156
+Q08955	UniProtKB	Chain	1	156	.	.	.	ID=PRO_0000079404;Note=Chromosome segregation in meiosis protein 4	
+Q08955	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47130 1 423
+P47130	UniProtKB	Chain	1	423	.	.	.	ID=PRO_0000121047;Note=Cop9 signalosome complex subunit 12	
+P47130	UniProtKB	Domain	298	415	.	.	.	Note=PCI	
+##sequence-region Q12468 1 440
+Q12468	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000194859;Note=COP9 signalosome complex subunit 5	
+Q12468	UniProtKB	Domain	71	218	.	.	.	Note=MPN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+Q12468	UniProtKB	Motif	164	177	.	.	.	Note=JAMM motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+Q12468	UniProtKB	Metal binding	164	164	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+Q12468	UniProtKB	Metal binding	166	166	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+Q12468	UniProtKB	Metal binding	177	177	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+Q12468	UniProtKB	Mutagenesis	164	164	.	.	.	Note=Abolishes deneddylation of CDC53. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12183637;Dbxref=PMID:12183637	
+Q12468	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Abolishes deneddylation of CDC53. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12183637;Dbxref=PMID:12183637	
+Q12468	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Abolishes deneddylation of CDC53. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12183637;Dbxref=PMID:12183637	
+##sequence-region P25355 1 563
+P25355	UniProtKB	Chain	1	563	.	.	.	ID=PRO_0000202572;Note=Copper transport protein 86	
+P25355	UniProtKB	Modified residue	433	433	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25355	UniProtKB	Modified residue	559	559	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P53923 1 493
+P53923	UniProtKB	Chain	1	493	.	.	.	ID=PRO_0000203432;Note=Cytoplasmic tRNA 2-thiolation protein 2	
+P53923	UniProtKB	Modified residue	489	489	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53923	UniProtKB	Natural variant	7	7	.	.	.	Note=In strain: YJM230 and YJM320. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53923	UniProtKB	Natural variant	71	71	.	.	.	Note=In strain: SK1%2C V1-09%2C YJM1129%2C YJM269%2C YJM270%2C YJM320%2C YJM326%2C YJM230%2C YJM339 and YJM627. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53923	UniProtKB	Natural variant	193	193	.	.	.	Note=In strain: SK1%2C V1-09%2C YJM230%2C YJM320 and YJM339. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53923	UniProtKB	Natural variant	409	409	.	.	.	Note=In strain: YJM627. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53923	UniProtKB	Natural variant	428	428	.	.	.	Note=In strain: YJM627. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53923	UniProtKB	Natural variant	436	436	.	.	.	Note=In strain: YJM230 and YJM320. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53923	UniProtKB	Natural variant	474	474	.	.	.	Note=In strain: YJM1129%2C YJM269%2C YJM270%2C YJM326 and YJM627. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53923	UniProtKB	Sequence conflict	36	36	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53830 1 285
+P53830	UniProtKB	Chain	1	285	.	.	.	ID=PRO_0000082037;Note=Cold sensitive U2 snRNA suppressor 2	
+P53830	UniProtKB	Domain	45	130	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P53830	UniProtKB	Domain	183	265	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P53830	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53830	UniProtKB	Sequence conflict	235	235	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00044 1 109
+P00044	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:5771953;Dbxref=PMID:5771953	
+P00044	UniProtKB	Chain	2	109	.	.	.	ID=PRO_0000108337;Note=Cytochrome c iso-1	
+P00044	UniProtKB	Metal binding	24	24	.	.	.	Note=Iron (heme axial ligand)	
+P00044	UniProtKB	Metal binding	86	86	.	.	.	Note=Iron (heme axial ligand)	
+P00044	UniProtKB	Binding site	20	20	.	.	.	Note=Heme (covalent)	
+P00044	UniProtKB	Binding site	23	23	.	.	.	Note=Heme (covalent)	
+P00044	UniProtKB	Modified residue	78	78	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B by CTM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10791961;Dbxref=PMID:10791961	
+P00044	UniProtKB	Modified residue	79	79	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10821864,ECO:0000269|PubMed:18390544;Dbxref=PMID:10821864,PMID:18390544	
+P00044	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Loss of methylation by CTM1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10791961;Dbxref=PMID:10791961	
+P00044	UniProtKB	Helix	9	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K	
+P00044	UniProtKB	Turn	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K	
+P00044	UniProtKB	Beta strand	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PCC	
+P00044	UniProtKB	Beta strand	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MU8	
+P00044	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5P	
+P00044	UniProtKB	Beta strand	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K	
+P00044	UniProtKB	Beta strand	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CID	
+P00044	UniProtKB	Helix	56	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K	
+P00044	UniProtKB	Beta strand	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MHM	
+P00044	UniProtKB	Helix	67	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K	
+P00044	UniProtKB	Helix	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K	
+P00044	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FHB	
+P00044	UniProtKB	Helix	84	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KKE	
+P00044	UniProtKB	Helix	94	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K	
+##sequence-region P32898 1 989
+P32898	UniProtKB	Chain	1	989	.	.	.	ID=PRO_0000178012;Note=Mitochondrial presequence protease	
+P32898	UniProtKB	Active site	87	87	.	.	.	Note=Proton acceptor	
+P32898	UniProtKB	Metal binding	84	84	.	.	.	Note=Zinc%3B catalytic	
+P32898	UniProtKB	Metal binding	88	88	.	.	.	Note=Zinc%3B catalytic	
+P32898	UniProtKB	Metal binding	185	185	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32898	UniProtKB	Modified residue	920	920	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P32898	UniProtKB	Mutagenesis	84	84	.	.	.	Note=Loss of function. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15772085;Dbxref=PMID:15772085	
+P32898	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15772085;Dbxref=PMID:15772085	
+P32898	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Loss of function. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15772085;Dbxref=PMID:15772085	
+##sequence-region P32623 1 467
+P32623	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Chain	24	445	.	.	.	ID=PRO_0000065745;Note=Probable glycosidase CRH2	
+P32623	UniProtKB	Propeptide	446	467	.	.	.	ID=PRO_0000232722;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Domain	63	280	.	.	.	Note=GH16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01098	
+P32623	UniProtKB	Compositional bias	354	442	.	.	.	Note=Ser-rich	
+P32623	UniProtKB	Active site	166	166	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32623	UniProtKB	Active site	170	170	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32623	UniProtKB	Lipidation	445	445	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Glycosylation	96	96	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Glycosylation	190	190	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Glycosylation	196	196	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Glycosylation	233	233	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Glycosylation	237	237	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Glycosylation	261	261	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Glycosylation	297	297	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Glycosylation	310	310	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32623	UniProtKB	Sequence conflict	130	130	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32623	UniProtKB	Sequence conflict	130	130	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32623	UniProtKB	Sequence conflict	130	130	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32623	UniProtKB	Sequence conflict	291	291	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32623	UniProtKB	Sequence conflict	291	291	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32623	UniProtKB	Sequence conflict	291	291	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32623	UniProtKB	Sequence conflict	354	354	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32623	UniProtKB	Sequence conflict	354	354	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32623	UniProtKB	Sequence conflict	354	354	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05790 1 422
+Q05790	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05790	UniProtKB	Chain	21	422	.	.	.	ID=PRO_0000228141;Note=Probable glycosidase CRR1	
+Q05790	UniProtKB	Domain	67	339	.	.	.	Note=GH16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01098	
+Q05790	UniProtKB	Active site	217	217	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05790	UniProtKB	Active site	221	221	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38308 1 924
+P38308	UniProtKB	Chain	1	924	.	.	.	ID=PRO_0000202509;Note=F-box protein COS111	
+P38308	UniProtKB	Domain	185	236	.	.	.	Note=F-box	
+P38308	UniProtKB	Compositional bias	2	162	.	.	.	Note=Ser-rich	
+P38308	UniProtKB	Compositional bias	354	475	.	.	.	Note=Ser-rich	
+P38308	UniProtKB	Sequence conflict	727	731	.	.	.	Note=TFRQH->SWRND;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38308	UniProtKB	Sequence conflict	727	731	.	.	.	Note=TFRQH->SWRND;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38308	UniProtKB	Sequence conflict	917	917	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38308	UniProtKB	Sequence conflict	917	917	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38308	UniProtKB	Sequence conflict	921	921	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38308	UniProtKB	Sequence conflict	921	921	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04368 1 295
+Q04368	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000079398;Note=Cop9 signalosome-interactor 1	
+##sequence-region P49573 1 406
+P49573	UniProtKB	Chain	1	406	.	.	.	ID=PRO_0000079496;Note=Copper transport protein CTR1	
+P49573	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49573	UniProtKB	Transmembrane	251	271	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49573	UniProtKB	Topological domain	272	406	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49573	UniProtKB	Repeat	9	27	.	.	.	Note=1	
+P49573	UniProtKB	Repeat	28	46	.	.	.	Note=2	
+P49573	UniProtKB	Repeat	47	65	.	.	.	Note=3	
+P49573	UniProtKB	Region	9	65	.	.	.	Note=3 X 19 AA tandem repeats of S-M-X-M-X-A-M-S-S-A-S-K-T-X-X-S-X-M-X	
+P49573	UniProtKB	Compositional bias	1	127	.	.	.	Note=Met/Ser-rich	
+P49573	UniProtKB	Compositional bias	114	117	.	.	.	Note=Poly-Ser	
+P49573	UniProtKB	Modified residue	344	344	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P49573	UniProtKB	Modified residue	349	349	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P49573	UniProtKB	Modified residue	356	356	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P49573	UniProtKB	Modified residue	369	369	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P49573	UniProtKB	Glycosylation	113	113	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49573	UniProtKB	Glycosylation	148	148	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49573	UniProtKB	Cross-link	345	345	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P38865 1 189
+P38865	UniProtKB	Chain	1	189	.	.	.	ID=PRO_0000195046;Note=Copper transport protein CTR2	
+P38865	UniProtKB	Topological domain	1	81	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38865	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38865	UniProtKB	Topological domain	103	142	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38865	UniProtKB	Transmembrane	143	163	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38865	UniProtKB	Topological domain	164	189	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P89105 1 1077
+P89105	UniProtKB	Chain	1	1077	.	.	.	ID=PRO_0000106280;Note=RNA polymerase-associated protein CTR9	
+P89105	UniProtKB	Repeat	56	89	.	.	.	Note=TPR 1	
+P89105	UniProtKB	Repeat	138	174	.	.	.	Note=TPR 2	
+P89105	UniProtKB	Repeat	183	216	.	.	.	Note=TPR 3	
+P89105	UniProtKB	Repeat	218	251	.	.	.	Note=TPR 4	
+P89105	UniProtKB	Repeat	298	332	.	.	.	Note=TPR 5	
+P89105	UniProtKB	Repeat	338	371	.	.	.	Note=TPR 6	
+P89105	UniProtKB	Repeat	373	405	.	.	.	Note=TPR 7	
+P89105	UniProtKB	Repeat	421	455	.	.	.	Note=TPR 8	
+P89105	UniProtKB	Repeat	462	495	.	.	.	Note=TPR 9	
+P89105	UniProtKB	Repeat	501	534	.	.	.	Note=TPR 10	
+P89105	UniProtKB	Repeat	540	572	.	.	.	Note=TPR 11	
+P89105	UniProtKB	Repeat	664	697	.	.	.	Note=TPR 12	
+P89105	UniProtKB	Repeat	699	731	.	.	.	Note=TPR 13	
+P89105	UniProtKB	Repeat	732	764	.	.	.	Note=TPR 14	
+P89105	UniProtKB	Repeat	768	801	.	.	.	Note=TPR 15	
+P89105	UniProtKB	Repeat	830	863	.	.	.	Note=TPR 16	
+P89105	UniProtKB	Modified residue	1015	1015	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P89105	UniProtKB	Modified residue	1017	1017	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P89105	UniProtKB	Sequence conflict	197	197	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	197	197	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	461	461	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	674	674	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	674	674	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	786	786	.	.	.	Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	786	786	.	.	.	Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	903	903	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	903	903	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	907	907	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	907	907	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	926	927	.	.	.	Note=GW->ER;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	926	927	.	.	.	Note=GW->ER;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	956	959	.	.	.	Note=LIQE->IFQV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	956	959	.	.	.	Note=LIQE->IFQV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	987	987	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	987	987	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P89105	UniProtKB	Sequence conflict	1045	1077	.	.	.	Note=DSDEEEAQMSGSEQNKNDDNDENNDNDDNDGLF->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04201 1 117
+Q04201	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000203244;Note=CUE domain-containing protein CUE4	
+Q04201	UniProtKB	Domain	74	116	.	.	.	Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468	
+Q04201	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q04201	UniProtKB	Cross-link	37	37	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q08412 1 411
+Q08412	UniProtKB	Chain	1	411	.	.	.	ID=PRO_0000270974;Note=Ubiquitin-binding protein CUE5	
+Q08412	UniProtKB	Domain	97	140	.	.	.	Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468	
+Q08412	UniProtKB	Motif	373	376	.	.	.	Note=AIM	
+Q08412	UniProtKB	Compositional bias	77	81	.	.	.	Note=Poly-Glu;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08412	UniProtKB	Compositional bias	204	207	.	.	.	Note=Poly-Arg;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08412	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08412	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08412	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08412	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q08412	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08412	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08412	UniProtKB	Modified residue	309	309	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08412	UniProtKB	Modified residue	318	318	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08412	UniProtKB	Modified residue	346	346	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08412	UniProtKB	Modified residue	348	348	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08412	UniProtKB	Modified residue	352	352	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08412	UniProtKB	Modified residue	364	364	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08412	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08412	UniProtKB	Modified residue	407	407	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08412	UniProtKB	Cross-link	15	15	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08412	UniProtKB	Cross-link	59	59	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08412	UniProtKB	Cross-link	76	76	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08412	UniProtKB	Cross-link	156	156	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08412	UniProtKB	Cross-link	354	354	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08412	UniProtKB	Cross-link	396	396	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+Q08412	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Impairs interaction with ubiquitin%3B when associated with A-110. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851	
+Q08412	UniProtKB	Mutagenesis	110	110	.	.	.	Note=Impairs interaction with ubiquitin%3B when associated with A-109. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851	
+Q08412	UniProtKB	Mutagenesis	135	135	.	.	.	Note=Impairs interaction with ubiquitin%3B when associated with A-136. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851	
+Q08412	UniProtKB	Mutagenesis	136	136	.	.	.	Note=Impairs interaction with ubiquitin%3B when associated with A-135. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851	
+Q08412	UniProtKB	Mutagenesis	373	373	.	.	.	Note=Impairs interaction with ATG8. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851	
+Q08412	UniProtKB	Mutagenesis	376	376	.	.	.	Note=Impairs interaction with ATG8. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851	
+##sequence-region P47050 1 842
+P47050	UniProtKB	Chain	1	842	.	.	.	ID=PRO_0000119807;Note=Cullin-8	
+P47050	UniProtKB	Region	1	50	.	.	.	Note=Required for interaction with MMS1	
+P47050	UniProtKB	Cross-link	791	791	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14519104;Dbxref=PMID:14519104	
+P47050	UniProtKB	Mutagenesis	680	686	.	.	.	Note=Disrupts interaction with HRT1 and prevents RUB1/NEDD8 modification. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12676951;Dbxref=PMID:12676951	
+P47050	UniProtKB	Mutagenesis	791	791	.	.	.	Note=Prevents RUB1/NEDD8 modification. K->A%2CR;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12676951,ECO:0000269|PubMed:14519104;Dbxref=PMID:12676951,PMID:14519104	
+##sequence-region P28320 1 278
+P28320	UniProtKB	Chain	1	278	.	.	.	ID=PRO_0000203163;Note=Protein CWC16	
+P28320	UniProtKB	Motif	242	258	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28320	UniProtKB	Motif	260	278	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28320	UniProtKB	Helix	17	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28320	UniProtKB	Beta strand	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28320	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28320	UniProtKB	Beta strand	50	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28320	UniProtKB	Beta strand	64	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28320	UniProtKB	Beta strand	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28320	UniProtKB	Beta strand	82	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28320	UniProtKB	Beta strand	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28320	UniProtKB	Beta strand	94	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28320	UniProtKB	Beta strand	101	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P53854 1 179
+P53854	UniProtKB	Chain	1	179	.	.	.	ID=PRO_0000079596;Note=Pre-mRNA-splicing factor CWC25	
+P53854	UniProtKB	Coiled coil	25	57	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53854	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53854	UniProtKB	Helix	6	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53854	UniProtKB	Beta strand	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53854	UniProtKB	Helix	19	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region Q12046 1 339
+Q12046	UniProtKB	Chain	1	339	.	.	.	ID=PRO_0000081552;Note=Pre-mRNA-splicing factor CWC2	
+Q12046	UniProtKB	Domain	135	228	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q12046	UniProtKB	Zinc finger	67	94	.	.	.	Note=C3H1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q12046	UniProtKB	Modified residue	335	335	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12046	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12046	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Inhibits cell growth. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19435883;Dbxref=PMID:19435883	
+Q12046	UniProtKB	Mutagenesis	79	79	.	.	.	Note=No effect. Synthetic lethal when associated with CLF1 lacking a TPR domain. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12871902;Dbxref=PMID:12871902	
+Q12046	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Inhibits cell growth. C->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19435883;Dbxref=PMID:19435883	
+Q12046	UniProtKB	Mutagenesis	186	186	.	.	.	Note=Inhibits cell growth. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19435883;Dbxref=PMID:19435883	
+Q12046	UniProtKB	Helix	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Beta strand	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TP2	
+Q12046	UniProtKB	Helix	30	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Beta strand	41	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	55	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	63	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Beta strand	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	96	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Beta strand	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Beta strand	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TP2	
+Q12046	UniProtKB	Helix	129	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TP2	
+Q12046	UniProtKB	Beta strand	136	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	153	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Beta strand	170	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Beta strand	181	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	189	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Beta strand	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12046	UniProtKB	Helix	212	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Beta strand	222	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L	
+Q12046	UniProtKB	Helix	232	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P53008 1 833
+P53008	UniProtKB	Chain	1	833	.	.	.	ID=PRO_0000057713;Note=Mannosyl-oligosaccharide glucosidase	
+P53008	UniProtKB	Topological domain	1	10	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53008	UniProtKB	Transmembrane	11	28	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53008	UniProtKB	Topological domain	29	833	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53008	UniProtKB	Active site	601	601	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181	
+P53008	UniProtKB	Active site	804	804	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181	
+P53008	UniProtKB	Binding site	42	42	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181	
+P53008	UniProtKB	Binding site	122	122	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181	
+P53008	UniProtKB	Binding site	143	143	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181	
+P53008	UniProtKB	Glycosylation	42	42	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53008	UniProtKB	Glycosylation	122	122	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53008	UniProtKB	Glycosylation	135	135	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53008	UniProtKB	Glycosylation	787	787	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53008	UniProtKB	Disulfide bond	669	685	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181	
+P53008	UniProtKB	Mutagenesis	601	601	.	.	.	Note=Abrogates catalytic activity. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181	
+P53008	UniProtKB	Mutagenesis	804	804	.	.	.	Note=Abrogates catalytic activity. E->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181	
+P53008	UniProtKB	Helix	35	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	54	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	68	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	97	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Turn	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	109	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Turn	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	121	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	136	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	152	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	164	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	171	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	183	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Turn	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	193	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	227	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	235	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	241	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	270	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	286	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	302	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	320	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	354	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	373	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	401	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Turn	415	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	420	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	423	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	438	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	461	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	466	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	475	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	489	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	529	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	534	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	567	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	576	578	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	596	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	616	635	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	639	658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Turn	663	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	670	673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Turn	675	677	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	681	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	689	696	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	706	715	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Turn	717	720	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	725	729	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Turn	734	737	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	742	745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	749	762	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	764	767	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	776	798	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	804	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Turn	808	810	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Beta strand	813	818	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	822	825	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+P53008	UniProtKB	Helix	826	831	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T	
+##sequence-region P28319 1 239
+P28319	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7768807;Dbxref=PMID:7768807	
+P28319	UniProtKB	Chain	21	217	.	.	.	ID=PRO_0000033250;Note=Cell wall protein CWP1	
+P28319	UniProtKB	Propeptide	218	239	.	.	.	ID=PRO_0000033251;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28319	UniProtKB	Repeat	194	212	.	.	.	Note=PIR1/2/3	
+P28319	UniProtKB	Compositional bias	106	198	.	.	.	Note=Ser-rich	
+P28319	UniProtKB	Site	204	204	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28319	UniProtKB	Lipidation	217	217	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28319	UniProtKB	Natural variant	19	27	.	.	.	Note=In strain: CLIB 410. IADSEEFGL->LPIPKNSAW	
+P28319	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28319	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28319	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28319	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28319	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28319	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28319	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28319	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28319	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28319	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07560 1 283
+Q07560	UniProtKB	Chain	1	283	.	.	.	ID=PRO_0000056810;Note=Cardiolipin synthase (CMP-forming)	
+Q07560	UniProtKB	Transmembrane	83	103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07560	UniProtKB	Transmembrane	155	175	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07560	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08226 1 957
+Q08226	UniProtKB	Chain	1	957	.	.	.	ID=PRO_0000235920;Note=Protein CRT10	
+Q08226	UniProtKB	Modified residue	704	704	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08226	UniProtKB	Sequence conflict	604	604	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53859 1 292
+P53859	UniProtKB	Chain	1	292	.	.	.	ID=PRO_0000079403;Note=Exosome complex component CSL4	
+P53859	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P53859	UniProtKB	Beta strand	9	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	15	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	41	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	51	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	60	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	106	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Helix	115	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+P53859	UniProtKB	Turn	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+P53859	UniProtKB	Helix	124	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+P53859	UniProtKB	Beta strand	138	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	148	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Helix	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Turn	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Turn	195	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+P53859	UniProtKB	Beta strand	202	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Helix	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Helix	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Helix	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	229	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	240	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	253	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Turn	259	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	268	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Turn	278	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53859	UniProtKB	Beta strand	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+##sequence-region Q03981 1 162
+Q03981	UniProtKB	Chain	1	162	.	.	.	ID=PRO_0000121020;Note=COP9 signalosome complex subunit 9	
+Q03981	UniProtKB	Domain	6	118	.	.	.	Note=PCI	
+##sequence-region P38226 1 397
+P38226	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000208207;Note=Uncharacterized acyltransferase CST26	
+P38226	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38226	UniProtKB	Transmembrane	58	78	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38226	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38226	UniProtKB	Transmembrane	377	397	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38226	UniProtKB	Motif	112	117	.	.	.	Note=HXXXXD motif	
+##sequence-region P36075 1 443
+P36075	UniProtKB	Chain	1	443	.	.	.	ID=PRO_0000079558;Note=Ubiquitin-binding protein CUE2	
+P36075	UniProtKB	Domain	8	51	.	.	.	Note=CUE 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468	
+P36075	UniProtKB	Domain	55	98	.	.	.	Note=CUE 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468	
+P36075	UniProtKB	Domain	347	443	.	.	.	Note=Smr;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00321	
+P36075	UniProtKB	Helix	9	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OTR	
+P36075	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OTR	
+P36075	UniProtKB	Helix	25	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OTR	
+P36075	UniProtKB	Turn	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OTR	
+P36075	UniProtKB	Helix	40	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OTR	
+##sequence-region Q06469 1 252
+Q06469	UniProtKB	Chain	1	252	.	.	.	ID=PRO_0000257830;Note=Curing of [URE3] protein 1	
+##sequence-region P21657 1 970
+P21657	UniProtKB	Chain	1	970	.	.	.	ID=PRO_0000114947;Note=Transcriptional activator protein DAL81	
+P21657	UniProtKB	DNA binding	150	179	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P21657	UniProtKB	Compositional bias	24	50	.	.	.	Note=Asn-rich	
+P21657	UniProtKB	Compositional bias	73	88	.	.	.	Note=Poly-Gln	
+P21657	UniProtKB	Compositional bias	127	139	.	.	.	Note=Asn-rich	
+P21657	UniProtKB	Compositional bias	227	237	.	.	.	Note=Poly-Gln	
+P21657	UniProtKB	Modified residue	833	833	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21657	UniProtKB	Sequence conflict	77	82	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21657	UniProtKB	Sequence conflict	465	465	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21657	UniProtKB	Sequence conflict	497	497	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21657	UniProtKB	Sequence conflict	507	507	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21657	UniProtKB	Sequence conflict	760	760	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21657	UniProtKB	Sequence conflict	785	785	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47179 1 1161
+P47179	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47179	UniProtKB	Chain	20	1137	.	.	.	ID=PRO_0000033243;Note=Cell wall protein DAN4	
+P47179	UniProtKB	Propeptide	1138	1161	.	.	.	ID=PRO_0000033244;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47179	UniProtKB	Repeat	373	384	.	.	.	Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	385	396	.	.	.	Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	397	408	.	.	.	Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	409	420	.	.	.	Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	421	432	.	.	.	Note=1-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	433	444	.	.	.	Note=1-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	445	456	.	.	.	Note=1-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	457	468	.	.	.	Note=1-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	469	480	.	.	.	Note=1-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	481	492	.	.	.	Note=1-10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	493	504	.	.	.	Note=1-11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	505	516	.	.	.	Note=1-12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	517	528	.	.	.	Note=1-13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	529	540	.	.	.	Note=1-14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	826	913	.	.	.	Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	914	1001	.	.	.	Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Repeat	1002	1040	.	.	.	Note=2-3%3B truncated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P47179	UniProtKB	Region	134	286	.	.	.	Note=46 X 3 AA tandem repeats of T-[SP]-T	
+P47179	UniProtKB	Region	373	540	.	.	.	Note=14 X 12 AA approximate tandem repeats	
+P47179	UniProtKB	Region	826	1040	.	.	.	Note=2.5 X 88 AA approximate tandem repeats	
+P47179	UniProtKB	Compositional bias	124	794	.	.	.	Note=Ser/Thr-rich	
+P47179	UniProtKB	Lipidation	1137	1137	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P22204 1 572
+P22204	UniProtKB	Chain	1	572	.	.	.	ID=PRO_0000085918;Note=Cell cycle protein kinase DBF2	
+P22204	UniProtKB	Domain	177	477	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22204	UniProtKB	Domain	478	555	.	.	.	Note=AGC-kinase C-terminal	
+P22204	UniProtKB	Nucleotide binding	183	191	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22204	UniProtKB	Active site	300	300	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P22204	UniProtKB	Binding site	206	206	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22204	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22204	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22204	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22204	UniProtKB	Modified residue	374	374	.	.	.	Note=Phosphoserine%3B by CDC15;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:11404483;Dbxref=PMID:18407956,PMID:11404483	
+P22204	UniProtKB	Modified residue	544	544	.	.	.	Note=Phosphothreonine%3B by CDC15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11404483;Dbxref=PMID:11404483	
+P22204	UniProtKB	Sequence conflict	11	12	.	.	.	Note=LL->YM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22204	UniProtKB	Sequence conflict	114	114	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22204	UniProtKB	Sequence conflict	246	246	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36120 1 742
+P36120	UniProtKB	Chain	1	742	.	.	.	ID=PRO_0000055037;Note=ATP-dependent RNA helicase DBP7	
+P36120	UniProtKB	Domain	178	372	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P36120	UniProtKB	Domain	405	605	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P36120	UniProtKB	Nucleotide binding	191	198	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P36120	UniProtKB	Motif	143	172	.	.	.	Note=Q motif	
+P36120	UniProtKB	Motif	307	310	.	.	.	Note=DEGD box	
+##sequence-region P24309 1 405
+P24309	UniProtKB	Chain	1	405	.	.	.	ID=PRO_0000079797;Note=Lariat debranching enzyme	
+P24309	UniProtKB	Modified residue	269	269	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P32347 1 362
+P32347	UniProtKB	Chain	1	362	.	.	.	ID=PRO_0000187577;Note=Uroporphyrinogen decarboxylase	
+P32347	UniProtKB	Region	30	34	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32347	UniProtKB	Binding site	48	48	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32347	UniProtKB	Binding site	80	80	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32347	UniProtKB	Binding site	81	81	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32347	UniProtKB	Binding site	160	160	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32347	UniProtKB	Binding site	215	215	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32347	UniProtKB	Binding site	338	338	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32347	UniProtKB	Site	81	81	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32347	UniProtKB	Natural variant	59	59	.	.	.	Note=In HEM12-6 and HEM12-12. S->F	
+P32347	UniProtKB	Natural variant	62	62	.	.	.	Note=In HEM12-14. T->I	
+P32347	UniProtKB	Natural variant	107	107	.	.	.	Note=In HEM12-3 and HEM12-13. L->S	
+P32347	UniProtKB	Natural variant	215	215	.	.	.	Note=In HEM12-2 and HEM12-11. S->N	
+P32347	UniProtKB	Mutagenesis	33	33	.	.	.	Note=Inactivation. G->D	
+P32347	UniProtKB	Mutagenesis	300	300	.	.	.	Note=Inactivation. G->D	
+##sequence-region P36091 1 449
+P36091	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Chain	22	428	.	.	.	ID=PRO_0000012125;Note=Mannan endo-1%2C6-alpha-mannosidase DCW1	
+P36091	UniProtKB	Propeptide	429	449	.	.	.	ID=PRO_0000012126;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Lipidation	428	428	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	34	34	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	84	84	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	109	109	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	133	133	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	203	203	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	225	225	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	240	240	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	265	265	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	281	281	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	337	337	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	362	362	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Glycosylation	420	420	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36091	UniProtKB	Sequence conflict	276	276	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99321 1 188
+Q99321	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085096;Dbxref=PMID:10085096	
+Q99321	UniProtKB	Chain	2	188	.	.	.	ID=PRO_0000057067;Note=Diphosphoinositol polyphosphate phosphohydrolase DDP1	
+Q99321	UniProtKB	Domain	30	179	.	.	.	Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794	
+Q99321	UniProtKB	Motif	65	86	.	.	.	Note=Nudix box	
+Q99321	UniProtKB	Metal binding	80	80	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99321	UniProtKB	Metal binding	84	84	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53899 1 274
+P53899	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000203418;Note=CDC48-associated ubiquitin-like/zinc finger protein 1	
+P53899	UniProtKB	Zinc finger	15	58	.	.	.	Note=AN1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00449	
+P53899	UniProtKB	Region	170	266	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:24121501;Dbxref=PMID:24121501	
+P53899	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53899	UniProtKB	Beta strand	19	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4	
+P53899	UniProtKB	Beta strand	24	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4	
+P53899	UniProtKB	Turn	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4	
+P53899	UniProtKB	Helix	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4	
+P53899	UniProtKB	Helix	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4	
+P53899	UniProtKB	Helix	51	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4	
+##sequence-region P08678 1 2026
+P08678	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P08678	UniProtKB	Chain	2	2026	.	.	.	ID=PRO_0000195731;Note=Adenylate cyclase	
+P08678	UniProtKB	Domain	676	755	.	.	.	Note=Ras-associating;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00166	
+P08678	UniProtKB	Repeat	815	838	.	.	.	Note=LRR 1	
+P08678	UniProtKB	Repeat	842	862	.	.	.	Note=LRR 2	
+P08678	UniProtKB	Repeat	863	885	.	.	.	Note=LRR 3	
+P08678	UniProtKB	Repeat	886	908	.	.	.	Note=LRR 4	
+P08678	UniProtKB	Repeat	910	931	.	.	.	Note=LRR 5	
+P08678	UniProtKB	Repeat	932	955	.	.	.	Note=LRR 6	
+P08678	UniProtKB	Repeat	957	976	.	.	.	Note=LRR 7	
+P08678	UniProtKB	Repeat	977	999	.	.	.	Note=LRR 8	
+P08678	UniProtKB	Repeat	1001	1016	.	.	.	Note=LRR 9	
+P08678	UniProtKB	Repeat	1017	1040	.	.	.	Note=LRR 10	
+P08678	UniProtKB	Repeat	1042	1062	.	.	.	Note=LRR 11	
+P08678	UniProtKB	Repeat	1063	1086	.	.	.	Note=LRR 12	
+P08678	UniProtKB	Repeat	1088	1109	.	.	.	Note=LRR 13	
+P08678	UniProtKB	Repeat	1110	1132	.	.	.	Note=LRR 14	
+P08678	UniProtKB	Repeat	1134	1156	.	.	.	Note=LRR 15	
+P08678	UniProtKB	Repeat	1188	1209	.	.	.	Note=LRR 16	
+P08678	UniProtKB	Repeat	1210	1232	.	.	.	Note=LRR 17	
+P08678	UniProtKB	Repeat	1233	1256	.	.	.	Note=LRR 18	
+P08678	UniProtKB	Repeat	1258	1280	.	.	.	Note=LRR 19	
+P08678	UniProtKB	Repeat	1285	1308	.	.	.	Note=LRR 20	
+P08678	UniProtKB	Domain	1357	1624	.	.	.	Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082	
+P08678	UniProtKB	Domain	1668	1805	.	.	.	Note=Guanylate cyclase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00099	
+P08678	UniProtKB	Metal binding	1673	1673	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08678	UniProtKB	Metal binding	1716	1716	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08678	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P08678	UniProtKB	Modified residue	376	376	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P08678	UniProtKB	Modified residue	389	389	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P08678	UniProtKB	Modified residue	433	433	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08678	UniProtKB	Modified residue	487	487	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P08678	UniProtKB	Modified residue	497	497	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08678	UniProtKB	Modified residue	562	562	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08678	UniProtKB	Mutagenesis	1651	1651	.	.	.	Note=Attenuation of the response to Ras proteins. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1991451;Dbxref=PMID:1991451	
+P08678	UniProtKB	Mutagenesis	1651	1651	.	.	.	Note=Weak Ras-independent activity. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1991451;Dbxref=PMID:1991451	
+P08678	UniProtKB	Sequence conflict	262	262	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	548	548	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	592	592	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	709	709	.	.	.	Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	962	962	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	1388	1388	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	1427	1427	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	1461	1461	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	1566	1566	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	1735	1735	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	1956	1956	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	1996	1996	.	.	.	Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08678	UniProtKB	Sequence conflict	2009	2026	.	.	.	Note=NVVDELLQMVKNAKDLST->MLLTNFYKWLRTQRIYQLEFCS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00163 1 385
+P00163	UniProtKB	Chain	1	385	.	.	.	ID=PRO_0000061769;Note=Cytochrome b	
+P00163	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Transmembrane	76	98	.	.	.	Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Transmembrane	225	245	.	.	.	Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Transmembrane	289	309	.	.	.	Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Transmembrane	321	341	.	.	.	Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Transmembrane	348	368	.	.	.	Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Metal binding	82	82	.	.	.	Note=Iron 1 (heme b562 axial ligand);Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000244|PDB:1KB9,ECO:0000244|PDB:1KYO,ECO:0000244|PDB:1P84,ECO:0000244|PDB:2IBZ,ECO:0000244|PDB:3CX5,ECO:0000244|PDB:3CXH,ECO:0000244|PDB:4PD4,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Metal binding	96	96	.	.	.	Note=Iron 2 (heme b566 axial ligand);Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000244|PDB:1KB9,ECO:0000244|PDB:1KYO,ECO:0000244|PDB:1P84,ECO:0000244|PDB:2IBZ,ECO:0000244|PDB:3CX5,ECO:0000244|PDB:3CXH,ECO:0000244|PDB:4PD4,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Metal binding	183	183	.	.	.	Note=Iron 1 (heme b562 axial ligand);Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000244|PDB:1KB9,ECO:0000244|PDB:1KYO,ECO:0000244|PDB:1P84,ECO:0000244|PDB:2IBZ,ECO:0000244|PDB:3CX5,ECO:0000244|PDB:3CXH,ECO:0000244|PDB:4PD4,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Metal binding	197	197	.	.	.	Note=Iron 2 (heme b566 axial ligand);Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000244|PDB:1KB9,ECO:0000244|PDB:1KYO,ECO:0000244|PDB:1P84,ECO:0000244|PDB:2IBZ,ECO:0000244|PDB:3CX5,ECO:0000244|PDB:3CXH,ECO:0000244|PDB:4PD4,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631	
+P00163	UniProtKB	Binding site	202	202	.	.	.	Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
+P00163	UniProtKB	Natural variant	131	131	.	.	.	Note=In mutant W7 which is respiratory deficient. G->S	
+P00163	UniProtKB	Sequence conflict	122	122	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00163	UniProtKB	Sequence conflict	122	122	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00163	UniProtKB	Sequence conflict	269	269	.	.	.	Note=I->ID;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00163	UniProtKB	Sequence conflict	269	269	.	.	.	Note=I->ID;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00163	UniProtKB	Helix	3	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	10	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	32	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Turn	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	61	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	75	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Turn	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Turn	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYO	
+P00163	UniProtKB	Helix	111	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	138	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Turn	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	158	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Beta strand	168	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	173	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Beta strand	217	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Turn	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	224	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Turn	248	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	254	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	276	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Beta strand	285	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	288	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	301	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	305	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Beta strand	312	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	320	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	348	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00163	UniProtKB	Helix	366	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+##sequence-region P53206 1 393
+P53206	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000167130;Note=Putative cysteine synthase	
+P53206	UniProtKB	Transmembrane	12	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53206	UniProtKB	Region	230	234	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16703	
+P53206	UniProtKB	Binding site	338	338	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16703	
+P53206	UniProtKB	Modified residue	86	86	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16703	
+##sequence-region Q00873 1 224
+Q00873	UniProtKB	Chain	1	224	.	.	.	ID=PRO_0000121719;Note=Cytochrome c1 heme lyase	
+##sequence-region P43550 1 591
+P43550	UniProtKB	Chain	1	591	.	.	.	ID=PRO_0000121523;Note=Dihydroxyacetone kinase 2	
+P43550	UniProtKB	Domain	8	344	.	.	.	Note=DhaK;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00814	
+P43550	UniProtKB	Domain	384	587	.	.	.	Note=DhaL;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00813	
+P43550	UniProtKB	Nucleotide binding	413	416	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43550	UniProtKB	Nucleotide binding	459	460	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43550	UniProtKB	Nucleotide binding	511	512	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43550	UniProtKB	Nucleotide binding	572	574	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43550	UniProtKB	Region	58	61	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43550	UniProtKB	Active site	223	223	.	.	.	Note=Tele-hemiaminal-histidine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00814	
+P43550	UniProtKB	Binding site	109	109	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43550	UniProtKB	Binding site	114	114	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P47178 1 298
+P47178	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10322008;Dbxref=PMID:10322008	
+P47178	UniProtKB	Chain	20	275	.	.	.	ID=PRO_0000033239;Note=Cell wall protein DAN1	
+P47178	UniProtKB	Propeptide	276	298	.	.	.	ID=PRO_0000033240;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47178	UniProtKB	Lipidation	275	275	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47178	UniProtKB	Sequence conflict	115	115	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P18962 1 818
+P18962	UniProtKB	Chain	1	818	.	.	.	ID=PRO_0000122421;Note=Dipeptidyl aminopeptidase B	
+P18962	UniProtKB	Topological domain	1	29	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18962	UniProtKB	Transmembrane	30	45	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18962	UniProtKB	Topological domain	46	818	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18962	UniProtKB	Active site	679	679	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10084	
+P18962	UniProtKB	Active site	756	756	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10084	
+P18962	UniProtKB	Active site	789	789	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10084	
+P18962	UniProtKB	Glycosylation	63	63	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18962	UniProtKB	Glycosylation	79	79	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18962	UniProtKB	Glycosylation	110	110	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18962	UniProtKB	Glycosylation	139	139	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18962	UniProtKB	Glycosylation	372	372	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18962	UniProtKB	Glycosylation	392	392	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18962	UniProtKB	Glycosylation	421	421	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18962	UniProtKB	Glycosylation	738	738	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18962	UniProtKB	Sequence conflict	83	83	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18962	UniProtKB	Sequence conflict	125	125	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18962	UniProtKB	Sequence conflict	182	188	.	.	.	Note=FEEIGNE->LRRLET;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18962	UniProtKB	Sequence conflict	200	200	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18962	UniProtKB	Sequence conflict	318	318	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18962	UniProtKB	Sequence conflict	366	375	.	.	.	Note=TSNVVRNESS->DFKRGKERKF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18962	UniProtKB	Sequence conflict	808	818	.	.	.	Note=AKRAFDGQFVK->QSVLSMGNLTNELTIYSSSHRDIHKTFSYLHTMYI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18962	UniProtKB	Helix	34	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KL4	
+P18962	UniProtKB	Turn	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KL4	
+P18962	UniProtKB	Helix	42	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KL4	
+##sequence-region P47005 1 663
+P47005	UniProtKB	Chain	1	663	.	.	.	ID=PRO_0000119971;Note=F-box protein DAS1	
+P47005	UniProtKB	Domain	46	91	.	.	.	Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080	
+P47005	UniProtKB	Compositional bias	533	539	.	.	.	Note=Poly-Asp	
+P47005	UniProtKB	Compositional bias	647	652	.	.	.	Note=Poly-Asn	
+##sequence-region Q12084 1 232
+Q12084	UniProtKB	Chain	1	232	.	.	.	ID=PRO_0000242489;Note=Putative uridine kinase DAS2	
+Q12084	UniProtKB	Nucleotide binding	17	24	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12517 1 231
+Q12517	UniProtKB	Chain	1	231	.	.	.	ID=PRO_0000232998;Note=mRNA-decapping enzyme subunit 1	
+Q12517	UniProtKB	Mutagenesis	16	20	.	.	.	Note=In DCP1-17%3B partial loss of mRNA-decapping activity. EFYRK->AFYAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156	
+Q12517	UniProtKB	Mutagenesis	29	31	.	.	.	Note=In DCP1-2%3B strong loss of mRNA decapping activity at 36 degrees Celsius. RYD->AYA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10101156,ECO:0000269|PubMed:14758354;Dbxref=PMID:10101156,PMID:14758354	
+Q12517	UniProtKB	Mutagenesis	32	34	.	.	.	Note=Partial loss of mRNA-decapping activity. PKI->AKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14758354;Dbxref=PMID:14758354	
+Q12517	UniProtKB	Mutagenesis	37	38	.	.	.	Note=Strong loss of mRNA-decapping activity%3B when associated with A-217 and A-221. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14758354;Dbxref=PMID:14758354	
+Q12517	UniProtKB	Mutagenesis	47	47	.	.	.	Note=In DCP1-32%3B partial loss of mRNA decapping activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156	
+Q12517	UniProtKB	Mutagenesis	47	47	.	.	.	Note=In DCP1-35%3B partial loss of mRNA decapping activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156	
+Q12517	UniProtKB	Mutagenesis	48	50	.	.	.	Note=In DCP1-4%3B partial loss of mRNA decapping activity. In DCP1-43%3B strong loss of mRNA-decapping activity%3B when associated with A-187 and A-188. In DCP1-44%3B strong loss of mRNA-decapping activity%3B when associated with A-216 and A-219. KWD->AWA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156	
+Q12517	UniProtKB	Mutagenesis	56	56	.	.	.	Note=In DCP1-31%3B partial loss of mRNA decapping activity. W->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10101156,ECO:0000269|PubMed:14758354,ECO:0000269|PubMed:8757137;Dbxref=PMID:10101156,PMID:14758354,PMID:8757137	
+Q12517	UniProtKB	Mutagenesis	70	70	.	.	.	Note=In DCP1-33%3B strong loss of mRNA decapping activity. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10101156,ECO:0000269|PubMed:14758354;Dbxref=PMID:10101156,PMID:14758354	
+Q12517	UniProtKB	Mutagenesis	156	156	.	.	.	Note=In DCP1-1%3B strong loss of mRNA decapping activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156	
+Q12517	UniProtKB	Mutagenesis	187	188	.	.	.	Note=In DCP1-19%3B partial loss of mRNA decapping activity. In DCP1-43%3B strong loss of mRNA-decapping activity%3B when associated with A-48 and A-50. KD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156	
+Q12517	UniProtKB	Mutagenesis	204	204	.	.	.	Note=In DCP1-33%3B partial loss of mRNA decapping activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156	
+Q12517	UniProtKB	Mutagenesis	216	219	.	.	.	Note=In DCP1-25%3B partial loss of mRNA-decapping activity. In DCP1-44%3B strong loss of mRNA-decapping activity%3B when associated with A-48 and A-50. ELIK->ALIA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156	
+Q12517	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Strong loss of mRNA-decapping activity%3B when associated with A-37%3B A-38 and A-221. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14758354;Dbxref=PMID:14758354	
+Q12517	UniProtKB	Mutagenesis	221	221	.	.	.	Note=Strong loss of mRNA-decapping activity%3B when associated with A-37%3B A-38 and A-217. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14758354;Dbxref=PMID:14758354	
+Q12517	UniProtKB	Helix	24	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+Q12517	UniProtKB	Beta strand	34	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+Q12517	UniProtKB	Turn	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+Q12517	UniProtKB	Beta strand	55	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+Q12517	UniProtKB	Beta strand	139	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+Q12517	UniProtKB	Beta strand	152	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+Q12517	UniProtKB	Helix	160	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+Q12517	UniProtKB	Helix	171	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+Q12517	UniProtKB	Beta strand	183	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+Q12517	UniProtKB	Beta strand	190	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+Q12517	UniProtKB	Beta strand	200	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+Q12517	UniProtKB	Helix	208	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67	
+##sequence-region Q12123 1 353
+Q12123	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15240832;Dbxref=PMID:15240832	
+Q12123	UniProtKB	Chain	2	353	.	.	.	ID=PRO_0000109799;Note=Inactive diphosphatase DCS2	
+Q12123	UniProtKB	Motif	265	269	.	.	.	Note=Histidine triad motif;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12123	UniProtKB	Modified residue	341	341	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P06773 1 312
+P06773	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000171697;Note=Deoxycytidylate deaminase	
+P06773	UniProtKB	Domain	162	291	.	.	.	Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083	
+P06773	UniProtKB	Active site	235	235	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06773	UniProtKB	Metal binding	233	233	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06773	UniProtKB	Metal binding	260	260	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06773	UniProtKB	Metal binding	263	263	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06773	UniProtKB	Sequence conflict	78	78	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38877 1 133
+P38877	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000079494;Note=Chromosome transmission fidelity protein 8	
+P38877	UniProtKB	Beta strand	3	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P38877	UniProtKB	Helix	9	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P38877	UniProtKB	Beta strand	22	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P38877	UniProtKB	Beta strand	29	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P38877	UniProtKB	Helix	45	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P38877	UniProtKB	Turn	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P38877	UniProtKB	Beta strand	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P38877	UniProtKB	Beta strand	65	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P38877	UniProtKB	Turn	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P38877	UniProtKB	Beta strand	88	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P38877	UniProtKB	Turn	108	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P38877	UniProtKB	Beta strand	112	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+##sequence-region P46963 1 296
+P46963	UniProtKB	Chain	1	296	.	.	.	ID=PRO_0000079495;Note=CTD kinase subunit gamma	
+P46963	UniProtKB	Modified residue	35	35	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46963	UniProtKB	Mutagenesis	274	296	.	.	.	Note=No interaction with CTK2. Still interacts with CTK1. Missing	
+P46963	UniProtKB	Sequence conflict	101	101	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46963	UniProtKB	Sequence conflict	112	112	.	.	.	Note=M->MLM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46963	UniProtKB	Sequence conflict	163	163	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46963	UniProtKB	Sequence conflict	174	174	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46963	UniProtKB	Sequence conflict	295	295	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06686 1 241
+Q06686	UniProtKB	Chain	1	241	.	.	.	ID=PRO_0000195047;Note=Copper transport protein CTR3	
+Q06686	UniProtKB	Topological domain	1	41	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06686	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06686	UniProtKB	Topological domain	63	159	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06686	UniProtKB	Transmembrane	160	180	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06686	UniProtKB	Topological domain	181	182	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06686	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06686	UniProtKB	Topological domain	204	241	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53088 1 359
+P53088	UniProtKB	Chain	1	359	.	.	.	ID=PRO_0000219889;Note=Cytoplasmic tRNA 2-thiolation protein 1	
+P53088	UniProtKB	Sequence conflict	356	359	.	.	.	Note=KLSF->NSA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53137 1 624
+P53137	UniProtKB	Chain	1	624	.	.	.	ID=PRO_0000202749;Note=CUE domain-containing protein 3	
+P53137	UniProtKB	Domain	316	359	.	.	.	Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468	
+P53137	UniProtKB	Modified residue	377	377	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P15315 1 225
+P15315	UniProtKB	Chain	1	225	.	.	.	ID=PRO_0000194926;Note=Transcriptional activator protein CUP2	
+P15315	UniProtKB	DNA binding	1	40	.	.	.	Note=Copper-fist;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+P15315	UniProtKB	Region	1	108	.	.	.	Note=Binds copper and DNA	
+P15315	UniProtKB	Region	109	225	.	.	.	Note=Required for transcriptional activation	
+P15315	UniProtKB	Metal binding	11	11	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+P15315	UniProtKB	Metal binding	14	14	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+P15315	UniProtKB	Metal binding	23	23	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+P15315	UniProtKB	Metal binding	25	25	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+##sequence-region Q03772 1 175
+Q03772	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000218244;Note=Pre-mRNA-splicing factor CWC15	
+Q03772	UniProtKB	Coiled coil	85	110	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03772	UniProtKB	Helix	15	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03772	UniProtKB	Helix	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03772	UniProtKB	Beta strand	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03772	UniProtKB	Helix	164	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P46947 1 266
+P46947	UniProtKB	Chain	1	266	.	.	.	ID=PRO_0000079610;Note=Pre-mRNA-splicing factor CWC26	
+P46947	UniProtKB	Compositional bias	15	25	.	.	.	Note=Poly-Lys	
+P46947	UniProtKB	Helix	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MY2	
+P46947	UniProtKB	Helix	243	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MY2	
+P46947	UniProtKB	Beta strand	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UQT	
+##sequence-region Q02770 1 301
+Q02770	UniProtKB	Chain	1	301	.	.	.	ID=PRO_0000064189;Note=Peptidyl-prolyl isomerase CWC27	
+Q02770	UniProtKB	Domain	9	159	.	.	.	Note=PPIase cyclophilin-type	
+##sequence-region P07143 1 309
+P07143	UniProtKB	Transit peptide	1	61	.	.	.	Note=Mitochondrion	
+P07143	UniProtKB	Chain	62	309	.	.	.	ID=PRO_0000006566;Note=Cytochrome c1%2C heme protein%2C mitochondrial	
+P07143	UniProtKB	Transmembrane	273	287	.	.	.	Note=Helical%3B Note%3DAnchors to the membrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07143	UniProtKB	Domain	88	241	.	.	.	Note=Cytochrome c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00433	
+P07143	UniProtKB	Metal binding	105	105	.	.	.	Note=Iron (heme axial ligand)	
+P07143	UniProtKB	Metal binding	225	225	.	.	.	Note=Iron (heme axial ligand)	
+P07143	UniProtKB	Binding site	101	101	.	.	.	Note=Heme (covalent)	
+P07143	UniProtKB	Binding site	104	104	.	.	.	Note=Heme (covalent)	
+P07143	UniProtKB	Mutagenesis	272	272	.	.	.	Note=Loss of RIP1 from the bc1 complex. K->A	
+P07143	UniProtKB	Mutagenesis	288	288	.	.	.	Note=Loss of CYT1 and COB from the bc1 complex%3B when associated with L-289 and L-296. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11880631;Dbxref=PMID:11880631	
+P07143	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Loss of CYT1 and COB from the bc1 complex%3B when associated with L-288 and L-296. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11880631;Dbxref=PMID:11880631	
+P07143	UniProtKB	Mutagenesis	296	296	.	.	.	Note=Loss of CYT1 and COB from the bc1 complex%3B when associated with L-288 and L-289. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11880631;Dbxref=PMID:11880631	
+P07143	UniProtKB	Helix	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Helix	87	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Helix	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Helix	112	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Turn	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Helix	122	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Beta strand	132	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Beta strand	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PD4	
+P07143	UniProtKB	Beta strand	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Beta strand	158	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PD4	
+P07143	UniProtKB	Helix	162	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Turn	168	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Turn	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Beta strand	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PD4	
+P07143	UniProtKB	Helix	187	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Beta strand	216	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P84	
+P07143	UniProtKB	Beta strand	221	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Helix	244	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Helix	263	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07143	UniProtKB	Beta strand	299	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+##sequence-region P38909 1 366
+P38909	UniProtKB	Transit peptide	1	50	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38909	UniProtKB	Chain	51	366	.	.	.	ID=PRO_0000079749;Note=Cytochrome c mitochondrial import factor CYC2	
+P38909	UniProtKB	Domain	63	184	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+##sequence-region P15365 1 543
+P15365	UniProtKB	Chain	1	543	.	.	.	ID=PRO_0000121366;Note=Allantoate permease	
+P15365	UniProtKB	Topological domain	1	80	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	81	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	98	123	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	124	145	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	146	154	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	155	171	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	172	178	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	179	200	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	201	213	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	214	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	238	248	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	249	269	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	270	317	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	318	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	343	352	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	353	377	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	378	389	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	390	411	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	412	417	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	418	435	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	436	453	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	454	472	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	473	482	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Transmembrane	483	504	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15365	UniProtKB	Topological domain	505	543	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P26343 1 269
+P26343	UniProtKB	Chain	1	269	.	.	.	ID=PRO_0000083470;Note=Nitrogen regulatory protein DAL80	
+P26343	UniProtKB	Zinc finger	31	55	.	.	.	Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094	
+P26343	UniProtKB	Compositional bias	79	100	.	.	.	Note=Asn-rich	
+P26343	UniProtKB	Compositional bias	101	108	.	.	.	Note=Arg/Lys-rich (basic)	
+P26343	UniProtKB	Sequence conflict	6	6	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P26343	UniProtKB	Sequence conflict	207	207	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12091 1 152
+Q12091	UniProtKB	Chain	1	152	.	.	.	ID=PRO_0000121747;Note=Damage response protein 1	
+Q12091	UniProtKB	Domain	46	145	.	.	.	Note=Cytochrome b5 heme-binding	
+##sequence-region P24784 1 617
+P24784	UniProtKB	Chain	1	617	.	.	.	ID=PRO_0000055016;Note=ATP-dependent RNA helicase DBP1	
+P24784	UniProtKB	Domain	185	374	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P24784	UniProtKB	Domain	385	545	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P24784	UniProtKB	Nucleotide binding	198	205	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P24784	UniProtKB	Motif	154	182	.	.	.	Note=Q motif	
+P24784	UniProtKB	Motif	318	321	.	.	.	Note=DEAD box	
+P24784	UniProtKB	Sequence conflict	43	44	.	.	.	Note=ST->RS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24784	UniProtKB	Sequence conflict	48	48	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24784	UniProtKB	Sequence conflict	88	88	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24784	UniProtKB	Sequence conflict	115	115	.	.	.	Note=E->QK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24784	UniProtKB	Sequence conflict	496	496	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06218 1 594
+Q06218	UniProtKB	Chain	1	594	.	.	.	ID=PRO_0000055039;Note=ATP-dependent RNA helicase DBP9	
+Q06218	UniProtKB	Domain	49	233	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q06218	UniProtKB	Domain	246	476	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q06218	UniProtKB	Nucleotide binding	62	69	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q06218	UniProtKB	Motif	17	45	.	.	.	Note=Q motif	
+Q06218	UniProtKB	Motif	179	182	.	.	.	Note=DEAD box	
+Q06218	UniProtKB	Mutagenesis	413	413	.	.	.	Note=Impairs helicase activity in vitro. R->A%2CK%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15028736;Dbxref=PMID:15028736	
+Q06218	UniProtKB	Sequence conflict	24	24	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04895 1 635
+Q04895	UniProtKB	Chain	1	635	.	.	.	ID=PRO_0000197919;Note=Allantoin permease	
+Q04895	UniProtKB	Topological domain	1	144	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	166	174	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	196	198	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	220	243	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	244	264	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	265	269	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	270	290	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	291	311	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	312	332	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	333	351	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	352	372	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	373	401	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	402	422	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	423	443	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	444	464	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	465	466	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	467	487	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	488	522	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	523	543	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	544	560	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Transmembrane	561	581	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04895	UniProtKB	Topological domain	582	635	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12389 1 995
+Q12389	UniProtKB	Chain	1	995	.	.	.	ID=PRO_0000055040;Note=ATP-dependent RNA helicase DBP10	
+Q12389	UniProtKB	Domain	168	340	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q12389	UniProtKB	Domain	418	568	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q12389	UniProtKB	Nucleotide binding	181	188	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q12389	UniProtKB	Motif	137	165	.	.	.	Note=Q motif	
+Q12389	UniProtKB	Motif	288	291	.	.	.	Note=DEAD box	
+Q12389	UniProtKB	Modified residue	101	101	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12389	UniProtKB	Modified residue	398	398	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12389	UniProtKB	Modified residue	400	400	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12389	UniProtKB	Sequence conflict	733	741	.	.	.	Note=SHSIEDEIL->HILSKMKFW;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12389	UniProtKB	Sequence conflict	733	741	.	.	.	Note=SHSIEDEIL->HILSKMKFW;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12389	UniProtKB	Sequence conflict	746	746	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12389	UniProtKB	Sequence conflict	746	746	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12389	UniProtKB	Sequence conflict	764	764	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12389	UniProtKB	Sequence conflict	764	764	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P24783 1 546
+P24783	UniProtKB	Chain	1	546	.	.	.	ID=PRO_0000055000;Note=ATP-dependent RNA helicase DBP2	
+P24783	UniProtKB	Domain	144	319	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P24783	UniProtKB	Domain	347	494	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P24783	UniProtKB	Nucleotide binding	157	164	.	.	.	Note=ATP	
+P24783	UniProtKB	Region	505	530	.	.	.	Note=RNA-binding RGG-box	
+P24783	UniProtKB	Motif	113	141	.	.	.	Note=Q motif	
+P24783	UniProtKB	Motif	267	270	.	.	.	Note=DEAD box	
+P24783	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P24783	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P24783	UniProtKB	Cross-link	474	474	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P24783	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Decreases nonsense-mediated mRNA decay. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11585918;Dbxref=PMID:11585918	
+P24783	UniProtKB	Mutagenesis	268	268	.	.	.	Note=Decreases nonsense-mediated mRNA decay. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11585918;Dbxref=PMID:11585918	
+P24783	UniProtKB	Mutagenesis	300	300	.	.	.	Note=Decreases nonsense-mediated mRNA decay. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11585918;Dbxref=PMID:11585918	
+P24783	UniProtKB	Mutagenesis	447	447	.	.	.	Note=Decreases nonsense-mediated mRNA decay. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11585918;Dbxref=PMID:11585918	
+P24783	UniProtKB	Sequence conflict	425	425	.	.	.	Note=D->GN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P20447 1 523
+P20447	UniProtKB	Chain	1	523	.	.	.	ID=PRO_0000055017;Note=ATP-dependent RNA helicase DBP3	
+P20447	UniProtKB	Domain	143	315	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P20447	UniProtKB	Domain	344	493	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P20447	UniProtKB	Nucleotide binding	156	163	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P20447	UniProtKB	Motif	114	140	.	.	.	Note=Q motif	
+P20447	UniProtKB	Motif	262	265	.	.	.	Note=DEAD box	
+P20447	UniProtKB	Sequence conflict	441	441	.	.	.	Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20447	UniProtKB	Sequence conflict	444	444	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P20449 1 482
+P20449	UniProtKB	Chain	1	482	.	.	.	ID=PRO_0000055019;Note=ATP-dependent RNA helicase DBP5	
+P20449	UniProtKB	Domain	125	292	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P20449	UniProtKB	Domain	303	480	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P20449	UniProtKB	Nucleotide binding	138	145	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P20449	UniProtKB	Motif	92	120	.	.	.	Note=Q motif	
+P20449	UniProtKB	Motif	239	242	.	.	.	Note=DEAD box	
+P20449	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P20449	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P20449	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P20449	UniProtKB	Mutagenesis	170	170	.	.	.	Note=In RAT8-7%3B accumulates poly(A)+ RNA in the nucleus at 16 degrees Celsius. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564048;Dbxref=PMID:9564048	
+P20449	UniProtKB	Mutagenesis	171	171	.	.	.	Note=In DBP5-2%3B accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius%3B when associated with L-236 and F-245. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564047;Dbxref=PMID:9564047	
+P20449	UniProtKB	Mutagenesis	220	220	.	.	.	Note=In DBP5-1%3B accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius%3B when associated with S-466. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564047;Dbxref=PMID:9564047	
+P20449	UniProtKB	Mutagenesis	236	236	.	.	.	Note=In DBP5-2%3B accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius%3B when associated with P-171 and F-245. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564047;Dbxref=PMID:9564047	
+P20449	UniProtKB	Mutagenesis	267	267	.	.	.	Note=In RAT8-2%3B accumulates poly(A)+ RNA in the nucleus at 16 and 37 degrees Celsius. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564048;Dbxref=PMID:9564048	
+P20449	UniProtKB	Mutagenesis	345	345	.	.	.	Note=In DBP5-2%3B accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius%3B when associated with P-171 and L-236. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564047;Dbxref=PMID:9564047	
+P20449	UniProtKB	Mutagenesis	385	385	.	.	.	Note=In RAT8-3%3B accumulates poly(A)+ RNA in the nucleus at 16 and 37 degrees Celsius. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564048;Dbxref=PMID:9564048	
+P20449	UniProtKB	Mutagenesis	466	466	.	.	.	Note=In DBP5-1%3B accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius%3B when associated with P-220. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564047;Dbxref=PMID:9564047	
+P20449	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE	
+P20449	UniProtKB	Helix	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE	
+P20449	UniProtKB	Helix	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE	
+P20449	UniProtKB	Helix	94	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE	
+P20449	UniProtKB	Helix	101	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE	
+P20449	UniProtKB	Helix	117	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RRM	
+P20449	UniProtKB	Beta strand	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	144	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	172	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Turn	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	193	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	210	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	216	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	235	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	241	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	250	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Turn	261	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE	
+P20449	UniProtKB	Beta strand	266	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	276	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Turn	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GFP	
+P20449	UniProtKB	Beta strand	304	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	314	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Turn	326	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	330	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	340	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	358	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RRM	
+P20449	UniProtKB	Helix	366	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Turn	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBF	
+P20449	UniProtKB	Beta strand	383	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	388	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	391	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	399	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Beta strand	413	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	417	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	425	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+P20449	UniProtKB	Beta strand	434	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Helix	443	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+P20449	UniProtKB	Turn	456	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEU	
+P20449	UniProtKB	Beta strand	462	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GFP	
+P20449	UniProtKB	Helix	469	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY	
+##sequence-region P53734 1 629
+P53734	UniProtKB	Chain	1	629	.	.	.	ID=PRO_0000055036;Note=ATP-dependent RNA helicase DBP6	
+P53734	UniProtKB	Domain	221	401	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53734	UniProtKB	Domain	437	603	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P53734	UniProtKB	Nucleotide binding	234	241	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53734	UniProtKB	Motif	197	205	.	.	.	Note=Q motif	
+P53734	UniProtKB	Motif	341	344	.	.	.	Note=DEAD box	
+P53734	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53734	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53734	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P21182 1 396
+P21182	UniProtKB	Chain	1	87	.	.	.	ID=PRO_0000030033;Note=S-adenosylmethionine decarboxylase beta chain	
+P21182	UniProtKB	Chain	88	396	.	.	.	ID=PRO_0000030034;Note=S-adenosylmethionine decarboxylase alpha chain	
+P21182	UniProtKB	Active site	29	29	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21182	UniProtKB	Active site	32	32	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21182	UniProtKB	Active site	88	88	.	.	.	Note=Schiff-base intermediate with substrate%3B via pyruvic acid;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21182	UniProtKB	Active site	102	102	.	.	.	Note=Proton donor%3B for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21182	UniProtKB	Active site	287	287	.	.	.	Note=Proton acceptor%3B for processing activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21182	UniProtKB	Active site	301	301	.	.	.	Note=Proton acceptor%3B for processing activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21182	UniProtKB	Site	87	88	.	.	.	Note=Cleavage (non-hydrolytic)%3B by autolysis	
+P21182	UniProtKB	Modified residue	88	88	.	.	.	Note=Pyruvic acid (Ser)%3B by autocatalysis	
+##sequence-region P25559 1 380
+P25559	UniProtKB	Chain	1	380	.	.	.	ID=PRO_0000079802;Note=Sister chromatid cohesion protein DCC1	
+P25559	UniProtKB	Beta strand	3	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P25559	UniProtKB	Beta strand	15	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P25559	UniProtKB	Helix	22	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P25559	UniProtKB	Beta strand	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P25559	UniProtKB	Beta strand	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P25559	UniProtKB	Beta strand	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P25559	UniProtKB	Beta strand	57	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P25559	UniProtKB	Beta strand	96	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P25559	UniProtKB	Beta strand	105	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P25559	UniProtKB	Helix	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	147	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Beta strand	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	158	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Beta strand	170	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Beta strand	176	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	182	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	208	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P25559	UniProtKB	Helix	228	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Beta strand	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	254	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Beta strand	270	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	277	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	298	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Beta strand	304	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Beta strand	312	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	318	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	325	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Beta strand	337	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	341	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	349	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Helix	358	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Beta strand	366	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+P25559	UniProtKB	Beta strand	375	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN	
+##sequence-region P08432 1 466
+P08432	UniProtKB	Chain	1	466	.	.	.	ID=PRO_0000149909;Note=Ornithine decarboxylase	
+P08432	UniProtKB	Region	318	321	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
+P08432	UniProtKB	Region	362	363	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07805	
+P08432	UniProtKB	Active site	411	411	.	.	.	Note=Proton donor%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
+P08432	UniProtKB	Binding site	247	247	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
+P08432	UniProtKB	Binding site	286	286	.	.	.	Note=Pyridoxal phosphate%3B via amino nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
+P08432	UniProtKB	Binding site	412	412	.	.	.	Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07805	
+P08432	UniProtKB	Binding site	441	441	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
+P08432	UniProtKB	Site	244	244	.	.	.	Note=Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00860	
+P08432	UniProtKB	Modified residue	116	116	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926	
+##sequence-region Q05924 1 578
+Q05924	UniProtKB	Chain	1	578	.	.	.	ID=PRO_0000079819;Note=Phosphatase DCR2	
+Q05924	UniProtKB	Nucleotide binding	116	123	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05924	UniProtKB	Compositional bias	520	527	.	.	.	Note=Poly-Gly	
+Q05924	UniProtKB	Mutagenesis	338	338	.	.	.	Note=20%25 phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15590836;Dbxref=PMID:15590836	
+##sequence-region P06634 1 604
+P06634	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P06634	UniProtKB	Chain	2	604	.	.	.	ID=PRO_0000055043;Note=ATP-dependent RNA helicase DED1	
+P06634	UniProtKB	Domain	173	362	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P06634	UniProtKB	Domain	373	533	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P06634	UniProtKB	Nucleotide binding	186	193	.	.	.	Note=ATP	
+P06634	UniProtKB	Motif	142	170	.	.	.	Note=Q motif	
+P06634	UniProtKB	Motif	306	309	.	.	.	Note=DEAD box	
+P06634	UniProtKB	Compositional bias	10	75	.	.	.	Note=Asn-rich	
+P06634	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P06634	UniProtKB	Modified residue	62	62	.	.	.	Note=Dimethylated arginine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23865587;Dbxref=PMID:23865587	
+P06634	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06634	UniProtKB	Modified residue	218	218	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06634	UniProtKB	Modified residue	263	263	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P06634	UniProtKB	Modified residue	535	535	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P06634	UniProtKB	Modified residue	539	539	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P06634	UniProtKB	Modified residue	543	543	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P06634	UniProtKB	Modified residue	572	572	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P06634	UniProtKB	Modified residue	576	576	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P06634	UniProtKB	Modified residue	598	598	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06634	UniProtKB	Cross-link	158	158	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P06634	UniProtKB	Mutagenesis	108	108	.	.	.	Note=In DED1-120%3B impairs protein synthesis at 15 degrees Celsius%3B when associated with D-494. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9045610;Dbxref=PMID:9045610	
+P06634	UniProtKB	Mutagenesis	144	144	.	.	.	Note=Slow growth at 18 and 30 degrees Celsius and no growth at 16 degrees Celsius. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868	
+P06634	UniProtKB	Mutagenesis	144	144	.	.	.	Note=Lethal. F->D%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868	
+P06634	UniProtKB	Mutagenesis	162	162	.	.	.	Note=Lethal in vivo and inhibits ATPase and helicase activities in vitro. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868	
+P06634	UniProtKB	Mutagenesis	162	162	.	.	.	Note=Slow growth at 18 degrees Celsius. F->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868	
+P06634	UniProtKB	Mutagenesis	162	162	.	.	.	Note=Reduces RNA-helicase activity about 5-fold in vitro. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868	
+P06634	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Reduces RNA-helicase activity about 2.5-fold in vitro. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868	
+P06634	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Slow growth at 18 and 36 degrees Celsius in vivo%2C and reduces RNA-helicase activity about 5-fold in vitro. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868	
+P06634	UniProtKB	Mutagenesis	169	169	.	.	.	Note=Lethal in vivo and impairs ATPase and RNA-helicase activities in vitro. Q->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868	
+P06634	UniProtKB	Mutagenesis	169	169	.	.	.	Note=Lethal. Q->C%2CD%2CF%2CG%2CH%2CK%2CL%2CM%2CN%2CS%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868	
+P06634	UniProtKB	Mutagenesis	192	192	.	.	.	Note=Impairs RNA-helicase activity in vitro. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868	
+P06634	UniProtKB	Mutagenesis	237	237	.	.	.	Note=In DED1-18%3B impairs BMV RNA synthesis%3B when associated with D-317. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069307;Dbxref=PMID:11069307	
+P06634	UniProtKB	Mutagenesis	307	307	.	.	.	Note=Lethal in vivo and impairs ATPase and RNA-helicase activities in vitro. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10364207;Dbxref=PMID:10364207	
+P06634	UniProtKB	Mutagenesis	317	317	.	.	.	Note=In DED1-18%3B impairs BMV RNA synthesis%3B when associated with M-237. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069307;Dbxref=PMID:11069307	
+P06634	UniProtKB	Mutagenesis	368	368	.	.	.	Note=In DED1-199%3B impairs protein synthesis at 15 degrees Celsius. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9045610;Dbxref=PMID:9045610	
+P06634	UniProtKB	Mutagenesis	405	405	.	.	.	Note=Reduces strongly ATPase activity and strand displacement activity. F->Y%2CM%2CL%2CA%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18332124;Dbxref=PMID:18332124	
+P06634	UniProtKB	Mutagenesis	486	486	.	.	.	Note=Reduces ATPase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18332124;Dbxref=PMID:18332124	
+P06634	UniProtKB	Mutagenesis	494	494	.	.	.	Note=In DED1-120%3B impairs protein synthesis at 15 degrees Celsius%3B when associated with D-108. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9045610;Dbxref=PMID:9045610	
+P06634	UniProtKB	Sequence conflict	37	37	.	.	.	Note=S->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38307 1 211
+P38307	UniProtKB	Chain	1	211	.	.	.	ID=PRO_0000219053;Note=Degradation in the endoplasmic reticulum protein 1	
+P38307	UniProtKB	Topological domain	1	4	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38307	UniProtKB	Transmembrane	5	25	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38307	UniProtKB	Topological domain	26	55	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38307	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38307	UniProtKB	Topological domain	77	93	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38307	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38307	UniProtKB	Topological domain	115	142	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38307	UniProtKB	Transmembrane	143	163	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38307	UniProtKB	Topological domain	164	211	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38307	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23363603;Dbxref=PMID:23363603	
+P38307	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Cleavage of initiator methionine%2C acetylation of Ala-2 by NatA%2C slightly reduced acetylation levels but no significant effect on endogenous stability or ability to degrade CPY*. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23363603;Dbxref=PMID:23363603	
+P38307	UniProtKB	Mutagenesis	2	2	.	.	.	Note=No effect on ability to degrade CPY*. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23363603;Dbxref=PMID:23363603	
+P38307	UniProtKB	Mutagenesis	2	2	.	.	.	Note=N-terminus not predicted to be acetylated. Strongly decreases endogenous stability. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23363603;Dbxref=PMID:23363603	
+P38307	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Predicted to lead to acetylation by NatC. No effect on endogenous stability or ability to degrade CPY*. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23363603;Dbxref=PMID:23363603	
+P38307	UniProtKB	Mutagenesis	59	59	.	.	.	Note=In der1-2%3B impairs the ability to degrade misfolded proteins. S->L	
+P38307	UniProtKB	Sequence conflict	145	145	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04930 1 467
+Q04930	UniProtKB	Chain	1	467	.	.	.	ID=PRO_0000227691;Note=Transcription factor CRF1	
+##sequence-region Q04659 1 317
+Q04659	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000203277;Note=Chromosome segregation in meiosis protein 3	
+##sequence-region P40512 1 444
+P40512	UniProtKB	Chain	1	444	.	.	.	ID=PRO_0000121028;Note=Cop9 signalosome complex subunit 11	
+P40512	UniProtKB	Domain	258	364	.	.	.	Note=PCI	
+##sequence-region P49956 1 741
+P49956	UniProtKB	Chain	1	741	.	.	.	ID=PRO_0000089645;Note=Chromosome transmission fidelity protein 18	
+P49956	UniProtKB	Nucleotide binding	183	190	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49956	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Fails to unload PCNA. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15964801;Dbxref=PMID:15964801	
+P49956	UniProtKB	Beta strand	719	722	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+P49956	UniProtKB	Helix	736	739	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM	
+##sequence-region Q01454 1 927
+Q01454	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448101;Dbxref=PMID:1448101	
+Q01454	UniProtKB	Chain	2	927	.	.	.	ID=PRO_0000050948;Note=DNA polymerase alpha-binding protein	
+Q01454	UniProtKB	Repeat	10	49	.	.	.	Note=WD 1	
+Q01454	UniProtKB	Repeat	134	173	.	.	.	Note=WD 2	
+Q01454	UniProtKB	Repeat	227	266	.	.	.	Note=WD 3	
+Q01454	UniProtKB	Repeat	273	313	.	.	.	Note=WD 4	
+Q01454	UniProtKB	Repeat	699	739	.	.	.	Note=WD 5	
+Q01454	UniProtKB	Modified residue	377	377	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q01454	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q01454	UniProtKB	Modified residue	398	398	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q01454	UniProtKB	Modified residue	401	401	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q01454	UniProtKB	Modified residue	411	411	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q01454	UniProtKB	Modified residue	463	463	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q01454	UniProtKB	Sequence conflict	112	112	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01454	UniProtKB	Sequence conflict	112	112	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01454	UniProtKB	Sequence conflict	588	588	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01454	UniProtKB	Sequence conflict	590	590	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01454	UniProtKB	Sequence conflict	601	601	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01454	UniProtKB	Sequence conflict	835	835	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01454	UniProtKB	Beta strand	489	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	498	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	510	518	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Turn	520	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	526	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	536	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	541	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Turn	549	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	553	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	566	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	578	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	588	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	596	600	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	606	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	615	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	624	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Turn	632	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	635	642	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	649	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Helix	666	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Helix	674	679	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	686	689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	695	698	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	703	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Turn	713	715	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	717	723	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Helix	724	731	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Turn	732	734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HOG	
+Q01454	UniProtKB	Beta strand	738	748	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	751	760	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	772	775	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Helix	783	795	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Helix	819	844	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Beta strand	847	849	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Helix	851	874	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Turn	875	877	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Helix	879	886	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Helix	892	904	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+Q01454	UniProtKB	Helix	908	924	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H	
+##sequence-region Q03375 1 135
+Q03375	UniProtKB	Chain	1	135	.	.	.	ID=PRO_0000123505;Note=Pre-mRNA-splicing factor CWC21	
+Q03375	UniProtKB	Region	53	97	.	.	.	Note=Interaction with PRP8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19854871;Dbxref=PMID:19854871	
+Q03375	UniProtKB	Coiled coil	65	102	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03375	UniProtKB	Beta strand	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q03375	UniProtKB	Beta strand	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P53769 1 259
+P53769	UniProtKB	Chain	1	259	.	.	.	ID=PRO_0000055895;Note=Pre-mRNA-splicing factor CWC24	
+P53769	UniProtKB	Zinc finger	138	166	.	.	.	Note=C3H1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+P53769	UniProtKB	Zinc finger	199	237	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P53769	UniProtKB	Modified residue	33	33	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53769	UniProtKB	Modified residue	105	105	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+##sequence-region P00045 1 113
+P00045	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000108338;Note=Cytochrome c iso-2	
+P00045	UniProtKB	Metal binding	28	28	.	.	.	Note=Iron (heme axial ligand)	
+P00045	UniProtKB	Metal binding	90	90	.	.	.	Note=Iron (heme axial ligand)	
+P00045	UniProtKB	Binding site	24	24	.	.	.	Note=Heme (covalent)	
+P00045	UniProtKB	Binding site	27	27	.	.	.	Note=Heme (covalent)	
+P00045	UniProtKB	Beta strand	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC	
+P00045	UniProtKB	Helix	13	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC	
+P00045	UniProtKB	Turn	24	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC	
+P00045	UniProtKB	Helix	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC	
+P00045	UniProtKB	Beta strand	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YEA	
+P00045	UniProtKB	Helix	60	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC	
+P00045	UniProtKB	Helix	71	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC	
+P00045	UniProtKB	Helix	81	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC	
+P00045	UniProtKB	Helix	98	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC	
+##sequence-region P47103 1 393
+P47103	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000064174;Note=Peptidyl-prolyl cis-trans isomerase CYP7	
+P47103	UniProtKB	Domain	8	196	.	.	.	Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156	
+P47103	UniProtKB	Repeat	240	273	.	.	.	Note=TPR 1	
+P47103	UniProtKB	Repeat	292	325	.	.	.	Note=TPR 2	
+P47103	UniProtKB	Repeat	330	363	.	.	.	Note=TPR 3	
+P47103	UniProtKB	Sequence conflict	237	237	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47103	UniProtKB	Beta strand	6	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	16	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Turn	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	31	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	61	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Turn	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	70	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Turn	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Turn	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	100	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	125	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	144	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Turn	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	160	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	168	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	189	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Beta strand	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	233	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	256	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Turn	277	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	281	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	308	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	326	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	346	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+P47103	UniProtKB	Helix	366	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE	
+##sequence-region P35176 1 225
+P35176	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35176	UniProtKB	Chain	23	225	.	.	.	ID=PRO_0000025488;Note=Peptidyl-prolyl cis-trans isomerase D	
+P35176	UniProtKB	Domain	37	195	.	.	.	Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156	
+P35176	UniProtKB	Motif	222	225	.	.	.	Note=Prevents secretion from ER	
+P35176	UniProtKB	Glycosylation	139	139	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P14832 1 162
+P14832	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:2687115;Dbxref=PMID:22814378,PMID:2687115	
+P14832	UniProtKB	Chain	2	162	.	.	.	ID=PRO_0000064132;Note=Peptidyl-prolyl cis-trans isomerase	
+P14832	UniProtKB	Domain	5	161	.	.	.	Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156	
+P14832	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:2687115,ECO:0000269|PubMed:8431466;Dbxref=PMID:22814378,PMID:2687115,PMID:8431466	
+P14832	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14832	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14832	UniProtKB	Modified residue	145	145	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P14832	UniProtKB	Cross-link	29	29	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14832	UniProtKB	Cross-link	42	42	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14832	UniProtKB	Cross-link	123	123	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14832	UniProtKB	Cross-link	139	139	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14832	UniProtKB	Cross-link	151	151	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14832	UniProtKB	Cross-link	158	158	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14832	UniProtKB	Beta strand	3	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Beta strand	13	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Turn	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Helix	28	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Turn	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Turn	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Beta strand	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Turn	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Beta strand	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Beta strand	92	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Beta strand	110	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Turn	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Beta strand	126	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Helix	134	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+P14832	UniProtKB	Beta strand	154	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN	
+##sequence-region P31373 1 394
+P31373	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8511969;Dbxref=PMID:8511969	
+P31373	UniProtKB	Chain	2	394	.	.	.	ID=PRO_0000114754;Note=Cystathionine gamma-lyase	
+P31373	UniProtKB	Binding site	52	52	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P31373	UniProtKB	Binding site	104	104	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P31373	UniProtKB	Binding site	109	109	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P31373	UniProtKB	Binding site	334	334	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P31373	UniProtKB	Modified residue	204	204	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P31373	UniProtKB	Modified residue	362	362	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P31373	UniProtKB	Helix	9	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	38	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Turn	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	56	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	72	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	80	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	96	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	105	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Turn	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	123	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	128	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	138	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Turn	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	158	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Turn	169	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	175	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	184	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	190	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	196	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Turn	202	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	215	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	222	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	241	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	254	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Turn	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	279	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	293	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	307	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	317	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	328	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	342	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Turn	346	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Turn	356	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	361	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Beta strand	368	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+P31373	UniProtKB	Helix	378	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P	
+##sequence-region Q12248 1 94
+Q12248	UniProtKB	Chain	1	94	.	.	.	ID=PRO_0000127613;Note=DASH complex subunit DAD1	
+Q12248	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P69850 1 94
+P69850	UniProtKB	Chain	1	94	.	.	.	ID=PRO_0000175951;Note=DASH complex subunit DAD3	
+##sequence-region P25334 1 318
+P25334	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25334	UniProtKB	Chain	21	318	.	.	.	ID=PRO_0000025494;Note=Peptidyl-prolyl cis-trans isomerase CPR4	
+P25334	UniProtKB	Transmembrane	286	303	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25334	UniProtKB	Domain	55	225	.	.	.	Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156	
+P25334	UniProtKB	Glycosylation	166	166	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P06106 1 444
+P06106	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7765825,ECO:0000269|PubMed:8511969;Dbxref=PMID:7765825,PMID:8511969	
+P06106	UniProtKB	Chain	2	444	.	.	.	ID=PRO_0000114776;Note=Homocysteine/cysteine synthase	
+P06106	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P06106	UniProtKB	Modified residue	209	209	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06721	
+P06106	UniProtKB	Cross-link	160	160	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P38719 1 431
+P38719	UniProtKB	Chain	1	431	.	.	.	ID=PRO_0000055038;Note=ATP-dependent RNA helicase DBP8	
+P38719	UniProtKB	Domain	33	209	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P38719	UniProtKB	Domain	242	389	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P38719	UniProtKB	Nucleotide binding	46	53	.	.	.	Note=ATP	
+P38719	UniProtKB	Motif	2	30	.	.	.	Note=Q motif	
+P38719	UniProtKB	Motif	155	158	.	.	.	Note=DEAD box	
+P38719	UniProtKB	Mutagenesis	51	52	.	.	.	Note=In DBP8-1%3B loss of activity. GK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11222764;Dbxref=PMID:11222764	
+P38719	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Decreases ATPase activity in vitro. K->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16772403;Dbxref=PMID:16772403	
+P38719	UniProtKB	Mutagenesis	155	156	.	.	.	Note=In DBP8-2%3B loss of activity. DE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11222764;Dbxref=PMID:11222764	
+P38719	UniProtKB	Mutagenesis	155	155	.	.	.	Note=Decreases ATPase activity in vitro. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16772403;Dbxref=PMID:16772403	
+P38719	UniProtKB	Mutagenesis	188	190	.	.	.	Note=In DBP8-3%3B severely affects growth. TAT->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11222764;Dbxref=PMID:11222764	
+P38719	UniProtKB	Mutagenesis	341	342	.	.	.	Note=In DBP8-4%3B no effect on growth. RS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11222764;Dbxref=PMID:11222764	
+##sequence-region P32460 1 244
+P32460	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000079806;Note=Protein DCG1	
+##sequence-region P0CH63 1 225
+P0CH63	UniProtKB	Chain	1	225	.	.	.	ID=PRO_0000202670;Note=Cyanamide hydratase DDI2	
+P0CH63	UniProtKB	Domain	52	162	.	.	.	Note=HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01175	
+##sequence-region Q99288 1 334
+Q99288	UniProtKB	Chain	1	334	.	.	.	ID=PRO_0000244436;Note=Broad-range acid phosphatase DET1	
+Q99288	UniProtKB	Region	44	45	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99288	UniProtKB	Region	168	171	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99288	UniProtKB	Region	195	205	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99288	UniProtKB	Active site	32	32	.	.	.	Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707	
+Q99288	UniProtKB	Active site	126	126	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707	
+Q99288	UniProtKB	Binding site	38	38	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99288	UniProtKB	Binding site	108	108	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99288	UniProtKB	Modified residue	248	248	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q05080 1 669
+Q05080	UniProtKB	Chain	1	669	.	.	.	ID=PRO_0000079750;Note=Cytokinesis protein 2	
+Q05080	UniProtKB	Domain	1	261	.	.	.	Note=F-BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01077	
+Q05080	UniProtKB	Domain	599	667	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+Q05080	UniProtKB	Coiled coil	134	200	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05080	UniProtKB	Modified residue	337	337	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05080	UniProtKB	Modified residue	366	366	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05080	UniProtKB	Modified residue	421	421	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05080	UniProtKB	Helix	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE	
+Q05080	UniProtKB	Helix	15	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE	
+Q05080	UniProtKB	Helix	31	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE	
+Q05080	UniProtKB	Helix	70	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE	
+Q05080	UniProtKB	Helix	102	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE	
+Q05080	UniProtKB	Helix	158	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE	
+Q05080	UniProtKB	Helix	164	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE	
+Q05080	UniProtKB	Helix	258	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE	
+##sequence-region P53728 1 308
+P53728	UniProtKB	Chain	1	308	.	.	.	ID=PRO_0000064175;Note=Peptidyl-prolyl cis-trans isomerase CYP8	
+P53728	UniProtKB	Domain	56	215	.	.	.	Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156	
+P53728	UniProtKB	Sequence conflict	8	8	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P23285 1 205
+P23285	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23285	UniProtKB	Chain	21	205	.	.	.	ID=PRO_0000025486;Note=Peptidyl-prolyl cis-trans isomerase B	
+P23285	UniProtKB	Domain	39	198	.	.	.	Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156	
+##sequence-region P25719 1 182
+P25719	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1547957;Dbxref=PMID:1547957	
+P25719	UniProtKB	Chain	21	182	.	.	.	ID=PRO_0000025487;Note=Peptidyl-prolyl cis-trans isomerase C%2C mitochondrial	
+P25719	UniProtKB	Domain	25	181	.	.	.	Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156	
+P25719	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10025965;Dbxref=PMID:10025965	
+P25719	UniProtKB	Mutagenesis	144	144	.	.	.	Note=Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10025965;Dbxref=PMID:10025965	
+##sequence-region P21705 1 255
+P21705	UniProtKB	Chain	1	255	.	.	.	ID=PRO_0000079776;Note=Protein DAL82	
+P21705	UniProtKB	Compositional bias	100	108	.	.	.	Note=Poly-Ser	
+P21705	UniProtKB	Sequence conflict	87	87	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21705	UniProtKB	Sequence conflict	104	104	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P20448 1 770
+P20448	UniProtKB	Chain	1	770	.	.	.	ID=PRO_0000055018;Note=ATP-dependent RNA helicase HCA4	
+P20448	UniProtKB	Domain	72	246	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P20448	UniProtKB	Domain	278	437	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P20448	UniProtKB	Nucleotide binding	85	92	.	.	.	Note=ATP	
+P20448	UniProtKB	Motif	41	69	.	.	.	Note=Q motif	
+P20448	UniProtKB	Motif	194	197	.	.	.	Note=DEAD box	
+P20448	UniProtKB	Modified residue	692	692	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P20448	UniProtKB	Modified residue	710	710	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P20448	UniProtKB	Modified residue	714	714	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P20448	UniProtKB	Modified residue	743	743	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P20448	UniProtKB	Mutagenesis	91	91	.	.	.	Note=Lethal and prevents release of U14 snoRNA from pre-ribosomes. K->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16209945;Dbxref=PMID:16209945	
+P20448	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Lethal and prevents release of U14 snoRNA from pre-ribosomes%3B when associated with A-227. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16209945;Dbxref=PMID:16209945	
+P20448	UniProtKB	Mutagenesis	227	227	.	.	.	Note=Lethal and prevents release of U14 snoRNA from pre-ribosomes%3B when associated with A-225. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16209945;Dbxref=PMID:16209945	
+P20448	UniProtKB	Sequence conflict	36	36	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20448	UniProtKB	Sequence conflict	381	381	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20448	UniProtKB	Sequence conflict	465	465	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20448	UniProtKB	Sequence conflict	512	512	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20448	UniProtKB	Sequence conflict	668	673	.	.	.	Note=KQEKKR->NKRRRG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20448	UniProtKB	Sequence conflict	675	675	.	.	.	Note=R->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08558 1 271
+Q08558	UniProtKB	Chain	1	271	.	.	.	ID=PRO_0000232996;Note=Delta(3%2C5)-Delta(2%2C4)-dienoyl-CoA isomerase	
+Q08558	UniProtKB	Region	62	66	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05871	
+Q08558	UniProtKB	Motif	269	271	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08558	UniProtKB	Active site	152	152	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05871	
+Q08558	UniProtKB	Binding site	120	120	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05871	
+##sequence-region P40087 1 428
+P40087	UniProtKB	Chain	1	428	.	.	.	ID=PRO_0000210997;Note=DNA damage-inducible protein 1	
+P40087	UniProtKB	Domain	1	80	.	.	.	Note=Ubiquitin-like	
+P40087	UniProtKB	Domain	389	428	.	.	.	Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
+P40087	UniProtKB	Cross-link	171	171	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P40087	UniProtKB	Cross-link	257	257	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538	
+P40087	UniProtKB	Beta strand	3	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP	
+P40087	UniProtKB	Turn	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP	
+P40087	UniProtKB	Beta strand	13	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP	
+P40087	UniProtKB	Helix	25	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP	
+P40087	UniProtKB	Helix	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP	
+P40087	UniProtKB	Beta strand	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP	
+P40087	UniProtKB	Beta strand	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N7E	
+P40087	UniProtKB	Helix	60	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP	
+P40087	UniProtKB	Beta strand	70	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP	
+P40087	UniProtKB	Turn	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP	
+P40087	UniProtKB	Helix	90	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES	
+P40087	UniProtKB	Helix	105	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES	
+P40087	UniProtKB	Helix	118	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES	
+P40087	UniProtKB	Helix	125	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES	
+P40087	UniProtKB	Helix	133	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES	
+P40087	UniProtKB	Helix	155	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES	
+P40087	UniProtKB	Helix	168	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES	
+P40087	UniProtKB	Beta strand	205	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Beta strand	213	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Beta strand	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Helix	230	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Helix	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Beta strand	260	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Beta strand	272	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Beta strand	286	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Helix	291	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Beta strand	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Turn	303	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Beta strand	307	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Beta strand	313	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Helix	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z	
+P40087	UniProtKB	Helix	392	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR9	
+P40087	UniProtKB	Turn	400	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR9	
+P40087	UniProtKB	Helix	405	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR9	
+P40087	UniProtKB	Helix	419	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR9	
+##sequence-region P69851 1 72
+P69851	UniProtKB	Chain	1	72	.	.	.	ID=PRO_0000176053;Note=DASH complex subunit DAD4	
+P69851	UniProtKB	Coiled coil	19	47	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P69851	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P32328 1 564
+P32328	UniProtKB	Chain	1	564	.	.	.	ID=PRO_0000085917;Note=Serine/threonine-protein kinase DBF20	
+P32328	UniProtKB	Domain	169	469	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32328	UniProtKB	Domain	470	547	.	.	.	Note=AGC-kinase C-terminal	
+P32328	UniProtKB	Nucleotide binding	175	183	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32328	UniProtKB	Active site	292	292	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P32328	UniProtKB	Binding site	198	198	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32328	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22204	
+P32328	UniProtKB	Modified residue	366	366	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32328	UniProtKB	Modified residue	536	536	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22204	
+P32328	UniProtKB	Sequence conflict	81	81	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32328	UniProtKB	Sequence conflict	337	337	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32328	UniProtKB	Sequence conflict	350	350	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33750 1 489
+P33750	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000051222;Note=Protein SOF1	
+P33750	UniProtKB	Repeat	65	105	.	.	.	Note=WD 1	
+P33750	UniProtKB	Repeat	113	158	.	.	.	Note=WD 2	
+P33750	UniProtKB	Repeat	177	214	.	.	.	Note=WD 3	
+P33750	UniProtKB	Repeat	217	257	.	.	.	Note=WD 4	
+P33750	UniProtKB	Repeat	259	299	.	.	.	Note=WD 5	
+P33750	UniProtKB	Repeat	303	342	.	.	.	Note=WD 6	
+P33750	UniProtKB	Repeat	346	385	.	.	.	Note=WD 7	
+##sequence-region P53550 1 970
+P53550	UniProtKB	Chain	1	970	.	.	.	ID=PRO_0000057054;Note=m7GpppN-mRNA hydrolase	
+P53550	UniProtKB	Domain	101	228	.	.	.	Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794	
+P53550	UniProtKB	Motif	134	155	.	.	.	Note=Nudix box	
+P53550	UniProtKB	Compositional bias	345	430	.	.	.	Note=Pro-rich	
+P53550	UniProtKB	Compositional bias	436	439	.	.	.	Note=Poly-Ser	
+P53550	UniProtKB	Metal binding	149	149	.	.	.	Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53550	UniProtKB	Metal binding	153	153	.	.	.	Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53550	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53550	UniProtKB	Modified residue	439	439	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53550	UniProtKB	Modified residue	677	677	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53550	UniProtKB	Modified residue	679	679	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53550	UniProtKB	Modified residue	682	682	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53550	UniProtKB	Modified residue	751	751	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53550	UniProtKB	Modified residue	771	771	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53550	UniProtKB	Modified residue	773	773	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53550	UniProtKB	Modified residue	778	778	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53550	UniProtKB	Natural variant	188	188	.	.	.	Note=In strain: YJM339. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	288	288	.	.	.	Note=In strain: V1-09%2C YJM269%2C YJM270%2C YJM326%2C YJM339%2C YJM627 and YJM1129. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	301	301	.	.	.	Note=In strain: YJM280%2C YJM 20 and YJM339. L->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	319	319	.	.	.	Note=In strain: YJM627. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	494	494	.	.	.	Note=In strain: YJM339. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	505	505	.	.	.	Note=In strain: SK1%2C V1-09%2C YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326%2C YJM339%2C YJM627 and YJM1129. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	522	522	.	.	.	Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	547	547	.	.	.	Note=In strain: YJM280 and YJM320. N->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	567	567	.	.	.	Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	574	574	.	.	.	Note=In strain: YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326 and YJM1129. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	577	577	.	.	.	Note=In strain: V1-09%2C YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326%2C YJM339 and YJM1129. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	622	622	.	.	.	Note=In strain: V1-09 and YJM339. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	650	650	.	.	.	Note=In strain: YJM280 and YJM320. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	740	740	.	.	.	Note=In strain: YJM269 and YJM270. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	807	807	.	.	.	Note=In strain: YJM 69%2C YJM270%2C YJM326 and YJM1129. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	823	823	.	.	.	Note=In strain: YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326 and YJM1129. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	835	835	.	.	.	Note=In strain: YJM280 and YJM320. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	844	844	.	.	.	Note=In strain: V1-09. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	851	851	.	.	.	Note=In strain: YJM280%2C YJM320 and YJM627. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	854	854	.	.	.	Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	864	864	.	.	.	Note=In strain: YJM269 and YJM270. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	865	865	.	.	.	Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	866	866	.	.	.	Note=In strain: YJM627. D->A	
+P53550	UniProtKB	Natural variant	909	909	.	.	.	Note=In strain: YJM280 and YJM320. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	945	945	.	.	.	Note=In strain: YJM627. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Natural variant	951	951	.	.	.	Note=In strain: V1-09. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53550	UniProtKB	Mutagenesis	60	60	.	.	.	Note=In DCP2-7%3B impairs mRNA decay at 37 degrees Celsius%3B when associated with V-68 and V-142. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11139489;Dbxref=PMID:11139489	
+P53550	UniProtKB	Mutagenesis	68	68	.	.	.	Note=In DCP2-7%3B impairs mRNA decay at 37 degrees Celsius%3B when associated with D-60 and V-142. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11139489;Dbxref=PMID:11139489	
+P53550	UniProtKB	Mutagenesis	142	142	.	.	.	Note=In DCP2-7%3B impairs mRNA decay at 37 degrees Celsius%3B when associated with D-60 and V-68. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11139489;Dbxref=PMID:11139489	
+P53550	UniProtKB	Sequence conflict	425	425	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53550	UniProtKB	Beta strand	105	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Beta strand	117	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Beta strand	132	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Beta strand	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVB	
+P53550	UniProtKB	Helix	142	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Beta strand	167	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Beta strand	175	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Beta strand	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVB	
+P53550	UniProtKB	Beta strand	194	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Helix	207	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Helix	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Beta strand	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Helix	224	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Helix	228	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+P53550	UniProtKB	Helix	242	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3	
+##sequence-region P18899 1 430
+P18899	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2114092,ECO:0000269|PubMed:8444852;Dbxref=PMID:2114092,PMID:8444852	
+P18899	UniProtKB	Chain	2	430	.	.	.	ID=PRO_0000079849;Note=Stress protein DDR48	
+P18899	UniProtKB	Repeat	74	81	.	.	.	Note=1	
+P18899	UniProtKB	Repeat	82	89	.	.	.	Note=2	
+P18899	UniProtKB	Repeat	90	97	.	.	.	Note=3	
+P18899	UniProtKB	Repeat	98	105	.	.	.	Note=4	
+P18899	UniProtKB	Repeat	106	113	.	.	.	Note=5	
+P18899	UniProtKB	Repeat	114	121	.	.	.	Note=6	
+P18899	UniProtKB	Repeat	124	131	.	.	.	Note=7%3B approximate	
+P18899	UniProtKB	Repeat	132	139	.	.	.	Note=8	
+P18899	UniProtKB	Repeat	141	148	.	.	.	Note=9	
+P18899	UniProtKB	Repeat	149	156	.	.	.	Note=10	
+P18899	UniProtKB	Repeat	157	164	.	.	.	Note=11	
+P18899	UniProtKB	Repeat	165	172	.	.	.	Note=12	
+P18899	UniProtKB	Repeat	175	182	.	.	.	Note=13%3B approximate	
+P18899	UniProtKB	Repeat	183	190	.	.	.	Note=14	
+P18899	UniProtKB	Repeat	191	198	.	.	.	Note=15	
+P18899	UniProtKB	Repeat	201	208	.	.	.	Note=16%3B approximate	
+P18899	UniProtKB	Repeat	209	216	.	.	.	Note=17	
+P18899	UniProtKB	Repeat	217	224	.	.	.	Note=18	
+P18899	UniProtKB	Repeat	225	232	.	.	.	Note=19	
+P18899	UniProtKB	Repeat	233	240	.	.	.	Note=20	
+P18899	UniProtKB	Repeat	243	250	.	.	.	Note=21%3B approximate	
+P18899	UniProtKB	Repeat	251	258	.	.	.	Note=22	
+P18899	UniProtKB	Repeat	260	267	.	.	.	Note=23	
+P18899	UniProtKB	Repeat	268	275	.	.	.	Note=24	
+P18899	UniProtKB	Repeat	278	285	.	.	.	Note=25%3B approximate	
+P18899	UniProtKB	Repeat	287	294	.	.	.	Note=26	
+P18899	UniProtKB	Repeat	296	303	.	.	.	Note=27	
+P18899	UniProtKB	Repeat	306	313	.	.	.	Note=28%3B approximate	
+P18899	UniProtKB	Repeat	314	321	.	.	.	Note=29	
+P18899	UniProtKB	Repeat	322	329	.	.	.	Note=30	
+P18899	UniProtKB	Repeat	332	339	.	.	.	Note=31%3B approximate	
+P18899	UniProtKB	Repeat	340	347	.	.	.	Note=32	
+P18899	UniProtKB	Repeat	348	355	.	.	.	Note=33	
+P18899	UniProtKB	Repeat	358	365	.	.	.	Note=34%3B approximate	
+P18899	UniProtKB	Repeat	366	373	.	.	.	Note=35	
+P18899	UniProtKB	Repeat	375	382	.	.	.	Note=36	
+P18899	UniProtKB	Repeat	393	400	.	.	.	Note=37%3B approximate	
+P18899	UniProtKB	Repeat	407	414	.	.	.	Note=38	
+P18899	UniProtKB	Region	74	414	.	.	.	Note=38 X 8 AA approximate tandem repeats of S-[NS]-N-[ND]-D-S-Y-G	
+P18899	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P18899	UniProtKB	Modified residue	191	191	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P18899	UniProtKB	Modified residue	314	314	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P18899	UniProtKB	Modified residue	322	322	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P18899	UniProtKB	Sequence conflict	9	9	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18899	UniProtKB	Sequence conflict	38	38	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P31385 1 405
+P31385	UniProtKB	Chain	1	405	.	.	.	ID=PRO_0000079864;Note=Transcriptional regulatory protein DEP1	
+P31385	UniProtKB	Compositional bias	81	177	.	.	.	Note=Glu-rich	
+P31385	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P31385	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P31385	UniProtKB	Modified residue	370	370	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P36108 1 232
+P36108	UniProtKB	Chain	1	232	.	.	.	ID=PRO_0000211477;Note=DOA4-independent degradation protein 4	
+P36108	UniProtKB	Region	183	232	.	.	.	Note=Interaction with VPS4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17949747;Dbxref=PMID:17949747	
+P36108	UniProtKB	Coiled coil	14	97	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36108	UniProtKB	Motif	219	229	.	.	.	Note=MIT-interacting motif	
+P36108	UniProtKB	Mutagenesis	221	221	.	.	.	Note=Abolishes interaction with VPS4. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861	
+P36108	UniProtKB	Mutagenesis	224	224	.	.	.	Note=Abolishes interaction with VPS4. Impairs sorting. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861	
+P36108	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Abolishes interaction with VPS4. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861	
+P36108	UniProtKB	Mutagenesis	228	229	.	.	.	Note=Greatly impairs sorting. LK->DD	
+P36108	UniProtKB	Mutagenesis	228	228	.	.	.	Note=Abolishes interaction with VPS4. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861	
+P36108	UniProtKB	Mutagenesis	229	229	.	.	.	Note=Abolishes interaction with VPS4. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861	
+P36108	UniProtKB	Helix	188	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6X	
+P36108	UniProtKB	Helix	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6X	
+P36108	UniProtKB	Beta strand	201	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6X	
+P36108	UniProtKB	Helix	219	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6X	
+##sequence-region P52868 1 283
+P52868	UniProtKB	Chain	1	283	.	.	.	ID=PRO_0000071129;Note=Pre-mRNA-splicing factor CWC23	
+P52868	UniProtKB	Domain	15	87	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+##sequence-region P40312 1 120
+P40312	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000166035;Note=Cytochrome b5	
+P40312	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40312	UniProtKB	Domain	2	78	.	.	.	Note=Cytochrome b5 heme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+P40312	UniProtKB	Metal binding	37	37	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+P40312	UniProtKB	Metal binding	61	61	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+P40312	UniProtKB	Sequence conflict	17	17	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P14922 1 966
+P14922	UniProtKB	Chain	1	966	.	.	.	ID=PRO_0000106327;Note=General transcriptional corepressor CYC8	
+P14922	UniProtKB	Repeat	46	79	.	.	.	Note=TPR 1	
+P14922	UniProtKB	Repeat	80	113	.	.	.	Note=TPR 2	
+P14922	UniProtKB	Repeat	114	147	.	.	.	Note=TPR 3	
+P14922	UniProtKB	Repeat	150	183	.	.	.	Note=TPR 4	
+P14922	UniProtKB	Repeat	187	220	.	.	.	Note=TPR 5	
+P14922	UniProtKB	Repeat	224	257	.	.	.	Note=TPR 6	
+P14922	UniProtKB	Repeat	262	295	.	.	.	Note=TPR 7	
+P14922	UniProtKB	Repeat	296	329	.	.	.	Note=TPR 8	
+P14922	UniProtKB	Repeat	330	363	.	.	.	Note=TPR 9	
+P14922	UniProtKB	Repeat	364	398	.	.	.	Note=TPR 10	
+P14922	UniProtKB	Region	467	682	.	.	.	Note=Prion domain (PrD)	
+P14922	UniProtKB	Compositional bias	15	30	.	.	.	Note=Poly-Gln	
+P14922	UniProtKB	Modified residue	429	429	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14922	UniProtKB	Modified residue	475	475	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14922	UniProtKB	Modified residue	710	710	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P14922	UniProtKB	Modified residue	741	741	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14922	UniProtKB	Modified residue	768	768	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14922	UniProtKB	Modified residue	815	815	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P14922	UniProtKB	Modified residue	817	817	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P14922	UniProtKB	Modified residue	866	866	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14922	UniProtKB	Modified residue	943	943	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P14922	UniProtKB	Sequence conflict	547	547	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14922	UniProtKB	Sequence conflict	547	547	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07533 1 885
+Q07533	UniProtKB	Chain	1	885	.	.	.	ID=PRO_0000079751;Note=Cytokinesis protein 3	
+Q07533	UniProtKB	Domain	9	70	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+Q07533	UniProtKB	Modified residue	209	209	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q07533	UniProtKB	Modified residue	292	292	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07533	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q07533	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q07533	UniProtKB	Modified residue	391	391	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P36162 1 133
+P36162	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000211598;Note=DASH complex subunit DAD2	
+P36162	UniProtKB	Coiled coil	1	51	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36162	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P53267 1 343
+P53267	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53267	UniProtKB	Chain	2	343	.	.	.	ID=PRO_0000127663;Note=DASH complex subunit DAM1	
+P53267	UniProtKB	Coiled coil	125	158	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53267	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53267	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphoserine%3B by IPL1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861	
+P53267	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53267	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphoserine%3B by IPL1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861	
+P53267	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphoserine%3B by IPL1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:19779198,PMID:12408861	
+P53267	UniProtKB	Modified residue	292	292	.	.	.	Note=Phosphoserine%3B by IPL1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:19779198,PMID:12408861	
+P53267	UniProtKB	Mutagenesis	111	111	.	.	.	Note=In DAM1-1%3B produces abnormal spindles resulting in growth arrest at 34 degrees Celsius. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10397771;Dbxref=PMID:10397771	
+##sequence-region P13483 1 248
+P13483	UniProtKB	Chain	1	248	.	.	.	ID=PRO_0000079787;Note=Oligo(A)/oligo(T)-binding protein	
+P13483	UniProtKB	Repeat	8	12	.	.	.	Note=1	
+P13483	UniProtKB	Repeat	14	18	.	.	.	Note=2	
+P13483	UniProtKB	Repeat	26	30	.	.	.	Note=3	
+P13483	UniProtKB	DNA binding	1	36	.	.	.	.	
+P13483	UniProtKB	Region	8	30	.	.	.	Note=3 X 5 AA repeats of G-R-K-P-G	
+P13483	UniProtKB	Compositional bias	111	127	.	.	.	Note=Poly-Gln	
+P13483	UniProtKB	Compositional bias	155	188	.	.	.	Note=Asn-rich	
+##sequence-region P53202 1 744
+P53202	UniProtKB	Chain	1	744	.	.	.	ID=PRO_0000119806;Note=Cullin-3	
+P53202	UniProtKB	Cross-link	688	688	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13616	
+##sequence-region Q02554 1 436
+Q02554	UniProtKB	Chain	1	436	.	.	.	ID=PRO_0000079565;Note=Cold sensitive U2 snRNA suppressor 1	
+Q02554	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02554	UniProtKB	Modified residue	112	112	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02554	UniProtKB	Modified residue	114	114	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02554	UniProtKB	Natural variant	181	181	.	.	.	Note=In allele CUS1-54%3B cold-sensitive growth suppressor. E->K	
+##sequence-region P00175 1 591
+P00175	UniProtKB	Transit peptide	1	80	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:165435,ECO:0000269|PubMed:6365548;Dbxref=PMID:165435,PMID:6365548	
+P00175	UniProtKB	Chain	81	591	.	.	.	ID=PRO_0000006480;Note=Cytochrome b2%2C mitochondrial	
+P00175	UniProtKB	Domain	88	165	.	.	.	Note=Cytochrome b5 heme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+P00175	UniProtKB	Domain	197	563	.	.	.	Note=FMN hydroxy acid dehydrogenase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00683	
+P00175	UniProtKB	Region	177	190	.	.	.	Note=Hinge	
+P00175	UniProtKB	Region	567	591	.	.	.	Note=Tail (wraps around the molecular 4-fold axis)	
+P00175	UniProtKB	Active site	453	453	.	.	.	Note=Proton acceptor	
+P00175	UniProtKB	Metal binding	123	123	.	.	.	Note=Iron (heme axial ligand)	
+P00175	UniProtKB	Metal binding	146	146	.	.	.	Note=Iron (heme axial ligand)	
+P00175	UniProtKB	Binding site	177	177	.	.	.	Note=Heme b	
+P00175	UniProtKB	Binding site	219	219	.	.	.	Note=Heme b	
+P00175	UniProtKB	Binding site	223	223	.	.	.	Note=Heme b	
+P00175	UniProtKB	Binding site	376	376	.	.	.	Note=Heme b	
+P00175	UniProtKB	Binding site	456	456	.	.	.	Note=Substrate	
+P00175	UniProtKB	Sequence conflict	165	165	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00175	UniProtKB	Sequence conflict	165	165	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00175	UniProtKB	Sequence conflict	466	466	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00175	UniProtKB	Sequence conflict	513	513	.	.	.	Note=R->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00175	UniProtKB	Sequence conflict	570	570	.	.	.	Note=V->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00175	UniProtKB	Helix	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	104	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	112	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Turn	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	127	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Turn	132	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	139	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	150	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	160	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	170	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FCB	
+P00175	UniProtKB	Helix	183	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	205	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	218	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDC	
+P00175	UniProtKB	Helix	232	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	240	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	266	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Turn	285	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	289	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	298	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	315	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FCB	
+P00175	UniProtKB	Beta strand	329	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	339	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	357	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	370	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	398	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	404	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LTD	
+P00175	UniProtKB	Helix	412	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	426	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	434	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	446	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Turn	453	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	464	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Turn	477	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	481	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FCB	
+P00175	UniProtKB	Beta strand	484	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	495	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Beta strand	507	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	513	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	550	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	555	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Turn	561	564	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+P00175	UniProtKB	Helix	574	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI	
+##sequence-region P54838 1 584
+P54838	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P54838	UniProtKB	Chain	2	584	.	.	.	ID=PRO_0000121522;Note=Dihydroxyacetone kinase 1	
+P54838	UniProtKB	Domain	7	353	.	.	.	Note=DhaK;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00814	
+P54838	UniProtKB	Domain	386	582	.	.	.	Note=DhaL;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00813	
+P54838	UniProtKB	Nucleotide binding	415	418	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54838	UniProtKB	Nucleotide binding	459	460	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54838	UniProtKB	Nucleotide binding	514	515	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54838	UniProtKB	Nucleotide binding	567	569	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54838	UniProtKB	Region	51	54	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54838	UniProtKB	Active site	220	220	.	.	.	Note=Tele-hemiaminal-histidine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00814	
+P54838	UniProtKB	Binding site	103	103	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54838	UniProtKB	Binding site	108	108	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54838	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P54838	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P54838	UniProtKB	Modified residue	5	5	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P54838	UniProtKB	Modified residue	365	365	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P54838	UniProtKB	Modified residue	512	512	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q12382 1 290
+Q12382	UniProtKB	Chain	1	290	.	.	.	ID=PRO_0000240382;Note=CTP-dependent diacylglycerol kinase 1	
+Q12382	UniProtKB	Topological domain	1	77	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Transmembrane	78	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Topological domain	96	103	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Topological domain	125	140	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Topological domain	162	163	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Topological domain	185	203	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Topological domain	225	244	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Transmembrane	245	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Topological domain	266	290	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12382	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12382	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12382	UniProtKB	Glycosylation	11	11	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Glycosylation	197	197	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Glycosylation	270	270	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12382	UniProtKB	Mutagenesis	76	76	.	.	.	Note=Loss of kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18458076;Dbxref=PMID:18458076	
+Q12382	UniProtKB	Mutagenesis	77	77	.	.	.	Note=Loss of kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18458076;Dbxref=PMID:18458076	
+Q12382	UniProtKB	Mutagenesis	177	177	.	.	.	Note=No kinase activity. Not temperature-sensitive for growth. Does not trigger nuclear membrane expansion. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18458075,ECO:0000269|PubMed:18458076;Dbxref=PMID:18458075,PMID:18458076	
+Q12382	UniProtKB	Mutagenesis	184	184	.	.	.	Note=70%25 reduction in kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18458076;Dbxref=PMID:18458076	
+##sequence-region Q3E808 1 48
+Q3E808	UniProtKB	Transit peptide	1	28	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E808	UniProtKB	Chain	29	48	.	.	.	ID=PRO_0000247800;Note=2-deoxy-glucose resistant protein 1%2C mitochondrial	
+##sequence-region P21623 1 536
+P21623	UniProtKB	Chain	1	536	.	.	.	ID=PRO_0000079920;Note=Spore wall maturation protein DIT1	
+P21623	UniProtKB	Sequence conflict	273	273	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P54861 1 757
+P54861	UniProtKB	Chain	1	757	.	.	.	ID=PRO_0000206586;Note=Dynamin-related protein DNM1	
+P54861	UniProtKB	Domain	25	333	.	.	.	Note=Dynamin-type G	
+P54861	UniProtKB	Domain	670	757	.	.	.	Note=GED;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00720	
+P54861	UniProtKB	Nucleotide binding	35	42	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54861	UniProtKB	Nucleotide binding	175	179	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54861	UniProtKB	Nucleotide binding	244	247	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54861	UniProtKB	Modified residue	629	629	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P54861	UniProtKB	Mutagenesis	705	705	.	.	.	Note=Induces an increase of mitochondrial fission. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11553714;Dbxref=PMID:11553714	
+P54861	UniProtKB	Sequence conflict	124	124	.	.	.	Note=H->ISPD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40059 1 670
+P40059	UniProtKB	Chain	1	670	.	.	.	ID=PRO_0000197108;Note=Transcriptional regulatory protein DOT6	
+P40059	UniProtKB	Domain	67	121	.	.	.	Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P40059	UniProtKB	DNA binding	94	117	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P40059	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40059	UniProtKB	Modified residue	247	247	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40059	UniProtKB	Modified residue	487	487	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40059	UniProtKB	Modified residue	489	489	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40059	UniProtKB	Modified residue	491	491	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P47027 1 764
+P47027	UniProtKB	Chain	1	764	.	.	.	ID=PRO_0000079989;Note=DNA replication regulator DPB11	
+P47027	UniProtKB	Domain	1	99	.	.	.	Note=BRCT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P47027	UniProtKB	Domain	129	220	.	.	.	Note=BRCT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P47027	UniProtKB	Domain	322	418	.	.	.	Note=BRCT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P47027	UniProtKB	Sequence conflict	72	72	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47027	UniProtKB	Sequence conflict	295	296	.	.	.	Note=QQ->HR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47027	UniProtKB	Sequence conflict	515	515	.	.	.	Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47027	UniProtKB	Sequence conflict	603	603	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47027	UniProtKB	Sequence conflict	656	656	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32469 1 300
+P32469	UniProtKB	Chain	1	300	.	.	.	ID=PRO_0000156147;Note=Diphthine methyl ester synthase	
+P32469	UniProtKB	Region	113	114	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32469	UniProtKB	Binding site	9	9	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32469	UniProtKB	Binding site	85	85	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32469	UniProtKB	Binding site	88	88	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32469	UniProtKB	Binding site	164	164	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32469	UniProtKB	Binding site	222	222	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32469	UniProtKB	Binding site	247	247	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32469	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32469	UniProtKB	Modified residue	298	298	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32469	UniProtKB	Sequence conflict	287	287	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38332 1 387
+P38332	UniProtKB	Chain	1	387	.	.	.	ID=PRO_0000202523;Note=Diphthine methyltransferase	
+P38332	UniProtKB	Repeat	62	102	.	.	.	Note=WD 1	
+P38332	UniProtKB	Repeat	119	159	.	.	.	Note=WD 2	
+P38332	UniProtKB	Repeat	195	237	.	.	.	Note=WD 3	
+P38332	UniProtKB	Repeat	241	286	.	.	.	Note=WD 4	
+P38332	UniProtKB	Repeat	357	387	.	.	.	Note=WD 5	
+##sequence-region P32892 1 752
+P32892	UniProtKB	Chain	1	752	.	.	.	ID=PRO_0000055045;Note=ATP-dependent RNA helicase DRS1	
+P32892	UniProtKB	Domain	262	437	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32892	UniProtKB	Domain	448	639	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P32892	UniProtKB	Nucleotide binding	275	282	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32892	UniProtKB	Coiled coil	621	667	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32892	UniProtKB	Motif	231	259	.	.	.	Note=Q motif	
+P32892	UniProtKB	Motif	385	388	.	.	.	Note=DEAD box	
+P32892	UniProtKB	Compositional bias	170	190	.	.	.	Note=Poly-Glu	
+P32892	UniProtKB	Modified residue	208	208	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32892	UniProtKB	Mutagenesis	191	191	.	.	.	Note=No growth at 13 degrees Celsius%3B when associated with Q-431 and G-472. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	260	260	.	.	.	Note=No growth at 13 degrees Celsius%3B when associated with P-564. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	273	273	.	.	.	Note=No growth at 13 degrees Celsius. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	288	288	.	.	.	Note=No growth at 13 degrees Celsius. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	291	291	.	.	.	Note=No growth at 13 degrees Celsius%3B when associated with G-637. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	305	305	.	.	.	Note=No growth at 13 degrees Celsius%3B when associated with V-306. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	306	306	.	.	.	Note=No growth at 13 degrees Celsius%3B when associated with D-305. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	414	414	.	.	.	Note=No growth at 13 degrees Celsius. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	429	429	.	.	.	Note=No growth at 13 degrees Celsius. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	431	431	.	.	.	Note=No growth at 13 degrees Celsius%3B when associated with T-191 and G-472. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	472	472	.	.	.	Note=No growth at 13 degrees Celsius%3B when associated with T-191 and Q-431. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	509	509	.	.	.	Note=No growth at 13 degrees Celsius. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	563	563	.	.	.	Note=No growth at 13 degrees Celsius. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	564	564	.	.	.	Note=No growth at 13 degrees Celsius%3B when associated with V-260. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+P32892	UniProtKB	Mutagenesis	637	637	.	.	.	Note=No growth at 13 degrees Celsius%3B when associated with V-291. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362	
+##sequence-region P23501 1 404
+P23501	UniProtKB	Chain	1	404	.	.	.	ID=PRO_0000203216;Note=Dihydrosphingosine 1-phosphate phosphatase YSR3	
+P23501	UniProtKB	Topological domain	1	86	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013	
+P23501	UniProtKB	Transmembrane	87	107	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23501	UniProtKB	Topological domain	108	113	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013	
+P23501	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23501	UniProtKB	Topological domain	135	154	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013	
+P23501	UniProtKB	Transmembrane	155	176	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23501	UniProtKB	Topological domain	177	182	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013	
+P23501	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23501	UniProtKB	Topological domain	204	215	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013	
+P23501	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23501	UniProtKB	Topological domain	237	241	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013	
+P23501	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23501	UniProtKB	Topological domain	263	319	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013	
+P23501	UniProtKB	Transmembrane	320	340	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23501	UniProtKB	Topological domain	341	379	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013	
+P23501	UniProtKB	Transmembrane	380	400	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23501	UniProtKB	Topological domain	401	404	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013	
+P23501	UniProtKB	Region	129	137	.	.	.	Note=Phosphatase sequence motif I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23501	UniProtKB	Region	158	161	.	.	.	Note=Phosphatase sequence motif II;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23501	UniProtKB	Region	204	215	.	.	.	Note=Phosphatase sequence motif III;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23501	UniProtKB	Active site	161	161	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924	
+P23501	UniProtKB	Active site	211	211	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924	
+P23501	UniProtKB	Site	215	215	.	.	.	Note=Stabilizes the active site histidine for nucleophilic attack;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924	
+P23501	UniProtKB	Glycosylation	62	62	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53720 1 384
+P53720	UniProtKB	Chain	1	384	.	.	.	ID=PRO_0000162154;Note=tRNA-dihydrouridine(20) synthase [NAD(P)+]	
+P53720	UniProtKB	Nucleotide binding	12	14	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53720	UniProtKB	Nucleotide binding	222	224	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53720	UniProtKB	Nucleotide binding	249	250	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53720	UniProtKB	Active site	117	117	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53720	UniProtKB	Binding site	88	88	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53720	UniProtKB	Binding site	160	160	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53720	UniProtKB	Binding site	188	188	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+##sequence-region P07262 1 454
+P07262	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07262	UniProtKB	Chain	2	454	.	.	.	ID=PRO_0000182798;Note=NADP-specific glutamate dehydrogenase 1	
+P07262	UniProtKB	Nucleotide binding	174	203	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07262	UniProtKB	Active site	110	110	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10011	
+P07262	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07262	UniProtKB	Cross-link	325	325	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P07262	UniProtKB	Cross-link	371	371	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P07262	UniProtKB	Cross-link	433	433	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P07262	UniProtKB	Sequence conflict	83	83	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07262	UniProtKB	Sequence conflict	198	198	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07262	UniProtKB	Sequence conflict	255	255	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07262	UniProtKB	Sequence conflict	266	266	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07262	UniProtKB	Sequence conflict	358	364	.	.	.	Note=ATGPSEA->PLDQAT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P37298 1 181
+P37298	UniProtKB	Transit peptide	1	31	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8120006;Dbxref=PMID:8120006	
+P37298	UniProtKB	Chain	32	181	.	.	.	ID=PRO_0000006496;Note=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit%2C mitochondrial	
+P37298	UniProtKB	Topological domain	32	66	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37298	UniProtKB	Transmembrane	67	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37298	UniProtKB	Topological domain	89	98	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37298	UniProtKB	Transmembrane	99	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37298	UniProtKB	Topological domain	119	127	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37298	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37298	UniProtKB	Topological domain	149	181	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37298	UniProtKB	Metal binding	109	109	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37298	UniProtKB	Binding site	120	120	.	.	.	Note=Ubiquinone%3B shared with IP/SDHB;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P37298	UniProtKB	Mutagenesis	100	100	.	.	.	Note=Impairs respiratory growth and reduces quinone reductase activity. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11279023;Dbxref=PMID:11279023	
+P37298	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Impairs respiratory growth and reduces quinone reductase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11279023;Dbxref=PMID:11279023	
+P37298	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Decreases SDH cytochrome b content. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14672930;Dbxref=PMID:14672930	
+P37298	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Abolishes quinone reductase activity. Little effect on complex assembly. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17208193;Dbxref=PMID:17208193	
+P37298	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Reduces SDH FAD content. Probably impairs complex assembly. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11279023;Dbxref=PMID:11279023	
+##sequence-region Q08496 1 732
+Q08496	UniProtKB	Chain	1	732	.	.	.	ID=PRO_0000233003;Note=Protein DIA2	
+Q08496	UniProtKB	Repeat	15	48	.	.	.	Note=TPR 1	
+Q08496	UniProtKB	Repeat	78	111	.	.	.	Note=TPR 2	
+Q08496	UniProtKB	Repeat	113	145	.	.	.	Note=TPR 3	
+Q08496	UniProtKB	Domain	204	251	.	.	.	Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080	
+Q08496	UniProtKB	Repeat	425	449	.	.	.	Note=LRR 1	
+Q08496	UniProtKB	Repeat	480	505	.	.	.	Note=LRR 2	
+Q08496	UniProtKB	Repeat	509	532	.	.	.	Note=LRR 3	
+Q08496	UniProtKB	Repeat	550	574	.	.	.	Note=LRR 4	
+Q08496	UniProtKB	Repeat	579	602	.	.	.	Note=LRR 5	
+Q08496	UniProtKB	Repeat	616	637	.	.	.	Note=LRR 6	
+Q08496	UniProtKB	Repeat	645	669	.	.	.	Note=LRR 7	
+Q08496	UniProtKB	Modified residue	393	393	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q12086 1 430
+Q12086	UniProtKB	Chain	1	430	.	.	.	ID=PRO_0000154046;Note=DNA damage-inducible protein DIN7	
+Q12086	UniProtKB	Region	1	96	.	.	.	Note=N-domain	
+Q12086	UniProtKB	Region	114	247	.	.	.	Note=I-domain	
+Q12086	UniProtKB	Metal binding	30	30	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12086	UniProtKB	Metal binding	78	78	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12086	UniProtKB	Metal binding	150	150	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12086	UniProtKB	Metal binding	152	152	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12086	UniProtKB	Metal binding	171	171	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12086	UniProtKB	Metal binding	173	173	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12086	UniProtKB	Metal binding	227	227	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P04819 1 755
+P04819	UniProtKB	Transit peptide	1	44	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04819	UniProtKB	Chain	45	755	.	.	.	ID=PRO_0000007274;Note=DNA ligase 1	
+P04819	UniProtKB	Region	309	318	.	.	.	Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Region	493	495	.	.	.	Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Active site	419	419	.	.	.	Note=N6-AMP-lysine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10135	
+P04819	UniProtKB	Metal binding	472	472	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Metal binding	571	571	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Binding site	417	417	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Binding site	424	424	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Binding site	440	440	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Binding site	576	576	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Binding site	590	590	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Binding site	596	596	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Site	164	164	.	.	.	Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Site	441	441	.	.	.	Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Site	622	622	.	.	.	Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Site	647	647	.	.	.	Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04819	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P04819	UniProtKB	Modified residue	75	75	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P04819	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04819	UniProtKB	Modified residue	123	123	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04819	UniProtKB	Alternative sequence	1	23	.	.	.	ID=VSP_018719;Note=In isoform Nuclear. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04819	UniProtKB	Sequence conflict	69	69	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04819	UniProtKB	Sequence conflict	186	186	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04819	UniProtKB	Sequence conflict	671	671	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04819	UniProtKB	Sequence conflict	724	724	.	.	.	Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04819	UniProtKB	Helix	41	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OD8	
+##sequence-region Q08387 1 944
+Q08387	UniProtKB	Chain	1	944	.	.	.	ID=PRO_0000059582;Note=DNA ligase 4	
+Q08387	UniProtKB	Domain	681	780	.	.	.	Note=BRCT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+Q08387	UniProtKB	Domain	836	941	.	.	.	Note=BRCT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+Q08387	UniProtKB	Active site	282	282	.	.	.	Note=N6-AMP-lysine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10135	
+Q08387	UniProtKB	Metal binding	340	340	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08387	UniProtKB	Metal binding	442	442	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08387	UniProtKB	Binding site	280	280	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08387	UniProtKB	Binding site	287	287	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08387	UniProtKB	Binding site	304	304	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08387	UniProtKB	Binding site	447	447	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08387	UniProtKB	Binding site	458	458	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08387	UniProtKB	Binding site	464	464	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38821 1 490
+P38821	UniProtKB	Chain	1	490	.	.	.	ID=PRO_0000173455;Note=Aspartyl aminopeptidase 4	
+P38821	UniProtKB	Metal binding	97	97	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38821	UniProtKB	Metal binding	273	273	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38821	UniProtKB	Metal binding	273	273	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38821	UniProtKB	Metal binding	309	309	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38821	UniProtKB	Metal binding	362	362	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38821	UniProtKB	Metal binding	456	456	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38821	UniProtKB	Binding site	173	173	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38821	UniProtKB	Binding site	308	308	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38821	UniProtKB	Binding site	362	362	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38821	UniProtKB	Binding site	365	365	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38821	UniProtKB	Binding site	390	390	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38821	UniProtKB	Binding site	397	397	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38774 1 246
+P38774	UniProtKB	Chain	1	246	.	.	.	ID=PRO_0000079974;Note=2-deoxyglucose-6-phosphate phosphatase 1	
+P38774	UniProtKB	Active site	12	12	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38774	UniProtKB	Active site	14	14	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38774	UniProtKB	Metal binding	12	12	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38774	UniProtKB	Metal binding	14	14	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38774	UniProtKB	Metal binding	183	183	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03921 1 1698
+Q03921	UniProtKB	Chain	1	1698	.	.	.	ID=PRO_0000190976;Note=Protein dopey	
+Q03921	UniProtKB	Modified residue	244	244	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P46957 1 487
+P46957	UniProtKB	Chain	1	487	.	.	.	ID=PRO_0000096174;Note=DNA polymerase delta small subunit	
+P46957	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P46957	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46957	UniProtKB	Sequence conflict	156	156	.	.	.	Note=L->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46957	UniProtKB	Sequence conflict	465	465	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P15801 1 1254
+P15801	UniProtKB	Chain	1	1254	.	.	.	ID=PRO_0000101278;Note=DNA polymerase gamma	
+P15801	UniProtKB	Sequence conflict	8	8	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15801	UniProtKB	Sequence conflict	35	35	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15801	UniProtKB	Sequence conflict	222	222	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15801	UniProtKB	Sequence conflict	357	357	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15801	UniProtKB	Sequence conflict	540	541	.	.	.	Note=TH->MN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15801	UniProtKB	Sequence conflict	616	616	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15801	UniProtKB	Sequence conflict	661	661	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15801	UniProtKB	Sequence conflict	978	978	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15801	UniProtKB	Sequence conflict	986	986	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36152 1 348
+P36152	UniProtKB	Chain	1	348	.	.	.	ID=PRO_0000203219;Note=Fe-S cluster assembly protein DRE2	
+P36152	UniProtKB	Region	1	158	.	.	.	Note=N-terminal domain	
+P36152	UniProtKB	Region	159	242	.	.	.	Note=Linker	
+P36152	UniProtKB	Region	243	348	.	.	.	Note=Intrinsically disordered	
+P36152	UniProtKB	Motif	311	314	.	.	.	Note=Cx2C motif 1	
+P36152	UniProtKB	Motif	322	325	.	.	.	Note=Cx2C motif 2	
+P36152	UniProtKB	Metal binding	252	252	.	.	.	Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03115	
+P36152	UniProtKB	Metal binding	263	263	.	.	.	Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03115	
+P36152	UniProtKB	Metal binding	266	266	.	.	.	Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03115	
+P36152	UniProtKB	Metal binding	268	268	.	.	.	Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03115	
+P36152	UniProtKB	Modified residue	206	206	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P36152	UniProtKB	Beta strand	5	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+P36152	UniProtKB	Helix	13	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+P36152	UniProtKB	Helix	19	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+P36152	UniProtKB	Beta strand	34	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+P36152	UniProtKB	Helix	42	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+P36152	UniProtKB	Beta strand	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+P36152	UniProtKB	Beta strand	59	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+P36152	UniProtKB	Helix	75	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+P36152	UniProtKB	Helix	96	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+P36152	UniProtKB	Beta strand	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+P36152	UniProtKB	Beta strand	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+P36152	UniProtKB	Beta strand	116	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1	
+##sequence-region Q04792 1 585
+Q04792	UniProtKB	Chain	1	585	.	.	.	ID=PRO_0000146977;Note=Glutamate decarboxylase	
+Q04792	UniProtKB	Modified residue	318	318	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P35732 1 738
+P35732	UniProtKB	Chain	1	738	.	.	.	ID=PRO_0000203177;Note=RNA polymerase II degradation factor 1	
+P35732	UniProtKB	Domain	21	63	.	.	.	Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468	
+P35732	UniProtKB	Compositional bias	382	718	.	.	.	Note=Gln-rich	
+P35732	UniProtKB	Compositional bias	574	580	.	.	.	Note=Poly-Ala	
+P35732	UniProtKB	Compositional bias	708	716	.	.	.	Note=Poly-Ala	
+P35732	UniProtKB	Modified residue	260	260	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P35732	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P35732	UniProtKB	Modified residue	307	307	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35732	UniProtKB	Modified residue	338	338	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P35732	UniProtKB	Modified residue	646	646	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q99234 1 619
+Q99234	UniProtKB	Chain	1	619	.	.	.	ID=PRO_0000079873;Note=Protein DFG16	
+Q99234	UniProtKB	Topological domain	1	1	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Transmembrane	2	22	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Topological domain	23	167	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Topological domain	189	203	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Topological domain	225	291	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Transmembrane	292	312	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Topological domain	313	321	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Transmembrane	322	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Topological domain	343	378	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Transmembrane	379	399	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Topological domain	400	410	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Transmembrane	411	431	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Topological domain	432	619	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99234	UniProtKB	Compositional bias	510	517	.	.	.	Note=Poly-Arg	
+##sequence-region P32330 1 852
+P32330	UniProtKB	Chain	1	852	.	.	.	ID=PRO_0000051479;Note=2-deoxy-glucose resistant protein 2	
+P32330	UniProtKB	Repeat	171	210	.	.	.	Note=WD 1	
+P32330	UniProtKB	Repeat	278	316	.	.	.	Note=WD 2	
+P32330	UniProtKB	Repeat	318	358	.	.	.	Note=WD 3	
+P32330	UniProtKB	Repeat	426	471	.	.	.	Note=WD 4	
+P32330	UniProtKB	Repeat	476	515	.	.	.	Note=WD 5	
+P32330	UniProtKB	Repeat	651	689	.	.	.	Note=WD 6	
+P32330	UniProtKB	Modified residue	716	716	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P39708 1 457
+P39708	UniProtKB	Chain	1	457	.	.	.	ID=PRO_0000182799;Note=NADP-specific glutamate dehydrogenase 2	
+P39708	UniProtKB	Nucleotide binding	175	204	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39708	UniProtKB	Active site	111	111	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10011	
+P39708	UniProtKB	Cross-link	326	326	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07262	
+P39708	UniProtKB	Cross-link	372	372	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07262	
+P39708	UniProtKB	Cross-link	436	436	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07262	
+##sequence-region Q04603 1 196
+Q04603	UniProtKB	Chain	1	196	.	.	.	ID=PRO_0000191754;Note=DNA polymerase epsilon subunit D	
+Q04603	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q3E840 1 82
+Q3E840	UniProtKB	Chain	1	82	.	.	.	ID=PRO_0000082639;Note=Diphthamide biosynthesis protein 3	
+Q3E840	UniProtKB	Zinc finger	3	59	.	.	.	Note=DPH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00456	
+Q3E840	UniProtKB	Compositional bias	79	82	.	.	.	Note=Poly-Ala	
+Q3E840	UniProtKB	Beta strand	4	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+Q3E840	UniProtKB	Helix	9	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+Q3E840	UniProtKB	Beta strand	12	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+Q3E840	UniProtKB	Turn	16	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+Q3E840	UniProtKB	Beta strand	20	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+Q3E840	UniProtKB	Beta strand	28	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+Q3E840	UniProtKB	Helix	35	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+Q3E840	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+Q3E840	UniProtKB	Beta strand	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4D4O	
+Q3E840	UniProtKB	Beta strand	53	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33	
+Q3E840	UniProtKB	Helix	60	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AX2	
+##sequence-region P39517 1 506
+P39517	UniProtKB	Chain	1	506	.	.	.	ID=PRO_0000055044;Note=ATP-dependent RNA helicase DHH1	
+P39517	UniProtKB	Domain	77	247	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P39517	UniProtKB	Domain	257	417	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P39517	UniProtKB	Nucleotide binding	90	97	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P39517	UniProtKB	Motif	46	74	.	.	.	Note=Q motif	
+P39517	UniProtKB	Motif	195	198	.	.	.	Note=DEAD box	
+P39517	UniProtKB	Compositional bias	434	505	.	.	.	Note=Gln-rich	
+P39517	UniProtKB	Mutagenesis	89	89	.	.	.	Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius%3B when associated with A-91. Impairs RNA binding in vitro. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810	
+P39517	UniProtKB	Mutagenesis	91	91	.	.	.	Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius%3B when associated with A-89. Impairs RNA binding in vitro. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810	
+P39517	UniProtKB	Mutagenesis	195	195	.	.	.	Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810	
+P39517	UniProtKB	Mutagenesis	196	196	.	.	.	Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810	
+P39517	UniProtKB	Mutagenesis	345	345	.	.	.	Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810	
+P39517	UniProtKB	Mutagenesis	346	346	.	.	.	Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810	
+P39517	UniProtKB	Mutagenesis	369	369	.	.	.	Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810	
+P39517	UniProtKB	Mutagenesis	370	370	.	.	.	Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810	
+P39517	UniProtKB	Helix	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	55	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	71	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	86	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	96	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	124	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Turn	138	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	154	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	166	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	172	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	191	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	203	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	221	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	231	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	245	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	258	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	270	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	284	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	293	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	310	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	319	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	333	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	343	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	352	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	364	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	381	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	389	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Helix	392	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+P39517	UniProtKB	Beta strand	406	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRW	
+P39517	UniProtKB	Helix	415	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M	
+##sequence-region Q04217 1 1267
+Q04217	UniProtKB	Chain	1	1267	.	.	.	ID=PRO_0000055162;Note=Probable ATP-dependent RNA helicase DHR1	
+Q04217	UniProtKB	Domain	401	580	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q04217	UniProtKB	Domain	675	858	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q04217	UniProtKB	Nucleotide binding	414	421	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q04217	UniProtKB	Motif	516	519	.	.	.	Note=DEAH box	
+Q04217	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P35497 1 357
+P35497	UniProtKB	Chain	1	357	.	.	.	ID=PRO_0000160821;Note=Sorbitol dehydrogenase 1	
+P35497	UniProtKB	Metal binding	43	43	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35497	UniProtKB	Metal binding	68	68	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35497	UniProtKB	Metal binding	69	69	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35497	UniProtKB	Binding site	49	49	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35497	UniProtKB	Binding site	154	154	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35497	UniProtKB	Binding site	301	301	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35497	UniProtKB	Binding site	302	302	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region O13577 1 133
+O13577	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000247354;Note=Damage-regulated import facilitator 1	
+O13577	UniProtKB	Compositional bias	16	32	.	.	.	Note=Poly-Gln	
+##sequence-region P40318 1 1319
+P40318	UniProtKB	Chain	1	1319	.	.	.	ID=PRO_0000072214;Note=ERAD-associated E3 ubiquitin-protein ligase DOA10	
+P40318	UniProtKB	Topological domain	1	131	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	153	203	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	225	468	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	469	489	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	490	491	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	492	512	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	513	626	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	627	647	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	648	660	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	661	681	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	682	739	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	740	760	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	761	777	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	778	797	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	798	965	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	966	986	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	987	1019	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	1020	1040	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	1041	1113	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	1114	1134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	1135	1168	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	1169	1189	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	1190	1213	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	1214	1234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	1235	1270	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Transmembrane	1271	1291	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Topological domain	1292	1319	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40318	UniProtKB	Zinc finger	31	100	.	.	.	Note=RING-CH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00623	
+P40318	UniProtKB	Compositional bias	288	291	.	.	.	Note=Poly-Ala	
+P40318	UniProtKB	Compositional bias	293	296	.	.	.	Note=Poly-Asn	
+P40318	UniProtKB	Compositional bias	332	341	.	.	.	Note=Asp/Gln/Ser-rich (acidic)	
+P40318	UniProtKB	Compositional bias	369	374	.	.	.	Note=Poly-Gln	
+P40318	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40318	UniProtKB	Sequence conflict	241	241	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40318	UniProtKB	Sequence conflict	743	743	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40318	UniProtKB	Sequence conflict	1085	1085	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40318	UniProtKB	Sequence conflict	1186	1186	.	.	.	Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40318	UniProtKB	Beta strand	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M6M	
+P40318	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M6M	
+P40318	UniProtKB	Helix	67	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M6M	
+P40318	UniProtKB	Beta strand	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M6M	
+##sequence-region P47110 1 350
+P47110	UniProtKB	Chain	1	350	.	.	.	ID=PRO_0000186050;Note=DNA polymerase delta subunit 3	
+P47110	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47110	UniProtKB	Modified residue	230	230	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P14284 1 1504
+P14284	UniProtKB	Chain	1	1504	.	.	.	ID=PRO_0000046470;Note=DNA polymerase zeta catalytic subunit	
+P14284	UniProtKB	Zinc finger	1398	1417	.	.	.	Note=CysA-type	
+P14284	UniProtKB	Motif	1446	1473	.	.	.	Note=CysB motif	
+P14284	UniProtKB	Metal binding	1398	1398	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14284	UniProtKB	Metal binding	1401	1401	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14284	UniProtKB	Metal binding	1414	1414	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14284	UniProtKB	Metal binding	1417	1417	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14284	UniProtKB	Metal binding	1446	1446	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14284	UniProtKB	Metal binding	1449	1449	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14284	UniProtKB	Metal binding	1468	1468	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14284	UniProtKB	Metal binding	1473	1473	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53255 1 507
+P53255	UniProtKB	Chain	1	507	.	.	.	ID=PRO_0000202810;Note=CWF19-like protein DRN1	
+P53255	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53255	UniProtKB	Mutagenesis	269	269	.	.	.	Note=Causes accumulation of pre-mRNA splicing intermediates. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24919400;Dbxref=PMID:24919400	
+P53255	UniProtKB	Mutagenesis	272	272	.	.	.	Note=Causes accumulation of pre-mRNA splicing intermediates. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24919400;Dbxref=PMID:24919400	
+P53255	UniProtKB	Mutagenesis	366	366	.	.	.	Note=Causes accumulation of pre-mRNA splicing intermediates. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24919400;Dbxref=PMID:24919400	
+P53255	UniProtKB	Mutagenesis	459	459	.	.	.	Note=Causes accumulation of pre-mRNA splicing intermediates. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24919400;Dbxref=PMID:24919400	
+P53255	UniProtKB	Mutagenesis	474	474	.	.	.	Note=Causes accumulation of pre-mRNA splicing intermediates. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24919400;Dbxref=PMID:24919400	
+##sequence-region P32325 1 704
+P32325	UniProtKB	Chain	1	704	.	.	.	ID=PRO_0000079791;Note=DDK kinase regulatory subunit DBF4	
+P32325	UniProtKB	Zinc finger	654	703	.	.	.	Note=DBF4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00600	
+P32325	UniProtKB	Region	10	19	.	.	.	Note=D box 1	
+P32325	UniProtKB	Region	62	70	.	.	.	Note=D box 2	
+P32325	UniProtKB	Motif	83	88	.	.	.	Note=POLO box domain (PBD)-binding	
+P32325	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32325	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32325	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32325	UniProtKB	Modified residue	623	623	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32325	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Defective for interaction with CDC5. R->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905	
+P32325	UniProtKB	Mutagenesis	84	84	.	.	.	Note=No effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905	
+P32325	UniProtKB	Mutagenesis	85	85	.	.	.	Note=Defective for interaction with CDC5. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905	
+P32325	UniProtKB	Mutagenesis	86	86	.	.	.	Note=No effect. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905	
+P32325	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Defective for interaction with CDC5. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905	
+P32325	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Defective for interaction with CDC5. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905	
+P32325	UniProtKB	Mutagenesis	661	661	.	.	.	Note=In DBF4-AAHH%3B weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands%3B when associated with A-664. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20436286;Dbxref=PMID:20436286	
+P32325	UniProtKB	Mutagenesis	664	664	.	.	.	Note=In DBF4-AAHH%3B weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands%3B when associated with A-661. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20436286;Dbxref=PMID:20436286	
+P32325	UniProtKB	Mutagenesis	674	674	.	.	.	Note=In DBF4-CCAA%3B weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands%3B when associated with A-680. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20436286;Dbxref=PMID:20436286	
+P32325	UniProtKB	Mutagenesis	680	680	.	.	.	Note=Weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands. In DBF4-CCAA%3B weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands%3B when associated with A-674. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20436286;Dbxref=PMID:20436286	
+P32325	UniProtKB	Mutagenesis	680	680	.	.	.	Note=Weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands. H->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20436286;Dbxref=PMID:20436286	
+P32325	UniProtKB	Sequence conflict	159	160	.	.	.	Note=GA->NT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32325	UniProtKB	Sequence conflict	177	177	.	.	.	Note=R->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32325	UniProtKB	Sequence conflict	197	197	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32325	UniProtKB	Sequence conflict	256	256	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32325	UniProtKB	Sequence conflict	416	425	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32325	UniProtKB	Sequence conflict	439	439	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32325	UniProtKB	Helix	106	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T2S	
+P32325	UniProtKB	Beta strand	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4	
+P32325	UniProtKB	Helix	138	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4	
+P32325	UniProtKB	Beta strand	161	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4	
+P32325	UniProtKB	Beta strand	172	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4	
+P32325	UniProtKB	Helix	179	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4	
+P32325	UniProtKB	Helix	190	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4	
+P32325	UniProtKB	Beta strand	200	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4	
+P32325	UniProtKB	Helix	204	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4	
+P32325	UniProtKB	Helix	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4	
+P32325	UniProtKB	Helix	233	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4	
+##sequence-region P47089 1 198
+P47089	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000130609;Note=Translation machinery-associated protein 22	
+P47089	UniProtKB	Domain	99	170	.	.	.	Note=SUI1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00200	
+##sequence-region Q12743 1 341
+Q12743	UniProtKB	Chain	1	341	.	.	.	ID=PRO_0000219054;Note=DER1-like family member protein 1	
+Q12743	UniProtKB	Topological domain	1	41	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12743	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12743	UniProtKB	Topological domain	63	122	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12743	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12743	UniProtKB	Topological domain	144	170	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12743	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12743	UniProtKB	Topological domain	192	192	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12743	UniProtKB	Transmembrane	193	213	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12743	UniProtKB	Topological domain	214	341	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07786 1 357
+Q07786	UniProtKB	Chain	1	357	.	.	.	ID=PRO_0000160822;Note=Sorbitol dehydrogenase 2	
+Q07786	UniProtKB	Metal binding	43	43	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07786	UniProtKB	Metal binding	68	68	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07786	UniProtKB	Metal binding	69	69	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07786	UniProtKB	Binding site	49	49	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07786	UniProtKB	Binding site	154	154	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07786	UniProtKB	Binding site	301	301	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07786	UniProtKB	Binding site	302	302	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38791 1 387
+P38791	UniProtKB	Chain	1	387	.	.	.	ID=PRO_0000134488;Note=Deoxyhypusine synthase	
+P38791	UniProtKB	Nucleotide binding	108	112	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Nucleotide binding	134	136	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Nucleotide binding	329	330	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Nucleotide binding	363	364	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Region	139	140	.	.	.	Note=Spermidine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Region	335	337	.	.	.	Note=Spermidine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Region	344	350	.	.	.	Note=Spermidine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Active site	350	350	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Binding site	140	140	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Binding site	257	257	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Binding site	262	262	.	.	.	Note=Spermidine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Binding site	304	304	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38791	UniProtKB	Binding site	309	309	.	.	.	Note=Spermidine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03373 1 323
+Q03373	UniProtKB	Chain	1	323	.	.	.	ID=PRO_0000079898;Note=Down-regulator of invasive growth 2	
+Q03373	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q03373	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956	
+Q03373	UniProtKB	Modified residue	266	266	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03373	UniProtKB	Modified residue	270	270	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40366 1 167
+P40366	UniProtKB	Chain	1	167	.	.	.	ID=PRO_0000203057;Note=Protein DLS1	
+P40366	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q06819 1 143
+Q06819	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06819	UniProtKB	Chain	2	143	.	.	.	ID=PRO_0000218286;Note=Spliceosomal protein DIB1	
+Q06819	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P40564 1 432
+P40564	UniProtKB	Chain	1	432	.	.	.	ID=PRO_0000071141;Note=DnaJ-like protein 1	
+P40564	UniProtKB	Domain	4	73	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P40564	UniProtKB	Sequence conflict	325	325	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39976 1 496
+P39976	UniProtKB	Chain	1	496	.	.	.	ID=PRO_0000128176;Note=D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3	
+P39976	UniProtKB	Domain	64	243	.	.	.	Note=FAD-binding PCMH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00718	
+P39976	UniProtKB	Cross-link	17	17	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region Q04216 1 342
+Q04216	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000203299;Note=Defect at low temperature protein 1	
+Q04216	UniProtKB	Topological domain	1	15	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04216	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04216	UniProtKB	Topological domain	37	47	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04216	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04216	UniProtKB	Topological domain	69	342	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03652 1 475
+Q03652	UniProtKB	Chain	1	475	.	.	.	ID=PRO_0000203331;Note=Protein DML1	
+##sequence-region P31116 1 359
+P31116	UniProtKB	Chain	1	359	.	.	.	ID=PRO_0000066707;Note=Homoserine dehydrogenase	
+P31116	UniProtKB	Nucleotide binding	11	18	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284	
+P31116	UniProtKB	Active site	223	223	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31116	UniProtKB	Binding site	93	93	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284	
+P31116	UniProtKB	Binding site	117	117	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284	
+P31116	UniProtKB	Binding site	208	208	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284	
+P31116	UniProtKB	Cross-link	290	290	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P31116	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Loss of activity. K->A	
+P31116	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Increases KM for aspartate-semialdehyde 48-fold and reduces Kcat by 50%25. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284	
+P31116	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Loss of activity. E->L%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284	
+P31116	UniProtKB	Mutagenesis	219	219	.	.	.	Note=Reduces Kcat 150-fold. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284	
+P31116	UniProtKB	Mutagenesis	223	223	.	.	.	Note=Loss of activity. K->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284	
+P31116	UniProtKB	Sequence conflict	134	134	.	.	.	Note=K->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31116	UniProtKB	Sequence conflict	152	152	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31116	UniProtKB	Sequence conflict	327	327	.	.	.	Note=R->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31116	UniProtKB	Sequence conflict	333	333	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31116	UniProtKB	Beta strand	4	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	15	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	30	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	41	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Turn	54	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBU	
+P31116	UniProtKB	Helix	59	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	73	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	87	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	96	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	102	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	124	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBU	
+P31116	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Turn	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBU	
+P31116	UniProtKB	Helix	153	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	166	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	175	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	194	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	212	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	218	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	249	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	255	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TVE	
+P31116	UniProtKB	Helix	258	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	265	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	268	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Turn	279	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	283	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Turn	293	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	297	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	310	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	319	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Beta strand	332	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+P31116	UniProtKB	Helix	341	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF	
+##sequence-region Q06143 1 298
+Q06143	UniProtKB	Chain	1	298	.	.	.	ID=PRO_0000233005;Note=Mitochondrial dicarboxylate transporter	
+Q06143	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06143	UniProtKB	Transmembrane	58	76	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06143	UniProtKB	Transmembrane	105	126	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06143	UniProtKB	Transmembrane	170	189	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06143	UniProtKB	Transmembrane	211	231	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06143	UniProtKB	Transmembrane	265	283	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06143	UniProtKB	Repeat	11	95	.	.	.	Note=Solcar 1	
+Q06143	UniProtKB	Repeat	103	195	.	.	.	Note=Solcar 2	
+Q06143	UniProtKB	Repeat	205	289	.	.	.	Note=Solcar 3	
+##sequence-region P36037 1 715
+P36037	UniProtKB	Chain	1	715	.	.	.	ID=PRO_0000050958;Note=Protein DOA1	
+P36037	UniProtKB	Repeat	11	40	.	.	.	Note=WD 1	
+P36037	UniProtKB	Repeat	53	82	.	.	.	Note=WD 2	
+P36037	UniProtKB	Repeat	97	125	.	.	.	Note=WD 3	
+P36037	UniProtKB	Repeat	135	166	.	.	.	Note=WD 4	
+P36037	UniProtKB	Repeat	177	206	.	.	.	Note=WD 5	
+P36037	UniProtKB	Repeat	218	247	.	.	.	Note=WD 6	
+P36037	UniProtKB	Repeat	259	288	.	.	.	Note=WD 7	
+P36037	UniProtKB	Domain	352	449	.	.	.	Note=PFU;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00727	
+P36037	UniProtKB	Domain	465	715	.	.	.	Note=PUL;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00729	
+P36037	UniProtKB	Repeat	478	512	.	.	.	Note=ARM 1	
+P36037	UniProtKB	Repeat	513	543	.	.	.	Note=ARM 2	
+P36037	UniProtKB	Repeat	544	582	.	.	.	Note=ARM 3	
+P36037	UniProtKB	Repeat	583	635	.	.	.	Note=ARM 4	
+P36037	UniProtKB	Repeat	636	680	.	.	.	Note=ARM 5	
+P36037	UniProtKB	Repeat	681	715	.	.	.	Note=ARM 6	
+P36037	UniProtKB	Modified residue	332	332	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P36037	UniProtKB	Mutagenesis	541	541	.	.	.	Note=Depletion of cellular ubiquitin pools and reduced activity of the ubiquitin fusion degradation pathway. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805280;Dbxref=PMID:19805280	
+P36037	UniProtKB	Mutagenesis	669	669	.	.	.	Note=Depletion of cellular ubiquitin pools and reduced activity of the ubiquitin fusion degradation pathway. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805280;Dbxref=PMID:19805280	
+P36037	UniProtKB	Sequence conflict	180	180	.	.	.	Note=D->DI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36037	UniProtKB	Beta strand	4	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	16	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	26	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	34	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	57	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Turn	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	78	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	102	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	111	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	119	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	128	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	140	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Turn	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	152	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	162	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	169	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	182	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	192	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	200	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Turn	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	212	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	223	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	234	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	241	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Turn	248	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	253	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	264	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	275	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	284	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Helix	291	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT	
+P36037	UniProtKB	Beta strand	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F	
+P36037	UniProtKB	Beta strand	383	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F	
+P36037	UniProtKB	Beta strand	400	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F	
+P36037	UniProtKB	Helix	410	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F	
+P36037	UniProtKB	Helix	425	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F	
+P36037	UniProtKB	Helix	428	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F	
+P36037	UniProtKB	Helix	480	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	499	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	512	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	534	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	544	546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	550	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	554	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	566	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Turn	583	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	586	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	593	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	599	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Beta strand	608	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSP	
+P36037	UniProtKB	Helix	612	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	642	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Turn	652	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	658	662	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	664	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	682	685	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Turn	688	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	692	701	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+P36037	UniProtKB	Helix	705	714	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE	
+##sequence-region P33309 1 386
+P33309	UniProtKB	Chain	1	386	.	.	.	ID=PRO_0000143191;Note=Protein DOM34	
+P33309	UniProtKB	Beta strand	2	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	16	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	25	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	40	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	63	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Turn	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	80	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	104	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	115	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	124	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Turn	136	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	142	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	151	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	162	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	186	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Turn	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	209	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	219	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	237	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	241	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	246	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Turn	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGM	
+P33309	UniProtKB	Helix	257	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	266	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	269	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	278	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Turn	292	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	296	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	302	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	314	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	323	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	329	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	348	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Helix	357	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Turn	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+P33309	UniProtKB	Beta strand	368	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN	
+##sequence-region Q12395 1 269
+Q12395	UniProtKB	Chain	1	269	.	.	.	ID=PRO_0000129518;Note=Defective in cullin neddylation protein 1	
+Q12395	UniProtKB	Domain	14	51	.	.	.	Note=UBA-like	
+Q12395	UniProtKB	Domain	70	266	.	.	.	Note=DCUN1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00574	
+Q12395	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12395	UniProtKB	Helix	13	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Helix	29	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Turn	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Helix	43	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Helix	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L4F	
+Q12395	UniProtKB	Helix	73	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Helix	90	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Helix	107	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Helix	127	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Helix	142	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Helix	160	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Beta strand	180	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Helix	184	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Beta strand	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P	
+Q12395	UniProtKB	Helix	205	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Beta strand	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Helix	225	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Helix	241	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+Q12395	UniProtKB	Beta strand	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P	
+Q12395	UniProtKB	Helix	256	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3	
+##sequence-region Q06151 1 350
+Q06151	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06151	UniProtKB	Chain	2	350	.	.	.	ID=PRO_0000109798;Note=m7GpppX diphosphatase	
+Q06151	UniProtKB	Region	259	270	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06151	UniProtKB	Motif	266	270	.	.	.	Note=Histidine triad motif;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06151	UniProtKB	Active site	268	268	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96C86	
+Q06151	UniProtKB	Binding site	171	171	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96C86	
+Q06151	UniProtKB	Binding site	196	196	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96C86	
+Q06151	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06151	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q06151	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15240832;Dbxref=PMID:19779198,PMID:15240832	
+Q06151	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphothreonine%3B by YAK1;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PubMed:19779198,ECO:0000305|PubMed:15240832;Dbxref=PMID:19779198,PMID:15240832	
+Q06151	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06151	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06151	UniProtKB	Mutagenesis	66	66	.	.	.	Note=Stronly reduces phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15240832;Dbxref=PMID:15240832	
+Q06151	UniProtKB	Mutagenesis	268	268	.	.	.	Note=Loss of function. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12198172;Dbxref=PMID:12198172	
+Q06151	UniProtKB	Sequence conflict	66	66	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06151	UniProtKB	Helix	8	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	16	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Turn	25	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	29	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	39	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Turn	78	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	82	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	94	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Turn	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	110	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	121	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	132	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	139	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	160	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	189	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	206	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	219	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	227	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Turn	245	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	251	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	254	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	263	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	268	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Turn	280	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Turn	285	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	288	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	291	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Turn	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	305	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Beta strand	311	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	320	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+Q06151	UniProtKB	Helix	326	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3	
+##sequence-region P0CH64 1 225
+P0CH64	UniProtKB	Chain	1	225	.	.	.	ID=PRO_0000397875;Note=Cyanamide hydratase DDI3	
+P0CH64	UniProtKB	Domain	52	162	.	.	.	Note=HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01175	
+##sequence-region P89113 1 61
+P89113	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P89113	UniProtKB	Chain	23	61	.	.	.	ID=PRO_0000021096;Note=Protein DDR2	
+P89113	UniProtKB	Glycosylation	24	24	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P89113	UniProtKB	Glycosylation	27	27	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P54005 1 336
+P54005	UniProtKB	Chain	1	336	.	.	.	ID=PRO_0000203358;Note=Protein DIA1	
+##sequence-region P69771 1 204
+P69771	UniProtKB	Chain	1	204	.	.	.	ID=PRO_0000211461;Note=Vacuolar protein-sorting-associated protein 46	
+P69771	UniProtKB	Region	1	103	.	.	.	Note=Interaction with VSP24	
+P69771	UniProtKB	Region	104	204	.	.	.	Note=Interaction with VSP4	
+P69771	UniProtKB	Region	176	204	.	.	.	Note=Interaction with VTA1	
+P69771	UniProtKB	Coiled coil	9	56	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P69771	UniProtKB	Coiled coil	109	129	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P69771	UniProtKB	Modified residue	5	5	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P69771	UniProtKB	Mutagenesis	198	198	.	.	.	Note=Impairs sorting. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861	
+P69771	UniProtKB	Mutagenesis	199	199	.	.	.	Note=Impairs sorting%3B when associated with D-202. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861	
+P69771	UniProtKB	Mutagenesis	202	202	.	.	.	Note=Impairs sorting%3B when associated with D-199. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861	
+P69771	UniProtKB	Helix	186	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H7P	
+##sequence-region P32891 1 587
+P32891	UniProtKB	Domain	146	327	.	.	.	Note=FAD-binding PCMH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00718	
+P32891	UniProtKB	Sequence conflict	439	439	.	.	.	Note=A->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32891	UniProtKB	Sequence conflict	572	587	.	.	.	Note=DKIFKTDPNEPANDYR->GQNL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P09624 1 499
+P09624	UniProtKB	Transit peptide	1	21	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3279419;Dbxref=PMID:3279419	
+P09624	UniProtKB	Chain	22	499	.	.	.	ID=PRO_0000030301;Note=Dihydrolipoyl dehydrogenase%2C mitochondrial	
+P09624	UniProtKB	Nucleotide binding	56	65	.	.	.	Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9538259,ECO:0000269|Ref.9;Dbxref=PMID:9538259	
+P09624	UniProtKB	Nucleotide binding	174	176	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09624	UniProtKB	Nucleotide binding	211	218	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09624	UniProtKB	Nucleotide binding	352	355	.	.	.	Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9538259,ECO:0000269|Ref.9;Dbxref=PMID:9538259	
+P09624	UniProtKB	Active site	478	478	.	.	.	Note=Proton acceptor	
+P09624	UniProtKB	Binding site	74	74	.	.	.	Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9538259,ECO:0000269|Ref.9;Dbxref=PMID:9538259	
+P09624	UniProtKB	Binding site	139	139	.	.	.	Note=FAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9538259,ECO:0000269|Ref.9;Dbxref=PMID:9538259	
+P09624	UniProtKB	Binding site	234	234	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09624	UniProtKB	Binding site	268	268	.	.	.	Note=NAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09624	UniProtKB	Binding site	305	305	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09624	UniProtKB	Binding site	346	346	.	.	.	Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9538259,ECO:0000269|Ref.9;Dbxref=PMID:9538259	
+P09624	UniProtKB	Disulfide bond	65	70	.	.	.	Note=Redox-active;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9538259;Dbxref=PMID:9538259	
+P09624	UniProtKB	Beta strand	23	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	36	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	52	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	63	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	70	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	105	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	133	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	153	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JEH	
+P09624	UniProtKB	Beta strand	163	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	188	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	194	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	205	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	214	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	229	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	235	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	245	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	265	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Turn	275	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	279	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Turn	287	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	291	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Turn	311	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JEH	
+P09624	UniProtKB	Turn	315	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	345	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	348	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	354	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JEH	
+P09624	UniProtKB	Beta strand	382	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	386	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	397	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	407	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	418	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	429	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Turn	436	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Beta strand	440	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	451	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	468	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+P09624	UniProtKB	Helix	483	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59	
+##sequence-region Q07505 1 273
+Q07505	UniProtKB	Chain	1	273	.	.	.	ID=PRO_0000161585;Note=Putative carboxymethylenebutenolidase	
+Q07505	UniProtKB	Active site	130	130	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07505	UniProtKB	Active site	191	191	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07505	UniProtKB	Active site	223	223	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38823 1 416
+P38823	UniProtKB	Chain	1	416	.	.	.	ID=PRO_0000056338;Note=E3 ubiquitin-protein ligase DMA1	
+P38823	UniProtKB	Domain	189	252	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+P38823	UniProtKB	Zinc finger	327	371	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P38823	UniProtKB	Cross-link	150	150	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P38823	UniProtKB	Cross-link	204	204	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P38823	UniProtKB	Cross-link	217	217	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P38823	UniProtKB	Cross-link	237	237	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P38823	UniProtKB	Cross-link	240	240	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P38823	UniProtKB	Cross-link	260	260	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P38823	UniProtKB	Cross-link	300	300	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P38823	UniProtKB	Cross-link	306	306	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P38823	UniProtKB	Cross-link	313	313	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P38823	UniProtKB	Cross-link	317	317	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P38823	UniProtKB	Mutagenesis	192	192	.	.	.	Note=Decreases the interaction with CDC123. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434	
+P38823	UniProtKB	Mutagenesis	220	220	.	.	.	Note=Decreases the interaction with CDC123%2C when associated with L-223. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434	
+P38823	UniProtKB	Mutagenesis	223	223	.	.	.	Note=Decreases the interaction with CDC123%2C when associated with A-220. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434	
+P38823	UniProtKB	Mutagenesis	345	345	.	.	.	Note=Decreases the interaction with CDC123%2C when associated with A-350. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434	
+P38823	UniProtKB	Mutagenesis	350	350	.	.	.	Note=Decreases the interaction with CDC123%2C when associated with S-345. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434	
+##sequence-region P25453 1 334
+P25453	UniProtKB	Chain	1	334	.	.	.	ID=PRO_0000122915;Note=Meiotic recombination protein DMC1	
+P25453	UniProtKB	Nucleotide binding	121	128	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25453	UniProtKB	Binding site	223	223	.	.	.	Note=ssDNA or dsDNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25453	UniProtKB	Binding site	226	226	.	.	.	Note=ssDNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25453	UniProtKB	Binding site	229	229	.	.	.	Note=ssDNA or dsDNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25453	UniProtKB	Binding site	235	235	.	.	.	Note=ssDNA or dsDNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25453	UniProtKB	Binding site	305	305	.	.	.	Note=ssDNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25453	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Recessive mutant%3B phenotypically null. Eliminates the ability for self-association. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9335591;Dbxref=PMID:9335591	
+P25453	UniProtKB	Mutagenesis	126	126	.	.	.	Note=Dominant mutant%3B phenotypically null. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9335591;Dbxref=PMID:9335591	
+##sequence-region P43595 1 202
+P43595	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43595	UniProtKB	Chain	19	202	.	.	.	ID=PRO_0000014319;Note=Protein DCV1	
+P43595	UniProtKB	Transmembrane	91	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43595	UniProtKB	Transmembrane	137	155	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43595	UniProtKB	Transmembrane	168	189	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08949 1 612
+Q08949	UniProtKB	Chain	1	612	.	.	.	ID=PRO_0000239638;Note=DNA damage checkpoint protein 1	
+Q08949	UniProtKB	Modified residue	436	436	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P40526 1 253
+P40526	UniProtKB	Chain	1	253	.	.	.	ID=PRO_0000213682;Note=Polyprenol reductase	
+P40526	UniProtKB	Transmembrane	18	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40526	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40526	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40526	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05031 1 458
+Q05031	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05031	UniProtKB	Chain	27	437	.	.	.	ID=PRO_0000012127;Note=Mannan endo-1%2C6-alpha-mannosidase DFG5	
+Q05031	UniProtKB	Propeptide	438	458	.	.	.	ID=PRO_0000012128;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05031	UniProtKB	Lipidation	437	437	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05031	UniProtKB	Glycosylation	89	89	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05031	UniProtKB	Glycosylation	114	114	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05031	UniProtKB	Glycosylation	138	138	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05031	UniProtKB	Glycosylation	208	208	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05031	UniProtKB	Glycosylation	231	231	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05031	UniProtKB	Glycosylation	245	245	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05031	UniProtKB	Glycosylation	270	270	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05031	UniProtKB	Glycosylation	273	273	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05031	UniProtKB	Glycosylation	417	417	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08650 1 418
+Q08650	UniProtKB	Chain	1	418	.	.	.	ID=PRO_0000233001;Note=Diacylglycerol O-acyltransferase 1	
+Q08650	UniProtKB	Topological domain	1	71	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08650	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08650	UniProtKB	Topological domain	93	186	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08650	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08650	UniProtKB	Topological domain	208	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08650	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08650	UniProtKB	Topological domain	237	289	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08650	UniProtKB	Transmembrane	290	310	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08650	UniProtKB	Topological domain	311	418	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08650	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08650	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Retains more than 40%25 of the wild-type enzyme activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129	
+Q08650	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Retains more than 40%25 of the wild-type enzyme activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129	
+Q08650	UniProtKB	Mutagenesis	129	131	.	.	.	Note=Almost complete loss of enzyme activity. YFP->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129	
+Q08650	UniProtKB	Mutagenesis	193	196	.	.	.	Note=Complete loss of enzyme activity. HPHG->EPHS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129	
+Q08650	UniProtKB	Mutagenesis	193	193	.	.	.	Note=Almost complete loss of enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129	
+Q08650	UniProtKB	Mutagenesis	195	195	.	.	.	Note=Complete loss of enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129	
+##sequence-region P13663 1 365
+P13663	UniProtKB	Chain	1	365	.	.	.	ID=PRO_0000141400;Note=Aspartate-semialdehyde dehydrogenase	
+P13663	UniProtKB	Nucleotide binding	13	16	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13663	UniProtKB	Nucleotide binding	40	41	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13663	UniProtKB	Nucleotide binding	187	188	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13663	UniProtKB	Nucleotide binding	343	344	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13663	UniProtKB	Active site	156	156	.	.	.	Note=Acyl-thioester intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13663	UniProtKB	Active site	256	256	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13663	UniProtKB	Binding site	112	112	.	.	.	Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13663	UniProtKB	Binding site	184	184	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13663	UniProtKB	Binding site	211	211	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13663	UniProtKB	Binding site	214	214	.	.	.	Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13663	UniProtKB	Binding site	249	249	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13663	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P13663	UniProtKB	Modified residue	318	318	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P13663	UniProtKB	Modified residue	323	323	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P33327 1 1092
+P33327	UniProtKB	Chain	1	1092	.	.	.	ID=PRO_0000182733;Note=NAD-specific glutamate dehydrogenase	
+P33327	UniProtKB	Active site	626	626	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10011	
+##sequence-region P36009 1 735
+P36009	UniProtKB	Chain	1	735	.	.	.	ID=PRO_0000055163;Note=Probable ATP-dependent RNA helicase DHR2	
+P36009	UniProtKB	Domain	91	257	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P36009	UniProtKB	Domain	262	456	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P36009	UniProtKB	Nucleotide binding	104	111	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P36009	UniProtKB	Motif	203	206	.	.	.	Note=DEAH box	
+P36009	UniProtKB	Sequence conflict	28	28	.	.	.	Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36009	UniProtKB	Sequence conflict	80	98	.	.	.	Note=TLPVYQHKREIMSYIESNP->HFRLPTQARNNVIYSKQS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36009	UniProtKB	Sequence conflict	277	288	.	.	.	Note=DAVIRCCIQINQ->ALSSGVYTNKP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36009	UniProtKB	Sequence conflict	339	339	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03063 1 452
+Q03063	UniProtKB	Chain	1	452	.	.	.	ID=PRO_0000079897;Note=Down-regulator of invasive growth 1	
+Q03063	UniProtKB	Region	212	452	.	.	.	Note=Interaction with FUS3 and KSS1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8918885;Dbxref=PMID:8918885	
+Q03063	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03063	UniProtKB	Modified residue	126	126	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03063	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03063	UniProtKB	Modified residue	272	272	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03063	UniProtKB	Modified residue	275	275	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q03063	UniProtKB	Modified residue	330	330	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03063	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03063	UniProtKB	Modified residue	395	395	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q03063	UniProtKB	Modified residue	428	428	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P41819 1 318
+P41819	UniProtKB	Chain	1	318	.	.	.	ID=PRO_0000101464;Note=Dimethyladenosine transferase	
+P41819	UniProtKB	Compositional bias	3	16	.	.	.	Note=Lys-rich	
+P41819	UniProtKB	Binding site	37	37	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026	
+P41819	UniProtKB	Binding site	39	39	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026	
+P41819	UniProtKB	Binding site	64	64	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026	
+P41819	UniProtKB	Binding site	85	85	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026	
+P41819	UniProtKB	Binding site	113	113	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026	
+P41819	UniProtKB	Binding site	128	128	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026	
+##sequence-region P53388 1 608
+P53388	UniProtKB	Chain	1	608	.	.	.	ID=PRO_0000054150;Note=Dicarboxylic amino acid permease	
+P53388	UniProtKB	Topological domain	1	90	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	112	119	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	120	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	143	156	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	178	201	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	223	231	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	253	285	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	286	306	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	307	322	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	323	343	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	344	372	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	394	423	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	424	444	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	445	454	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	455	475	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	476	501	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	502	522	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	523	530	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Transmembrane	531	551	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Topological domain	552	608	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53388	UniProtKB	Compositional bias	574	577	.	.	.	Note=Poly-Glu	
+P53388	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53388	UniProtKB	Cross-link	76	76	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P46681 1 530
+P46681	UniProtKB	Domain	98	277	.	.	.	Note=FAD-binding PCMH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00718	
+P46681	UniProtKB	Sequence conflict	239	239	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53924 1 522
+P53924	UniProtKB	Chain	1	522	.	.	.	ID=PRO_0000056342;Note=E3 ubiquitin-protein ligase DMA2	
+P53924	UniProtKB	Domain	295	358	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+P53924	UniProtKB	Zinc finger	433	477	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P53924	UniProtKB	Modified residue	206	206	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53924	UniProtKB	Cross-link	211	211	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Cross-link	256	256	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Cross-link	258	258	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Cross-link	288	288	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Cross-link	310	310	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Cross-link	333	333	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Cross-link	343	343	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Cross-link	346	346	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Cross-link	366	366	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Cross-link	406	406	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Cross-link	412	412	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Cross-link	423	423	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552	
+P53924	UniProtKB	Natural variant	13	13	.	.	.	Note=In strain: YJM 269%2C YJM 270%2C YJM 326 and YJM 1129. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53924	UniProtKB	Natural variant	111	111	.	.	.	Note=In strain: YJM 269%2C YJM 270%2C YJM 326 and YJM 1129. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53924	UniProtKB	Natural variant	149	149	.	.	.	Note=In strain: YJM 269%2C YJM 270%2C YJM 326 and YJM 1129. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53924	UniProtKB	Natural variant	165	165	.	.	.	Note=In strain: YJM 267. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53924	UniProtKB	Natural variant	202	202	.	.	.	Note=In strain: YJM 269%2C YJM 270%2C YJM 326 and YJM 1129. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53924	UniProtKB	Natural variant	239	239	.	.	.	Note=In strain: YJM 267. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53924	UniProtKB	Natural variant	428	428	.	.	.	Note=In strain: SK1%2C V1-09%2C YJM 267%2C YJM 269%2C YJM 270%2C YJM 280%2C YJM 320%2CYJM 326%2C YJM 339 and YJM 1129. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53924	UniProtKB	Natural variant	511	522	.	.	.	Note=In strain: SK1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+##sequence-region P38859 1 1522
+P38859	UniProtKB	Chain	1	1522	.	.	.	ID=PRO_0000080711;Note=DNA replication ATP-dependent helicase/nuclease DNA2	
+P38859	UniProtKB	Nucleotide binding	1074	1081	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38859	UniProtKB	Region	450	900	.	.	.	Note=Nuclease activity	
+P38859	UniProtKB	Region	901	1522	.	.	.	Note=Helicase activity	
+P38859	UniProtKB	Metal binding	519	519	.	.	.	Note=Iron-sulfur (4Fe-4S)	
+P38859	UniProtKB	Metal binding	768	768	.	.	.	Note=Iron-sulfur (4Fe-4S)	
+P38859	UniProtKB	Metal binding	771	771	.	.	.	Note=Iron-sulfur (4Fe-4S)	
+P38859	UniProtKB	Metal binding	777	777	.	.	.	Note=Iron-sulfur (4Fe-4S)	
+P38859	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
+P38859	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
+P38859	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
+P38859	UniProtKB	Modified residue	962	962	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38859	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Abolishes phosphorylation by CDK1%2C leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with A-17 and A-237. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
+P38859	UniProtKB	Mutagenesis	17	17	.	.	.	Note=Abolishes phosphorylation by CDK1%2C leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with A-4 and A-237. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
+P38859	UniProtKB	Mutagenesis	17	17	.	.	.	Note=Mimics phosphorylation%3B restores nuclear localization and recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with D-237. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
+P38859	UniProtKB	Mutagenesis	237	237	.	.	.	Note=Abolishes phosphorylation by CDK1%2C leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with A-4 and A-17. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
+P38859	UniProtKB	Mutagenesis	237	237	.	.	.	Note=Mimics phosphorylation%3B restores nuclear localization and recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with D-17. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
+P38859	UniProtKB	Mutagenesis	504	504	.	.	.	Note=In dna2-1%3B temperature-sensitive mutant unable to grow at 37 degrees Celsius%2C probably due to abolition of iron-sulfur-binding. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504	
+P38859	UniProtKB	Mutagenesis	519	519	.	.	.	Note=Abolishes iron-sulfur-binding%3B when associated with A-768%3B A-771 and A-777. Impaired nuclease and ATPase activities%3B when associated with A-768. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504	
+P38859	UniProtKB	Mutagenesis	675	675	.	.	.	Note=Nuclease dead mutant. No helicase activity when the 5'-end of the substrate is blocked. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20929864;Dbxref=PMID:20929864	
+P38859	UniProtKB	Mutagenesis	677	677	.	.	.	Note=Nuclease dead mutant. No helicase activity when the 5'-end of the substrate is blocked. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20929864;Dbxref=PMID:20929864	
+P38859	UniProtKB	Mutagenesis	768	768	.	.	.	Note=Abolishes iron-sulfur-binding%3B when associated with A-519%3B A-771 and A-777. Impaired nuclease and ATPase activities%3B when associated with A-519. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504	
+P38859	UniProtKB	Mutagenesis	771	771	.	.	.	Note=Abolishes iron-sulfur-binding%3B when associated with A-519%3B A-768 and A-777. Impaired nuclease and ATPase activities%3B when associated with A-777. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504	
+P38859	UniProtKB	Mutagenesis	777	777	.	.	.	Note=Abolishes iron-sulfur-binding%3B when associated with A-519%3B A-768 and A-771. Impaired nuclease and ATPase activities%3B when associated with A-771. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504	
+P38859	UniProtKB	Helix	212	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HOG	
+##sequence-region P53871 1 357
+P53871	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53871	UniProtKB	Chain	2	357	.	.	.	ID=PRO_0000203401;Note=Probable glutamine amidotransferase DUG3	
+P53871	UniProtKB	Domain	2	260	.	.	.	Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609	
+P53871	UniProtKB	Active site	2	2	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04110 1 302
+Q04110	UniProtKB	Chain	1	302	.	.	.	ID=PRO_0000086912;Note=Protein ECM11	
+##sequence-region Q06011 1 112
+Q06011	UniProtKB	Chain	1	112	.	.	.	ID=PRO_0000086915;Note=Protein ECM19	
+Q06011	UniProtKB	Transmembrane	35	57	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03214 1 1411
+Q03214	UniProtKB	Chain	1	1411	.	.	.	ID=PRO_0000200597;Note=Protein ECM5	
+Q03214	UniProtKB	Domain	118	159	.	.	.	Note=JmjN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00537	
+Q03214	UniProtKB	Domain	185	279	.	.	.	Note=ARID;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00355	
+Q03214	UniProtKB	Domain	476	695	.	.	.	Note=JmjC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538	
+Q03214	UniProtKB	Zinc finger	1238	1290	.	.	.	Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+##sequence-region P33412 1 323
+P33412	UniProtKB	Chain	1	323	.	.	.	ID=PRO_0000208465;Note=Ethanolamine-phosphate cytidylyltransferase	
+P33412	UniProtKB	Sequence conflict	252	252	.	.	.	Note=S->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40023 1 145
+P40023	UniProtKB	Chain	1	145	.	.	.	ID=PRO_0000202626;Note=Enhancer of mRNA-decapping protein 2	
+##sequence-region P02994 1 458
+P02994	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26545399;Dbxref=PMID:26545399	
+P02994	UniProtKB	Chain	2	458	.	.	.	ID=PRO_0000090973;Note=Elongation factor 1-alpha	
+P02994	UniProtKB	Domain	5	240	.	.	.	Note=tr-type G	
+P02994	UniProtKB	Nucleotide binding	14	21	.	.	.	Note=GTP	
+P02994	UniProtKB	Nucleotide binding	91	95	.	.	.	Note=GTP	
+P02994	UniProtKB	Nucleotide binding	153	156	.	.	.	Note=GTP	
+P02994	UniProtKB	Region	14	21	.	.	.	Note=G1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02994	UniProtKB	Region	70	74	.	.	.	Note=G2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02994	UniProtKB	Region	91	94	.	.	.	Note=G3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02994	UniProtKB	Region	153	156	.	.	.	Note=G4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02994	UniProtKB	Region	192	194	.	.	.	Note=G5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02994	UniProtKB	Site	298	298	.	.	.	Note=Not modified	
+P02994	UniProtKB	Site	372	372	.	.	.	Note=Not modified	
+P02994	UniProtKB	Modified residue	2	2	.	.	.	Note=N%2CN%2CN-trimethylglycine%3B by EFM7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26545399;Dbxref=PMID:26545399	
+P02994	UniProtKB	Modified residue	3	3	.	.	.	Note=N6%2CN6-dimethyllysine%3B by EFM7%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26545399;Dbxref=PMID:26545399	
+P02994	UniProtKB	Modified residue	3	3	.	.	.	Note=N6-methyllysine%3B by EFM7%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26545399;Dbxref=PMID:26545399	
+P02994	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P02994	UniProtKB	Modified residue	30	30	.	.	.	Note=N6-methyllysine%3B by EFM1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:8476932;Dbxref=PMID:22522802,PMID:24517342,PMID:8476932	
+P02994	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P02994	UniProtKB	Modified residue	79	79	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B by EFM5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25446118,ECO:0000269|PubMed:8476932;Dbxref=PMID:22522802,PMID:24517342,PMID:25446118,PMID:8476932	
+P02994	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P02994	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P02994	UniProtKB	Modified residue	259	259	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P02994	UniProtKB	Modified residue	289	289	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P02994	UniProtKB	Modified residue	316	316	.	.	.	Note=N6%2CN6-dimethyllysine%3B by EFM4%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:8476932;Dbxref=PMID:22522802,PMID:24517342,PMID:8476932	
+P02994	UniProtKB	Modified residue	316	316	.	.	.	Note=N6-methyllysine%3B by EFM4%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24517342;Dbxref=PMID:24517342	
+P02994	UniProtKB	Modified residue	390	390	.	.	.	Note=N6-methyllysine%3B by EFM6;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:26115316,ECO:0000269|PubMed:8476932;Dbxref=PMID:22522802,PMID:24517342,PMID:26115316,PMID:8476932	
+P02994	UniProtKB	Modified residue	414	414	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P02994	UniProtKB	Modified residue	430	430	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P02994	UniProtKB	Modified residue	458	458	.	.	.	Note=Lysine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10973948;Dbxref=PMID:10973948	
+P02994	UniProtKB	Cross-link	224	224	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P02994	UniProtKB	Cross-link	242	242	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P02994	UniProtKB	Cross-link	253	253	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P02994	UniProtKB	Cross-link	271	271	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P02994	UniProtKB	Cross-link	393	393	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P02994	UniProtKB	Cross-link	437	437	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P02994	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Reduces interaction with YEF3. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9990316;Dbxref=PMID:9990316	
+P02994	UniProtKB	Mutagenesis	153	153	.	.	.	Note=Increases KM for GTP to 2.7 mM. N->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10514524,ECO:0000269|PubMed:9786872;Dbxref=PMID:10514524,PMID:9786872	
+P02994	UniProtKB	Mutagenesis	153	153	.	.	.	Note=Increases KM for GTP to 6.0 mM and reduces translation fidelity. Increases Km for GTP to 10.3 mM and reduces translation fidelity%3B when associated with E-156. N->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10514524,ECO:0000269|PubMed:9786872;Dbxref=PMID:10514524,PMID:9786872	
+P02994	UniProtKB	Mutagenesis	156	156	.	.	.	Note=Increases KM for GTP to 10.3 mM and reduces translation fidelity%3B when associated with T-152. D->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10514524,ECO:0000269|PubMed:15601860,ECO:0000269|PubMed:9786872;Dbxref=PMID:10514524,PMID:15601860,PMID:9786872	
+P02994	UniProtKB	Mutagenesis	156	156	.	.	.	Note=Increases KM for GTP to 13.1 mM and reduces translation fidelity. Confers hyperresistance to canavanine. D->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10514524,ECO:0000269|PubMed:15601860,ECO:0000269|PubMed:9786872;Dbxref=PMID:10514524,PMID:15601860,PMID:9786872	
+P02994	UniProtKB	Mutagenesis	156	156	.	.	.	Note=Increases KM for GTP to 4.2 mM. Preferres XTP over GTP as substrate. D->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10514524,ECO:0000269|PubMed:15601860,ECO:0000269|PubMed:9786872;Dbxref=PMID:10514524,PMID:15601860,PMID:9786872	
+P02994	UniProtKB	Mutagenesis	286	286	.	.	.	Note=In TEF2-1%3B strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3066688;Dbxref=PMID:3066688	
+P02994	UniProtKB	Mutagenesis	317	317	.	.	.	Note=In TEF2-2%3B strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3066688;Dbxref=PMID:3066688	
+P02994	UniProtKB	Sequence conflict	86	86	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02994	UniProtKB	Beta strand	6	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	20	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	36	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	56	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	78	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	83	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	98	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	110	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	120	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	132	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	147	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	155	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	162	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Turn	193	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Turn	197	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	212	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	217	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	226	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	239	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7C	
+P02994	UniProtKB	Beta strand	245	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Turn	255	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	258	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	275	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Turn	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	283	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	295	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7C	
+P02994	UniProtKB	Beta strand	305	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Turn	315	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	323	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	336	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	358	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	364	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Turn	379	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	384	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	397	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Turn	413	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Helix	417	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	420	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P02994	UniProtKB	Beta strand	429	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+##sequence-region P25039 1 761
+P25039	UniProtKB	Transit peptide	1	42	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03061	
+P25039	UniProtKB	Chain	43	761	.	.	.	ID=PRO_0000007449;Note=Elongation factor G%2C mitochondrial	
+P25039	UniProtKB	Domain	68	349	.	.	.	Note=tr-type G	
+P25039	UniProtKB	Nucleotide binding	77	84	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03061	
+P25039	UniProtKB	Nucleotide binding	148	152	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03061	
+P25039	UniProtKB	Nucleotide binding	202	205	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03061	
+P25039	UniProtKB	Sequence conflict	2	2	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25039	UniProtKB	Sequence conflict	66	66	.	.	.	Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25039	UniProtKB	Sequence conflict	233	233	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25039	UniProtKB	Sequence conflict	478	478	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25039	UniProtKB	Sequence conflict	629	629	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38347 1 419
+P38347	UniProtKB	Chain	1	419	.	.	.	ID=PRO_0000202531;Note=Protein-lysine N-methyltransferase EFM2	
+P38347	UniProtKB	Region	261	263	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+P38347	UniProtKB	Binding site	222	222	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+P38347	UniProtKB	Binding site	290	290	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+P38347	UniProtKB	Binding site	318	318	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+P38347	UniProtKB	Binding site	340	340	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+##sequence-region P40516 1 257
+P40516	UniProtKB	Chain	1	257	.	.	.	ID=PRO_0000202983;Note=Protein-lysine N-methyltransferase EFM4	
+P40516	UniProtKB	Sequence conflict	104	104	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53970 1 246
+P53970	UniProtKB	Chain	1	246	.	.	.	ID=PRO_0000203460;Note=Protein-lysine N-methyltransferase EFM6	
+P53970	UniProtKB	Region	87	89	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H867,ECO:0000255|HAMAP-Rule:MF_03198	
+P53970	UniProtKB	Binding site	51	51	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H867,ECO:0000255|HAMAP-Rule:MF_03198	
+P53970	UniProtKB	Binding site	115	115	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H867,ECO:0000255|HAMAP-Rule:MF_03198	
+P53970	UniProtKB	Binding site	143	143	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H867,ECO:0000255|HAMAP-Rule:MF_03198	
+P53970	UniProtKB	Binding site	169	169	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H867,ECO:0000255|HAMAP-Rule:MF_03198	
+##sequence-region Q03653 1 782
+Q03653	UniProtKB	Chain	1	782	.	.	.	ID=PRO_0000203332;Note=Protein EFR3	
+Q03653	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q03653	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q03653	UniProtKB	Modified residue	564	564	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03653	UniProtKB	Modified residue	625	625	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03653	UniProtKB	Modified residue	632	632	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03653	UniProtKB	Modified residue	643	643	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q03653	UniProtKB	Modified residue	675	675	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q03653	UniProtKB	Modified residue	687	687	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q03653	UniProtKB	Modified residue	690	690	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03653	UniProtKB	Modified residue	735	735	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q03653	UniProtKB	Modified residue	771	771	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03653	UniProtKB	Modified residue	774	774	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03653	UniProtKB	Helix	12	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	33	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	47	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	70	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	88	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	95	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Turn	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	115	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	134	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	141	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Turn	159	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	165	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Turn	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	188	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Turn	201	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	207	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Beta strand	236	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	246	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	260	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	280	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	292	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	296	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Beta strand	311	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	315	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	337	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	355	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	377	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	396	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	420	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	431	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	434	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	448	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	464	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	479	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	499	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	515	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	533	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Turn	543	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+Q03653	UniProtKB	Helix	549	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A	
+##sequence-region P09032 1 578
+P09032	UniProtKB	Chain	1	578	.	.	.	ID=PRO_0000156083;Note=Translation initiation factor eIF-2B subunit gamma	
+P09032	UniProtKB	Modified residue	296	296	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P09032	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P09032	UniProtKB	Modified residue	306	306	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P09032	UniProtKB	Sequence conflict	217	240	.	.	.	Note=QKQQQFFTVYSENEDSERQPILLD->AKNNSNFSLFIQKTKTQRGSQYFWN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09032	UniProtKB	Sequence conflict	491	492	.	.	.	Note=IG->SV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05610 1 365
+Q05610	UniProtKB	Chain	1	365	.	.	.	ID=PRO_0000079977;Note=Donuts protein 1	
+Q05610	UniProtKB	Domain	82	125	.	.	.	Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468	
+Q05610	UniProtKB	Compositional bias	286	292	.	.	.	Note=Poly-Glu	
+Q05610	UniProtKB	Sequence conflict	327	327	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32461 1 534
+P32461	UniProtKB	Chain	1	534	.	.	.	ID=PRO_0000083394;Note=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2	
+##sequence-region P38121 1 705
+P38121	UniProtKB	Chain	1	705	.	.	.	ID=PRO_0000194041;Note=DNA polymerase alpha subunit B	
+P38121	UniProtKB	Compositional bias	80	83	.	.	.	Note=Poly-Ser	
+P38121	UniProtKB	Modified residue	126	126	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38121	UniProtKB	Helix	254	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	294	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	315	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	322	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	329	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	347	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	355	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	360	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	375	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	378	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	393	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	411	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	427	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	435	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	441	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	461	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	470	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	480	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	497	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Turn	505	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Turn	512	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	515	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	520	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	529	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	538	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	545	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	549	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	556	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	614	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	623	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	629	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	640	644	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	647	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	664	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	675	678	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	680	683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	685	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	689	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Helix	694	697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P38121	UniProtKB	Beta strand	698	704	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+##sequence-region P13382 1 1468
+P13382	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P13382	UniProtKB	Chain	2	1468	.	.	.	ID=PRO_0000046440;Note=DNA polymerase alpha catalytic subunit A	
+P13382	UniProtKB	Zinc finger	1287	1317	.	.	.	Note=CysA-type	
+P13382	UniProtKB	Region	1246	1381	.	.	.	Note=DNA-binding region;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13382	UniProtKB	Motif	1348	1372	.	.	.	Note=CysB motif	
+P13382	UniProtKB	Metal binding	1287	1287	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13382	UniProtKB	Metal binding	1290	1290	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13382	UniProtKB	Metal binding	1314	1314	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13382	UniProtKB	Metal binding	1317	1317	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13382	UniProtKB	Metal binding	1348	1348	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13382	UniProtKB	Metal binding	1353	1353	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13382	UniProtKB	Metal binding	1367	1367	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13382	UniProtKB	Metal binding	1372	1372	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13382	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P13382	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P13382	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13382	UniProtKB	Modified residue	83	83	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13382	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13382	UniProtKB	Modified residue	169	169	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13382	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P13382	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13382	UniProtKB	Modified residue	240	240	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P13382	UniProtKB	Modified residue	274	274	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P13382	UniProtKB	Modified residue	309	309	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13382	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P13382	UniProtKB	Natural variant	493	493	.	.	.	Note=In temperature sensitive mutant. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3287376;Dbxref=PMID:3287376	
+P13382	UniProtKB	Mutagenesis	236	236	.	.	.	Note=Increase in length of X' and Y' telomeres. No effect on telomere position effect. Reduced interaction with CDC13. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792	
+P13382	UniProtKB	Mutagenesis	238	238	.	.	.	Note=Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792	
+P13382	UniProtKB	Mutagenesis	241	241	.	.	.	Note=Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. P->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792	
+P13382	UniProtKB	Sequence conflict	759	760	.	.	.	Note=MI->IV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13382	UniProtKB	Helix	141	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C93	
+P13382	UniProtKB	Helix	217	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ	
+P13382	UniProtKB	Beta strand	351	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	365	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	379	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	390	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	403	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	425	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	441	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	469	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	481	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	496	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	503	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	511	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	522	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	525	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	536	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Turn	549	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	553	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	569	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B08	
+P13382	UniProtKB	Beta strand	580	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	589	593	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	598	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	606	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	616	630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	633	639	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Turn	640	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	644	654	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	660	663	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	664	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Turn	673	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FXD	
+P13382	UniProtKB	Helix	682	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	694	698	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	702	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	716	724	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	739	742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	744	767	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	770	781	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	785	790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	794	807	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	854	856	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	860	864	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	868	875	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Turn	880	882	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	905	926	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	930	947	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	948	950	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	951	955	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	964	987	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	991	995	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	997	1003	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	1009	1026	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	1033	1045	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	1048	1054	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	1064	1071	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	1072	1074	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FXD	
+P13382	UniProtKB	Helix	1080	1093	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	1094	1097	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	1101	1118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	1124	1127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	1129	1132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	1137	1139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	1143	1145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	1147	1158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	1167	1173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Turn	1189	1192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Beta strand	1193	1195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	1196	1200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	1202	1204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	1210	1215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Turn	1216	1218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Helix	1219	1225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM	
+P13382	UniProtKB	Turn	1226	1228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FXD	
+P13382	UniProtKB	Helix	1234	1239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FXD	
+P13382	UniProtKB	Turn	1274	1279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Beta strand	1283	1286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Turn	1288	1290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Beta strand	1293	1296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Beta strand	1298	1300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Beta strand	1303	1308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Beta strand	1311	1314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Turn	1315	1317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Helix	1323	1343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Beta strand	1346	1349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Turn	1351	1353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Beta strand	1356	1358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Beta strand	1375	1380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Helix	1382	1395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Helix	1398	1402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Helix	1424	1433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+P13382	UniProtKB	Helix	1435	1449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO	
+##sequence-region Q05521 1 289
+Q05521	UniProtKB	Chain	1	289	.	.	.	ID=PRO_0000220918;Note=Diacylglycerol pyrophosphate phosphatase 1	
+Q05521	UniProtKB	Topological domain	1	21	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Transmembrane	22	42	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Topological domain	43	65	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Topological domain	87	92	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Topological domain	114	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Transmembrane	194	214	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Topological domain	215	222	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Transmembrane	223	243	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Topological domain	244	289	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05521	UniProtKB	Region	118	126	.	.	.	Note=Phosphatase sequence motif I	
+Q05521	UniProtKB	Region	166	169	.	.	.	Note=Phosphatase sequence motif II	
+Q05521	UniProtKB	Region	216	227	.	.	.	Note=Phosphatase sequence motif III	
+Q05521	UniProtKB	Modified residue	285	285	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q05521	UniProtKB	Mutagenesis	125	125	.	.	.	Note=Complete loss of DGPP phosphatase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10545184;Dbxref=PMID:10545184	
+Q05521	UniProtKB	Mutagenesis	169	169	.	.	.	Note=91%25 decrease of DGPP phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10545184;Dbxref=PMID:10545184	
+Q05521	UniProtKB	Mutagenesis	223	223	.	.	.	Note=Complete loss of DGPP phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10545184;Dbxref=PMID:10545184	
+##sequence-region Q08729 1 430
+Q08729	UniProtKB	Chain	1	430	.	.	.	ID=PRO_0000233007;Note=Protein DSE3	
+Q08729	UniProtKB	Modified residue	395	395	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P48510 1 373
+P48510	UniProtKB	Chain	1	373	.	.	.	ID=PRO_0000114900;Note=Ubiquitin domain-containing protein DSK2	
+P48510	UniProtKB	Domain	1	76	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+P48510	UniProtKB	Domain	327	371	.	.	.	Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
+P48510	UniProtKB	Cross-link	13	13	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P48510	UniProtKB	Cross-link	76	76	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P48510	UniProtKB	Sequence conflict	109	109	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48510	UniProtKB	Sequence conflict	296	296	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48510	UniProtKB	Beta strand	1	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF	
+P48510	UniProtKB	Beta strand	12	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF	
+P48510	UniProtKB	Helix	24	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF	
+P48510	UniProtKB	Helix	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF	
+P48510	UniProtKB	Beta strand	42	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF	
+P48510	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF	
+P48510	UniProtKB	Beta strand	67	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF	
+P48510	UniProtKB	Helix	328	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UN2	
+P48510	UniProtKB	Helix	333	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UN2	
+P48510	UniProtKB	Helix	347	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UN2	
+P48510	UniProtKB	Helix	361	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UN2	
+##sequence-region P40568 1 576
+P40568	UniProtKB	Chain	1	576	.	.	.	ID=PRO_0000080024;Note=Kinetochore-associated protein DSN1	
+P40568	UniProtKB	Modified residue	250	250	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40568	UniProtKB	Helix	561	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+##sequence-region P33413 1 735
+P33413	UniProtKB	Chain	1	735	.	.	.	ID=PRO_0000105397;Note=Urea active transporter	
+P33413	UniProtKB	Topological domain	1	14	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	15	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	36	85	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	107	130	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	152	166	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	167	187	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	188	189	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	190	210	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	211	253	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	254	274	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	275	295	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	296	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	317	343	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	344	364	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	365	403	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	404	424	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	425	425	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	426	446	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	447	454	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	455	475	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	476	496	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	497	517	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	518	618	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	619	639	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	640	650	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Transmembrane	651	671	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Topological domain	672	735	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33413	UniProtKB	Sequence conflict	58	63	.	.	.	Note=GLVAAA->RLSGCS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06063 1 367
+Q06063	UniProtKB	Chain	1	367	.	.	.	ID=PRO_0000162156;Note=tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]	
+Q06063	UniProtKB	Nucleotide binding	45	47	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06063	UniProtKB	Nucleotide binding	231	233	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06063	UniProtKB	Nucleotide binding	255	256	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06063	UniProtKB	Active site	128	128	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06063	UniProtKB	Binding site	99	99	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06063	UniProtKB	Binding site	169	169	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06063	UniProtKB	Binding site	197	197	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+##sequence-region P47128 1 113
+P47128	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000086901;Note=Chromatin modification-related protein EAF6	
+P47128	UniProtKB	Coiled coil	1	43	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47128	UniProtKB	Helix	2	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P47128	UniProtKB	Helix	8	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P47128	UniProtKB	Turn	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P47128	UniProtKB	Helix	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P47128	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P47128	UniProtKB	Helix	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+##sequence-region P36049 1 427
+P36049	UniProtKB	Chain	1	427	.	.	.	ID=PRO_0000120000;Note=rRNA-processing protein EBP2	
+P36049	UniProtKB	Coiled coil	45	174	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36049	UniProtKB	Coiled coil	234	265	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36049	UniProtKB	Coiled coil	291	348	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36049	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36049	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36049	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36049	UniProtKB	Mutagenesis	36	37	.	.	.	Note=Reduces sumoylation and impairs interaction with SIZ2%2C WSS1 and ULS1%2C when associated with R-61 and R-62. KK->RR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18603780;Dbxref=PMID:18603780	
+P36049	UniProtKB	Mutagenesis	61	62	.	.	.	Note=Reduces sumoylation and impairs interaction with SIZ2%2C WSS1 and ULS1%2C when associated with R-36 and R-37. KK->RR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18603780;Dbxref=PMID:18603780	
+##sequence-region P48235 1 211
+P48235	UniProtKB	Chain	1	211	.	.	.	ID=PRO_0000202828;Note=Extender of the chronological lifespan protein 1	
+##sequence-region Q04623 1 453
+Q04623	UniProtKB	Chain	1	453	.	.	.	ID=PRO_0000086914;Note=Protein ECM18	
+Q04623	UniProtKB	Domain	130	435	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04623	UniProtKB	Motif	428	433	.	.	.	Note=HXXXXD motif;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P32525 1 599
+P32525	UniProtKB	Chain	1	599	.	.	.	ID=PRO_0000086918;Note=Protein ECM25	
+P32525	UniProtKB	Domain	181	359	.	.	.	Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172	
+P32525	UniProtKB	Compositional bias	363	493	.	.	.	Note=Ser-rich	
+##sequence-region Q99252 1 613
+Q99252	UniProtKB	Chain	1	613	.	.	.	ID=PRO_0000086921;Note=Protein ECM3	
+Q99252	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99252	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99252	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99252	UniProtKB	Transmembrane	143	163	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99252	UniProtKB	Transmembrane	432	452	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99252	UniProtKB	Transmembrane	471	491	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99252	UniProtKB	Transmembrane	546	566	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99252	UniProtKB	Transmembrane	587	607	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99252	UniProtKB	Compositional bias	199	203	.	.	.	Note=Poly-Ser	
+Q99252	UniProtKB	Modified residue	291	291	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q99252	UniProtKB	Modified residue	338	338	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q3E705 1 233
+Q3E705	UniProtKB	Chain	1	233	.	.	.	ID=PRO_0000245390;Note=rRNA-processing protein EFG1	
+Q3E705	UniProtKB	Coiled coil	26	109	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E705	UniProtKB	Sequence conflict	152	152	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53168 1 247
+P53168	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53168	UniProtKB	Chain	2	247	.	.	.	ID=PRO_0000215595;Note=DASH complex subunit DUO1	
+P53168	UniProtKB	Coiled coil	152	180	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53168	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53168	UniProtKB	Mutagenesis	67	67	.	.	.	Note=In DUO1-1%3B produces abnormal spindles resulting in growth arrest at 37 degrees Celsius%3B when associated with V-157. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9817759;Dbxref=PMID:9817759	
+P53168	UniProtKB	Mutagenesis	117	117	.	.	.	Note=In DUO1-2%3B produces abnormal spindles resulting in growth arrest at 37 degrees Celsius%3B when associated with I-124. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9817759;Dbxref=PMID:9817759	
+P53168	UniProtKB	Mutagenesis	124	124	.	.	.	Note=In DUO1-2%3B produces abnormal spindles resulting in growth arrest at 37 degrees Celsius%3B when associated with T-117. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9817759;Dbxref=PMID:9817759	
+P53168	UniProtKB	Mutagenesis	157	157	.	.	.	Note=In DUO1-1%3B produces abnormal spindles resulting in growth arrest at 37 degrees Celsius%3B when associated with K-67. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9817759;Dbxref=PMID:9817759	
+##sequence-region Q06053 1 668
+Q06053	UniProtKB	Chain	1	668	.	.	.	ID=PRO_0000162155;Note=tRNA-dihydrouridine(47) synthase [NAD(P)(+)]	
+Q06053	UniProtKB	Zinc finger	92	122	.	.	.	Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q06053	UniProtKB	Zinc finger	134	164	.	.	.	Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q06053	UniProtKB	Nucleotide binding	299	301	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06053	UniProtKB	Nucleotide binding	509	511	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06053	UniProtKB	Nucleotide binding	534	535	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06053	UniProtKB	Active site	386	386	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06053	UniProtKB	Binding site	354	354	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06053	UniProtKB	Binding site	426	426	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+Q06053	UniProtKB	Binding site	457	457	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+##sequence-region P36041 1 632
+P36041	UniProtKB	Chain	1	632	.	.	.	ID=PRO_0000203133;Note=Protein EAP1	
+P36041	UniProtKB	Nucleotide binding	440	447	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36041	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36041	UniProtKB	Modified residue	281	281	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36041	UniProtKB	Modified residue	282	282	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P36041	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P36041	UniProtKB	Modified residue	344	344	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36041	UniProtKB	Modified residue	387	387	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36041	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Abolishes interaction with eIF4E%3B when associated with A-114. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10848587,ECO:0000269|PubMed:15848184;Dbxref=PMID:10848587,PMID:15848184	
+P36041	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Abolishes interaction with eIF4E%3B when associated with A-109. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15848184;Dbxref=PMID:15848184	
+##sequence-region P38195 1 257
+P38195	UniProtKB	Chain	1	257	.	.	.	ID=PRO_0000086913;Note=Protein ECM13	
+P38195	UniProtKB	Compositional bias	107	147	.	.	.	Note=Asp-rich	
+##sequence-region P35195 1 104
+P35195	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000147621;Note=UPF0045 protein ECM15	
+P35195	UniProtKB	Beta strand	5	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ	
+P35195	UniProtKB	Helix	23	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ	
+P35195	UniProtKB	Beta strand	36	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ	
+P35195	UniProtKB	Beta strand	46	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ	
+P35195	UniProtKB	Helix	53	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ	
+P35195	UniProtKB	Beta strand	74	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ	
+P35195	UniProtKB	Helix	91	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ	
+##sequence-region P47144 1 725
+P47144	UniProtKB	Chain	1	725	.	.	.	ID=PRO_0000209503;Note=Protein ECM27	
+P47144	UniProtKB	Transmembrane	21	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Transmembrane	178	198	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Transmembrane	397	417	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Transmembrane	439	459	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Transmembrane	470	490	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Transmembrane	526	546	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Transmembrane	559	579	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Transmembrane	621	641	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Transmembrane	668	688	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Transmembrane	704	724	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47144	UniProtKB	Sequence conflict	219	219	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02202 1 377
+Q02202	UniProtKB	Chain	1	377	.	.	.	ID=PRO_0000086925;Note=Protein ECM9	
+##sequence-region P38073 1 919
+P38073	UniProtKB	Chain	1	919	.	.	.	ID=PRO_0000114991;Note=Transcriptional regulatory protein EDS1	
+P38073	UniProtKB	DNA binding	56	85	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P42835 1 1041
+P42835	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Chain	21	1020	.	.	.	ID=PRO_0000021159;Note=Protein EGT2	
+P42835	UniProtKB	Propeptide	1021	1041	.	.	.	ID=PRO_0000372451;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Repeat	457	492	.	.	.	Note=1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P42835	UniProtKB	Repeat	577	606	.	.	.	Note=2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P42835	UniProtKB	Repeat	613	647	.	.	.	Note=3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P42835	UniProtKB	Repeat	716	745	.	.	.	Note=4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P42835	UniProtKB	Repeat	773	802	.	.	.	Note=5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P42835	UniProtKB	Repeat	811	840	.	.	.	Note=6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P42835	UniProtKB	Repeat	849	886	.	.	.	Note=7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P42835	UniProtKB	Repeat	887	924	.	.	.	Note=8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P42835	UniProtKB	Repeat	925	962	.	.	.	Note=9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P42835	UniProtKB	Region	457	962	.	.	.	Note=9 X approximate repeats	
+P42835	UniProtKB	Compositional bias	301	764	.	.	.	Note=Ser-rich	
+P42835	UniProtKB	Compositional bias	403	1003	.	.	.	Note=Thr-rich	
+P42835	UniProtKB	Lipidation	1020	1020	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	65	65	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	161	161	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	175	175	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	249	249	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	332	332	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	401	401	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	435	435	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	465	465	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	485	485	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	506	506	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	526	526	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	544	544	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	556	556	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	635	635	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	636	636	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	657	657	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	709	709	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Glycosylation	756	756	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42835	UniProtKB	Sequence conflict	577	577	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P42835	UniProtKB	Sequence conflict	577	577	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P42835	UniProtKB	Sequence conflict	577	577	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47120 1 325
+P47120	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03101,ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P47120	UniProtKB	Chain	2	325	.	.	.	ID=PRO_0000203100;Note=Deoxyhypusine hydroxylase	
+P47120	UniProtKB	Repeat	77	103	.	.	.	Note=HEAT-like PBS-type 1	
+P47120	UniProtKB	Repeat	110	136	.	.	.	Note=HEAT-like PBS-type 2	
+P47120	UniProtKB	Repeat	202	231	.	.	.	Note=HEAT-like PBS-type 3	
+P47120	UniProtKB	Repeat	235	261	.	.	.	Note=HEAT-like PBS-type 4	
+P47120	UniProtKB	Repeat	268	294	.	.	.	Note=HEAT-like PBS-type 5	
+P47120	UniProtKB	Metal binding	79	79	.	.	.	Note=Iron 1	
+P47120	UniProtKB	Metal binding	80	80	.	.	.	Note=Iron 1	
+P47120	UniProtKB	Metal binding	112	112	.	.	.	Note=Iron 1	
+P47120	UniProtKB	Metal binding	113	113	.	.	.	Note=Iron 1	
+P47120	UniProtKB	Metal binding	237	237	.	.	.	Note=Iron 2	
+P47120	UniProtKB	Metal binding	238	238	.	.	.	Note=Iron 2	
+P47120	UniProtKB	Metal binding	270	270	.	.	.	Note=Iron 2	
+P47120	UniProtKB	Metal binding	271	271	.	.	.	Note=Iron 2	
+P47120	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03101,ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P47120	UniProtKB	Modified residue	126	126	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47120	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47120	UniProtKB	Modified residue	281	281	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47120	UniProtKB	Mutagenesis	79	79	.	.	.	Note=Abolishes both iron-binding and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
+P47120	UniProtKB	Mutagenesis	80	80	.	.	.	Note=Abolishes enzyme activity and impairs iron-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
+P47120	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Abolishes both iron-binding and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
+P47120	UniProtKB	Mutagenesis	113	113	.	.	.	Note=Abolishes iron-binding%2C substrate-binding%2C and enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
+P47120	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Abolishes substrate-binding and enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
+P47120	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Reduces enzyme activity by 97%25. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
+P47120	UniProtKB	Mutagenesis	237	237	.	.	.	Note=Abolishes both iron-binding and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
+P47120	UniProtKB	Mutagenesis	238	238	.	.	.	Note=Abolishes substrate-binding%2C enzyme activity%2C and impairs iron-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
+P47120	UniProtKB	Mutagenesis	270	270	.	.	.	Note=Abolishes iron-binding%2C substrate-binding%2C and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
+P47120	UniProtKB	Mutagenesis	271	271	.	.	.	Note=Abolishes iron-binding%2C substrate-binding%2C and enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
+P47120	UniProtKB	Mutagenesis	274	274	.	.	.	Note=Abolishes substrate-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996	
+##sequence-region P27344 1 201
+P27344	UniProtKB	Chain	1	201	.	.	.	ID=PRO_0000208350;Note=DNA polymerase epsilon subunit C	
+P27344	UniProtKB	Compositional bias	120	154	.	.	.	Note=Asp/Glu-rich (acidic)	
+P27344	UniProtKB	Modified residue	186	186	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P27344	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27344	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27344	UniProtKB	Sequence conflict	196	196	.	.	.	Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40487 1 425
+P40487	UniProtKB	Chain	1	425	.	.	.	ID=PRO_0000083381;Note=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1	
+P40487	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q12429 1 685
+Q12429	UniProtKB	Chain	1	685	.	.	.	ID=PRO_0000262869;Note=Diphthine--ammonia ligase	
+Q12429	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Completely inactivates the enzyme. G->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23468660;Dbxref=PMID:23468660	
+Q12429	UniProtKB	Mutagenesis	220	220	.	.	.	Note=Completely inactivates the enzyme. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23468660;Dbxref=PMID:23468660	
+##sequence-region Q08225 1 711
+Q08225	UniProtKB	Chain	1	711	.	.	.	ID=PRO_0000078243;Note=Probable dipeptidyl peptidase 3	
+Q08225	UniProtKB	Active site	461	461	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O55096	
+Q08225	UniProtKB	Metal binding	460	460	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NY33	
+Q08225	UniProtKB	Metal binding	465	465	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NY33	
+Q08225	UniProtKB	Metal binding	517	517	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NY33	
+Q08225	UniProtKB	Beta strand	12	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Turn	18	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	27	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	44	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	55	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Turn	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	78	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Turn	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	115	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	133	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	154	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Turn	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Turn	167	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	184	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	191	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	202	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	212	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	221	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Turn	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	242	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	252	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	261	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	281	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	299	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	316	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	327	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	336	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	346	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	359	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	366	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	370	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	384	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	397	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	405	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	414	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	419	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Turn	439	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	442	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	472	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	477	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	482	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	491	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	504	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	509	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	512	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	531	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	542	562	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	563	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Turn	569	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	577	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	592	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	598	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	610	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	616	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Turn	619	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	622	639	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	643	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	658	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	664	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	676	678	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	681	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Beta strand	690	693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+Q08225	UniProtKB	Helix	699	710	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK	
+##sequence-region P47013 1 409
+P47013	UniProtKB	Chain	1	409	.	.	.	ID=PRO_0000203037;Note=Dihydrosphingosine 1-phosphate phosphatase LCB3	
+P47013	UniProtKB	Topological domain	1	86	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P47013	UniProtKB	Transmembrane	87	107	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47013	UniProtKB	Topological domain	108	112	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P47013	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47013	UniProtKB	Topological domain	134	182	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P47013	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47013	UniProtKB	Topological domain	204	207	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P47013	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47013	UniProtKB	Topological domain	229	245	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P47013	UniProtKB	Transmembrane	246	266	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47013	UniProtKB	Topological domain	267	276	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P47013	UniProtKB	Transmembrane	277	297	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47013	UniProtKB	Topological domain	298	315	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P47013	UniProtKB	Transmembrane	316	336	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47013	UniProtKB	Topological domain	337	384	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P47013	UniProtKB	Transmembrane	385	405	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47013	UniProtKB	Topological domain	406	409	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P47013	UniProtKB	Region	128	136	.	.	.	Note=Phosphatase sequence motif I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47013	UniProtKB	Region	157	160	.	.	.	Note=Phosphatase sequence motif II;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47013	UniProtKB	Region	203	214	.	.	.	Note=Phosphatase sequence motif III;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47013	UniProtKB	Active site	160	160	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924	
+P47013	UniProtKB	Active site	210	210	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924	
+P47013	UniProtKB	Site	214	214	.	.	.	Note=Stabilizes the active site histidine for nucleophilic attack;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924	
+P47013	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47013	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47013	UniProtKB	Mutagenesis	128	128	.	.	.	Note=Impairs dihydrosphingosine 1-phosphate phosphatase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12786943;Dbxref=PMID:12786943	
+P47013	UniProtKB	Mutagenesis	160	160	.	.	.	Note=Impairs dihydrosphingosine 1-phosphate phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12786943;Dbxref=PMID:12786943	
+P47013	UniProtKB	Mutagenesis	210	210	.	.	.	Note=Impairs dihydrosphingosine 1-phosphate phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12786943;Dbxref=PMID:12786943	
+##sequence-region P38844 1 325
+P38844	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38844	UniProtKB	Chain	22	308	.	.	.	ID=PRO_0000014328;Note=Protein DSE2	
+P38844	UniProtKB	Propeptide	309	325	.	.	.	ID=PRO_0000285355;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38844	UniProtKB	Compositional bias	72	281	.	.	.	Note=Ser-rich	
+P38844	UniProtKB	Lipidation	308	308	.	.	.	Note=GPI-anchor amidated aspartate;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39112 1 969
+P39112	UniProtKB	Transit peptide	1	41	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12426313;Dbxref=PMID:12426313	
+P39112	UniProtKB	Chain	42	969	.	.	.	ID=PRO_0000030820;Note=Exoribonuclease II%2C mitochondrial	
+P39112	UniProtKB	Sequence conflict	222	222	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39112	UniProtKB	Sequence conflict	870	870	.	.	.	Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38125 1 572
+P38125	UniProtKB	Chain	1	572	.	.	.	ID=PRO_0000173438;Note=Dityrosine transporter 1	
+P38125	UniProtKB	Topological domain	1	110	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	132	149	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	171	184	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	206	207	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	229	240	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	262	267	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	268	288	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	289	366	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	367	387	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	388	398	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	399	419	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	420	446	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	447	469	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	470	472	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	473	493	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	494	520	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	521	541	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	542	542	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Transmembrane	543	563	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Topological domain	564	572	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38125	UniProtKB	Region	548	572	.	.	.	Note=Required for the localization to the prospore membrane	
+##sequence-region P43616 1 481
+P43616	UniProtKB	Chain	1	481	.	.	.	ID=PRO_0000185275;Note=Cys-Gly metallodipeptidase DUG1	
+P43616	UniProtKB	Active site	104	104	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43616	UniProtKB	Active site	171	171	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43616	UniProtKB	Metal binding	102	102	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43616	UniProtKB	Metal binding	137	137	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43616	UniProtKB	Metal binding	137	137	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43616	UniProtKB	Metal binding	172	172	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43616	UniProtKB	Metal binding	200	200	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43616	UniProtKB	Metal binding	450	450	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43616	UniProtKB	Modified residue	451	451	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43616	UniProtKB	Helix	5	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	16	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	39	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	59	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	83	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	96	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Turn	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Turn	133	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	139	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	161	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Turn	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	178	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Turn	186	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	195	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	204	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	210	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	217	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Turn	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Turn	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	244	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	267	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	276	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Turn	282	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	289	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	306	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	318	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	330	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	339	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	355	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	376	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	397	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	415	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	426	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	437	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	451	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Beta strand	455	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+P43616	UniProtKB	Helix	458	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P	
+##sequence-region P32528 1 1835
+P32528	UniProtKB	Chain	1	1835	.	.	.	ID=PRO_0000146832;Note=Urea amidolyase	
+P32528	UniProtKB	Domain	632	1075	.	.	.	Note=Biotin carboxylation	
+P32528	UniProtKB	Domain	751	948	.	.	.	Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P32528	UniProtKB	Domain	1754	1832	.	.	.	Note=Biotinyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066	
+P32528	UniProtKB	Nucleotide binding	122	129	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P32528	UniProtKB	Binding site	747	747	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32528	UniProtKB	Binding site	830	830	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32528	UniProtKB	Binding site	865	865	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32528	UniProtKB	Modified residue	803	803	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32528	UniProtKB	Modified residue	1798	1798	.	.	.	Note=N6-biotinyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066	
+P32528	UniProtKB	Sequence conflict	96	96	.	.	.	Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32528	UniProtKB	Sequence conflict	256	258	.	.	.	Note=LKK->KKN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32528	UniProtKB	Sequence conflict	459	459	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32528	UniProtKB	Sequence conflict	830	830	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32528	UniProtKB	Sequence conflict	1395	1395	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33317 1 147
+P33317	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000182937;Note=Deoxyuridine 5'-triphosphate nucleotidohydrolase	
+P33317	UniProtKB	Region	68	70	.	.	.	Note=Substrate binding	
+P33317	UniProtKB	Region	82	85	.	.	.	Note=Substrate binding	
+P33317	UniProtKB	Region	142	143	.	.	.	Note=Substrate binding	
+P33317	UniProtKB	Binding site	93	93	.	.	.	Note=Substrate%3B via amide nitrogen and carbonyl oxygen	
+P33317	UniProtKB	Binding site	137	137	.	.	.	Note=Substrate	
+P33317	UniProtKB	Sequence conflict	10	10	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33317	UniProtKB	Beta strand	8	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	22	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	29	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	45	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	53	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	61	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Helix	69	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	93	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	111	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48	
+P33317	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4F	
+##sequence-region P36022 1 4092
+P36022	UniProtKB	Chain	1	4092	.	.	.	ID=PRO_0000114643;Note=Dynein heavy chain%2C cytoplasmic	
+P36022	UniProtKB	Nucleotide binding	1796	1803	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Nucleotide binding	2074	2081	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Nucleotide binding	2418	2425	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Nucleotide binding	2760	2767	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Region	1	1757	.	.	.	Note=Stem;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36022	UniProtKB	Region	1758	1979	.	.	.	Note=AAA 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36022	UniProtKB	Region	2036	2273	.	.	.	Note=AAA 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36022	UniProtKB	Region	2379	2628	.	.	.	Note=AAA 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36022	UniProtKB	Region	2722	2984	.	.	.	Note=AAA 4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36022	UniProtKB	Region	2993	3300	.	.	.	Note=Stalk;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36022	UniProtKB	Region	3370	3599	.	.	.	Note=AAA 5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36022	UniProtKB	Region	3760	3970	.	.	.	Note=AAA 6;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36022	UniProtKB	Coiled coil	154	175	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Coiled coil	486	508	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Coiled coil	542	566	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Coiled coil	932	959	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Coiled coil	1042	1063	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Coiled coil	1681	1705	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Coiled coil	2993	3092	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Coiled coil	3242	3300	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Coiled coil	3532	3608	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36022	UniProtKB	Sequence conflict	589	589	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36022	UniProtKB	Sequence conflict	601	601	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36022	UniProtKB	Sequence conflict	1364	1364	.	.	.	Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36022	UniProtKB	Sequence conflict	2118	2119	.	.	.	Note=ML->IV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36022	UniProtKB	Helix	1366	1378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1384	1387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1389	1391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1393	1396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1399	1414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	1420	1424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1425	1458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1464	1468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1470	1491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1497	1501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1505	1533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1537	1540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1542	1550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	1551	1554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1556	1558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1559	1565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1567	1574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1576	1584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1589	1597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1604	1631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1636	1640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1645	1666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1669	1688	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1692	1717	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1721	1730	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1733	1736	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1743	1745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1747	1751	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1754	1757	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1773	1787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1791	1795	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1802	1811	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	1812	1814	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1818	1821	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1828	1841	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1844	1849	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1855	1874	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1877	1880	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1882	1887	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1893	1898	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1902	1905	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1910	1913	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	1916	1920	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1926	1938	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1942	1959	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1970	1986	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	1991	2001	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2003	2005	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2008	2021	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2029	2032	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2033	2045	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2051	2066	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2068	2073	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2080	2094	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2098	2104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2106	2108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2111	2114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2120	2122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2130	2138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2146	2154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2160	2164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2167	2170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2175	2177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2179	2181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2183	2185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2188	2197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2204	2209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2210	2214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2222	2238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2243	2256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2259	2270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2280	2297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2300	2302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2303	2305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AI6	
+P36022	UniProtKB	Helix	2307	2327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2333	2345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2348	2350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2363	2365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2383	2385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2395	2410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2413	2417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2424	2433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2439	2444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2451	2461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2465	2467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2468	2470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2471	2480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2482	2487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2488	2490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2496	2498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2501	2511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2513	2516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2518	2520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2523	2535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2548	2551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2554	2558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2563	2565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2566	2578	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2583	2588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2589	2606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2609	2611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2619	2634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2641	2656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2657	2659	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2664	2680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2691	2693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2696	2703	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2709	2726	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2736	2750	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2751	2759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2761	2763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2766	2776	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2780	2782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2792	2808	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2813	2818	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2819	2821	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2825	2836	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2837	2839	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	2841	2843	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2847	2863	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2870	2884	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2886	2892	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2897	2904	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2906	2911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2912	2916	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2922	2932	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2961	2979	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	2983	2985	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	2991	3027	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3300	3304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	3305	3307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3308	3333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	3334	3336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AI6	
+P36022	UniProtKB	Helix	3339	3355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3366	3370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3373	3382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3388	3399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3402	3408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3414	3422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3423	3425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3426	3429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3436	3445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3449	3453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3455	3457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3463	3466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3477	3480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3482	3487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3493	3498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3507	3512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3513	3517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3523	3537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3539	3572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3573	3576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3580	3638	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3646	3655	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3670	3686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3692	3710	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3713	3726	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3727	3729	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	3738	3740	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3743	3752	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3756	3765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3774	3780	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3784	3790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3797	3805	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	3806	3808	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3813	3815	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3819	3835	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3839	3842	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3844	3847	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3848	3853	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3855	3861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	3865	3867	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3868	3870	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AI6	
+P36022	UniProtKB	Beta strand	3873	3876	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3879	3881	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3886	3891	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3892	3897	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3903	3913	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3914	3917	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3923	3944	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	3946	3949	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	3950	3952	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3958	3974	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3980	3982	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	3983	3991	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Turn	3995	3997	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	4001	4014	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	4018	4020	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	4023	4026	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	4038	4051	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	4058	4061	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Beta strand	4063	4065	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+P36022	UniProtKB	Helix	4067	4090	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG	
+##sequence-region P53759 1 423
+P53759	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53759	UniProtKB	Chain	2	423	.	.	.	ID=PRO_0000162153;Note=tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]	
+P53759	UniProtKB	Nucleotide binding	35	37	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53759	UniProtKB	Nucleotide binding	223	225	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53759	UniProtKB	Nucleotide binding	247	248	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53759	UniProtKB	Active site	121	121	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53759	UniProtKB	Binding site	92	92	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53759	UniProtKB	Binding site	160	160	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53759	UniProtKB	Binding site	188	188	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7	
+P53759	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q06349 1 442
+Q06349	UniProtKB	Chain	1	442	.	.	.	ID=PRO_0000253847;Note=Decapping and exoribonuclease protein 1	
+Q06349	UniProtKB	Compositional bias	41	46	.	.	.	Note=Poly-Ser	
+Q06349	UniProtKB	Metal binding	255	255	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06349	UniProtKB	Metal binding	295	295	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06349	UniProtKB	Metal binding	306	306	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53063 1 387
+P53063	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10805743;Dbxref=PMID:10805743	
+P53063	UniProtKB	Chain	2	387	.	.	.	ID=PRO_0000202708;Note=Decapping nuclease RAI1	
+P53063	UniProtKB	Region	273	387	.	.	.	Note=Interaction with RAT1	
+P53063	UniProtKB	Metal binding	172	172	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53063	UniProtKB	Metal binding	223	223	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53063	UniProtKB	Metal binding	241	241	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53063	UniProtKB	Metal binding	242	242	.	.	.	Note=Divalent metal cation%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53063	UniProtKB	Binding site	105	105	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53063	UniProtKB	Binding site	221	221	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53063	UniProtKB	Binding site	267	267	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53063	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53063	UniProtKB	Mutagenesis	221	221	.	.	.	Note=Abolishes the decapping activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20802481;Dbxref=PMID:20802481	
+P53063	UniProtKB	Mutagenesis	223	223	.	.	.	Note=Abolishes the decapping activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20802481;Dbxref=PMID:20802481	
+P53063	UniProtKB	Sequence conflict	8	8	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06337 1 982
+Q06337	UniProtKB	Chain	1	982	.	.	.	ID=PRO_0000065825;Note=Chromatin modification-related protein EAF1	
+Q06337	UniProtKB	Domain	346	425	.	.	.	Note=HSA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00549	
+Q06337	UniProtKB	Domain	642	704	.	.	.	Note=Myb-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133	
+Q06337	UniProtKB	Compositional bias	825	942	.	.	.	Note=Gln-rich	
+Q06337	UniProtKB	Modified residue	841	841	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06337	UniProtKB	Modified residue	971	971	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P39995 1 279
+P39995	UniProtKB	Chain	1	279	.	.	.	ID=PRO_0000086892;Note=Chromatin modification-related protein EAF5	
+##sequence-region P53911 1 425
+P53911	UniProtKB	Chain	1	425	.	.	.	ID=PRO_0000215882;Note=Chromatin modification-related protein EAF7	
+P53911	UniProtKB	Coiled coil	209	310	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53911	UniProtKB	Modified residue	200	200	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53911	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q03212 1 550
+Q03212	UniProtKB	Chain	1	550	.	.	.	ID=PRO_0000203316;Note=Protein EAR1	
+Q03212	UniProtKB	Topological domain	1	45	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03212	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03212	UniProtKB	Topological domain	67	550	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03212	UniProtKB	Domain	172	375	.	.	.	Note=B30.2/SPRY;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00548	
+Q03212	UniProtKB	Modified residue	519	519	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03212	UniProtKB	Modified residue	538	538	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03212	UniProtKB	Glycosylation	110	110	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03212	UniProtKB	Glycosylation	203	203	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03212	UniProtKB	Glycosylation	210	210	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03212	UniProtKB	Glycosylation	256	256	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03212	UniProtKB	Glycosylation	295	295	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05871 1 280
+Q05871	UniProtKB	Chain	1	280	.	.	.	ID=PRO_0000109263;Note=3%2C2-trans-enoyl-CoA isomerase	
+Q05871	UniProtKB	Region	68	72	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4ZDB,ECO:0000244|PDB:4ZDC,ECO:0000269|PubMed:26527136;Dbxref=PMID:26527136	
+Q05871	UniProtKB	Motif	278	280	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05871	UniProtKB	Active site	158	158	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26527136;Dbxref=PMID:26527136	
+Q05871	UniProtKB	Binding site	126	126	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4ZDC,ECO:0000269|PubMed:26527136;Dbxref=PMID:26527136	
+Q05871	UniProtKB	Mutagenesis	158	158	.	.	.	Note=Loss of activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11399063;Dbxref=PMID:11399063	
+Q05871	UniProtKB	Beta strand	11	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Beta strand	19	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	35	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Beta strand	56	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Beta strand	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Turn	77	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K39	
+Q05871	UniProtKB	Beta strand	82	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDB	
+Q05871	UniProtKB	Helix	89	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	98	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Beta strand	113	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	125	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Beta strand	134	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Beta strand	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	161	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	171	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	186	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Beta strand	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	206	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Turn	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	226	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Turn	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Helix	241	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+Q05871	UniProtKB	Turn	263	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF	
+##sequence-region P38167 1 1117
+P38167	UniProtKB	Chain	1	1117	.	.	.	ID=PRO_0000086917;Note=Protein ECM21	
+P38167	UniProtKB	Compositional bias	490	511	.	.	.	Note=Ser-rich	
+P38167	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38167	UniProtKB	Modified residue	115	115	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38167	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P38167	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38167	UniProtKB	Modified residue	527	527	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38167	UniProtKB	Modified residue	550	550	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38167	UniProtKB	Modified residue	775	775	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38167	UniProtKB	Modified residue	1035	1035	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38167	UniProtKB	Cross-link	191	191	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38167	UniProtKB	Cross-link	577	577	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12872131,ECO:0000269|PubMed:14557538;Dbxref=PMID:12872131,PMID:14557538	
+P38167	UniProtKB	Cross-link	651	651	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P38167	UniProtKB	Cross-link	712	712	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P38167	UniProtKB	Cross-link	794	794	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38167	UniProtKB	Cross-link	807	807	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P38167	UniProtKB	Cross-link	1024	1024	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P38167	UniProtKB	Sequence conflict	964	967	.	.	.	Note=PSGY->HPDT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38167	UniProtKB	Sequence conflict	964	967	.	.	.	Note=PSGY->HPDT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38737 1 1868
+P38737	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38737	UniProtKB	Chain	2	1868	.	.	.	ID=PRO_0000212558;Note=Proteasome component ECM29	
+P38737	UniProtKB	Repeat	32	69	.	.	.	Note=HEAT 1	
+P38737	UniProtKB	Repeat	116	153	.	.	.	Note=HEAT 2	
+P38737	UniProtKB	Repeat	256	292	.	.	.	Note=HEAT 3	
+P38737	UniProtKB	Repeat	313	351	.	.	.	Note=HEAT 4	
+P38737	UniProtKB	Repeat	384	422	.	.	.	Note=HEAT 5	
+P38737	UniProtKB	Repeat	439	476	.	.	.	Note=HEAT 6	
+P38737	UniProtKB	Repeat	590	627	.	.	.	Note=HEAT 7	
+P38737	UniProtKB	Repeat	707	745	.	.	.	Note=HEAT 8	
+P38737	UniProtKB	Repeat	748	780	.	.	.	Note=HEAT 9	
+P38737	UniProtKB	Repeat	781	818	.	.	.	Note=HEAT 10	
+P38737	UniProtKB	Repeat	846	885	.	.	.	Note=HEAT 11	
+P38737	UniProtKB	Repeat	945	982	.	.	.	Note=HEAT 12	
+P38737	UniProtKB	Repeat	988	1025	.	.	.	Note=HEAT 13	
+P38737	UniProtKB	Repeat	1030	1067	.	.	.	Note=HEAT 14	
+P38737	UniProtKB	Repeat	1137	1174	.	.	.	Note=HEAT 15	
+P38737	UniProtKB	Repeat	1178	1215	.	.	.	Note=HEAT 16	
+P38737	UniProtKB	Repeat	1272	1311	.	.	.	Note=HEAT 17	
+P38737	UniProtKB	Repeat	1361	1398	.	.	.	Note=HEAT 18	
+P38737	UniProtKB	Repeat	1422	1459	.	.	.	Note=HEAT 19	
+P38737	UniProtKB	Repeat	1503	1540	.	.	.	Note=HEAT 20	
+P38737	UniProtKB	Repeat	1544	1581	.	.	.	Note=HEAT 21	
+P38737	UniProtKB	Repeat	1649	1687	.	.	.	Note=HEAT 22	
+P38737	UniProtKB	Repeat	1746	1785	.	.	.	Note=HEAT 23	
+P38737	UniProtKB	Repeat	1830	1867	.	.	.	Note=HEAT 24	
+P38737	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38737	UniProtKB	Modified residue	1692	1692	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38246 1 354
+P38246	UniProtKB	Chain	1	354	.	.	.	ID=PRO_0000086924;Note=Protein ECM8	
+##sequence-region P38732 1 585
+P38732	UniProtKB	Chain	1	585	.	.	.	ID=PRO_0000202879;Note=Protein-lysine N-methyltransferase EFM1	
+P38732	UniProtKB	Domain	23	281	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+P38732	UniProtKB	Binding site	280	280	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+##sequence-region P53235 1 642
+P53235	UniProtKB	Chain	1	642	.	.	.	ID=PRO_0000202800;Note=Eukaryotic translation initiation factor 2A	
+P53235	UniProtKB	Repeat	69	115	.	.	.	Note=WD 1	
+P53235	UniProtKB	Repeat	186	224	.	.	.	Note=WD 2	
+P53235	UniProtKB	Repeat	289	331	.	.	.	Note=WD 3	
+P53235	UniProtKB	Repeat	374	419	.	.	.	Note=WD 4	
+P53235	UniProtKB	Modified residue	564	564	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53235	UniProtKB	Modified residue	567	567	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53235	UniProtKB	Modified residue	572	572	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53235	UniProtKB	Natural variant	145	145	.	.	.	Note=In strain: SK1. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P53235	UniProtKB	Natural variant	165	165	.	.	.	Note=In strain: SK1. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P53235	UniProtKB	Natural variant	569	569	.	.	.	Note=In strain: SK1. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+##sequence-region P32497 1 812
+P32497	UniProtKB	Chain	1	812	.	.	.	ID=PRO_0000123530;Note=Eukaryotic translation initiation factor 3 subunit C	
+P32497	UniProtKB	Domain	650	780	.	.	.	Note=PCI;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03002	
+P32497	UniProtKB	Compositional bias	15	147	.	.	.	Note=Asp/Glu-rich (acidic)	
+P32497	UniProtKB	Compositional bias	15	36	.	.	.	Note=Ser-rich	
+P32497	UniProtKB	Modified residue	98	98	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32497	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32497	UniProtKB	Modified residue	103	103	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32497	UniProtKB	Sequence conflict	111	111	.	.	.	Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32497	UniProtKB	Sequence conflict	583	583	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32497	UniProtKB	Sequence conflict	641	641	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32497	UniProtKB	Sequence conflict	643	643	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32497	UniProtKB	Helix	252	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Beta strand	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	272	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	289	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Turn	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Beta strand	310	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	315	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	338	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Turn	342	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Turn	350	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Turn	363	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	368	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	392	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	422	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Turn	439	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	445	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	469	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	478	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Turn	490	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	496	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	516	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	530	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	538	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	560	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	576	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	585	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	595	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	608	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	614	637	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	652	660	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	671	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	687	695	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	698	702	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	706	729	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Turn	730	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Beta strand	733	737	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	738	745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	749	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Beta strand	768	770	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Turn	771	774	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Beta strand	775	777	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+P32497	UniProtKB	Helix	784	793	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C	
+##sequence-region Q12050 1 791
+Q12050	UniProtKB	Chain	1	791	.	.	.	ID=PRO_0000086954;Note=Telomere length regulation protein ELG1	
+Q12050	UniProtKB	Compositional bias	86	91	.	.	.	Note=Poly-Asp	
+Q12050	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P25574 1 760
+P25574	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25574	UniProtKB	Chain	25	760	.	.	.	ID=PRO_0000202547;Note=ER membrane protein complex subunit 1	
+P25574	UniProtKB	Topological domain	25	723	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25574	UniProtKB	Transmembrane	724	744	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25574	UniProtKB	Topological domain	745	760	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25574	UniProtKB	Glycosylation	73	73	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25574	UniProtKB	Glycosylation	106	106	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25574	UniProtKB	Glycosylation	192	192	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25574	UniProtKB	Glycosylation	202	202	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25574	UniProtKB	Glycosylation	420	420	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25574	UniProtKB	Glycosylation	443	443	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25574	UniProtKB	Glycosylation	574	574	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25574	UniProtKB	Glycosylation	578	578	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47133 1 292
+P47133	UniProtKB	Chain	1	292	.	.	.	ID=PRO_0000203107;Note=ER membrane protein complex subunit 2	
+P47133	UniProtKB	Repeat	163	196	.	.	.	Note=TPR	
+P47133	UniProtKB	Sequence conflict	20	20	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53095 1 428
+P53095	UniProtKB	Chain	1	428	.	.	.	ID=PRO_0000202722;Note=D-serine dehydratase	
+P53095	UniProtKB	Sequence conflict	125	125	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53095	UniProtKB	Sequence conflict	125	125	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40077 1 573
+P40077	UniProtKB	Chain	1	573	.	.	.	ID=PRO_0000202647;Note=Protein DSE1	
+P40077	UniProtKB	Repeat	144	185	.	.	.	Note=WD 1	
+P40077	UniProtKB	Repeat	315	351	.	.	.	Note=WD 2	
+P40077	UniProtKB	Repeat	356	395	.	.	.	Note=WD 3	
+P40077	UniProtKB	Repeat	397	448	.	.	.	Note=WD 4	
+P40077	UniProtKB	Cross-link	553	553	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P0CX08 1 502
+P0CX08	UniProtKB	Chain	1	502	.	.	.	ID=PRO_0000170751;Note=Mannitol dehydrogenase DSF1	
+##sequence-region Q04949 1 312
+Q04949	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000203353;Note=Cytoplasmic dynein intermediate light chain DYN3	
+##sequence-region Q12432 1 401
+Q12432	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000088783;Note=Chromatin modification-related protein EAF3	
+Q12432	UniProtKB	Domain	216	399	.	.	.	Note=MRG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00972	
+Q12432	UniProtKB	Compositional bias	148	205	.	.	.	Note=Ser-rich	
+Q12432	UniProtKB	Modified residue	201	201	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12432	UniProtKB	Helix	3	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K3Y	
+Q12432	UniProtKB	Beta strand	13	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F	
+Q12432	UniProtKB	Beta strand	21	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F	
+Q12432	UniProtKB	Turn	33	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F	
+Q12432	UniProtKB	Beta strand	37	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F	
+Q12432	UniProtKB	Beta strand	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K3X	
+Q12432	UniProtKB	Beta strand	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K3Y	
+Q12432	UniProtKB	Turn	69	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F	
+Q12432	UniProtKB	Beta strand	76	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F	
+Q12432	UniProtKB	Helix	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F	
+Q12432	UniProtKB	Beta strand	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F	
+Q12432	UniProtKB	Turn	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F	
+Q12432	UniProtKB	Beta strand	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K3X	
+Q12432	UniProtKB	Helix	102	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F	
+##sequence-region Q03466 1 884
+Q03466	UniProtKB	Chain	1	884	.	.	.	ID=PRO_0000086907;Note=Protein EBS1	
+##sequence-region P32471 1 206
+P32471	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P32471	UniProtKB	Chain	2	206	.	.	.	ID=PRO_0000155042;Note=Elongation factor 1-beta	
+P32471	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P32471	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32471	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32471	UniProtKB	Cross-link	13	13	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32471	UniProtKB	Mutagenesis	120	122	.	.	.	Note=In TEF5-7%3B reduces translation efficiency and enhances translation fidelity. KSI->R	
+P32471	UniProtKB	Mutagenesis	121	121	.	.	.	Note=Reduces translation efficiency and enhances translation fidelity. S->I%2CL%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10409717;Dbxref=PMID:10409717	
+P32471	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Temperature-sensitive. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11106763;Dbxref=PMID:11106763	
+P32471	UniProtKB	Mutagenesis	205	205	.	.	.	Note=Loss of catalytic activity%2C but still binds to eEF1A. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11373622;Dbxref=PMID:11373622	
+P32471	UniProtKB	Sequence conflict	49	49	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32471	UniProtKB	Sequence conflict	57	57	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32471	UniProtKB	Sequence conflict	98	98	.	.	.	Note=L->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32471	UniProtKB	Sequence conflict	168	168	.	.	.	Note=L->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32471	UniProtKB	Beta strand	120	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P32471	UniProtKB	Helix	136	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P32471	UniProtKB	Beta strand	151	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P32471	UniProtKB	Beta strand	165	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P32471	UniProtKB	Turn	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P32471	UniProtKB	Helix	181	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P32471	UniProtKB	Turn	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+P32471	UniProtKB	Beta strand	195	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60	
+##sequence-region P29547 1 415
+P29547	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P29547	UniProtKB	Chain	2	415	.	.	.	ID=PRO_0000208831;Note=Elongation factor 1-gamma 1	
+P29547	UniProtKB	Domain	2	78	.	.	.	Note=GST N-terminal	
+P29547	UniProtKB	Domain	89	215	.	.	.	Note=GST C-terminal	
+P29547	UniProtKB	Domain	254	415	.	.	.	Note=EF-1-gamma C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00519	
+P29547	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P29547	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P29547	UniProtKB	Sequence conflict	191	191	.	.	.	Note=W->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29547	UniProtKB	Beta strand	5	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	12	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	37	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Beta strand	49	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Beta strand	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	63	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	90	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Turn	105	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	109	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	115	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	126	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Beta strand	151	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	160	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	179	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	186	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Turn	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+P29547	UniProtKB	Helix	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY	
+##sequence-region P32324 1 842
+P32324	UniProtKB	Chain	1	842	.	.	.	ID=PRO_0000091024;Note=Elongation factor 2	
+P32324	UniProtKB	Domain	17	346	.	.	.	Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32324	UniProtKB	Nucleotide binding	26	33	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32324	UniProtKB	Nucleotide binding	104	108	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32324	UniProtKB	Nucleotide binding	158	161	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32324	UniProtKB	Modified residue	509	509	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B by EFM3%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25086354;Dbxref=PMID:24517342,PMID:25086354	
+P32324	UniProtKB	Modified residue	509	509	.	.	.	Note=N6%2CN6-dimethyllysine%3B by EFM3%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25086354;Dbxref=PMID:22522802,PMID:24517342,PMID:25086354	
+P32324	UniProtKB	Modified residue	509	509	.	.	.	Note=N6-methyllysine%3B by EFM3%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25086354;Dbxref=PMID:24517342,PMID:25086354	
+P32324	UniProtKB	Modified residue	579	579	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32324	UniProtKB	Modified residue	613	613	.	.	.	Note=N6%2CN6-dimethyllysine%3B by EFM2%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25086354;Dbxref=PMID:24517342,PMID:25086354	
+P32324	UniProtKB	Modified residue	613	613	.	.	.	Note=N6-methyllysine%3B by EFM2%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25086354;Dbxref=PMID:24517342,PMID:25086354	
+P32324	UniProtKB	Modified residue	699	699	.	.	.	Note=Diphthamide;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:721806;Dbxref=PMID:721806	
+P32324	UniProtKB	Modified residue	713	713	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32324	UniProtKB	Modified residue	763	763	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32324	UniProtKB	Cross-link	841	841	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32324	UniProtKB	Mutagenesis	180	180	.	.	.	Note=Causes resistance to fusidic acid and reduces sensitivity to sordarin. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424	
+P32324	UniProtKB	Mutagenesis	187	187	.	.	.	Note=Causes resistance to fusidic acid and reduces sensitivity to sordarin. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424	
+P32324	UniProtKB	Mutagenesis	490	490	.	.	.	Note=Reduces sensitivity to sordarin. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424	
+P32324	UniProtKB	Mutagenesis	521	521	.	.	.	Note=Reduces sensitivity to fusidic acid and sordarin. Y->D%2CN%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424	
+P32324	UniProtKB	Mutagenesis	523	523	.	.	.	Note=Causes resistance to fusidic acid and sordarin. S->F%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424	
+P32324	UniProtKB	Mutagenesis	529	529	.	.	.	Note=Reduces sensitivity to sordarin. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424	
+P32324	UniProtKB	Mutagenesis	559	559	.	.	.	Note=Causes resistance to fusidic acid and sordarin. P->L%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424	
+P32324	UniProtKB	Mutagenesis	562	562	.	.	.	Note=Reduces sensitivity to fusidic acid and causes resistance to sordarin. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424	
+P32324	UniProtKB	Mutagenesis	580	580	.	.	.	Note=Causes impaired ribosomal translocation with an increased rate of -1 programmed ribosomal frameshift read-through during translation. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23001565;Dbxref=PMID:23001565	
+P32324	UniProtKB	Mutagenesis	699	699	.	.	.	Note=Prevents post-translational modification of this residue to diphthamide. Results in a functional protein that is resistant to diphtheria toxin. H->D%2CE%2CL%2CM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8473309;Dbxref=PMID:8473309	
+P32324	UniProtKB	Mutagenesis	701	701	.	.	.	Note=Prevents ADP-ribosylation of the diphthamide by diphtheria toxin. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8466491;Dbxref=PMID:8466491	
+P32324	UniProtKB	Mutagenesis	727	727	.	.	.	Note=Causes resistance to sordarin. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424	
+P32324	UniProtKB	Mutagenesis	774	774	.	.	.	Note=Causes resistance to sordarin. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424	
+P32324	UniProtKB	Mutagenesis	790	790	.	.	.	Note=Causes resistance to fusidic acid and sordarin. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424	
+P32324	UniProtKB	Beta strand	2	4	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E1R	
+P32324	UniProtKB	Helix	6	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	19	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	32	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	44	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E1R	
+P32324	UniProtKB	Beta strand	74	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	83	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	95	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZM9	
+P32324	UniProtKB	Helix	113	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Turn	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	137	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	152	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	160	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	171	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	209	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Turn	214	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	222	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Turn	231	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	237	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	245	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	249	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Turn	252	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	256	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0V	
+P32324	UniProtKB	Turn	264	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0V	
+P32324	UniProtKB	Helix	272	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	278	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	295	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	309	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	316	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	330	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	345	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	357	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	364	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	374	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B82	
+P32324	UniProtKB	Beta strand	379	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	394	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	410	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	420	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	426	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	433	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	441	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	453	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Turn	460	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	465	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	489	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	498	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	501	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	519	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	528	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	535	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	554	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	564	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	575	578	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	580	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZM9	
+P32324	UniProtKB	Beta strand	585	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	595	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	604	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0V	
+P32324	UniProtKB	Beta strand	608	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0V	
+P32324	UniProtKB	Helix	612	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	627	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	633	638	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Turn	639	641	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	642	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	656	672	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Turn	675	677	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	683	692	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	697	699	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	702	719	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	722	735	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	737	739	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	740	748	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Turn	749	751	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	753	758	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	766	773	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	774	776	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	780	787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Turn	788	790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	793	803	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Beta strand	811	813	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIT	
+P32324	UniProtKB	Helix	814	825	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+P32324	UniProtKB	Helix	835	838	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U	
+##sequence-region P47163 1 339
+P47163	UniProtKB	Chain	1	339	.	.	.	ID=PRO_0000203120;Note=Protein-lysine N-methyltransferase EFM3	
+P47163	UniProtKB	Region	174	176	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+P47163	UniProtKB	Binding site	137	137	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+P47163	UniProtKB	Binding site	199	199	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+P47163	UniProtKB	Binding site	233	233	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+P47163	UniProtKB	Binding site	248	248	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+P47163	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47163	UniProtKB	Sequence conflict	118	118	.	.	.	Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53200 1 248
+P53200	UniProtKB	Chain	1	248	.	.	.	ID=PRO_0000202778;Note=Protein-lysine N-methyltransferase EFM5	
+P53200	UniProtKB	Compositional bias	49	52	.	.	.	Note=Poly-Lys	
+##sequence-region Q05874 1 261
+Q05874	UniProtKB	Chain	1	261	.	.	.	ID=PRO_0000096901;Note=Protein N-terminal and lysine N-methyltransferase EFM7	
+Q05874	UniProtKB	Region	90	92	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q5VZV1,ECO:0000255|HAMAP-Rule:MF_03223	
+Q05874	UniProtKB	Binding site	64	64	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q5VZV1,ECO:0000255|HAMAP-Rule:MF_03223	
+Q05874	UniProtKB	Binding site	112	112	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q5VZV1,ECO:0000255|HAMAP-Rule:MF_03223	
+Q05874	UniProtKB	Binding site	144	144	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q5VZV1,ECO:0000255|HAMAP-Rule:MF_03223	
+Q05874	UniProtKB	Binding site	171	171	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q5VZV1,ECO:0000255|HAMAP-Rule:MF_03223	
+##sequence-region P54858 1 310
+P54858	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000079981;Note=Protein DOS2	
+P54858	UniProtKB	Domain	176	228	.	.	.	Note=BSD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00036	
+P54858	UniProtKB	Compositional bias	255	259	.	.	.	Note=Poly-Glu	
+P54858	UniProtKB	Compositional bias	302	308	.	.	.	Note=Poly-Asp	
+##sequence-region P40553 1 215
+P40553	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000135152;Note=Peroxiredoxin DOT5	
+P40553	UniProtKB	Domain	63	211	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P40553	UniProtKB	Active site	107	107	.	.	.	Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730197;Dbxref=PMID:12730197	
+P40553	UniProtKB	Disulfide bond	107	112	.	.	.	Note=Redox-active;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730197;Dbxref=PMID:12730197	
+P40553	UniProtKB	Mutagenesis	107	107	.	.	.	Note=No TPx activity%2C no effect on DOT activity. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10681558,ECO:0000269|PubMed:12730197,ECO:0000269|PubMed:12925864;Dbxref=PMID:10681558,PMID:12730197,PMID:12925864	
+P40553	UniProtKB	Mutagenesis	112	112	.	.	.	Note=No TPx activity%2C no effect on DOT activity. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12730197,ECO:0000269|PubMed:12925864;Dbxref=PMID:12730197,PMID:12925864	
+P40553	UniProtKB	Beta strand	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Helix	84	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Beta strand	92	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Beta strand	100	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Helix	105	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Turn	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Beta strand	126	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Helix	135	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Beta strand	148	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Helix	158	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Beta strand	166	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Beta strand	176	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Beta strand	184	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+P40553	UniProtKB	Helix	194	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V	
+##sequence-region P24482 1 689
+P24482	UniProtKB	Chain	1	689	.	.	.	ID=PRO_0000071573;Note=DNA polymerase epsilon subunit B	
+P24482	UniProtKB	Modified residue	122	122	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P24482	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14747467;Dbxref=PMID:14747467	
+P24482	UniProtKB	Modified residue	613	613	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14747467;Dbxref=PMID:14747467	
+P24482	UniProtKB	Sequence conflict	458	458	.	.	.	Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24482	UniProtKB	Sequence conflict	521	521	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24482	UniProtKB	Sequence conflict	565	565	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24482	UniProtKB	Sequence conflict	584	584	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24482	UniProtKB	Sequence conflict	644	644	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25615 1 582
+P25615	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8265341;Dbxref=PMID:8265341	
+P25615	UniProtKB	Chain	2	582	.	.	.	ID=PRO_0000218789;Note=DNA polymerase IV	
+P25615	UniProtKB	Region	360	369	.	.	.	Note=Involved in ssDNA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25615	UniProtKB	Compositional bias	472	478	.	.	.	Note=Poly-Glu	
+P25615	UniProtKB	Metal binding	367	367	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25615	UniProtKB	Metal binding	369	369	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25615	UniProtKB	Metal binding	502	502	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25615	UniProtKB	Mutagenesis	247	247	.	.	.	Note=Weakened DNA-binding. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10438542;Dbxref=PMID:10438542	
+P25615	UniProtKB	Mutagenesis	248	248	.	.	.	Note=Weakened DNA-binding. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10438542;Dbxref=PMID:10438542	
+P25615	UniProtKB	Mutagenesis	367	367	.	.	.	Note=Loss of nucleotidyl transfer. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10438542;Dbxref=PMID:10438542	
+##sequence-region P39985 1 1022
+P39985	UniProtKB	Chain	1	1022	.	.	.	ID=PRO_0000046472;Note=DNA polymerase V	
+P39985	UniProtKB	Modified residue	789	789	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39985	UniProtKB	Natural variant	625	625	.	.	.	Note=Lethal. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12093911;Dbxref=PMID:12093911	
+##sequence-region P21951 1 2222
+P21951	UniProtKB	Chain	1	2222	.	.	.	ID=PRO_0000046467;Note=DNA polymerase epsilon catalytic subunit A	
+P21951	UniProtKB	Zinc finger	2108	2133	.	.	.	Note=CysA-type	
+P21951	UniProtKB	Motif	2164	2181	.	.	.	Note=CysB motif	
+P21951	UniProtKB	Metal binding	2108	2108	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21951	UniProtKB	Metal binding	2111	2111	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21951	UniProtKB	Metal binding	2130	2130	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21951	UniProtKB	Metal binding	2133	2133	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21951	UniProtKB	Metal binding	2164	2164	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21951	UniProtKB	Metal binding	2167	2167	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21951	UniProtKB	Metal binding	2179	2179	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21951	UniProtKB	Metal binding	2181	2181	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21951	UniProtKB	Mutagenesis	644	644	.	.	.	Note=In POL2-9%3B temperature-sensitive mutant. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1537345;Dbxref=PMID:1537345	
+P21951	UniProtKB	Mutagenesis	710	710	.	.	.	Note=In POL2-18%3B temperature-sensitive mutant. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1537345;Dbxref=PMID:1537345	
+P21951	UniProtKB	Helix	33	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Turn	67	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	72	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	114	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	128	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	138	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	149	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Turn	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	166	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	186	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	196	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Turn	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	235	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	239	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	249	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	263	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	271	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	286	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Turn	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	308	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	318	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Turn	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	328	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PTF	
+P21951	UniProtKB	Beta strand	346	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	355	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	372	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Turn	379	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	383	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	398	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	415	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	422	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	434	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	439	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	456	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	459	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	467	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	489	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	500	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	504	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	512	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	546	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	558	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	564	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	572	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	578	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	604	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	607	609	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	610	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	629	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	634	641	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	644	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	656	658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	659	662	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	664	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	678	689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	694	705	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	708	710	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	720	722	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	723	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	728	747	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	752	766	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	769	797	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Turn	798	800	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	801	803	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	808	832	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	833	835	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	844	868	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	869	875	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	878	884	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	890	895	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	900	904	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	905	918	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	920	928	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Turn	929	932	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	933	939	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	944	955	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	969	972	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	978	984	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Turn	985	987	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	988	992	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	993	1002	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	1003	1007	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	1009	1011	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PTF	
+P21951	UniProtKB	Helix	1012	1031	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Turn	1032	1036	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	1039	1046	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	1048	1051	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	1056	1059	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	1065	1077	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	1079	1082	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	1083	1086	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	1088	1095	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	1097	1099	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PTF	
+P21951	UniProtKB	Helix	1102	1104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Beta strand	1106	1108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	1109	1113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	1116	1127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	1137	1140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	1143	1157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	1159	1164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+P21951	UniProtKB	Helix	1178	1183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O	
+##sequence-region P38213 1 736
+P38213	UniProtKB	Chain	1	736	.	.	.	ID=PRO_0000202467;Note=Protein DSF2	
+P38213	UniProtKB	Sequence conflict	205	205	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38213	UniProtKB	Sequence conflict	327	327	.	.	.	Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53847 1 754
+P53847	UniProtKB	Chain	1	754	.	.	.	ID=PRO_0000203383;Note=Protein transport protein DSL1	
+P53847	UniProtKB	Region	1	200	.	.	.	Note=Interaction with TIP20;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11739780;Dbxref=PMID:11739780	
+P53847	UniProtKB	Region	406	459	.	.	.	Note=Interaction with RET2	
+P53847	UniProtKB	Region	406	440	.	.	.	Note=Interaction with RET1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14504276;Dbxref=PMID:14504276	
+P53847	UniProtKB	Mutagenesis	413	413	.	.	.	Note=Viable and reduced interaction with RET2%2C strong Golgi-ER retrograde transport defect. Loss of interaction with RET2%3B when associated with A-455. Lethal and loss of interactions with RET1 and RET2%3B when associated with A-425. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14504276;Dbxref=PMID:14504276	
+P53847	UniProtKB	Mutagenesis	425	425	.	.	.	Note=Loss of interaction with RET1%3B when associated with A-413. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14504276;Dbxref=PMID:14504276	
+P53847	UniProtKB	Mutagenesis	455	455	.	.	.	Note=Viable and no effect. Lethal and loss of interaction with RET2 and reduced interaction with RET1%3B when associated with A-413. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14504276;Dbxref=PMID:14504276	
+P53847	UniProtKB	Mutagenesis	725	754	.	.	.	Note=In dsl1-22%3B strong Golgi-ER retrograde transport defect. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11493604;Dbxref=PMID:11493604	
+P53847	UniProtKB	Helix	45	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	77	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	102	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Beta strand	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Beta strand	136	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Beta strand	143	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Turn	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Beta strand	152	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	156	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	178	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	186	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	207	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Beta strand	222	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Turn	228	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Beta strand	232	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	246	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	266	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	292	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Beta strand	297	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	302	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	331	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV	
+P53847	UniProtKB	Helix	340	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETU	
+##sequence-region Q02647 1 92
+Q02647	UniProtKB	Chain	1	92	.	.	.	ID=PRO_0000195149;Note=Dynein light chain 1%2C cytoplasmic	
+Q02647	UniProtKB	Beta strand	10	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1	
+Q02647	UniProtKB	Helix	18	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1	
+Q02647	UniProtKB	Helix	38	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1	
+Q02647	UniProtKB	Beta strand	57	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1	
+Q02647	UniProtKB	Beta strand	75	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1	
+Q02647	UniProtKB	Beta strand	84	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1	
+##sequence-region P07807 1 211
+P07807	UniProtKB	Chain	1	211	.	.	.	ID=PRO_0000186378;Note=Dihydrofolate reductase	
+P07807	UniProtKB	Domain	7	210	.	.	.	Note=DHFR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00660	
+P07807	UniProtKB	Nucleotide binding	20	26	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07807	UniProtKB	Nucleotide binding	58	60	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07807	UniProtKB	Nucleotide binding	80	82	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07807	UniProtKB	Nucleotide binding	123	130	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07807	UniProtKB	Region	34	39	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07807	UniProtKB	Binding site	13	13	.	.	.	Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07807	UniProtKB	Binding site	74	74	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07807	UniProtKB	Sequence conflict	27	27	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06673 1 1274
+Q06673	UniProtKB	Chain	1	1274	.	.	.	ID=PRO_0000086919;Note=Protein ECM30	
+Q06673	UniProtKB	Compositional bias	247	253	.	.	.	Note=Poly-Leu	
+Q06673	UniProtKB	Compositional bias	416	419	.	.	.	Note=Poly-Ser	
+Q06673	UniProtKB	Compositional bias	425	428	.	.	.	Note=Poly-Ser	
+Q06673	UniProtKB	Compositional bias	491	498	.	.	.	Note=Poly-Ser	
+Q06673	UniProtKB	Compositional bias	1103	1109	.	.	.	Note=Poly-Ser	
+Q06673	UniProtKB	Compositional bias	1136	1166	.	.	.	Note=Asn-rich	
+Q06673	UniProtKB	Modified residue	635	635	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06673	UniProtKB	Modified residue	1065	1065	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P38728 1 170
+P38728	UniProtKB	Chain	1	170	.	.	.	ID=PRO_0000207532;Note=Protein ECM34	
+P38728	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38728	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38728	UniProtKB	Glycosylation	45	45	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05902 1 660
+Q05902	UniProtKB	Chain	1	469	.	.	.	ID=PRO_0000011078;Note=Glutathione hydrolase heavy chain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05902	UniProtKB	Chain	470	660	.	.	.	ID=PRO_0000011079;Note=Glutathione hydrolase light chain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05902	UniProtKB	Topological domain	1	13	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05902	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05902	UniProtKB	Topological domain	35	660	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05902	UniProtKB	Region	540	541	.	.	.	Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05902	UniProtKB	Region	562	563	.	.	.	Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05902	UniProtKB	Active site	470	470	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05902	UniProtKB	Binding site	177	177	.	.	.	Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05902	UniProtKB	Binding site	488	488	.	.	.	Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05902	UniProtKB	Binding site	490	490	.	.	.	Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05902	UniProtKB	Binding site	509	509	.	.	.	Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05902	UniProtKB	Binding site	512	512	.	.	.	Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05902	UniProtKB	Glycosylation	119	119	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05902	UniProtKB	Glycosylation	191	191	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05902	UniProtKB	Glycosylation	270	270	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05902	UniProtKB	Glycosylation	298	298	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05902	UniProtKB	Glycosylation	454	454	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05902	UniProtKB	Glycosylation	517	517	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05902	UniProtKB	Natural variant	171	171	.	.	.	Note=In strain: YPH499. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12868055;Dbxref=PMID:12868055	
+Q05902	UniProtKB	Natural variant	494	494	.	.	.	Note=In strain: YPH499%3B lack of gamma-glutamyl transferase activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12868055;Dbxref=PMID:12868055	
+##sequence-region P38773 1 246
+P38773	UniProtKB	Chain	1	246	.	.	.	ID=PRO_0000079975;Note=2-deoxyglucose-6-phosphate phosphatase 2	
+P38773	UniProtKB	Active site	12	12	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38773	UniProtKB	Active site	14	14	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38773	UniProtKB	Metal binding	12	12	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38773	UniProtKB	Metal binding	14	14	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38773	UniProtKB	Metal binding	183	183	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04089 1 582
+Q04089	UniProtKB	Chain	1	582	.	.	.	ID=PRO_0000186091;Note=Histone-lysine N-methyltransferase%2C H3 lysine-79 specific	
+Q04089	UniProtKB	Domain	254	568	.	.	.	Note=DOT1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00902	
+Q04089	UniProtKB	Region	158	172	.	.	.	Note=Required for interaction with nucleosomes and DNA	
+Q04089	UniProtKB	Region	372	375	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q04089	UniProtKB	Region	395	404	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q04089	UniProtKB	Region	459	460	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q04089	UniProtKB	Compositional bias	106	169	.	.	.	Note=Lys-rich	
+Q04089	UniProtKB	Binding site	422	422	.	.	.	Note=S-adenosyl-L-methionine	
+Q04089	UniProtKB	Mutagenesis	301	301	.	.	.	Note=Abolishes methyltransferase activity. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170	
+Q04089	UniProtKB	Mutagenesis	350	350	.	.	.	Note=Reduces methyltransferase activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170	
+Q04089	UniProtKB	Mutagenesis	372	372	.	.	.	Note=Reduces methyltransferase activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170	
+Q04089	UniProtKB	Mutagenesis	374	374	.	.	.	Note=Abolishes methyltransferase activity. E->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170	
+Q04089	UniProtKB	Mutagenesis	399	399	.	.	.	Note=Abolishes methyltransferase activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12080090;Dbxref=PMID:12080090	
+Q04089	UniProtKB	Mutagenesis	401	403	.	.	.	Note=Abolishes methyltransferase activity. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12080090;Dbxref=PMID:12080090	
+Q04089	UniProtKB	Mutagenesis	401	401	.	.	.	Note=Abolishes silencing function. G->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12086673;Dbxref=PMID:12086673	
+Q04089	UniProtKB	Mutagenesis	422	422	.	.	.	Note=Abolishes S-adenosyl-L-methionine binding and methyltransferase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170	
+Q04089	UniProtKB	Mutagenesis	422	422	.	.	.	Note=No effect. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170	
+Q04089	UniProtKB	Mutagenesis	543	543	.	.	.	Note=Abolishes methyltransferase activity%2C but not S-adenosyl-L-methionine binding. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170	
+Q04089	UniProtKB	Mutagenesis	550	550	.	.	.	Note=Abolishes methyltransferase activity%2C but not S-adenosyl-L-methionine binding. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170	
+Q04089	UniProtKB	Mutagenesis	550	550	.	.	.	Note=No effect. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170	
+Q04089	UniProtKB	Beta strand	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	196	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	236	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	248	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	255	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	264	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	284	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	293	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	305	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	324	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	336	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	340	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	355	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	368	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	377	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	394	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	404	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	416	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	425	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	452	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	464	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	470	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	474	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	485	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	503	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	519	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	525	528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	529	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	544	546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Beta strand	549	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+Q04089	UniProtKB	Helix	561	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z	
+##sequence-region P47138 1 172
+P47138	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P47138	UniProtKB	Chain	2	172	.	.	.	ID=PRO_0000071154;Note=Diphthamide biosynthesis protein 4	
+P47138	UniProtKB	Domain	6	77	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P47138	UniProtKB	Zinc finger	91	164	.	.	.	Note=DPH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00456	
+P47138	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P14020 1 267
+P14020	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+P14020	UniProtKB	Chain	2	267	.	.	.	ID=PRO_0000059175;Note=Dolichol-phosphate mannosyltransferase	
+P14020	UniProtKB	Topological domain	2	238	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14020	UniProtKB	Transmembrane	239	259	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14020	UniProtKB	Topological domain	260	267	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14020	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+P14020	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15548536;Dbxref=PMID:15548536	
+P14020	UniProtKB	Mutagenesis	141	141	.	.	.	Note=Reduces specific activity 2-fold. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15548536;Dbxref=PMID:15548536	
+##sequence-region P15436 1 1097
+P15436	UniProtKB	Chain	1	1097	.	.	.	ID=PRO_0000046454;Note=DNA polymerase delta catalytic subunit	
+P15436	UniProtKB	Zinc finger	1009	1027	.	.	.	Note=CysA-type	
+P15436	UniProtKB	Motif	1056	1074	.	.	.	Note=CysB motif	
+P15436	UniProtKB	Metal binding	1009	1009	.	.	.	Note=Zinc	
+P15436	UniProtKB	Metal binding	1012	1012	.	.	.	Note=Zinc	
+P15436	UniProtKB	Metal binding	1024	1024	.	.	.	Note=Zinc	
+P15436	UniProtKB	Metal binding	1027	1027	.	.	.	Note=Zinc	
+P15436	UniProtKB	Metal binding	1056	1056	.	.	.	Note=Iron-sulfur (4Fe-4S)	
+P15436	UniProtKB	Metal binding	1059	1059	.	.	.	Note=Iron-sulfur (4Fe-4S)	
+P15436	UniProtKB	Metal binding	1069	1069	.	.	.	Note=Iron-sulfur (4Fe-4S)	
+P15436	UniProtKB	Metal binding	1074	1074	.	.	.	Note=Iron-sulfur (4Fe-4S)	
+P15436	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P15436	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P15436	UniProtKB	Mutagenesis	1009	1009	.	.	.	Note=Impairs iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860	
+P15436	UniProtKB	Mutagenesis	1012	1012	.	.	.	Note=Impairs iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860	
+P15436	UniProtKB	Mutagenesis	1024	1024	.	.	.	Note=Impairs iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860	
+P15436	UniProtKB	Mutagenesis	1027	1027	.	.	.	Note=Impairs iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860	
+P15436	UniProtKB	Mutagenesis	1056	1056	.	.	.	Note=Abolishes iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860	
+P15436	UniProtKB	Mutagenesis	1059	1059	.	.	.	Note=Abolishes iron-sulfur-binding. C->A	
+P15436	UniProtKB	Mutagenesis	1069	1069	.	.	.	Note=Abolishes iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860	
+P15436	UniProtKB	Mutagenesis	1074	1074	.	.	.	Note=Abolishes iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860	
+P15436	UniProtKB	Mutagenesis	1074	1074	.	.	.	Note=In pol3-13%3B synthetically lethal with mutations of NBP35%2C DRE2 and TAH18. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860	
+P15436	UniProtKB	Sequence conflict	78	79	.	.	.	Note=EL->DV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15436	UniProtKB	Sequence conflict	78	79	.	.	.	Note=EL->DV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15436	UniProtKB	Sequence conflict	78	79	.	.	.	Note=EL->DV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15436	UniProtKB	Sequence conflict	189	189	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15436	UniProtKB	Sequence conflict	204	204	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15436	UniProtKB	Sequence conflict	347	363	.	.	.	Note=SIAGAKKPFIRNVFTLN->YLALRNHSFVMCYSD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15436	UniProtKB	Sequence conflict	647	649	.	.	.	Note=TPN->HY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15436	UniProtKB	Sequence conflict	870	870	.	.	.	Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15436	UniProtKB	Sequence conflict	974	974	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15436	UniProtKB	Turn	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	113	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	135	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	148	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	159	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	168	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	173	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Turn	185	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	191	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	211	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	223	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	254	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	269	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	282	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	290	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Turn	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	316	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Turn	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	339	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	355	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	371	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	379	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	396	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Turn	403	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	407	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	439	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Turn	444	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	447	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	460	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	464	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	479	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	499	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	507	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	533	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	550	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	556	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	598	600	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	604	609	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	612	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	624	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	630	635	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Turn	641	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	644	646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	652	654	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Turn	656	658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	662	682	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	687	711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	714	717	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	721	745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	748	750	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	757	760	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	762	769	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	775	790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	799	812	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	815	826	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	829	835	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	836	838	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	844	858	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	863	878	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	884	887	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	889	892	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	902	914	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	922	929	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Beta strand	931	933	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	935	937	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	942	947	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	954	960	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	963	974	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+P15436	UniProtKB	Helix	976	982	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY	
+##sequence-region P32601 1 143
+P32601	UniProtKB	Chain	1	143	.	.	.	ID=PRO_0000174180;Note=Protein DSS4	
+P32601	UniProtKB	Domain	1	131	.	.	.	Note=MSS4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01132	
+P32601	UniProtKB	Metal binding	6	6	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01132	
+P32601	UniProtKB	Metal binding	11	11	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01132	
+P32601	UniProtKB	Metal binding	104	104	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01132	
+P32601	UniProtKB	Metal binding	107	107	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01132	
+P32601	UniProtKB	Natural variant	108	108	.	.	.	Note=In DSS4-1%3B a dominant suppressor of SEC4-8. D->G	
+P32601	UniProtKB	Sequence conflict	136	136	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32601	UniProtKB	Sequence conflict	136	136	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07648 1 150
+Q07648	UniProtKB	Chain	1	150	.	.	.	ID=PRO_0000164634;Note=D-aminoacyl-tRNA deacylase	
+Q07648	UniProtKB	Motif	140	141	.	.	.	Note=Gly-cisPro motif%2C important for rejection of L-amino acids;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IIS0	
+##sequence-region P38149 1 878
+P38149	UniProtKB	Chain	1	878	.	.	.	ID=PRO_0000051469;Note=Probable di- and tripeptidase DUG2	
+P38149	UniProtKB	Repeat	18	57	.	.	.	Note=WD 1	
+P38149	UniProtKB	Repeat	68	107	.	.	.	Note=WD 2	
+P38149	UniProtKB	Repeat	235	274	.	.	.	Note=WD 3	
+P38149	UniProtKB	Repeat	282	322	.	.	.	Note=WD 4	
+P38149	UniProtKB	Repeat	362	405	.	.	.	Note=WD 5	
+P38149	UniProtKB	Repeat	608	651	.	.	.	Note=WD 6	
+P38149	UniProtKB	Active site	522	522	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38149	UniProtKB	Active site	586	586	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38149	UniProtKB	Metal binding	520	520	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38149	UniProtKB	Metal binding	553	553	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38149	UniProtKB	Metal binding	553	553	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38149	UniProtKB	Metal binding	587	587	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38149	UniProtKB	Metal binding	853	853	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P39009 1 513
+P39009	UniProtKB	Chain	1	513	.	.	.	ID=PRO_0000085930;Note=DNA damage response protein kinase DUN1	
+P39009	UniProtKB	Domain	56	112	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+P39009	UniProtKB	Domain	200	480	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P39009	UniProtKB	Nucleotide binding	206	214	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P39009	UniProtKB	Active site	328	328	.	.	.	Note=Proton acceptor	
+P39009	UniProtKB	Binding site	229	229	.	.	.	Note=ATP	
+P39009	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39009	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39009	UniProtKB	Modified residue	380	380	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39009	UniProtKB	Mutagenesis	229	229	.	.	.	Note=Loss of kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8261511;Dbxref=PMID:8261511	
+P39009	UniProtKB	Mutagenesis	328	328	.	.	.	Note=Loss of kinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8261511;Dbxref=PMID:8261511	
+P39009	UniProtKB	Beta strand	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Beta strand	33	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Beta strand	44	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Beta strand	56	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Beta strand	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Beta strand	77	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Beta strand	90	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQL	
+P39009	UniProtKB	Beta strand	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Beta strand	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Beta strand	121	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Turn	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Beta strand	131	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+P39009	UniProtKB	Beta strand	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQL	
+P39009	UniProtKB	Beta strand	154	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ	
+##sequence-region Q04067 1 274
+Q04067	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04067	UniProtKB	Chain	2	274	.	.	.	ID=PRO_0000123514;Note=Eukaryotic translation initiation factor 3 subunit G	
+Q04067	UniProtKB	Domain	191	270	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03006	
+Q04067	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04067	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04067	UniProtKB	Beta strand	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E	
+Q04067	UniProtKB	Beta strand	17	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E	
+Q04067	UniProtKB	Beta strand	28	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E	
+Q04067	UniProtKB	Helix	47	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E	
+Q04067	UniProtKB	Helix	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E	
+Q04067	UniProtKB	Helix	87	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E	
+##sequence-region Q03764 1 534
+Q03764	UniProtKB	Chain	1	534	.	.	.	ID=PRO_0000206230;Note=Ethanolamine kinase	
+Q03764	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q02884 1 456
+Q02884	UniProtKB	Chain	1	456	.	.	.	ID=PRO_0000235812;Note=Elongator complex protein 4	
+Q02884	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q02884	UniProtKB	Beta strand	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Turn	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Helix	91	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	99	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	107	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Helix	119	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	149	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Helix	158	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EJS	
+Q02884	UniProtKB	Beta strand	241	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EJS	
+Q02884	UniProtKB	Turn	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	256	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EJS	
+Q02884	UniProtKB	Helix	265	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Turn	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	282	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Turn	289	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Turn	294	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Helix	299	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Helix	304	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Turn	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	325	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Helix	333	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EJS	
+Q02884	UniProtKB	Helix	338	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	349	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Helix	359	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Turn	369	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Helix	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	379	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Helix	389	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	398	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q02884	UniProtKB	Beta strand	411	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+##sequence-region Q04409 1 500
+Q04409	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17709	
+Q04409	UniProtKB	Chain	2	500	.	.	.	ID=PRO_0000197604;Note=Putative glucokinase-2	
+Q04409	UniProtKB	Domain	12	498	.	.	.	Note=Hexokinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+Q04409	UniProtKB	Nucleotide binding	487	492	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04409	UniProtKB	Region	74	217	.	.	.	Note=Hexokinase small subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+Q04409	UniProtKB	Region	159	185	.	.	.	Note=Glucose-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04409	UniProtKB	Region	218	487	.	.	.	Note=Hexokinase large subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+Q04409	UniProtKB	Binding site	110	110	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04409	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17709	
+Q04409	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17709	
+Q04409	UniProtKB	Modified residue	470	470	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17709	
+##sequence-region P38333 1 483
+P38333	UniProtKB	Chain	1	483	.	.	.	ID=PRO_0000186118;Note=Essential nuclear protein 1	
+P38333	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38333	UniProtKB	Modified residue	190	190	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38333	UniProtKB	Modified residue	404	404	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P43572 1 832
+P43572	UniProtKB	Chain	1	832	.	.	.	ID=PRO_0000214167;Note=Enhancer of polycomb-like protein 1	
+P43572	UniProtKB	Compositional bias	419	428	.	.	.	Note=Poly-Ala	
+P43572	UniProtKB	Compositional bias	447	451	.	.	.	Note=Poly-Gln	
+P43572	UniProtKB	Compositional bias	454	461	.	.	.	Note=Poly-Gln	
+P43572	UniProtKB	Compositional bias	476	481	.	.	.	Note=Poly-Ser	
+P43572	UniProtKB	Compositional bias	777	795	.	.	.	Note=Poly-Gln	
+P43572	UniProtKB	Beta strand	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9U	
+P43572	UniProtKB	Beta strand	71	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9U	
+P43572	UniProtKB	Beta strand	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9U	
+P43572	UniProtKB	Helix	133	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Helix	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Helix	166	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Beta strand	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Helix	186	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Helix	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Helix	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Helix	217	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Helix	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Helix	232	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Helix	256	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Helix	264	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Turn	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Beta strand	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9W	
+P43572	UniProtKB	Beta strand	310	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9U	
+P43572	UniProtKB	Helix	324	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+P43572	UniProtKB	Helix	388	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9W	
+##sequence-region P41912 1 237
+P41912	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000213988;Note=Ras modification protein ERF4	
+P41912	UniProtKB	Mutagenesis	128	128	.	.	.	Note=In ERF4-1%3B loss of function. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12379641;Dbxref=PMID:12379641	
+P41912	UniProtKB	Mutagenesis	148	148	.	.	.	Note=In ERF4-2%3B loss of function. V->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12379641;Dbxref=PMID:12379641	
+P41912	UniProtKB	Mutagenesis	204	204	.	.	.	Note=In ERF4-3%3B loss of function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12379641;Dbxref=PMID:12379641	
+##sequence-region P32352 1 222
+P32352	UniProtKB	Chain	1	222	.	.	.	ID=PRO_0000087021;Note=C-8 sterol isomerase	
+P32352	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P54781 1 538
+P54781	UniProtKB	Chain	1	538	.	.	.	ID=PRO_0000052050;Note=Cytochrome P450 61	
+P54781	UniProtKB	Metal binding	476	476	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04798	
+P54781	UniProtKB	Cross-link	164	164	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P54781	UniProtKB	Cross-link	198	198	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P54781	UniProtKB	Sequence conflict	286	286	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P62651 1 68
+P62651	UniProtKB	Chain	1	68	.	.	.	ID=PRO_0000087028;Note=Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit	
+P62651	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P62651	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43613 1 295
+P43613	UniProtKB	Signal peptide	1	20	.	.	.	.	
+P43613	UniProtKB	Chain	21	295	.	.	.	ID=PRO_0000007272;Note=ER-localized J domain-containing protein 5	
+P43613	UniProtKB	Topological domain	21	130	.	.	.	Note=Lumenal	
+P43613	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43613	UniProtKB	Topological domain	152	295	.	.	.	Note=Cytoplasmic	
+P43613	UniProtKB	Domain	42	110	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+##sequence-region P53080 1 175
+P53080	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53080	UniProtKB	Chain	2	175	.	.	.	ID=PRO_0000202715;Note=Enhancer of mRNA-decapping protein 1	
+P53080	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53080	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P39998 1 551
+P39998	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000202613;Note=Enhancer of mRNA-decapping protein 3	
+P39998	UniProtKB	Domain	93	129	.	.	.	Note=DFDF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00845	
+P39998	UniProtKB	Domain	288	527	.	.	.	Note=YjeF N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00719	
+P39998	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P39998	UniProtKB	Modified residue	261	261	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39998	UniProtKB	Mutagenesis	360	361	.	.	.	Note=Abolishes homodimerization. RH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18678652;Dbxref=PMID:18678652	
+P39998	UniProtKB	Helix	91	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRU	
+P39998	UniProtKB	Turn	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRU	
+P39998	UniProtKB	Helix	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRU	
+##sequence-region P14741 1 305
+P14741	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P14741	UniProtKB	Chain	2	305	.	.	.	ID=PRO_0000156060;Note=Translation initiation factor eIF-2B subunit alpha	
+P14741	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P14741	UniProtKB	Modified residue	291	291	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32501 1 712
+P32501	UniProtKB	Chain	1	712	.	.	.	ID=PRO_0000156078;Note=Translation initiation factor eIF-2B subunit epsilon	
+P32501	UniProtKB	Domain	539	710	.	.	.	Note=W2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00695	
+P32501	UniProtKB	Modified residue	478	478	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32501	UniProtKB	Modified residue	481	481	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32501	UniProtKB	Modified residue	507	507	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32501	UniProtKB	Modified residue	525	525	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32501	UniProtKB	Modified residue	538	538	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32501	UniProtKB	Modified residue	707	707	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32501	UniProtKB	Mutagenesis	552	552	.	.	.	Note=Reduced exchange activity. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10805739;Dbxref=PMID:10805739	
+P32501	UniProtKB	Mutagenesis	569	569	.	.	.	Note=Lethal. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14681227;Dbxref=PMID:14681227	
+P32501	UniProtKB	Mutagenesis	576	576	.	.	.	Note=Reduced exchange activity. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10805739;Dbxref=PMID:10805739	
+P32501	UniProtKB	Mutagenesis	655	677	.	.	.	Note=Abolishes binding to SUI3. LFSALVSLYDNDIIEEDVIYKWW->AFSAAVSAADNDAAEAAVAAKWA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937	
+P32501	UniProtKB	Mutagenesis	696	706	.	.	.	Note=Abolishes binding to SUI3%3B probably impairs the conversion of eIF-2-GDP to eIF-2-GTP. WVEWLQNADEE->AAEAAQNAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937	
+P32501	UniProtKB	Helix	545	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ	
+P32501	UniProtKB	Helix	563	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ	
+P32501	UniProtKB	Helix	581	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ	
+P32501	UniProtKB	Helix	607	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ	
+P32501	UniProtKB	Helix	619	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ	
+P32501	UniProtKB	Helix	629	646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ	
+P32501	UniProtKB	Helix	651	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ	
+P32501	UniProtKB	Helix	670	678	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ	
+P32501	UniProtKB	Helix	684	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ	
+P32501	UniProtKB	Helix	687	702	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ	
+##sequence-region Q05775 1 265
+Q05775	UniProtKB	Chain	1	265	.	.	.	ID=PRO_0000123509;Note=Eukaryotic translation initiation factor 3 subunit J	
+Q05775	UniProtKB	Modified residue	75	75	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q05775	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05775	UniProtKB	Mutagenesis	215	215	.	.	.	Note=Increased association of the eIF-3 complex and 40S ribosomes. R->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16581774;Dbxref=PMID:16581774	
+##sequence-region P36053 1 145
+P36053	UniProtKB	Chain	1	145	.	.	.	ID=PRO_0000120950;Note=Transcription elongation factor 1	
+P36053	UniProtKB	Metal binding	25	25	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P60003	
+P36053	UniProtKB	Metal binding	28	28	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P60003	
+P36053	UniProtKB	Metal binding	49	49	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P60003	
+P36053	UniProtKB	Metal binding	52	52	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P60003	
+P36053	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36053	UniProtKB	Modified residue	117	117	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P36053	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P36053	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P25358 1 347
+P25358	UniProtKB	Chain	1	347	.	.	.	ID=PRO_0000207549;Note=Elongation of fatty acids protein 2	
+P25358	UniProtKB	Topological domain	1	62	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P25358	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25358	UniProtKB	Topological domain	84	96	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P25358	UniProtKB	Transmembrane	97	119	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25358	UniProtKB	Topological domain	120	122	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P25358	UniProtKB	Transmembrane	123	142	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25358	UniProtKB	Topological domain	143	146	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P25358	UniProtKB	Transmembrane	147	169	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25358	UniProtKB	Topological domain	170	200	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P25358	UniProtKB	Transmembrane	201	221	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25358	UniProtKB	Topological domain	222	231	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P25358	UniProtKB	Transmembrane	232	254	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25358	UniProtKB	Topological domain	255	275	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P25358	UniProtKB	Transmembrane	276	296	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25358	UniProtKB	Topological domain	297	347	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P25358	UniProtKB	Motif	344	347	.	.	.	Note=Di-lysine-like motif;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9832547;Dbxref=PMID:9832547	
+P25358	UniProtKB	Modified residue	334	334	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P25358	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P25358	UniProtKB	Modified residue	338	338	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P25358	UniProtKB	Glycosylation	32	32	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+##sequence-region P39013 1 349
+P39013	UniProtKB	Chain	1	349	.	.	.	ID=PRO_0000073648;Note=Actin cytoskeleton-regulatory complex protein END3	
+P39013	UniProtKB	Domain	8	98	.	.	.	Note=EH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077	
+P39013	UniProtKB	Domain	130	222	.	.	.	Note=EH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077	
+P39013	UniProtKB	Repeat	276	295	.	.	.	Note=1	
+P39013	UniProtKB	Repeat	315	334	.	.	.	Note=2	
+P39013	UniProtKB	Region	96	105	.	.	.	Note=Polyphosphoinositide (PIP2)-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39013	UniProtKB	Region	276	334	.	.	.	Note=2 X 20 AA approximate repeats	
+P39013	UniProtKB	Coiled coil	307	349	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39013	UniProtKB	Compositional bias	53	64	.	.	.	Note=Asp/Glu-rich (acidic)	
+P39013	UniProtKB	Modified residue	276	276	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39013	UniProtKB	Natural variant	245	245	.	.	.	Note=In strain: YJM 421. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579	
+P39013	UniProtKB	Natural variant	258	258	.	.	.	Note=In strain: YJM 280%2C YJM 320%2C YJM 326%2C YJM 627%2C YJM 789 and YJM 1129. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579	
+P39013	UniProtKB	Natural variant	268	268	.	.	.	Note=In strain: SK1%2C YJM 269%2C YJM 270%2C YJM 280%2C YJM 320%2C YJM 326%2C YJM 339%2C YJM 421%2C YJM 627%2C YJM 789 and YJM 1129. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108	
+##sequence-region P32626 1 227
+P32626	UniProtKB	Chain	1	227	.	.	.	ID=PRO_0000065746;Note=Enolase-phosphatase E1	
+P32626	UniProtKB	Region	118	119	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03117	
+P32626	UniProtKB	Metal binding	11	11	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03117,ECO:0000269|Ref.7	
+P32626	UniProtKB	Metal binding	13	13	.	.	.	Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03117,ECO:0000269|Ref.7	
+P32626	UniProtKB	Metal binding	186	186	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03117,ECO:0000269|Ref.7	
+P32626	UniProtKB	Binding site	161	161	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03117	
+P32626	UniProtKB	Sequence conflict	56	57	.	.	.	Note=ID->MH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32626	UniProtKB	Sequence conflict	56	57	.	.	.	Note=ID->MH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32626	UniProtKB	Sequence conflict	56	57	.	.	.	Note=ID->MH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32626	UniProtKB	Sequence conflict	179	179	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32626	UniProtKB	Sequence conflict	179	179	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32626	UniProtKB	Sequence conflict	179	179	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32626	UniProtKB	Beta strand	6	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Turn	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	26	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	46	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	59	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	77	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	102	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Beta strand	114	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	122	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	155	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	164	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Beta strand	181	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Helix	188	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Turn	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Beta strand	200	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+P32626	UniProtKB	Beta strand	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80	
+##sequence-region Q05785 1 613
+Q05785	UniProtKB	Chain	1	613	.	.	.	ID=PRO_0000074525;Note=Epsin-2	
+Q05785	UniProtKB	Domain	11	143	.	.	.	Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243	
+Q05785	UniProtKB	Domain	175	194	.	.	.	Note=UIM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+Q05785	UniProtKB	Domain	206	225	.	.	.	Note=UIM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+Q05785	UniProtKB	Compositional bias	138	166	.	.	.	Note=Arg-rich	
+Q05785	UniProtKB	Compositional bias	192	606	.	.	.	Note=Gln-rich	
+Q05785	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q05785	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q05785	UniProtKB	Modified residue	430	430	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q05785	UniProtKB	Modified residue	434	434	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q05785	UniProtKB	Modified residue	450	450	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q05785	UniProtKB	Modified residue	468	468	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q05785	UniProtKB	Modified residue	470	470	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05785	UniProtKB	Cross-link	426	426	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q05785	UniProtKB	Helix	18	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC	
+Q05785	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC	
+Q05785	UniProtKB	Helix	36	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC	
+Q05785	UniProtKB	Helix	49	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC	
+Q05785	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC	
+Q05785	UniProtKB	Helix	70	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC	
+Q05785	UniProtKB	Helix	89	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC	
+Q05785	UniProtKB	Helix	99	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC	
+Q05785	UniProtKB	Helix	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC	
+Q05785	UniProtKB	Helix	120	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC	
+Q05785	UniProtKB	Helix	136	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC	
+##sequence-region P53246 1 860
+P53246	UniProtKB	Chain	1	860	.	.	.	ID=PRO_0000202806;Note=Late endosome and vacuole interface protein 11	
+P53246	UniProtKB	Zinc finger	84	138	.	.	.	Note=BED-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00027	
+##sequence-region Q12003 1 364
+Q12003	UniProtKB	Chain	1	364	.	.	.	ID=PRO_0000255977;Note=Serine/threonine-protein kinase ENV7	
+Q12003	UniProtKB	Domain	30	364	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12003	UniProtKB	Nucleotide binding	36	44	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12003	UniProtKB	Active site	215	215	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12003	UniProtKB	Binding site	69	69	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12003	UniProtKB	Lipidation	13	13	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+Q12003	UniProtKB	Lipidation	14	14	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+Q12003	UniProtKB	Lipidation	15	15	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+##sequence-region O13529 1 151
+O13529	UniProtKB	Chain	1	151	.	.	.	ID=PRO_0000239641;Note=Protein ECM12	
+O13529	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13529	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13529	UniProtKB	Glycosylation	2	2	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13529	UniProtKB	Glycosylation	132	132	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13529	UniProtKB	Glycosylation	137	137	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39715 1 212
+P39715	UniProtKB	Chain	1	212	.	.	.	ID=PRO_0000086916;Note=Shuttling pre-60S factor ECM1	
+P39715	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39715	UniProtKB	Sequence conflict	102	102	.	.	.	Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02710 1 187
+Q02710	UniProtKB	Chain	1	187	.	.	.	ID=PRO_0000083483;Note=Protein ECM23	
+Q02710	UniProtKB	Zinc finger	126	180	.	.	.	Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094	
+##sequence-region P34216 1 1381
+P34216	UniProtKB	Chain	1	1381	.	.	.	ID=PRO_0000202457;Note=EH domain-containing and endocytosis protein 1	
+P34216	UniProtKB	Domain	14	113	.	.	.	Note=EH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077	
+P34216	UniProtKB	Domain	135	227	.	.	.	Note=EH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077	
+P34216	UniProtKB	Domain	277	366	.	.	.	Note=EH 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077	
+P34216	UniProtKB	Domain	1338	1380	.	.	.	Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
+P34216	UniProtKB	Region	1217	1381	.	.	.	Note=Able to bind biological membranes	
+P34216	UniProtKB	Coiled coil	593	882	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34216	UniProtKB	Compositional bias	550	575	.	.	.	Note=Ala-rich	
+P34216	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P34216	UniProtKB	Modified residue	241	241	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P34216	UniProtKB	Modified residue	244	244	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34216	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34216	UniProtKB	Modified residue	248	248	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34216	UniProtKB	Modified residue	249	249	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P34216	UniProtKB	Modified residue	251	251	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34216	UniProtKB	Modified residue	419	419	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34216	UniProtKB	Modified residue	450	450	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Modified residue	477	477	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Modified residue	487	487	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P34216	UniProtKB	Modified residue	495	495	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P34216	UniProtKB	Modified residue	848	848	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34216	UniProtKB	Modified residue	931	931	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P34216	UniProtKB	Modified residue	950	950	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34216	UniProtKB	Modified residue	964	964	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Modified residue	1008	1008	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Modified residue	1012	1012	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Modified residue	1020	1020	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Modified residue	1046	1046	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Modified residue	1069	1069	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34216	UniProtKB	Modified residue	1087	1087	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P34216	UniProtKB	Modified residue	1093	1093	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P34216	UniProtKB	Modified residue	1095	1095	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Modified residue	1096	1096	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34216	UniProtKB	Modified residue	1100	1100	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P34216	UniProtKB	Modified residue	1111	1111	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34216	UniProtKB	Modified residue	1181	1181	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Modified residue	1187	1187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Modified residue	1307	1307	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P34216	UniProtKB	Modified residue	1343	1343	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34216	UniProtKB	Cross-link	674	674	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P34216	UniProtKB	Cross-link	1329	1329	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P34216	UniProtKB	Mutagenesis	56	56	.	.	.	Note=Abnormal spatiotemporal behavior. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448668;Dbxref=PMID:18448668	
+P34216	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Abnormal spatiotemporal behavior. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448668;Dbxref=PMID:18448668	
+P34216	UniProtKB	Mutagenesis	319	319	.	.	.	Note=Abnormal spatiotemporal behavior. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448668;Dbxref=PMID:18448668	
+P34216	UniProtKB	Mutagenesis	1352	1352	.	.	.	Note=Reduced ubiquitin-binding. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16563434;Dbxref=PMID:16563434	
+P34216	UniProtKB	Mutagenesis	1370	1370	.	.	.	Note=Reduced ubiquitin-binding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16563434;Dbxref=PMID:16563434	
+P34216	UniProtKB	Mutagenesis	1374	1374	.	.	.	Note=Enhanced ubiquitin-binding. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16563434;Dbxref=PMID:16563434	
+P34216	UniProtKB	Mutagenesis	1378	1378	.	.	.	Note=Reduced ubiquitin-binding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16563434;Dbxref=PMID:16563434	
+P34216	UniProtKB	Helix	1341	1350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G3Q	
+P34216	UniProtKB	Turn	1351	1353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G3Q	
+P34216	UniProtKB	Helix	1356	1365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G3Q	
+P34216	UniProtKB	Helix	1370	1378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G3Q	
+##sequence-region P36008 1 412
+P36008	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36008	UniProtKB	Chain	2	412	.	.	.	ID=PRO_0000208832;Note=Elongation factor 1-gamma 2	
+P36008	UniProtKB	Domain	2	77	.	.	.	Note=GST N-terminal	
+P36008	UniProtKB	Domain	86	217	.	.	.	Note=GST C-terminal	
+P36008	UniProtKB	Domain	251	412	.	.	.	Note=EF-1-gamma C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00519	
+P36008	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36008	UniProtKB	Sequence conflict	8	8	.	.	.	Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36008	UniProtKB	Sequence conflict	347	347	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53978 1 1044
+P53978	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521	
+P53978	UniProtKB	Chain	2	1044	.	.	.	ID=PRO_0000093459;Note=Elongation factor 3B	
+P53978	UniProtKB	Repeat	5	42	.	.	.	Note=HEAT 1	
+P53978	UniProtKB	Repeat	86	123	.	.	.	Note=HEAT 2	
+P53978	UniProtKB	Repeat	124	162	.	.	.	Note=HEAT 3	
+P53978	UniProtKB	Repeat	166	203	.	.	.	Note=HEAT 4	
+P53978	UniProtKB	Repeat	205	241	.	.	.	Note=HEAT 5	
+P53978	UniProtKB	Repeat	242	279	.	.	.	Note=HEAT 6	
+P53978	UniProtKB	Repeat	285	323	.	.	.	Note=HEAT 7	
+P53978	UniProtKB	Domain	426	641	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P53978	UniProtKB	Domain	667	993	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P53978	UniProtKB	Nucleotide binding	463	470	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P53978	UniProtKB	Nucleotide binding	701	708	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P53978	UniProtKB	Compositional bias	1009	1031	.	.	.	Note=Lys-rich (basic)	
+P53978	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521	
+P53978	UniProtKB	Modified residue	187	187	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521	
+P53978	UniProtKB	Modified residue	196	196	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521	
+P53978	UniProtKB	Modified residue	789	789	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521	
+P53978	UniProtKB	Modified residue	972	972	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521	
+P53978	UniProtKB	Modified residue	974	974	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521	
+P53978	UniProtKB	Modified residue	1039	1039	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521	
+P53978	UniProtKB	Modified residue	1040	1040	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521	
+##sequence-region P12754 1 651
+P12754	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P12754	UniProtKB	Chain	2	651	.	.	.	ID=PRO_0000156072;Note=Translation initiation factor eIF-2B subunit delta	
+P12754	UniProtKB	Compositional bias	6	106	.	.	.	Note=Arg/Lys-rich (basic)	
+P12754	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P12754	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12754	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32801 1 640
+P32801	UniProtKB	Chain	1	640	.	.	.	ID=PRO_0000085951;Note=Serine/threonine-protein kinase ELM1	
+P32801	UniProtKB	Domain	88	420	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32801	UniProtKB	Nucleotide binding	94	102	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32801	UniProtKB	Active site	259	259	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P32801	UniProtKB	Binding site	117	117	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32801	UniProtKB	Modified residue	152	152	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32801	UniProtKB	Modified residue	516	516	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32801	UniProtKB	Modified residue	519	519	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32801	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Allows selective inhibition in vivo. T->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12917352;Dbxref=PMID:12917352	
+P32801	UniProtKB	Sequence conflict	390	390	.	.	.	Note=E->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32801	UniProtKB	Sequence conflict	484	485	.	.	.	Note=TV->SD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P42935 1 788
+P42935	UniProtKB	Chain	1	788	.	.	.	ID=PRO_0000051474;Note=Elongator complex protein 2	
+P42935	UniProtKB	Repeat	57	87	.	.	.	Note=WD 1	
+P42935	UniProtKB	Repeat	101	130	.	.	.	Note=WD 2	
+P42935	UniProtKB	Repeat	141	181	.	.	.	Note=WD 3	
+P42935	UniProtKB	Repeat	200	234	.	.	.	Note=WD 4	
+P42935	UniProtKB	Repeat	279	309	.	.	.	Note=WD 5	
+P42935	UniProtKB	Repeat	383	413	.	.	.	Note=WD 6	
+P42935	UniProtKB	Repeat	438	466	.	.	.	Note=WD 7	
+P42935	UniProtKB	Repeat	604	634	.	.	.	Note=WD 8	
+P42935	UniProtKB	Repeat	651	683	.	.	.	Note=WD 9	
+P42935	UniProtKB	Sequence conflict	579	579	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P42935	UniProtKB	Beta strand	4	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Turn	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	30	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	37	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	51	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	62	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	69	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	83	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	94	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	107	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	116	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	124	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	133	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	138	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	153	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	165	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	188	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	205	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	214	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XFV	
+P42935	UniProtKB	Beta strand	218	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	228	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	259	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	267	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	280	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	291	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	296	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	303	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Turn	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	317	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	344	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	352	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	364	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	376	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	384	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XFV	
+P42935	UniProtKB	Beta strand	388	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	398	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Turn	405	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	408	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	429	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	442	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	460	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Helix	469	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Helix	539	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	550	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	561	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	572	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	581	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	586	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Turn	592	594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	597	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	609	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	618	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	626	628	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XFV	
+P42935	UniProtKB	Beta strand	630	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Turn	637	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	641	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	656	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Helix	664	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	668	674	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	677	685	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	687	699	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	704	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	717	724	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	729	735	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	738	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Turn	747	749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	755	760	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	768	775	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+P42935	UniProtKB	Beta strand	780	786	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N	
+##sequence-region P40540 1 141
+P40540	UniProtKB	Chain	1	141	.	.	.	ID=PRO_0000202998;Note=ER membrane protein complex subunit 5	
+P40540	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40540	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40540	UniProtKB	Topological domain	28	48	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40540	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40540	UniProtKB	Topological domain	70	141	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12431 1 108
+Q12431	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000247112;Note=ER membrane protein complex subunit 6	
+Q12431	UniProtKB	Transmembrane	24	44	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12431	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12431	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P42842 1 904
+P42842	UniProtKB	Chain	1	904	.	.	.	ID=PRO_0000203365;Note=Essential for maintenance of the cell wall protein 1	
+P42842	UniProtKB	Repeat	510	544	.	.	.	Note=TPR 1	
+P42842	UniProtKB	Repeat	563	596	.	.	.	Note=TPR 2	
+P42842	UniProtKB	Repeat	603	636	.	.	.	Note=TPR 3	
+P42842	UniProtKB	Repeat	637	670	.	.	.	Note=TPR 4	
+P42842	UniProtKB	Repeat	671	704	.	.	.	Note=TPR 5	
+P42842	UniProtKB	Repeat	706	739	.	.	.	Note=TPR 6	
+P42842	UniProtKB	Compositional bias	149	158	.	.	.	Note=Poly-Leu	
+##sequence-region P18414 1 219
+P18414	UniProtKB	Chain	1	219	.	.	.	ID=PRO_0000194171;Note=ER lumen protein-retaining receptor	
+P18414	UniProtKB	Topological domain	1	2	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Transmembrane	3	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Topological domain	22	35	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Transmembrane	36	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Topological domain	54	62	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Transmembrane	63	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Topological domain	83	102	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Transmembrane	103	116	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Topological domain	117	123	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Transmembrane	124	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Topological domain	144	155	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Transmembrane	156	174	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Topological domain	175	185	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Transmembrane	186	206	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18414	UniProtKB	Topological domain	207	219	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06551 1 359
+Q06551	UniProtKB	Chain	1	359	.	.	.	ID=PRO_0000212948;Note=Palmitoyltransferase ERF2	
+Q06551	UniProtKB	Topological domain	1	75	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06551	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06551	UniProtKB	Topological domain	97	104	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06551	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06551	UniProtKB	Topological domain	126	217	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06551	UniProtKB	Transmembrane	218	238	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06551	UniProtKB	Topological domain	239	250	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06551	UniProtKB	Transmembrane	251	271	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06551	UniProtKB	Topological domain	272	359	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06551	UniProtKB	Domain	173	223	.	.	.	Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067	
+Q06551	UniProtKB	Mutagenesis	173	173	.	.	.	Note=In ERF2-1%3B loss of function. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490616;Dbxref=PMID:10490616	
+Q06551	UniProtKB	Mutagenesis	182	182	.	.	.	Note=In ERF2-7%3B loss of function. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490616;Dbxref=PMID:10490616	
+Q06551	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Abolishes palmitoyltransferase activity and interaction with SHR5. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10490616,ECO:0000269|PubMed:12193598;Dbxref=PMID:10490616,PMID:12193598	
+Q06551	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Loss of function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490616;Dbxref=PMID:10490616	
+Q06551	UniProtKB	Mutagenesis	201	201	.	.	.	Note=Abolishes palmitoyltransferase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12193598;Dbxref=PMID:12193598	
+Q06551	UniProtKB	Mutagenesis	203	203	.	.	.	Note=Abolishes palmitoyltransferase activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12193598;Dbxref=PMID:12193598	
+Q06551	UniProtKB	Mutagenesis	218	218	.	.	.	Note=In ERF2-2%3B loss of function. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490616;Dbxref=PMID:10490616	
+Q06551	UniProtKB	Sequence conflict	68	68	.	.	.	Note=R->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32476 1 496
+P32476	UniProtKB	Chain	1	496	.	.	.	ID=PRO_0000209851;Note=Squalene monooxygenase	
+P32476	UniProtKB	Topological domain	1	16	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32476	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32476	UniProtKB	Topological domain	38	474	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32476	UniProtKB	Transmembrane	475	495	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32476	UniProtKB	Topological domain	496	496	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32476	UniProtKB	Nucleotide binding	21	48	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32476	UniProtKB	Cross-link	284	284	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538	
+P32476	UniProtKB	Cross-link	289	289	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32476	UniProtKB	Cross-link	311	311	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32476	UniProtKB	Natural variant	251	251	.	.	.	Note=In strain: A2-M8%3B confers resistance to the allylamine antifungal terbinafine. L->F	
+##sequence-region P53199 1 349
+P53199	UniProtKB	Chain	1	349	.	.	.	ID=PRO_0000087798;Note=Sterol-4-alpha-carboxylate 3-dehydrogenase%2C decarboxylating	
+P53199	UniProtKB	Active site	151	151	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53199	UniProtKB	Binding site	155	155	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P0CX10 1 437
+P0CX10	UniProtKB	Chain	1	437	.	.	.	ID=PRO_0000134064;Note=Enolase-related protein 1	
+P0CX10	UniProtKB	Region	373	376	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX10	UniProtKB	Active site	212	212	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX10	UniProtKB	Active site	346	346	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX10	UniProtKB	Metal binding	247	247	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX10	UniProtKB	Metal binding	296	296	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX10	UniProtKB	Metal binding	321	321	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX10	UniProtKB	Binding site	160	160	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX10	UniProtKB	Binding site	169	169	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX10	UniProtKB	Binding site	296	296	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX10	UniProtKB	Binding site	321	321	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX10	UniProtKB	Binding site	397	397	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX10	UniProtKB	Sequence conflict	231	231	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53337 1 310
+P53337	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000127671;Note=ER-derived vesicles protein ERV29	
+P53337	UniProtKB	Topological domain	1	108	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Topological domain	130	137	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Transmembrane	138	158	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Topological domain	159	160	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Topological domain	182	209	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Transmembrane	210	230	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Topological domain	231	245	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Transmembrane	246	266	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Topological domain	267	282	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Transmembrane	283	303	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Topological domain	304	310	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53337	UniProtKB	Motif	307	310	.	.	.	Note=Di-lysine motif	
+P53337	UniProtKB	Sequence conflict	64	64	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12168 1 779
+Q12168	UniProtKB	Chain	1	779	.	.	.	ID=PRO_0000215819;Note=Endo-1%2C3(4)-beta-glucanase 2	
+##sequence-region Q99382 1 181
+Q99382	UniProtKB	Chain	1	181	.	.	.	ID=PRO_0000247246;Note=SRP-independent targeting protein 2	
+Q99382	UniProtKB	Topological domain	1	15	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q99382	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99382	UniProtKB	Topological domain	37	45	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q99382	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99382	UniProtKB	Topological domain	67	89	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q99382	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99382	UniProtKB	Topological domain	111	112	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q99382	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99382	UniProtKB	Topological domain	134	181	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+##sequence-region P22140 1 391
+P22140	UniProtKB	Chain	1	391	.	.	.	ID=PRO_0000056809;Note=Choline/ethanolaminephosphotransferase 1	
+P22140	UniProtKB	Topological domain	1	49	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Transmembrane	50	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Topological domain	70	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Topological domain	194	211	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Transmembrane	212	232	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Topological domain	233	264	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Transmembrane	265	282	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Topological domain	283	285	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Transmembrane	286	308	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Topological domain	309	321	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Transmembrane	322	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Topological domain	343	346	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Transmembrane	347	367	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Topological domain	368	391	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22140	UniProtKB	Sequence conflict	96	96	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22140	UniProtKB	Sequence conflict	98	98	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38819 1 212
+P38819	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38819	UniProtKB	Chain	21	212	.	.	.	ID=PRO_0000010412;Note=Protein ERP5	
+P38819	UniProtKB	Topological domain	21	178	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38819	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38819	UniProtKB	Topological domain	200	212	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38819	UniProtKB	Domain	31	124	.	.	.	Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096	
+P38819	UniProtKB	Glycosylation	171	171	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38312 1 142
+P38312	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000122237;Note=ER-derived vesicles protein ERV15	
+P38312	UniProtKB	Topological domain	1	7	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38312	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38312	UniProtKB	Topological domain	29	55	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38312	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38312	UniProtKB	Topological domain	77	114	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38312	UniProtKB	Transmembrane	115	135	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38312	UniProtKB	Topological domain	136	142	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08649 1 445
+Q08649	UniProtKB	Chain	1	445	.	.	.	ID=PRO_0000051562;Note=Histone acetyltransferase ESA1	
+Q08649	UniProtKB	Domain	33	86	.	.	.	Note=Chromo	
+Q08649	UniProtKB	Domain	162	433	.	.	.	Note=MYST-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063	
+Q08649	UniProtKB	Zinc finger	195	220	.	.	.	Note=C2HC MYST-type%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063	
+Q08649	UniProtKB	Region	303	307	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11106757,ECO:0000269|PubMed:12368900,ECO:0000269|PubMed:22020126;Dbxref=PMID:11106757,PMID:12368900,PMID:22020126	
+Q08649	UniProtKB	Region	312	318	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11106757,ECO:0000269|PubMed:12368900,ECO:0000269|PubMed:22020126;Dbxref=PMID:11106757,PMID:12368900,PMID:22020126	
+Q08649	UniProtKB	Motif	245	266	.	.	.	Note=ESA1-RPD3 motif	
+Q08649	UniProtKB	Active site	338	338	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000305;evidence=ECO:0000303|PubMed:12368900,ECO:0000303|PubMed:17223684,ECO:0000303|PubMed:18245364,ECO:0000303|PubMed:22020126,ECO:0000305;Dbxref=PMID:12368900,PMID:17223684,PMID:18245364,PMID:22020126	
+Q08649	UniProtKB	Binding site	342	342	.	.	.	Note=Acetyl-CoA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11106757,ECO:0000269|PubMed:12368900,ECO:0000269|PubMed:22020126;Dbxref=PMID:11106757,PMID:12368900,PMID:22020126	
+Q08649	UniProtKB	Site	304	304	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08649	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08649	UniProtKB	Modified residue	262	262	.	.	.	Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22020126;Dbxref=PMID:22020126	
+Q08649	UniProtKB	Mutagenesis	247	247	.	.	.	Note=Strongly reduces HAT activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+Q08649	UniProtKB	Mutagenesis	250	250	.	.	.	Note=Strongly reduces HAT activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+Q08649	UniProtKB	Mutagenesis	251	251	.	.	.	Note=Strongly reduces HAT activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+Q08649	UniProtKB	Mutagenesis	252	252	.	.	.	Note=Strongly reduces HAT activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+Q08649	UniProtKB	Mutagenesis	253	253	.	.	.	Note=Strongly reduces HAT activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+Q08649	UniProtKB	Mutagenesis	254	254	.	.	.	Note=Strongly reduces HAT activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+Q08649	UniProtKB	Mutagenesis	256	256	.	.	.	Note=Strongly reduces HAT activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+Q08649	UniProtKB	Mutagenesis	259	259	.	.	.	Note=Strongly reduces HAT activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+Q08649	UniProtKB	Mutagenesis	260	260	.	.	.	Note=Strongly reduces HAT activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+Q08649	UniProtKB	Mutagenesis	262	262	.	.	.	Note=Strongly reduces HAT activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+Q08649	UniProtKB	Mutagenesis	262	262	.	.	.	Note=Strongly reduces HAT activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22020126;Dbxref=PMID:22020126	
+Q08649	UniProtKB	Mutagenesis	304	304	.	.	.	Note=Reduces HAT activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17223684;Dbxref=PMID:17223684	
+Q08649	UniProtKB	Mutagenesis	304	304	.	.	.	Note=Strongly reduces HAT activity%2C but is not lethal (in vivo). Lethal%2C when associated with Q-338. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12368900,ECO:0000269|PubMed:17223684,ECO:0000269|PubMed:18245364;Dbxref=PMID:12368900,PMID:17223684,PMID:18245364	
+Q08649	UniProtKB	Mutagenesis	315	315	.	.	.	Note=Loss of function. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9520405;Dbxref=PMID:9520405	
+Q08649	UniProtKB	Mutagenesis	338	338	.	.	.	Note=Strongly reduces HAT activity at pH 9.2. Nearly abolishes HAT activity at pH 8.0%2C but is not lethal (in vivo). Lethal%3B when associated with S-334. E->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12368900,ECO:0000269|PubMed:17223684,ECO:0000269|PubMed:18245364;Dbxref=PMID:12368900,PMID:17223684,PMID:18245364	
+Q08649	UniProtKB	Beta strand	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RO0	
+Q08649	UniProtKB	Helix	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ	
+Q08649	UniProtKB	Beta strand	25	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ	
+Q08649	UniProtKB	Beta strand	35	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ	
+Q08649	UniProtKB	Beta strand	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ	
+Q08649	UniProtKB	Beta strand	51	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ	
+Q08649	UniProtKB	Beta strand	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ	
+Q08649	UniProtKB	Turn	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ	
+Q08649	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ	
+Q08649	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RO0	
+Q08649	UniProtKB	Helix	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+Q08649	UniProtKB	Beta strand	169	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Helix	187	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T	
+Q08649	UniProtKB	Beta strand	194	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Turn	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Helix	208	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	224	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	232	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Helix	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Helix	245	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	271	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	283	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	300	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Helix	309	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	313	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FY7	
+Q08649	UniProtKB	Helix	316	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	335	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Helix	343	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	366	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Helix	370	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Helix	381	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	394	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Beta strand	400	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Helix	407	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Helix	426	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7	
+Q08649	UniProtKB	Turn	438	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9U	
+##sequence-region Q06340 1 456
+Q06340	UniProtKB	Chain	1	456	.	.	.	ID=PRO_0000227693;Note=Protein ESC2	
+Q06340	UniProtKB	Repeat	169	287	.	.	.	Note=SUMO-like region 1	
+Q06340	UniProtKB	Repeat	380	456	.	.	.	Note=SUMO-like region 2	
+Q06340	UniProtKB	Coiled coil	301	360	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06340	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06340	UniProtKB	Modified residue	125	125	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06340	UniProtKB	Modified residue	126	126	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q06344 1 628
+Q06344	UniProtKB	Chain	1	628	.	.	.	ID=PRO_0000228158;Note=Pre-rRNA-processing protein ESF1	
+Q06344	UniProtKB	Coiled coil	426	495	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06344	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06344	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q06344	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06344	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+Q06344	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q06344	UniProtKB	Modified residue	369	369	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06344	UniProtKB	Modified residue	372	372	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06344	UniProtKB	Modified residue	542	542	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P22696 1 170
+P22696	UniProtKB	Chain	1	170	.	.	.	ID=PRO_0000193433;Note=Peptidyl-prolyl cis-trans isomerase ESS1	
+P22696	UniProtKB	Domain	9	43	.	.	.	Note=WW;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224	
+P22696	UniProtKB	Domain	57	170	.	.	.	Note=PpiC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00278	
+P22696	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22696	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Abolishes PPIase activity. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15728580;Dbxref=PMID:15728580	
+P22696	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Abolishes PPIase activity. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15728580;Dbxref=PMID:15728580	
+P22696	UniProtKB	Mutagenesis	127	127	.	.	.	Note=In PTF1-2%3B decreases the catalytic efficiency 20-fold. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9867817;Dbxref=PMID:9867817	
+P22696	UniProtKB	Mutagenesis	162	162	.	.	.	Note=In PTF1-5%3B decreases the catalytic efficiency 12-fold. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9867817;Dbxref=PMID:9867817	
+P22696	UniProtKB	Mutagenesis	164	164	.	.	.	Note=Abolishes PPIase activity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15728580;Dbxref=PMID:15728580	
+P22696	UniProtKB	Sequence conflict	8	8	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22696	UniProtKB	Sequence conflict	17	17	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22696	UniProtKB	Sequence conflict	128	128	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32474 1 517
+P32474	UniProtKB	Signal peptide	1	29	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32474	UniProtKB	Chain	30	517	.	.	.	ID=PRO_0000034219;Note=Protein disulfide-isomerase EUG1	
+P32474	UniProtKB	Domain	30	141	.	.	.	Note=Thioredoxin 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P32474	UniProtKB	Domain	355	487	.	.	.	Note=Thioredoxin 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P32474	UniProtKB	Motif	514	517	.	.	.	Note=Prevents secretion from ER	
+P32474	UniProtKB	Glycosylation	159	159	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32474	UniProtKB	Glycosylation	174	174	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32474	UniProtKB	Glycosylation	207	207	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32474	UniProtKB	Glycosylation	293	293	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32474	UniProtKB	Glycosylation	462	462	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32474	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Increases PDI activity. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11485577;Dbxref=PMID:11485577	
+P32474	UniProtKB	Mutagenesis	408	408	.	.	.	Note=Increases PDI activity. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11485577;Dbxref=PMID:11485577	
+P32474	UniProtKB	Sequence conflict	364	364	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P02992 1 437
+P02992	UniProtKB	Transit peptide	1	38	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02992	UniProtKB	Chain	39	437	.	.	.	ID=PRO_0000007465;Note=Elongation factor Tu%2C mitochondrial	
+P02992	UniProtKB	Domain	46	242	.	.	.	Note=tr-type G	
+P02992	UniProtKB	Nucleotide binding	55	62	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02992	UniProtKB	Nucleotide binding	117	121	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02992	UniProtKB	Nucleotide binding	172	175	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02992	UniProtKB	Region	55	62	.	.	.	Note=G1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02992	UniProtKB	Region	96	100	.	.	.	Note=G2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02992	UniProtKB	Region	117	120	.	.	.	Note=G3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02992	UniProtKB	Region	172	175	.	.	.	Note=G4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P02992	UniProtKB	Region	210	212	.	.	.	Note=G5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q06706 1 1349
+Q06706	UniProtKB	Chain	1	1349	.	.	.	ID=PRO_0000084179;Note=Elongator complex protein 1	
+Q06706	UniProtKB	Helix	923	930	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	934	943	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	948	950	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	952	959	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	963	974	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	977	984	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	995	1004	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1007	1013	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1014	1016	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1018	1032	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Turn	1033	1036	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1038	1047	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1051	1060	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1064	1073	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Turn	1076	1078	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1079	1092	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1096	1107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1110	1119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1123	1132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1138	1141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1143	1170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1253	1282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1286	1308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+Q06706	UniProtKB	Helix	1345	1347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS	
+##sequence-region Q02908 1 557
+Q02908	UniProtKB	Chain	1	557	.	.	.	ID=PRO_0000235811;Note=Elongator complex protein 3	
+Q02908	UniProtKB	Domain	405	557	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+Q02908	UniProtKB	Metal binding	108	108	.	.	.	Note=Iron-sulfur (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352	
+Q02908	UniProtKB	Metal binding	118	118	.	.	.	Note=Iron-sulfur (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352	
+Q02908	UniProtKB	Metal binding	121	121	.	.	.	Note=Iron-sulfur (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352	
+Q02908	UniProtKB	Cross-link	453	453	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+Q02908	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Eliminates iron contents%3B when associated with S-118 and S-121. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352	
+Q02908	UniProtKB	Mutagenesis	118	118	.	.	.	Note=Eliminates iron contents%3B when associated with S-108 and S-121. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352	
+Q02908	UniProtKB	Mutagenesis	121	121	.	.	.	Note=Eliminates iron contents%3B when associated with S-108 and S-118. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352	
+##sequence-region P00925 1 437
+P00925	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8935650,ECO:0000269|Ref.4;Dbxref=PMID:8935650	
+P00925	UniProtKB	Chain	2	437	.	.	.	ID=PRO_0000134063;Note=Enolase 2	
+P00925	UniProtKB	Active site	160	160	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00925	UniProtKB	Metal binding	247	247	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00925	UniProtKB	Metal binding	296	296	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00925	UniProtKB	Metal binding	321	321	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00925	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00925	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00925	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00925	UniProtKB	Modified residue	324	324	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00925	UniProtKB	Cross-link	60	60	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00925	UniProtKB	Cross-link	243	243	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00925	UniProtKB	Cross-link	358	358	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q12518 1 454
+Q12518	UniProtKB	Chain	1	454	.	.	.	ID=PRO_0000074524;Note=Epsin-1	
+Q12518	UniProtKB	Domain	11	143	.	.	.	Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243	
+Q12518	UniProtKB	Domain	165	184	.	.	.	Note=UIM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+Q12518	UniProtKB	Domain	189	208	.	.	.	Note=UIM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+Q12518	UniProtKB	Region	447	454	.	.	.	Note=Clathrin-binding	
+Q12518	UniProtKB	Compositional bias	211	349	.	.	.	Note=Gln-rich	
+Q12518	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12518	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12518	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12518	UniProtKB	Modified residue	328	328	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12518	UniProtKB	Modified residue	364	364	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12518	UniProtKB	Modified residue	366	366	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12518	UniProtKB	Modified residue	384	384	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12518	UniProtKB	Modified residue	386	386	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12518	UniProtKB	Modified residue	388	388	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12518	UniProtKB	Modified residue	395	395	.	.	.	Note=Phosphothreonine%3B by PRK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11694597;Dbxref=PMID:11694597	
+Q12518	UniProtKB	Modified residue	415	415	.	.	.	Note=Phosphothreonine%3B by PRK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11694597;Dbxref=PMID:11694597	
+Q12518	UniProtKB	Cross-link	357	357	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q12518	UniProtKB	Mutagenesis	395	395	.	.	.	Note=No phosphorylation. T->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11694597;Dbxref=PMID:11694597	
+Q12518	UniProtKB	Mutagenesis	415	415	.	.	.	Note=No phosphorylation. T->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11694597;Dbxref=PMID:11694597	
+Q12518	UniProtKB	Helix	18	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ	
+Q12518	UniProtKB	Helix	36	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ	
+Q12518	UniProtKB	Helix	49	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ	
+Q12518	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ	
+Q12518	UniProtKB	Helix	70	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ	
+Q12518	UniProtKB	Helix	89	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ	
+Q12518	UniProtKB	Helix	99	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ	
+Q12518	UniProtKB	Helix	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ	
+Q12518	UniProtKB	Helix	119	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ	
+Q12518	UniProtKB	Helix	136	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ	
+##sequence-region P47160 1 408
+P47160	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P47160	UniProtKB	Chain	2	408	.	.	.	ID=PRO_0000074526;Note=Epsin-3	
+P47160	UniProtKB	Domain	24	157	.	.	.	Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243	
+P47160	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P47160	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47160	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47160	UniProtKB	Modified residue	203	203	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47160	UniProtKB	Modified residue	212	212	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47160	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47160	UniProtKB	Mutagenesis	272	272	.	.	.	Note=Reduced binding to GGA2. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220	
+P47160	UniProtKB	Mutagenesis	275	275	.	.	.	Note=Reduced binding to GGA2. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220	
+P47160	UniProtKB	Helix	31	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK	
+P47160	UniProtKB	Helix	49	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK	
+P47160	UniProtKB	Helix	62	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK	
+P47160	UniProtKB	Helix	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONL	
+P47160	UniProtKB	Helix	84	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK	
+P47160	UniProtKB	Helix	103	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK	
+P47160	UniProtKB	Helix	113	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK	
+P47160	UniProtKB	Helix	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK	
+P47160	UniProtKB	Helix	133	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK	
+P47160	UniProtKB	Helix	150	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK	
+##sequence-region Q03769 1 411
+Q03769	UniProtKB	Chain	1	411	.	.	.	ID=PRO_0000074528;Note=Epsin-5	
+Q03769	UniProtKB	Domain	25	184	.	.	.	Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243	
+Q03769	UniProtKB	Compositional bias	304	323	.	.	.	Note=Asn-rich	
+Q03769	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03769	UniProtKB	Modified residue	322	322	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03769	UniProtKB	Modified residue	324	324	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03769	UniProtKB	Modified residue	363	363	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03769	UniProtKB	Modified residue	368	368	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03769	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03769	UniProtKB	Modified residue	401	401	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03769	UniProtKB	Mutagenesis	331	331	.	.	.	Note=Reduced binding to GGA2. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220	
+Q03769	UniProtKB	Mutagenesis	334	334	.	.	.	Note=Reduced binding to GGA2. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220	
+Q03769	UniProtKB	Helix	32	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Beta strand	43	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Helix	50	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Helix	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Helix	65	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Helix	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Turn	96	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Helix	101	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Helix	123	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Helix	137	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Turn	141	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Helix	156	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Helix	177	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+Q03769	UniProtKB	Turn	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08	
+##sequence-region Q08651 1 330
+Q08651	UniProtKB	Chain	1	330	.	.	.	ID=PRO_0000245256;Note=Probable oxidoreductase ENV9	
+Q08651	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08651	UniProtKB	Transmembrane	245	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08651	UniProtKB	Nucleotide binding	47	53	.	.	.	Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08651	UniProtKB	Active site	202	202	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08651	UniProtKB	Binding site	173	173	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08651	UniProtKB	Glycosylation	282	282	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25340 1 473
+P25340	UniProtKB	Chain	1	473	.	.	.	ID=PRO_0000207491;Note=Delta(24(24(1)))-sterol reductase	
+P25340	UniProtKB	Topological domain	1	39	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Transmembrane	40	64	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Topological domain	65	101	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Transmembrane	102	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Topological domain	124	138	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Transmembrane	139	157	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Topological domain	158	174	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Transmembrane	175	197	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Topological domain	198	232	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Transmembrane	233	249	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Topological domain	250	326	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Transmembrane	327	346	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Topological domain	347	414	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Transmembrane	415	439	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Topological domain	440	473	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25340	UniProtKB	Sequence conflict	33	33	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25340	UniProtKB	Sequence conflict	366	366	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25340	UniProtKB	Sequence conflict	366	366	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25087 1 383
+P25087	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P25087	UniProtKB	Chain	2	383	.	.	.	ID=PRO_0000124799;Note=Sterol 24-C-methyltransferase	
+P25087	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P25087	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25087	UniProtKB	Sequence conflict	380	380	.	.	.	Note=E->EE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P24521 1 451
+P24521	UniProtKB	Chain	1	451	.	.	.	ID=PRO_0000156671;Note=Phosphomevalonate kinase	
+P24521	UniProtKB	Nucleotide binding	150	160	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24521	UniProtKB	Sequence conflict	213	213	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24521	UniProtKB	Sequence conflict	418	423	.	.	.	Note=TANDKR->PLMTKD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12450 1 207
+Q12450	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12450	UniProtKB	Chain	22	207	.	.	.	ID=PRO_0000010411;Note=Protein ERP4	
+Q12450	UniProtKB	Topological domain	22	174	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12450	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12450	UniProtKB	Topological domain	196	207	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12450	UniProtKB	Domain	36	118	.	.	.	Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096	
+##sequence-region P40456 1 1118
+P40456	UniProtKB	Chain	1	1118	.	.	.	ID=PRO_0000202957;Note=EST/SMG-like protein 1	
+P40456	UniProtKB	Domain	947	1087	.	.	.	Note=PINc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40456	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40456	UniProtKB	Modified residue	190	190	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q03018 1 1630
+Q03018	UniProtKB	Chain	1	1630	.	.	.	ID=PRO_0000205904;Note=Separin	
+Q03018	UniProtKB	Domain	1443	1542	.	.	.	Note=Peptidase C50	
+Q03018	UniProtKB	Active site	1531	1531	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03018	UniProtKB	Mutagenesis	1568	1570	.	.	.	Note=Reduces function. Loss of function. DKD->AKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11149918;Dbxref=PMID:11149918	
+Q03018	UniProtKB	Sequence conflict	136	136	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03018	UniProtKB	Sequence conflict	250	253	.	.	.	Note=TVEC->IRRV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03018	UniProtKB	Sequence conflict	540	540	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03018	UniProtKB	Sequence conflict	636	636	.	.	.	Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03018	UniProtKB	Sequence conflict	782	782	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03018	UniProtKB	Sequence conflict	800	800	.	.	.	Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03018	UniProtKB	Sequence conflict	1146	1146	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03018	UniProtKB	Sequence conflict	1295	1295	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03018	UniProtKB	Sequence conflict	1333	1336	.	.	.	Note=QEID->ARKSI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03018	UniProtKB	Sequence conflict	1443	1443	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03018	UniProtKB	Helix	54	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S	
+Q03018	UniProtKB	Helix	75	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S	
+Q03018	UniProtKB	Helix	82	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	103	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	125	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	147	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	157	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	163	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	180	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	194	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	206	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	224	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	242	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	251	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	261	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	267	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	273	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S	
+Q03018	UniProtKB	Helix	292	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	298	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	324	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S	
+Q03018	UniProtKB	Helix	332	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	353	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	376	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	399	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	422	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	442	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	462	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	465	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	482	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	495	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	504	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	519	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	535	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	552	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	557	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	574	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	586	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	591	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	612	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	624	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	627	630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	636	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	655	667	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	669	672	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	673	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	676	689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	693	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	709	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	714	723	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	727	729	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	730	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	734	742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	744	748	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	750	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	763	786	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	790	809	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	810	812	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S	
+Q03018	UniProtKB	Helix	816	839	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	843	859	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	863	879	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	883	897	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	902	904	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	906	915	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	919	925	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	927	930	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	931	933	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	939	946	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	953	955	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	958	960	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	961	980	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	984	989	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	994	997	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1046	1062	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1065	1067	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1070	1088	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1096	1106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1109	1122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1126	1130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1145	1161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1165	1173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	1175	1177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1180	1186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	1187	1190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1191	1197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1214	1232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1234	1237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1243	1271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	1272	1275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1276	1279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1286	1303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1305	1309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1313	1315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S	
+Q03018	UniProtKB	Helix	1321	1328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1337	1354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1361	1363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1366	1381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1390	1396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1398	1400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1405	1407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	1409	1413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1416	1420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1422	1431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	1432	1434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1436	1441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1446	1450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1457	1470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1478	1483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1487	1495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1498	1505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	1509	1511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1514	1517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1526	1528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	1531	1534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1537	1539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S	
+Q03018	UniProtKB	Beta strand	1542	1545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S	
+Q03018	UniProtKB	Helix	1547	1553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1557	1564	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1568	1582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1598	1605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Helix	1606	1608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1609	1611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Turn	1612	1617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1619	1623	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+Q03018	UniProtKB	Beta strand	1626	1629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+##sequence-region Q07872 1 247
+Q07872	UniProtKB	Chain	1	247	.	.	.	ID=PRO_0000074527;Note=Epsin-4	
+Q07872	UniProtKB	Domain	7	146	.	.	.	Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243	
+Q07872	UniProtKB	Modified residue	195	195	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40557 1 701
+P40557	UniProtKB	Signal peptide	1	27	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40557	UniProtKB	Chain	28	701	.	.	.	ID=PRO_0000034221;Note=ER-retained PMA1-suppressing protein 1	
+P40557	UniProtKB	Transmembrane	646	666	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40557	UniProtKB	Domain	28	142	.	.	.	Note=Thioredoxin 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P40557	UniProtKB	Domain	408	446	.	.	.	Note=Thioredoxin 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P40557	UniProtKB	Glycosylation	85	85	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40557	UniProtKB	Glycosylation	264	264	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40557	UniProtKB	Glycosylation	299	299	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40557	UniProtKB	Glycosylation	370	370	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40557	UniProtKB	Disulfide bond	60	63	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P40557	UniProtKB	Disulfide bond	200	203	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+##sequence-region P38767 1 581
+P38767	UniProtKB	Chain	1	581	.	.	.	ID=PRO_0000164256;Note=Ethionine resistance-conferring protein 1	
+P38767	UniProtKB	Topological domain	1	172	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38767	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38767	UniProtKB	Topological domain	194	248	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38767	UniProtKB	Transmembrane	249	269	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38767	UniProtKB	Topological domain	270	281	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38767	UniProtKB	Transmembrane	282	302	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38767	UniProtKB	Topological domain	303	345	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38767	UniProtKB	Transmembrane	346	366	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38767	UniProtKB	Topological domain	367	471	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38767	UniProtKB	Transmembrane	472	492	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38767	UniProtKB	Topological domain	493	581	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32462 1 438
+P32462	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000207494;Note=Delta(14)-sterol reductase	
+P32462	UniProtKB	Topological domain	1	13	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Topological domain	35	71	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Transmembrane	72	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Topological domain	91	109	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Transmembrane	110	127	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Topological domain	128	147	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Transmembrane	148	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Topological domain	173	242	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Topological domain	264	308	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Transmembrane	309	328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Topological domain	329	368	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Transmembrane	369	387	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Topological domain	388	438	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32462	UniProtKB	Nucleotide binding	370	371	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86	
+P32462	UniProtKB	Nucleotide binding	414	418	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86	
+P32462	UniProtKB	Binding site	335	335	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86	
+P32462	UniProtKB	Binding site	339	339	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86	
+P32462	UniProtKB	Binding site	358	358	.	.	.	Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86	
+P32462	UniProtKB	Binding site	363	363	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86	
+P32462	UniProtKB	Binding site	410	410	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86	
+P32462	UniProtKB	Binding site	425	425	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86	
+P32462	UniProtKB	Sequence conflict	253	253	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38604 1 731
+P38604	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8134375,ECO:0000269|Ref.7;Dbxref=PMID:8134375	
+P38604	UniProtKB	Chain	2	731	.	.	.	ID=PRO_0000072657;Note=Lanosterol synthase	
+P38604	UniProtKB	Repeat	125	167	.	.	.	Note=PFTB 1	
+P38604	UniProtKB	Repeat	566	603	.	.	.	Note=PFTB 2	
+P38604	UniProtKB	Repeat	615	661	.	.	.	Note=PFTB 3	
+P38604	UniProtKB	Active site	234	234	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38604	UniProtKB	Active site	456	456	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38604	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+P38604	UniProtKB	Natural variant	359	731	.	.	.	Note=In strain: SGL9%3B loss of activity. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3	
+P38604	UniProtKB	Mutagenesis	457	457	.	.	.	Note=Reduces thermal stability and enzyme activity%3B when associated with A-526 or C-526. No effect%3B when associated with D-526 or Q-526. C->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16235265;Dbxref=PMID:16235265	
+P38604	UniProtKB	Mutagenesis	526	526	.	.	.	Note=Reduces thermal stability and enzyme activity%3B when associated with D-457. E->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16235265;Dbxref=PMID:16235265	
+P38604	UniProtKB	Mutagenesis	526	526	.	.	.	Note=No effect%3B when associated with D-457. E->D%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16235265;Dbxref=PMID:16235265	
+P38604	UniProtKB	Sequence conflict	61	61	.	.	.	Note=H->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38604	UniProtKB	Sequence conflict	530	530	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38604	UniProtKB	Sequence conflict	530	530	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53198 1 216
+P53198	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53198	UniProtKB	Chain	20	216	.	.	.	ID=PRO_0000010413;Note=Protein ERP6	
+P53198	UniProtKB	Topological domain	20	183	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53198	UniProtKB	Transmembrane	184	204	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53198	UniProtKB	Topological domain	205	216	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53198	UniProtKB	Domain	29	130	.	.	.	Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096	
+P53198	UniProtKB	Sequence conflict	106	106	.	.	.	Note=C->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CX11 1 437
+P0CX11	UniProtKB	Chain	1	437	.	.	.	ID=PRO_0000409749;Note=Enolase-related protein 2	
+P0CX11	UniProtKB	Region	373	376	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX11	UniProtKB	Active site	212	212	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX11	UniProtKB	Active site	346	346	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX11	UniProtKB	Metal binding	247	247	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX11	UniProtKB	Metal binding	296	296	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX11	UniProtKB	Metal binding	321	321	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX11	UniProtKB	Binding site	160	160	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX11	UniProtKB	Binding site	169	169	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX11	UniProtKB	Binding site	296	296	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX11	UniProtKB	Binding site	321	321	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX11	UniProtKB	Binding site	397	397	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04651 1 352
+Q04651	UniProtKB	Chain	1	352	.	.	.	ID=PRO_0000203251;Note=ER-derived vesicles protein ERV41	
+Q04651	UniProtKB	Topological domain	1	23	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04651	UniProtKB	Transmembrane	24	44	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04651	UniProtKB	Topological domain	45	311	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04651	UniProtKB	Transmembrane	312	332	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04651	UniProtKB	Topological domain	333	352	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04651	UniProtKB	Motif	349	350	.	.	.	Note=Isoleucine-leucine motif	
+Q04651	UniProtKB	Beta strand	52	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	63	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Helix	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	80	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	98	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Helix	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Helix	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	162	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	184	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Helix	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	201	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Turn	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	233	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Turn	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	254	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Helix	266	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	278	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+Q04651	UniProtKB	Beta strand	287	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC	
+##sequence-region P36168 1 1195
+P36168	UniProtKB	Chain	1	1195	.	.	.	ID=PRO_0000203229;Note=EST/SMG-like protein 2	
+P36168	UniProtKB	Domain	1025	1164	.	.	.	Note=PINc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36168	UniProtKB	Compositional bias	210	250	.	.	.	Note=Asn-rich	
+##sequence-region Q03096 1 181
+Q03096	UniProtKB	Chain	1	181	.	.	.	ID=PRO_0000021206;Note=Telomere replication protein EST3	
+Q03096	UniProtKB	Alternative sequence	93	93	.	.	.	ID=VSP_035813;Note=In isoform 2. V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03096	UniProtKB	Alternative sequence	94	181	.	.	.	ID=VSP_035814;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03096	UniProtKB	Mutagenesis	3	3	.	.	.	Note=Causes telomere shortening. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502	
+Q03096	UniProtKB	Mutagenesis	21	21	.	.	.	Note=Causes telomere shortening. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	49	49	.	.	.	Note=Reduces ability to dimerize and causes telomere shortening. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502	
+Q03096	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Reduces ability to dimerize and causes telomere shortening. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Causes telomere shortening. K->E%2CS%2CY;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Causes telomere shortening%2C but does not impair interaction with the telomerase RNP. K->A%2CE;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	72	72	.	.	.	Note=Causes telomere shortening. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502	
+Q03096	UniProtKB	Mutagenesis	82	82	.	.	.	Note=Causes telomere shortening. A->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502	
+Q03096	UniProtKB	Mutagenesis	86	86	.	.	.	Note=Causes progressive telomere shortening and cell senescence. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502	
+Q03096	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Causes telomere shortening. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502	
+Q03096	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Causes telomere shortening. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502	
+Q03096	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Causes telomere shortening. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502	
+Q03096	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Reduces binding to DNA and RNA%2C and causes progressive telomere shortening and cell senescence. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16884717,ECO:0000269|PubMed:19172754;Dbxref=PMID:16884717,PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Impairs interaction with the telomerase RNP and causes progressive telomere shortening and cell senescence. E->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16884717,ECO:0000269|PubMed:19172754;Dbxref=PMID:16884717,PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	110	110	.	.	.	Note=Causes progressive telomere shortening and cell senescence%2C but does not impair interaction with the telomerase RNP. R->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Impairs interaction with the telomerase RNP and causes telomere shortening. E->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	115	115	.	.	.	Note=Impairs interaction with the telomerase RNP and causes telomere shortening. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Impairs interaction with the telomerase RNP and causes telomere shortening. N->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	164	164	.	.	.	Note=Causes telomere shortening%2C but does not impair interaction with the telomerase RNP. D->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Reduces ability to dimerize and causes telomere shortening. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Impairs interaction with the telomerase RNP and causes telomere shortening. D->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754	
+Q03096	UniProtKB	Mutagenesis	168	168	.	.	.	Note=Causes telomere shortening. V->A%2CD%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754	
+Q03096	UniProtKB	Helix	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Helix	22	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Turn	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Helix	47	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Helix	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Helix	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Helix	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Beta strand	66	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Beta strand	79	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Beta strand	90	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Helix	97	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Beta strand	118	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Beta strand	126	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Helix	132	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Beta strand	148	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+Q03096	UniProtKB	Turn	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V	
+##sequence-region P38836 1 430
+P38836	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38836	UniProtKB	Chain	25	430	.	.	.	ID=PRO_0000004417;Note=Putative metallocarboxypeptidase ECM14	
+P38836	UniProtKB	Region	182	185	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38836	UniProtKB	Region	257	258	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38836	UniProtKB	Region	311	312	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38836	UniProtKB	Metal binding	182	182	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38836	UniProtKB	Metal binding	185	185	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38836	UniProtKB	Metal binding	310	310	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38836	UniProtKB	Binding site	240	240	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38836	UniProtKB	Glycosylation	41	41	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38836	UniProtKB	Glycosylation	295	295	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38836	UniProtKB	Disulfide bond	251	272	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q05958 1 814
+Q05958	UniProtKB	Chain	1	814	.	.	.	ID=PRO_0000114948;Note=Sterol regulatory element-binding protein ECM22	
+Q05958	UniProtKB	DNA binding	43	73	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+Q05958	UniProtKB	Modified residue	431	431	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q05958	UniProtKB	Modified residue	445	445	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q05958	UniProtKB	Modified residue	464	464	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q05958	UniProtKB	Mutagenesis	790	790	.	.	.	Note=Increases aerobic sterol uptake. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11208779;Dbxref=PMID:11208779	
+##sequence-region P32644 1 1121
+P32644	UniProtKB	Chain	1	1121	.	.	.	ID=PRO_0000080725;Note=Putative ATP-dependent RNA helicase ECM32	
+P32644	UniProtKB	Nucleotide binding	670	677	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32644	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32644	UniProtKB	Modified residue	392	392	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P32644	UniProtKB	Modified residue	465	465	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38248 1 429
+P38248	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Chain	20	406	.	.	.	ID=PRO_0000033191;Note=Cell wall protein ECM33	
+P38248	UniProtKB	Propeptide	407	429	.	.	.	ID=PRO_0000033192;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Compositional bias	311	404	.	.	.	Note=Ser-rich	
+P38248	UniProtKB	Modified residue	339	339	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P38248	UniProtKB	Lipidation	406	406	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	21	21	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	56	56	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	196	196	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	209	209	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	227	227	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	234	234	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	241	241	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	267	267	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	279	279	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	304	304	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	328	328	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38248	UniProtKB	Glycosylation	389	389	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06200 1 448
+Q06200	UniProtKB	Chain	1	448	.	.	.	ID=PRO_0000086923;Note=Protein ECM7	
+Q06200	UniProtKB	Topological domain	1	28	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06200	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06200	UniProtKB	Topological domain	50	204	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06200	UniProtKB	Transmembrane	205	225	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06200	UniProtKB	Topological domain	226	246	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06200	UniProtKB	Transmembrane	247	267	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06200	UniProtKB	Topological domain	268	287	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06200	UniProtKB	Transmembrane	288	308	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06200	UniProtKB	Topological domain	309	448	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43605 1 281
+P43605	UniProtKB	Chain	1	281	.	.	.	ID=PRO_0000074550;Note=N-acetyltransferase ECO1	
+P43605	UniProtKB	Zinc finger	33	57	.	.	.	Note=CCHH-type	
+P43605	UniProtKB	Modified residue	223	223	.	.	.	Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+P43605	UniProtKB	Mutagenesis	35	35	.	.	.	Note=In ctf7-109%3B loss of function. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15668154;Dbxref=PMID:15668154	
+P43605	UniProtKB	Mutagenesis	53	53	.	.	.	Note=In ctf7-108%3B loss of function. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15668154;Dbxref=PMID:15668154	
+P43605	UniProtKB	Mutagenesis	211	211	.	.	.	Note=Abolishes acetyltransferase activity%3B but not chromatid cohesion activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+P43605	UniProtKB	Mutagenesis	222	223	.	.	.	Note=Abolishes acetyltransferase activity%3B but not chromatid cohesion activity. RK->GG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+P43605	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Abolishes acetyltransferase activity%3B but not chromatid cohesion activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+P43605	UniProtKB	Mutagenesis	232	232	.	.	.	Note=Abolishes acetyltransferase activity%3B but not chromatid cohesion activity. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+##sequence-region P38249 1 964
+P38249	UniProtKB	Chain	1	964	.	.	.	ID=PRO_0000123544;Note=Eukaryotic translation initiation factor 3 subunit A	
+P38249	UniProtKB	Domain	382	493	.	.	.	Note=PCI;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03000	
+P38249	UniProtKB	Coiled coil	625	668	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03000	
+P38249	UniProtKB	Coiled coil	702	734	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03000	
+P38249	UniProtKB	Coiled coil	796	869	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03000	
+P38249	UniProtKB	Compositional bias	506	542	.	.	.	Note=Glu-rich	
+P38249	UniProtKB	Modified residue	508	508	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38249	UniProtKB	Modified residue	691	691	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38249	UniProtKB	Modified residue	935	935	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38249	UniProtKB	Mutagenesis	692	701	.	.	.	Note=Reduces interaction of eIF-3 with the 40S ribosome. LDLDTIKQVI->AAAAAAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18765792;Dbxref=PMID:18765792	
+P38249	UniProtKB	Helix	8	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	24	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	49	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	65	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	83	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	112	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	152	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	176	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	196	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	230	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	253	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Helix	279	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	296	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	318	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	349	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	363	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	374	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	382	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Turn	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	400	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Beta strand	415	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	418	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	421	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Beta strand	441	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	445	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	456	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Helix	462	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+P38249	UniProtKB	Beta strand	481	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D	
+P38249	UniProtKB	Beta strand	487	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51	
+##sequence-region P40217 1 347
+P40217	UniProtKB	Chain	1	347	.	.	.	ID=PRO_0000051041;Note=Eukaryotic translation initiation factor 3 subunit I	
+P40217	UniProtKB	Repeat	8	47	.	.	.	Note=WD 1	
+P40217	UniProtKB	Repeat	50	89	.	.	.	Note=WD 2	
+P40217	UniProtKB	Repeat	149	190	.	.	.	Note=WD 3	
+P40217	UniProtKB	Repeat	194	233	.	.	.	Note=WD 4	
+P40217	UniProtKB	Repeat	291	330	.	.	.	Note=WD 5	
+P40217	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40217	UniProtKB	Beta strand	1	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	13	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	24	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	34	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Turn	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	44	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	55	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	64	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	74	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Turn	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	86	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	96	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	105	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	121	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Turn	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	136	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	144	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	156	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Helix	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	167	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	175	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Turn	182	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	187	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	199	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	208	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	218	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Turn	225	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	230	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	240	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	247	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	274	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Turn	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	285	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	296	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	305	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Beta strand	315	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Helix	324	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+P40217	UniProtKB	Helix	332	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL	
+##sequence-region Q05050 1 843
+Q05050	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q05050	UniProtKB	Chain	2	843	.	.	.	ID=PRO_0000203273;Note=Eisosome protein 1	
+Q05050	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q05050	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q05050	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05050	UniProtKB	Modified residue	130	130	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17761666;Dbxref=PMID:17287358,PMID:17761666	
+Q05050	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05050	UniProtKB	Modified residue	401	401	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q05050	UniProtKB	Modified residue	584	584	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:19779198	
+Q05050	UniProtKB	Modified residue	710	710	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q05050	UniProtKB	Modified residue	720	720	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q05050	UniProtKB	Modified residue	763	763	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05050	UniProtKB	Modified residue	775	775	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05050	UniProtKB	Modified residue	816	816	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q05050	UniProtKB	Modified residue	828	828	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05050	UniProtKB	Modified residue	829	829	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05050	UniProtKB	Modified residue	838	838	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P40319 1 345
+P40319	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000207550;Note=Elongation of fatty acids protein 3	
+P40319	UniProtKB	Topological domain	1	73	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40319	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40319	UniProtKB	Topological domain	95	105	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40319	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40319	UniProtKB	Topological domain	127	155	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40319	UniProtKB	Transmembrane	156	176	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40319	UniProtKB	Topological domain	177	180	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40319	UniProtKB	Transmembrane	181	201	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40319	UniProtKB	Topological domain	202	207	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40319	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40319	UniProtKB	Topological domain	229	242	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40319	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40319	UniProtKB	Topological domain	264	283	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40319	UniProtKB	Transmembrane	284	304	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40319	UniProtKB	Topological domain	305	345	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P40319	UniProtKB	Motif	308	311	.	.	.	Note=Di-lysine motif 1;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9832547;Dbxref=PMID:9832547	
+P40319	UniProtKB	Motif	312	315	.	.	.	Note=Di-lysine motif 2;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9832547;Dbxref=PMID:9832547	
+P40319	UniProtKB	Motif	316	319	.	.	.	Note=Di-lysine motif 3;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9832547;Dbxref=PMID:9832547	
+P40319	UniProtKB	Glycosylation	2	2	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P40319	UniProtKB	Glycosylation	20	20	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P40319	UniProtKB	Glycosylation	66	66	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P40319	UniProtKB	Sequence conflict	35	35	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40319	UniProtKB	Sequence conflict	208	208	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40319	UniProtKB	Sequence conflict	330	331	.	.	.	Note=ST->FY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53861 1 379
+P53861	UniProtKB	Chain	1	379	.	.	.	ID=PRO_0000203386;Note=Elongin-A	
+P53861	UniProtKB	Domain	19	63	.	.	.	Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080	
+P53861	UniProtKB	Region	1	143	.	.	.	Note=ELC1-binding	
+P53861	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53861	UniProtKB	Modified residue	278	278	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+##sequence-region P43555 1 445
+P43555	UniProtKB	Signal peptide	1	28	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8314797;Dbxref=PMID:8314797	
+P43555	UniProtKB	Chain	29	445	.	.	.	ID=PRO_0000021173;Note=Protein EMP47	
+P43555	UniProtKB	Topological domain	29	412	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43555	UniProtKB	Transmembrane	413	433	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43555	UniProtKB	Topological domain	434	445	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43555	UniProtKB	Domain	36	254	.	.	.	Note=L-type lectin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00658	
+P43555	UniProtKB	Region	430	433	.	.	.	Note=Mediates the interactions with COPI and COPII coat complexes;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43555	UniProtKB	Motif	441	445	.	.	.	Note=Di-lysine motif	
+P43555	UniProtKB	Disulfide bond	179	213	.	.	.	.	
+P43555	UniProtKB	Sequence conflict	52	52	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43555	UniProtKB	Sequence conflict	77	77	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43555	UniProtKB	Sequence conflict	125	125	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43555	UniProtKB	Helix	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Helix	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	59	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	71	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	81	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	90	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Y	
+P43555	UniProtKB	Beta strand	96	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	114	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	139	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	152	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Helix	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Helix	171	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	176	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	186	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Helix	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	201	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	211	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	223	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Helix	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+P43555	UniProtKB	Beta strand	243	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z	
+##sequence-region P53753 1 1117
+P53753	UniProtKB	Signal peptide	1	16	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53753	UniProtKB	Chain	17	1117	.	.	.	ID=PRO_0000012133;Note=Endo-1%2C3(4)-beta-glucanase 1	
+P53753	UniProtKB	Compositional bias	342	345	.	.	.	Note=Poly-Ser	
+P53753	UniProtKB	Compositional bias	365	370	.	.	.	Note=Poly-Ser	
+P53753	UniProtKB	Compositional bias	376	383	.	.	.	Note=Poly-Ser	
+P53753	UniProtKB	Glycosylation	138	138	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53753	UniProtKB	Glycosylation	186	186	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53753	UniProtKB	Glycosylation	223	223	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53753	UniProtKB	Glycosylation	259	259	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53753	UniProtKB	Glycosylation	280	280	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53753	UniProtKB	Glycosylation	303	303	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53753	UniProtKB	Glycosylation	307	307	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53753	UniProtKB	Glycosylation	393	393	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53753	UniProtKB	Glycosylation	533	533	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53753	UniProtKB	Glycosylation	886	886	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P06103 1 763
+P06103	UniProtKB	Chain	1	763	.	.	.	ID=PRO_0000123535;Note=Eukaryotic translation initiation factor 3 subunit B	
+P06103	UniProtKB	Domain	77	162	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03001	
+P06103	UniProtKB	Repeat	228	266	.	.	.	Note=WD 1	
+P06103	UniProtKB	Repeat	277	325	.	.	.	Note=WD 2	
+P06103	UniProtKB	Repeat	373	416	.	.	.	Note=WD 3	
+P06103	UniProtKB	Repeat	484	524	.	.	.	Note=WD 4	
+P06103	UniProtKB	Repeat	544	589	.	.	.	Note=WD 5	
+P06103	UniProtKB	Repeat	605	650	.	.	.	Note=WD 6	
+P06103	UniProtKB	Region	1	136	.	.	.	Note=Sufficient for interaction with HCR1 and TIF32;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16581774;Dbxref=PMID:16581774	
+P06103	UniProtKB	Region	28	261	.	.	.	Note=Sufficient for interaction with PIC8	
+P06103	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P06103	UniProtKB	Modified residue	67	67	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06103	UniProtKB	Modified residue	669	669	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P06103	UniProtKB	Mutagenesis	124	130	.	.	.	Note=Impairs interaction with HCR1 and TIF32%2C impairs interaction of the eIF-3 complex with eIF-1%2C eIF-2 and the 40S ribosome%2C and impairs initiation of translation. KGFLFVE->AAAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16581774;Dbxref=PMID:16581774	
+P06103	UniProtKB	Beta strand	78	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6	
+P06103	UniProtKB	Helix	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6	
+P06103	UniProtKB	Helix	92	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6	
+P06103	UniProtKB	Beta strand	109	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6	
+P06103	UniProtKB	Turn	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6	
+P06103	UniProtKB	Beta strand	125	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6	
+P06103	UniProtKB	Helix	134	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6	
+P06103	UniProtKB	Beta strand	148	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6	
+P06103	UniProtKB	Beta strand	156	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6	
+P06103	UniProtKB	Helix	161	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6	
+P06103	UniProtKB	Helix	186	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Helix	191	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	201	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	207	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	224	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	245	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	250	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Turn	258	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	262	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	272	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	283	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Helix	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	312	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Turn	317	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	322	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	338	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	345	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	355	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Helix	361	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Helix	371	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	380	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	395	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	400	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	411	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	416	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	427	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	435	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	447	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	464	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	480	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	486	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	501	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	519	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	538	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	551	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	558	565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	571	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	575	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	593	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	600	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	611	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	622	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Turn	628	630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	636	641	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	646	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Beta strand	657	660	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F	
+P06103	UniProtKB	Helix	694	728	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E	
+##sequence-region P39540 1 310
+P39540	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000207548;Note=Elongation of fatty acids protein 1	
+P39540	UniProtKB	Topological domain	1	63	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P39540	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39540	UniProtKB	Topological domain	85	100	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P39540	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39540	UniProtKB	Topological domain	122	141	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P39540	UniProtKB	Transmembrane	142	163	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39540	UniProtKB	Topological domain	164	174	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P39540	UniProtKB	Transmembrane	175	196	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39540	UniProtKB	Topological domain	197	201	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P39540	UniProtKB	Transmembrane	202	223	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39540	UniProtKB	Topological domain	224	234	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P39540	UniProtKB	Transmembrane	235	255	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39540	UniProtKB	Topological domain	256	271	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P39540	UniProtKB	Transmembrane	272	292	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39540	UniProtKB	Topological domain	293	310	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P39540	UniProtKB	Motif	304	307	.	.	.	Note=Di-lysine motif;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8702485;Dbxref=PMID:8702485	
+##sequence-region P38874 1 309
+P38874	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000084178;Note=Elongator complex protein 5	
+P38874	UniProtKB	Helix	8	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Beta strand	23	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Helix	36	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Beta strand	55	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Beta strand	70	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Helix	80	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Beta strand	102	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Helix	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Helix	117	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Beta strand	129	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Turn	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EJS	
+P38874	UniProtKB	Helix	157	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Beta strand	166	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Helix	181	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Beta strand	200	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Beta strand	215	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Turn	224	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+P38874	UniProtKB	Beta strand	228	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+##sequence-region P53073 1 190
+P53073	UniProtKB	Chain	1	190	.	.	.	ID=PRO_0000202711;Note=ER membrane protein complex subunit 4	
+P53073	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53073	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12396 1 444
+Q12396	UniProtKB	Signal peptide	1	46	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087	
+Q12396	UniProtKB	Chain	47	444	.	.	.	ID=PRO_0000239645;Note=Protein EMP46	
+Q12396	UniProtKB	Topological domain	47	408	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12396	UniProtKB	Transmembrane	409	429	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12396	UniProtKB	Topological domain	430	444	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12396	UniProtKB	Domain	52	269	.	.	.	Note=L-type lectin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00658	
+Q12396	UniProtKB	Region	429	432	.	.	.	Note=Mediates the interactions with COPI and COPII coat complexes	
+Q12396	UniProtKB	Motif	440	444	.	.	.	Note=Di-lysine motif	
+Q12396	UniProtKB	Metal binding	177	177	.	.	.	Note=Potassium	
+Q12396	UniProtKB	Disulfide bond	196	230	.	.	.	.	
+Q12396	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Impairs potassium-binding. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16439369;Dbxref=PMID:16439369	
+Q12396	UniProtKB	Mutagenesis	429	429	.	.	.	Note=Impairs interaction with COP1%2C SEC21 and SEC23 and loss of reticulum endoplasmic exit. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087	
+Q12396	UniProtKB	Mutagenesis	432	432	.	.	.	Note=Impairs interaction with COP1%2C SEC21 and SEC23 and loss of reticulum endoplasmic exit. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087	
+Q12396	UniProtKB	Mutagenesis	440	444	.	.	.	Note=Loss of endoplasmic reticulum exit. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087	
+Q12396	UniProtKB	Mutagenesis	440	442	.	.	.	Note=Impairs interaction with COP1 and SEC21 and mislocalizes to the vacuole. KVK->SVS%2CRVR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087	
+Q12396	UniProtKB	Mutagenesis	443	444	.	.	.	Note=Loss of endoplasmic reticulum exit. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087	
+Q12396	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Turn	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Helix	71	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Turn	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	78	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	90	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	100	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	115	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	133	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Turn	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	158	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Turn	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	171	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Turn	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	193	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	207	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Helix	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	219	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	228	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Helix	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	244	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+Q12396	UniProtKB	Beta strand	258	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V	
+##sequence-region P00924 1 437
+P00924	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7005235,ECO:0000269|Ref.6;Dbxref=PMID:7005235	
+P00924	UniProtKB	Chain	2	437	.	.	.	ID=PRO_0000134062;Note=Enolase 1	
+P00924	UniProtKB	Region	373	376	.	.	.	Note=Substrate binding	
+P00924	UniProtKB	Active site	212	212	.	.	.	Note=Proton donor;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00924	UniProtKB	Active site	346	346	.	.	.	Note=Proton acceptor	
+P00924	UniProtKB	Metal binding	247	247	.	.	.	Note=Magnesium;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8605183;Dbxref=PMID:8605183	
+P00924	UniProtKB	Metal binding	296	296	.	.	.	Note=Magnesium;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8605183;Dbxref=PMID:8605183	
+P00924	UniProtKB	Metal binding	321	321	.	.	.	Note=Magnesium;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8605183;Dbxref=PMID:8605183	
+P00924	UniProtKB	Binding site	160	160	.	.	.	Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8605183,ECO:0000269|PubMed:9376357;Dbxref=PMID:8605183,PMID:9376357	
+P00924	UniProtKB	Binding site	169	169	.	.	.	Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8605183,ECO:0000269|PubMed:9376357;Dbxref=PMID:8605183,PMID:9376357	
+P00924	UniProtKB	Binding site	296	296	.	.	.	Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8605183,ECO:0000269|PubMed:9376357;Dbxref=PMID:8605183,PMID:9376357	
+P00924	UniProtKB	Binding site	321	321	.	.	.	Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8605183,ECO:0000269|PubMed:9376357;Dbxref=PMID:8605183,PMID:9376357	
+P00924	UniProtKB	Binding site	397	397	.	.	.	Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8605183,ECO:0000269|PubMed:9376357;Dbxref=PMID:8605183,PMID:9376357	
+P00924	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00924	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925	
+P00924	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925	
+P00924	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925	
+P00924	UniProtKB	Modified residue	324	324	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925	
+P00924	UniProtKB	Cross-link	60	60	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925	
+P00924	UniProtKB	Cross-link	243	243	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925	
+P00924	UniProtKB	Cross-link	358	358	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00924	UniProtKB	Mutagenesis	40	40	.	.	.	Note=Reduces activity by 99.9%25. S->A	
+P00924	UniProtKB	Mutagenesis	160	160	.	.	.	Note=Reduces activity by 99%25. H->A%2CF%2CN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11027610,ECO:0000269|PubMed:13678299;Dbxref=PMID:11027610,PMID:13678299	
+P00924	UniProtKB	Mutagenesis	169	169	.	.	.	Note=Reduces Kcat over 100000-fold. E->Q	
+P00924	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Reduces activity by 44%25. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:13678299;Dbxref=PMID:13678299	
+P00924	UniProtKB	Mutagenesis	212	212	.	.	.	Note=Reduces Kcat over 100000-fold. E->Q	
+P00924	UniProtKB	Mutagenesis	346	346	.	.	.	Note=Reduces Kcat over 100000-fold. Abolishes of the proton exchange reaction that initiates the enzymatic reaction. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8634301;Dbxref=PMID:8634301	
+P00924	UniProtKB	Sequence conflict	242	242	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00924	UniProtKB	Beta strand	5	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	18	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	29	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBH	
+P00924	UniProtKB	Helix	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	63	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	73	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	87	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBH	
+P00924	UniProtKB	Turn	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	108	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	130	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	152	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	158	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	161	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	169	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	180	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P48	
+P00924	UniProtKB	Helix	222	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Turn	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	243	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	250	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Turn	261	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	276	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	292	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	304	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Turn	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL2	
+P00924	UniProtKB	Beta strand	316	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Turn	322	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	328	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	341	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	347	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	353	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	369	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	383	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	394	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	404	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	421	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Beta strand	424	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	428	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+P00924	UniProtKB	Helix	434	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1	
+##sequence-region P32353 1 365
+P32353	UniProtKB	Chain	1	365	.	.	.	ID=PRO_0000117027;Note=Delta(7)-sterol 5(6)-desaturase	
+P32353	UniProtKB	Topological domain	1	92	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32353	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32353	UniProtKB	Topological domain	114	140	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32353	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32353	UniProtKB	Topological domain	162	242	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32353	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32353	UniProtKB	Topological domain	264	365	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32353	UniProtKB	Motif	200	204	.	.	.	Note=Histidine box-1	
+P32353	UniProtKB	Motif	213	217	.	.	.	Note=Histidine box-2	
+P32353	UniProtKB	Motif	288	292	.	.	.	Note=Histidine box-3	
+P32353	UniProtKB	Cross-link	324	324	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P32353	UniProtKB	Cross-link	344	344	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region Q12403 1 225
+Q12403	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12403	UniProtKB	Chain	24	225	.	.	.	ID=PRO_0000010410;Note=Protein ERP3	
+Q12403	UniProtKB	Topological domain	24	195	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12403	UniProtKB	Transmembrane	196	216	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12403	UniProtKB	Topological domain	217	225	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12403	UniProtKB	Domain	33	172	.	.	.	Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096	
+##sequence-region Q12284 1 196
+Q12284	UniProtKB	Chain	1	196	.	.	.	ID=PRO_0000001188;Note=FAD-linked sulfhydryl oxidase ERV2	
+Q12284	UniProtKB	Topological domain	1	12	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12284	UniProtKB	Transmembrane	13	35	.	.	.	Note=Helical%3B Signal-anchor;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12284	UniProtKB	Topological domain	36	196	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12284	UniProtKB	Domain	72	174	.	.	.	Note=ERV/ALR sulfhydryl oxidase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00654	
+Q12284	UniProtKB	Region	78	86	.	.	.	Note=FAD-binding	
+Q12284	UniProtKB	Region	153	174	.	.	.	Note=FAD-binding	
+Q12284	UniProtKB	Disulfide bond	121	124	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00654	
+Q12284	UniProtKB	Disulfide bond	150	167	.	.	.	Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00654,ECO:0000269|PubMed:11740506;Dbxref=PMID:11740506	
+Q12284	UniProtKB	Disulfide bond	176	178	.	.	.	Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00654,ECO:0000269|PubMed:11740506;Dbxref=PMID:11740506	
+Q12284	UniProtKB	Mutagenesis	121	121	.	.	.	Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584268;Dbxref=PMID:11584268	
+Q12284	UniProtKB	Mutagenesis	124	124	.	.	.	Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584268;Dbxref=PMID:11584268	
+Q12284	UniProtKB	Helix	75	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JR8	
+Q12284	UniProtKB	Helix	102	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JR8	
+Q12284	UniProtKB	Helix	122	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JR8	
+Q12284	UniProtKB	Helix	142	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JR8	
+Q12284	UniProtKB	Helix	170	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JR8	
+##sequence-region Q12480 1 344
+Q12480	UniProtKB	Nucleotide binding	284	312	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03071 1 99
+Q03071	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q03071	UniProtKB	Chain	2	99	.	.	.	ID=PRO_0000239644;Note=Elongin-C	
+Q03071	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q03071	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q03071	UniProtKB	Sequence conflict	64	64	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03071	UniProtKB	Beta strand	4	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2	
+Q03071	UniProtKB	Turn	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2	
+Q03071	UniProtKB	Beta strand	14	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2	
+Q03071	UniProtKB	Helix	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2	
+Q03071	UniProtKB	Helix	27	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2	
+Q03071	UniProtKB	Turn	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2	
+Q03071	UniProtKB	Beta strand	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2	
+Q03071	UniProtKB	Helix	51	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2	
+Q03071	UniProtKB	Helix	84	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2	
+##sequence-region Q04868 1 273
+Q04868	UniProtKB	Chain	1	273	.	.	.	ID=PRO_0000203355;Note=Elongator complex protein 6	
+Q04868	UniProtKB	Helix	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Beta strand	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Beta strand	30	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	43	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Beta strand	76	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	86	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Beta strand	103	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	112	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Turn	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	122	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Beta strand	143	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	154	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	163	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	171	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Beta strand	179	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Helix	202	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Beta strand	216	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Beta strand	234	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Beta strand	257	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+Q04868	UniProtKB	Beta strand	267	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J	
+##sequence-region P36039 1 253
+P36039	UniProtKB	Chain	1	253	.	.	.	ID=PRO_0000211411;Note=ER membrane protein complex subunit 3	
+P36039	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36039	UniProtKB	Transmembrane	126	146	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36039	UniProtKB	Transmembrane	176	196	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04406 1 187
+Q04406	UniProtKB	Chain	1	187	.	.	.	ID=PRO_0000223039;Note=Early meiotic induction protein 1	
+##sequence-region P32803 1 203
+P32803	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10713261,ECO:0000269|PubMed:8314797;Dbxref=PMID:10713261,PMID:8314797	
+P32803	UniProtKB	Chain	21	203	.	.	.	ID=PRO_0000010407;Note=Endosomal protein P24B	
+P32803	UniProtKB	Topological domain	21	172	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32803	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32803	UniProtKB	Topological domain	194	203	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32803	UniProtKB	Domain	30	118	.	.	.	Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096	
+P32803	UniProtKB	Mutagenesis	202	203	.	.	.	Note=No change in COPII-binding. LV->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11560939;Dbxref=PMID:11560939	
+P32803	UniProtKB	Sequence conflict	32	32	.	.	.	Note=C->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08299 1 606
+Q08299	UniProtKB	Chain	1	606	.	.	.	ID=PRO_0000084865;Note=Siderophore iron transporter ENB1	
+Q08299	UniProtKB	Topological domain	1	140	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	162	187	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	209	224	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	225	245	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	246	279	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	280	300	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	301	310	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	311	331	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	332	337	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	338	358	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	359	360	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	361	381	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	382	390	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	391	410	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	411	414	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	415	432	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	433	435	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	436	456	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	457	480	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	481	501	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	502	550	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Transmembrane	551	571	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08299	UniProtKB	Topological domain	572	606	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53938 1 366
+P53938	UniProtKB	Chain	1	366	.	.	.	ID=PRO_0000203446;Note=N-glycosylation protein EOS1	
+P53938	UniProtKB	Topological domain	1	136	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53938	UniProtKB	Transmembrane	137	157	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53938	UniProtKB	Topological domain	158	167	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53938	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53938	UniProtKB	Topological domain	189	195	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53938	UniProtKB	Transmembrane	196	216	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53938	UniProtKB	Topological domain	217	321	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53938	UniProtKB	Transmembrane	322	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53938	UniProtKB	Topological domain	343	366	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53938	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53938	UniProtKB	Glycosylation	104	104	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P16151 1 362
+P16151	UniProtKB	Chain	1	362	.	.	.	ID=PRO_0000087009;Note=Protein ERD1	
+P16151	UniProtKB	Topological domain	1	24	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16151	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16151	UniProtKB	Topological domain	46	84	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16151	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16151	UniProtKB	Topological domain	106	109	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16151	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16151	UniProtKB	Topological domain	131	362	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16151	UniProtKB	Domain	181	362	.	.	.	Note=EXS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00712	
+P16151	UniProtKB	Sequence conflict	168	168	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12452 1 347
+Q12452	UniProtKB	Chain	1	347	.	.	.	ID=PRO_0000054595;Note=3-keto-steroid reductase	
+Q12452	UniProtKB	Active site	202	202	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12452	UniProtKB	Modified residue	345	345	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q05359 1 219
+Q05359	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10713261;Dbxref=PMID:10713261	
+Q05359	UniProtKB	Chain	23	219	.	.	.	ID=PRO_0000010408;Note=Protein ERP1	
+Q05359	UniProtKB	Topological domain	23	186	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05359	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05359	UniProtKB	Topological domain	208	219	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05359	UniProtKB	Domain	32	131	.	.	.	Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096	
+Q05359	UniProtKB	Sequence conflict	152	152	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38748 1 585
+P38748	UniProtKB	Chain	1	585	.	.	.	ID=PRO_0000056337;Note=RING finger protein ETP1	
+P38748	UniProtKB	Zinc finger	240	280	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P38748	UniProtKB	Zinc finger	299	360	.	.	.	Note=UBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
+P38748	UniProtKB	Modified residue	376	376	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38748	UniProtKB	Cross-link	369	369	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38748	UniProtKB	Cross-link	410	410	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12872131,ECO:0000269|PubMed:14557538;Dbxref=PMID:12872131,PMID:14557538	
+P38748	UniProtKB	Cross-link	450	450	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38748	UniProtKB	Sequence conflict	558	558	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38071 1 380
+P38071	UniProtKB	Transit peptide	1	9	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8195160;Dbxref=PMID:8195160	
+P38071	UniProtKB	Chain	10	380	.	.	.	ID=PRO_0000160924;Note=Enoyl-[acyl-carrier-protein] reductase%2C mitochondrial	
+P38071	UniProtKB	Nucleotide binding	185	188	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3	
+P38071	UniProtKB	Nucleotide binding	208	210	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3	
+P38071	UniProtKB	Nucleotide binding	283	286	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3	
+P38071	UniProtKB	Nucleotide binding	308	310	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3	
+P38071	UniProtKB	Active site	73	73	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3	
+P38071	UniProtKB	Binding site	157	157	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3	
+P38071	UniProtKB	Binding site	373	373	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3	
+P38071	UniProtKB	Modified residue	339	339	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38071	UniProtKB	Mutagenesis	73	73	.	.	.	Note=0.1%25 of catalytic activity. No specific ARS1 binding. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12614607;Dbxref=PMID:12614607	
+P38071	UniProtKB	Sequence conflict	24	24	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P23776 1 448
+P23776	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23776	UniProtKB	Propeptide	20	40	.	.	.	ID=PRO_0000007892;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1900250,ECO:0000269|PubMed:2125957,ECO:0000269|PubMed:8488724,ECO:0000269|PubMed:9748433;Dbxref=PMID:1900250,PMID:2125957,PMID:8488724,PMID:9748433	
+P23776	UniProtKB	Chain	41	448	.	.	.	ID=PRO_0000007893;Note=Glucan 1%2C3-beta-glucosidase I/II	
+P23776	UniProtKB	Active site	232	232	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23776	UniProtKB	Active site	334	334	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23776	UniProtKB	Glycosylation	165	165	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730348;Dbxref=PMID:14730348	
+P23776	UniProtKB	Glycosylation	325	325	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730348;Dbxref=PMID:14730348	
+P23776	UniProtKB	Sequence conflict	41	41	.	.	.	Note=Y->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23776	UniProtKB	Sequence conflict	46	46	.	.	.	Note=H->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23776	UniProtKB	Sequence conflict	77	77	.	.	.	Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23776	UniProtKB	Beta strand	53	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Beta strand	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Turn	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	70	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	90	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	99	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	116	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Beta strand	129	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	152	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Beta strand	169	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	198	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Beta strand	224	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	240	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	248	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Beta strand	265	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	276	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Beta strand	289	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	302	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	309	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Beta strand	327	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Beta strand	339	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Turn	344	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Turn	373	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	383	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Turn	401	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Beta strand	405	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	421	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+P23776	UniProtKB	Helix	442	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P	
+##sequence-region P52911 1 562
+P52911	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Chain	23	562	.	.	.	ID=PRO_0000007894;Note=Glucan 1%2C3-beta-glucosidase 2	
+P52911	UniProtKB	Active site	254	254	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52911	UniProtKB	Active site	334	334	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52911	UniProtKB	Glycosylation	50	50	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	77	77	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	86	86	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	90	90	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	106	106	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	157	157	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	220	220	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	281	281	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	285	285	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	310	310	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	317	317	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	322	322	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	401	401	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	480	480	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52911	UniProtKB	Glycosylation	539	539	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04660 1 807
+Q04660	UniProtKB	Chain	1	807	.	.	.	ID=PRO_0000050968;Note=Ribosome biogenesis protein ERB1	
+Q04660	UniProtKB	Repeat	435	474	.	.	.	Note=WD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027	
+Q04660	UniProtKB	Repeat	483	523	.	.	.	Note=WD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027	
+Q04660	UniProtKB	Repeat	592	634	.	.	.	Note=WD 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027	
+Q04660	UniProtKB	Repeat	637	675	.	.	.	Note=WD 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027	
+Q04660	UniProtKB	Repeat	678	717	.	.	.	Note=WD 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027	
+Q04660	UniProtKB	Repeat	721	760	.	.	.	Note=WD 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027	
+Q04660	UniProtKB	Repeat	776	807	.	.	.	Note=WD 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027	
+Q04660	UniProtKB	Region	265	383	.	.	.	Note=Required for interaction with NOP7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448671;Dbxref=PMID:18448671	
+Q04660	UniProtKB	Region	383	419	.	.	.	Note=Required for interaction with YTM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448671;Dbxref=PMID:18448671	
+Q04660	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956	
+Q04660	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q04660	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q04660	UniProtKB	Modified residue	146	146	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04660	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04660	UniProtKB	Modified residue	418	418	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q04660	UniProtKB	Cross-link	127	127	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q04660	UniProtKB	Mutagenesis	465	465	.	.	.	Note=Disrupts the interaction with YTM1 and cannot sustain growth. E->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26476442,ECO:0000269|PubMed:26657628;Dbxref=PMID:26476442,PMID:26657628	
+Q04660	UniProtKB	Mutagenesis	470	470	.	.	.	Note=Weakens the interaction with YTM1%2C impairs pre-rRNA processing and leads to a deficiency in 60S ribosomal subunits. Disrupts the interaction with YTM1 and cannot sustain growth%3B when associated with R-790. R->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26476442,ECO:0000269|PubMed:26657628;Dbxref=PMID:26476442,PMID:26657628	
+Q04660	UniProtKB	Mutagenesis	790	790	.	.	.	Note=Disrupts the interaction with YTM1 and cannot sustain growth%3B when associated with E-470. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26657628;Dbxref=PMID:26657628	
+Q04660	UniProtKB	Helix	419	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	428	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	440	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	451	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	459	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Turn	466	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	471	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	488	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	502	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	509	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Helix	520	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	573	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Helix	580	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Turn	584	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	587	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	599	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	606	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Helix	617	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	620	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Helix	626	628	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	630	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	642	647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	649	660	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	662	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Turn	667	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	671	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	683	688	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	692	699	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	704	708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Turn	709	711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	716	719	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	726	731	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	733	742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	747	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	756	759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	763	770	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	781	786	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	788	791	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	793	797	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+Q04660	UniProtKB	Beta strand	802	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A	
+##sequence-region P05453 1 685
+P05453	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P05453	UniProtKB	Chain	2	685	.	.	.	ID=PRO_0000091482;Note=Eukaryotic peptide chain release factor GTP-binding subunit	
+P05453	UniProtKB	Domain	258	484	.	.	.	Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P05453	UniProtKB	Nucleotide binding	267	274	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05453	UniProtKB	Nucleotide binding	344	348	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05453	UniProtKB	Nucleotide binding	406	409	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05453	UniProtKB	Region	2	239	.	.	.	Note=Interaction with PAB1	
+P05453	UniProtKB	Region	5	135	.	.	.	Note=Prion domain (PrD)	
+P05453	UniProtKB	Region	139	249	.	.	.	Note=Charged	
+P05453	UniProtKB	Region	267	274	.	.	.	Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P05453	UniProtKB	Region	323	327	.	.	.	Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P05453	UniProtKB	Region	344	347	.	.	.	Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P05453	UniProtKB	Region	406	409	.	.	.	Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P05453	UniProtKB	Region	448	450	.	.	.	Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P05453	UniProtKB	Site	273	273	.	.	.	Note=Interacts with GTP/GDP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05453	UniProtKB	Site	407	407	.	.	.	Note=Interacts with GTP/GDP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05453	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P05453	UniProtKB	Modified residue	571	571	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P05453	UniProtKB	Sequence conflict	53	53	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P42222 1 437
+P42222	UniProtKB	Chain	1	437	.	.	.	ID=PRO_0000134065;Note=Enolase-related protein 3	
+P42222	UniProtKB	Region	373	376	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42222	UniProtKB	Active site	212	212	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42222	UniProtKB	Active site	346	346	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42222	UniProtKB	Metal binding	247	247	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42222	UniProtKB	Metal binding	296	296	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42222	UniProtKB	Metal binding	321	321	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42222	UniProtKB	Binding site	160	160	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42222	UniProtKB	Binding site	169	169	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42222	UniProtKB	Binding site	296	296	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42222	UniProtKB	Binding site	321	321	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42222	UniProtKB	Binding site	397	397	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38140 1 529
+P38140	UniProtKB	Chain	1	529	.	.	.	ID=PRO_0000114993;Note=Transcription activator of gluconeogenesis ERT1	
+P38140	UniProtKB	Domain	408	480	.	.	.	Note=PAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00140	
+P38140	UniProtKB	DNA binding	40	68	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P27882 1 189
+P27882	UniProtKB	Chain	1	189	.	.	.	ID=PRO_0000001187;Note=Mitochondrial FAD-linked sulfhydryl oxidase ERV1	
+P27882	UniProtKB	Domain	83	183	.	.	.	Note=ERV/ALR sulfhydryl oxidase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00654	
+P27882	UniProtKB	Region	166	183	.	.	.	Note=FAD-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27882	UniProtKB	Disulfide bond	130	133	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00654	
+P27882	UniProtKB	Disulfide bond	159	176	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00654	
+P27882	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Reduces catalytic activity 3-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008	
+P27882	UniProtKB	Mutagenesis	33	33	.	.	.	Note=Reduces catalytic activity 2-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008	
+P27882	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008	
+P27882	UniProtKB	Mutagenesis	133	133	.	.	.	Note=Loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008	
+P27882	UniProtKB	Mutagenesis	159	159	.	.	.	Note=Reduces catalytic activity 3.3-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008	
+P27882	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Reduces catalytic activity 2.6-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008	
+P27882	UniProtKB	Beta strand	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E0I	
+P27882	UniProtKB	Beta strand	26	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E0I	
+P27882	UniProtKB	Helix	36	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E0I	
+P27882	UniProtKB	Turn	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E0I	
+P27882	UniProtKB	Helix	87	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y	
+P27882	UniProtKB	Helix	111	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y	
+P27882	UniProtKB	Helix	131	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y	
+P27882	UniProtKB	Helix	151	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y	
+P27882	UniProtKB	Helix	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y	
+P27882	UniProtKB	Helix	179	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y	
+##sequence-region P39727 1 415
+P39727	UniProtKB	Chain	1	415	.	.	.	ID=PRO_0000202419;Note=ER-derived vesicles protein ERV46	
+P39727	UniProtKB	Topological domain	1	24	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39727	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39727	UniProtKB	Topological domain	46	376	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39727	UniProtKB	Transmembrane	377	397	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39727	UniProtKB	Topological domain	398	415	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39727	UniProtKB	Motif	402	403	.	.	.	Note=Phenylalanine-tyrosine motif	
+##sequence-region P19097 1 1887
+P19097	UniProtKB	Chain	1	1887	.	.	.	ID=PRO_0000180287;Note=Fatty acid synthase subunit alpha	
+P19097	UniProtKB	Domain	145	220	.	.	.	Note=Carrier;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258	
+P19097	UniProtKB	Region	675	874	.	.	.	Note=Beta-ketoacyl reductase	
+P19097	UniProtKB	Region	1149	1363	.	.	.	Note=Beta-ketoacyl synthase	
+P19097	UniProtKB	Region	1772	1774	.	.	.	Note=Acetyl-CoA binding	
+P19097	UniProtKB	Region	1817	1833	.	.	.	Note=Acetyl-CoA binding	
+P19097	UniProtKB	Region	1841	1844	.	.	.	Note=Acetyl-CoA binding	
+P19097	UniProtKB	Region	1871	1873	.	.	.	Note=Acetyl-CoA binding	
+P19097	UniProtKB	Active site	1305	1305	.	.	.	Note=For beta-ketoacyl synthase activity	
+P19097	UniProtKB	Metal binding	1772	1772	.	.	.	Note=Magnesium	
+P19097	UniProtKB	Metal binding	1773	1773	.	.	.	Note=Magnesium%3B via carbonyl oxygen	
+P19097	UniProtKB	Metal binding	1774	1774	.	.	.	Note=Magnesium	
+P19097	UniProtKB	Metal binding	1872	1872	.	.	.	Note=Magnesium	
+P19097	UniProtKB	Metal binding	1873	1873	.	.	.	Note=Magnesium%3B via carbonyl oxygen	
+P19097	UniProtKB	Binding site	1798	1798	.	.	.	Note=Acetyl-CoA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086	
+P19097	UniProtKB	Binding site	1808	1808	.	.	.	Note=Acetyl-CoA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086	
+P19097	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P19097	UniProtKB	Modified residue	180	180	.	.	.	Note=O-(pantetheine 4'-phosphoryl)serine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00258,ECO:0000269|PubMed:17431182;Dbxref=PMID:17431182	
+P19097	UniProtKB	Modified residue	523	523	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19097	UniProtKB	Modified residue	958	958	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P19097	UniProtKB	Modified residue	1440	1440	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P19097	UniProtKB	Cross-link	37	37	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P19097	UniProtKB	Mutagenesis	1250	1250	.	.	.	Note=Cerulenin-resistance. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041367;Dbxref=PMID:8041367	
+P19097	UniProtKB	Mutagenesis	1769	1769	.	.	.	Note=Does not affect oligomerization%3B when associated with S-1771 and L-1773 or S-1771%3B L-1773%3B S-1879 and E-1881. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086	
+P19097	UniProtKB	Mutagenesis	1770	1770	.	.	.	Note=Loss of transferase activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086	
+P19097	UniProtKB	Mutagenesis	1771	1771	.	.	.	Note=Does not affect oligomerization but lacks transferase activity%3B when associated with D-1769 and L-1773 or D-1769%3B L-1773%3B S-1879 and E-1881. V->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086	
+P19097	UniProtKB	Mutagenesis	1772	1772	.	.	.	Note=Loss of transferase activity%3B when associated with S-1774. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086	
+P19097	UniProtKB	Mutagenesis	1773	1773	.	.	.	Note=Does not affect oligomerization but lacks transferase activity%3B when associated with D-1769 and S-1771 or D-1769%3B S-1771%3B S-1879 and E-1881. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086	
+P19097	UniProtKB	Mutagenesis	1774	1774	.	.	.	Note=Loss of transferase activity%3B when associated with S-1772. E->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086	
+P19097	UniProtKB	Mutagenesis	1841	1841	.	.	.	Note=Loss off transferase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086	
+P19097	UniProtKB	Mutagenesis	1879	1879	.	.	.	Note=Does not affect oligomerization but lacks transferase activity%3B when associated with D-1769%3B S-1771%3B L-1773 and E-1881. V->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086	
+P19097	UniProtKB	Mutagenesis	1881	1881	.	.	.	Note=Does not affect oligomerization but lacks transferase activity%3B when associated with D-1769%3B S-1771%3B L-1773 and S-1879. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086	
+P19097	UniProtKB	Sequence conflict	310	310	.	.	.	Note=G->GTTGTGG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19097	UniProtKB	Sequence conflict	594	594	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19097	UniProtKB	Sequence conflict	941	1019	.	.	.	Note=AKLRKELVETSEVRKAVSIETALEHKVVNGNSADAAYAQVEIQPRANIQLDFPELKPYKQVKQIAPAELEGLLDLERVI->CLNCVKSWLKLLKLERQFPSKLLWSIRLSMAIALMLHMLKSKFNQELTFNWTSQNRNHTNRLNKLLPLSLRVCWIWKELF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19097	UniProtKB	Sequence conflict	1036	1041	.	.	.	Note=RWEMEA->KMGNGS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19097	UniProtKB	Sequence conflict	1408	1408	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19097	UniProtKB	Sequence conflict	1671	1671	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19097	UniProtKB	Helix	3	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	28	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	42	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	52	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	66	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	85	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	147	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	158	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	172	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	180	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	206	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	223	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	243	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	261	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ML8	
+P19097	UniProtKB	Helix	280	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	329	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	356	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	384	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	396	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	400	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	405	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	430	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	445	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	460	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	464	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	497	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	509	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	522	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	605	607	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	609	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	626	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	637	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	649	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	653	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	677	682	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	685	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	688	698	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	702	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	712	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	731	736	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	742	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	756	759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	766	770	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	781	783	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	786	795	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	797	811	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	812	814	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	820	826	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	839	845	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	846	848	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	849	855	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	859	861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	862	869	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	885	889	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	898	906	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	907	909	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	911	919	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	922	927	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	930	932	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	933	935	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	936	968	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	971	976	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	998	1004	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1007	1009	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	1010	1012	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1015	1017	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1019	1028	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1033	1042	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1047	1056	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1059	1067	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1070	1077	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	1078	1080	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1086	1088	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1089	1099	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1101	1105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1108	1111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1118	1126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1134	1136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1138	1148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1149	1151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1152	1156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	1158	1160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1163	1167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1172	1179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1185	1187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	1195	1199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1202	1207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1210	1225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1231	1233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1234	1237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1240	1242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1243	1245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1248	1251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1254	1261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	1262	1267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1274	1278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1282	1290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1304	1306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1307	1320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1325	1333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1337	1345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1352	1357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1362	1364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1381	1389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1390	1396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1402	1410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1424	1429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1441	1443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1445	1474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1483	1508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	1512	1515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1517	1519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1521	1527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	1528	1530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1533	1535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1536	1540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1547	1564	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1572	1575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1578	1581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1585	1587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1588	1600	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1612	1614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1616	1620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1638	1645	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	1646	1648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1649	1656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1659	1662	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1667	1693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1708	1710	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1711	1716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1726	1728	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1730	1732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Turn	1735	1739	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Helix	1742	1745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P19097	UniProtKB	Beta strand	1769	1775	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+P19097	UniProtKB	Helix	1776	1778	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+P19097	UniProtKB	Helix	1784	1790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+P19097	UniProtKB	Helix	1793	1800	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+P19097	UniProtKB	Beta strand	1802	1804	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+P19097	UniProtKB	Helix	1805	1823	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+P19097	UniProtKB	Beta strand	1837	1842	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+P19097	UniProtKB	Beta strand	1845	1851	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+P19097	UniProtKB	Helix	1853	1860	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+P19097	UniProtKB	Turn	1861	1863	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+P19097	UniProtKB	Beta strand	1866	1873	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+P19097	UniProtKB	Beta strand	1875	1885	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS	
+##sequence-region Q12283 1 360
+Q12283	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12283	UniProtKB	Chain	25	360	.	.	.	ID=PRO_0000257811;Note=Malonyl CoA-acyl carrier protein transacylase%2C mitochondrial	
+Q12283	UniProtKB	Active site	105	105	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12283	UniProtKB	Active site	235	235	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53917 1 953
+P53917	UniProtKB	Chain	1	953	.	.	.	ID=PRO_0000087190;Note=Factor arrest protein 11	
+P53917	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P53917	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53917	UniProtKB	Modified residue	524	524	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53917	UniProtKB	Modified residue	527	527	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53917	UniProtKB	Modified residue	528	528	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P21268 1 830
+P21268	UniProtKB	Chain	1	830	.	.	.	ID=PRO_0000055910;Note=Cyclin-dependent kinase inhibitor FAR1	
+P21268	UniProtKB	Zinc finger	202	252	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P21268	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21268	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P21268	UniProtKB	Modified residue	114	114	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P21268	UniProtKB	Modified residue	306	306	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P21268	UniProtKB	Natural variant	87	87	.	.	.	Note=In FAR1-22P%3B induces cell cycle arrest in the absence of alpha-factor. S->P	
+P21268	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Prevents cell cycle-dependent degradation of FAR1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632750;Dbxref=PMID:9632750	
+P21268	UniProtKB	Mutagenesis	306	306	.	.	.	Note=Abolishes G1 arrest function. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632750;Dbxref=PMID:9632750	
+P21268	UniProtKB	Sequence conflict	20	20	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21268	UniProtKB	Sequence conflict	568	568	.	.	.	Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43592 1 221
+P43592	UniProtKB	Chain	1	221	.	.	.	ID=PRO_0000087192;Note=Factor arrest protein 7	
+P43592	UniProtKB	Compositional bias	11	22	.	.	.	Note=Poly-Gln	
+##sequence-region P15646 1 327
+P15646	UniProtKB	Chain	1	327	.	.	.	ID=PRO_0000148527;Note=rRNA 2'-O-methyltransferase fibrillarin	
+P15646	UniProtKB	Region	8	83	.	.	.	Note=RGG-box	
+P15646	UniProtKB	Region	22	42	.	.	.	Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15646	UniProtKB	Region	58	75	.	.	.	Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15646	UniProtKB	Region	179	180	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15646	UniProtKB	Region	198	199	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15646	UniProtKB	Region	223	224	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15646	UniProtKB	Region	243	246	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15646	UniProtKB	Region	281	313	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15646	UniProtKB	Compositional bias	6	83	.	.	.	Note=DMA/Gly-rich	
+P15646	UniProtKB	Modified residue	16	16	.	.	.	Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	16	16	.	.	.	Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	22	22	.	.	.	Note=Omega-N-methylarginine%3B by HMT1;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	30	30	.	.	.	Note=Asymmetric dimethylarginine%3B by HMT1;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	34	34	.	.	.	Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	34	34	.	.	.	Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	40	40	.	.	.	Note=Omega-N-methylarginine%3B by HMT1;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	48	48	.	.	.	Note=Asymmetric dimethylarginine%3B by HMT1;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	52	52	.	.	.	Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	52	52	.	.	.	Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	58	58	.	.	.	Note=Omega-N-methylarginine%3B by HMT1;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	70	70	.	.	.	Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	70	70	.	.	.	Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	73	73	.	.	.	Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	73	73	.	.	.	Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	81	81	.	.	.	Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Modified residue	81	81	.	.	.	Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332	
+P15646	UniProtKB	Cross-link	150	150	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P15646	UniProtKB	Mutagenesis	87	87	.	.	.	Note=In nop1.3%3B thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature%3B when associated with G-103%3B V-175 and S-219. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239	
+P15646	UniProtKB	Mutagenesis	103	103	.	.	.	Note=In nop1.3%3B thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature%3B when associated with D-87%3B V-175 and S-219. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239	
+P15646	UniProtKB	Mutagenesis	175	175	.	.	.	Note=In nop1.3%3B thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature%3B when associated with D-87%3B G-103 and S-219. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239	
+P15646	UniProtKB	Mutagenesis	219	219	.	.	.	Note=In nop1.3%3B thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature%3B when associated with D-87%3B G-103 and V-175. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239	
+##sequence-region Q03034 1 503
+Q03034	UniProtKB	Chain	1	503	.	.	.	ID=PRO_0000157387;Note=Ferulic acid decarboxylase 1	
+Q03034	UniProtKB	Region	170	175	.	.	.	Note=prenyl-FMN binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754	
+Q03034	UniProtKB	Region	192	193	.	.	.	Note=prenyl-FMN binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754	
+Q03034	UniProtKB	Active site	285	285	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000305;evidence=ECO:0000250|UniProtKB:A2QHE5,ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000305|PubMed:25862228;Dbxref=PMID:25862228	
+Q03034	UniProtKB	Metal binding	170	170	.	.	.	Note=Manganese;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754	
+Q03034	UniProtKB	Metal binding	193	193	.	.	.	Note=Manganese;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754	
+Q03034	UniProtKB	Metal binding	236	236	.	.	.	Note=Manganese;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754	
+Q03034	UniProtKB	Binding site	236	236	.	.	.	Note=prenyl-FMN;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754	
+Q03034	UniProtKB	Binding site	394	394	.	.	.	Note=prenyl-FMN;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754	
+Q03034	UniProtKB	Mutagenesis	285	285	.	.	.	Note=Abolishes catalytic activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25862228;Dbxref=PMID:25862228	
+Q03034	UniProtKB	Turn	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	10	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	35	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	61	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	82	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	96	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	126	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	152	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	158	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	169	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	180	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	193	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Turn	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	210	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	220	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	236	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	249	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	254	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	265	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	296	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	312	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	325	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	330	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	349	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	356	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	362	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	369	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	379	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Turn	395	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	401	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	414	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Turn	427	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	431	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	436	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	444	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	451	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Beta strand	459	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	467	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	481	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+Q03034	UniProtKB	Helix	487	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC	
+##sequence-region P29704 1 444
+P29704	UniProtKB	Chain	1	444	.	.	.	ID=PRO_0000067454;Note=Squalene synthase	
+P29704	UniProtKB	Transmembrane	291	311	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29704	UniProtKB	Transmembrane	421	441	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29704	UniProtKB	Sequence conflict	48	48	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29704	UniProtKB	Sequence conflict	286	286	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29704	UniProtKB	Sequence conflict	320	320	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29704	UniProtKB	Sequence conflict	330	330	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29704	UniProtKB	Sequence conflict	429	429	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P26793 1 382
+P26793	UniProtKB	Chain	1	382	.	.	.	ID=PRO_0000154038;Note=Flap endonuclease 1	
+P26793	UniProtKB	Region	1	105	.	.	.	Note=N-domain	
+P26793	UniProtKB	Region	120	251	.	.	.	Note=I-domain	
+P26793	UniProtKB	Region	339	347	.	.	.	Note=Interaction with PCNA;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Metal binding	34	34	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Metal binding	87	87	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Metal binding	156	156	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Metal binding	158	158	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Metal binding	177	177	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Metal binding	179	179	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Metal binding	231	231	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Binding site	47	47	.	.	.	Note=DNA substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Binding site	71	71	.	.	.	Note=DNA substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Binding site	156	156	.	.	.	Note=DNA substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Binding site	229	229	.	.	.	Note=DNA substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Binding site	231	231	.	.	.	Note=DNA substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140	
+P26793	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Deficient in double and single flap endonuclease cleavage and exonucleolytic cleavage. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16837458;Dbxref=PMID:16837458	
+P26793	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Deficient in exonuclease and gap endonuclease activities%2C but retains almost all of its flap endonuclease activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17138563;Dbxref=PMID:17138563	
+P26793	UniProtKB	Mutagenesis	240	240	.	.	.	Note=Can only cleave double-flap structures with a 3' 1-nucleotide tail. Has no exonuclease activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11825897;Dbxref=PMID:11825897	
+P26793	UniProtKB	Mutagenesis	346	347	.	.	.	Note=Reduces interaction with POL30 more than 100 fold. FF->GA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899134;Dbxref=PMID:10899134	
+##sequence-region P40988 1 552
+P40988	UniProtKB	Chain	1	552	.	.	.	ID=PRO_0000087233;Note=Low-affinity Fe(2+) transport protein	
+P40988	UniProtKB	Topological domain	1	97	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Topological domain	119	225	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Transmembrane	226	246	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Topological domain	247	271	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Transmembrane	272	292	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Topological domain	293	354	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Transmembrane	355	375	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Topological domain	376	383	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Transmembrane	384	404	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Topological domain	405	465	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Transmembrane	466	486	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Topological domain	487	493	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Transmembrane	494	514	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Topological domain	515	552	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40988	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40988	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40988	UniProtKB	Cross-link	39	39	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40988	UniProtKB	Sequence conflict	283	283	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40988	UniProtKB	Sequence conflict	441	441	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40988	UniProtKB	Sequence conflict	450	450	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53918 1 673
+P53918	UniProtKB	Chain	1	673	.	.	.	ID=PRO_0000211405;Note=Uncharacterized transporter ESBP6	
+P53918	UniProtKB	Topological domain	1	208	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Topological domain	230	255	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Transmembrane	256	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Topological domain	277	277	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Transmembrane	278	298	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Topological domain	299	315	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Transmembrane	316	336	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Topological domain	337	339	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Transmembrane	340	360	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Topological domain	361	372	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Topological domain	394	426	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Transmembrane	427	447	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Topological domain	448	504	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Transmembrane	505	525	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Topological domain	526	549	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Transmembrane	550	570	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Topological domain	571	584	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Transmembrane	585	605	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Topological domain	606	673	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53918	UniProtKB	Modified residue	112	112	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53918	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53918	UniProtKB	Modified residue	637	637	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53918	UniProtKB	Glycosylation	230	230	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Glycosylation	471	471	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53918	UniProtKB	Glycosylation	492	492	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08119 1 714
+Q08119	UniProtKB	Chain	1	714	.	.	.	ID=PRO_0000227694;Note=Protein ESC8	
+##sequence-region P17214 1 699
+P17214	UniProtKB	Chain	1	699	.	.	.	ID=PRO_0000087072;Note=Telomere elongation protein EST1	
+P17214	UniProtKB	Sequence conflict	49	49	.	.	.	Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17214	UniProtKB	Sequence conflict	85	85	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17214	UniProtKB	Sequence conflict	287	287	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17214	UniProtKB	Sequence conflict	351	351	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17214	UniProtKB	Sequence conflict	535	535	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17214	UniProtKB	Sequence conflict	571	571	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17214	UniProtKB	Sequence conflict	579	579	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17214	UniProtKB	Sequence conflict	582	582	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17214	UniProtKB	Sequence conflict	665	665	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08822 1 631
+Q08822	UniProtKB	Domain	591	620	.	.	.	Note=4Fe-4S ferredoxin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00711	
+Q08822	UniProtKB	Nucleotide binding	65	79	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08822	UniProtKB	Metal binding	574	574	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08822	UniProtKB	Metal binding	600	600	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08822	UniProtKB	Metal binding	603	603	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08822	UniProtKB	Metal binding	606	606	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P35731 1 278
+P35731	UniProtKB	Chain	1	278	.	.	.	ID=PRO_0000054872;Note=3-oxoacyl-[acyl-carrier-protein] reductase	
+P35731	UniProtKB	Nucleotide binding	8	32	.	.	.	Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35731	UniProtKB	Active site	198	198	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001	
+P35731	UniProtKB	Binding site	183	183	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35731	UniProtKB	Beta strand	2	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	15	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Beta strand	30	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	38	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Beta strand	60	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	72	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Beta strand	79	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Beta strand	91	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	100	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Beta strand	108	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	134	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	146	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	167	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Beta strand	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FD3	
+P35731	UniProtKB	Beta strand	177	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Beta strand	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	196	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Beta strand	222	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+P35731	UniProtKB	Helix	246	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HBG	
+P35731	UniProtKB	Helix	260	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA	
+##sequence-region P38913 1 306
+P38913	UniProtKB	Chain	1	306	.	.	.	ID=PRO_0000100691;Note=FAD synthase	
+P38913	UniProtKB	Helix	3	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	25	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Turn	44	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Beta strand	51	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	64	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Beta strand	102	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	114	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Beta strand	129	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	144	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Beta strand	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Beta strand	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Beta strand	177	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Beta strand	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Turn	193	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	199	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	215	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Turn	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	248	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Turn	255	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	274	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Turn	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Helix	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+P38913	UniProtKB	Turn	299	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI	
+##sequence-region P38224 1 298
+P38224	UniProtKB	Chain	1	298	.	.	.	ID=PRO_0000087242;Note=Factor-induced gene 1 protein	
+P38224	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38224	UniProtKB	Transmembrane	163	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38224	UniProtKB	Transmembrane	195	215	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38224	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38224	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38224	UniProtKB	Modified residue	293	293	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38224	UniProtKB	Modified residue	296	296	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38224	UniProtKB	Natural variant	1	5	.	.	.	Note=In strain: CLIB 556 haplotype Ha1 and CLIB 630. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38224	UniProtKB	Natural variant	153	153	.	.	.	Note=In strain: CLIB 413 haplotype Ha1. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38224	UniProtKB	Natural variant	203	203	.	.	.	Note=In strain: CLIB 630. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38224	UniProtKB	Natural variant	204	204	.	.	.	Note=In strain: K1. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38224	UniProtKB	Natural variant	220	220	.	.	.	Note=In strain: CLIB 413 haplotype Ha2. A->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38224	UniProtKB	Natural variant	223	223	.	.	.	Note=In strain: CLIB 630. R->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38224	UniProtKB	Natural variant	236	236	.	.	.	Note=In strain: CLIB 219. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P38224	UniProtKB	Natural variant	241	241	.	.	.	Note=In strain: CLIB 388 haplotype Ha2. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+##sequence-region P40020 1 876
+P40020	UniProtKB	Chain	1	876	.	.	.	ID=PRO_0000058446;Note=Factor interacting with REF2	
+P40020	UniProtKB	Compositional bias	655	683	.	.	.	Note=Ser-rich	
+P40020	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40020	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40020	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40020	UniProtKB	Natural variant	614	614	.	.	.	Note=In strain: ATCC 200060 / W303. P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9236779;Dbxref=PMID:9236779	
+##sequence-region Q08906 1 153
+Q08906	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08906	UniProtKB	Chain	19	130	.	.	.	ID=PRO_0000021267;Note=Facilitator of iron transport 2	
+Q08906	UniProtKB	Propeptide	131	153	.	.	.	ID=PRO_0000021268;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08906	UniProtKB	Compositional bias	5	106	.	.	.	Note=Thr-rich	
+Q08906	UniProtKB	Compositional bias	111	129	.	.	.	Note=Poly-Ser	
+Q08906	UniProtKB	Lipidation	130	130	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08906	UniProtKB	Glycosylation	92	92	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P12385 1 437
+P12385	UniProtKB	Chain	1	437	.	.	.	ID=PRO_0000143167;Note=Eukaryotic peptide chain release factor subunit 1	
+P12385	UniProtKB	Modified residue	182	182	.	.	.	Note=N5-methylglutamine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15509572,ECO:0000269|PubMed:16321977;Dbxref=PMID:15509572,PMID:16321977	
+P12385	UniProtKB	Modified residue	421	421	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12385	UniProtKB	Cross-link	331	331	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P12385	UniProtKB	Sequence conflict	41	41	.	.	.	Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12385	UniProtKB	Sequence conflict	41	41	.	.	.	Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40030 1 148
+P40030	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000193908;Note=Ergosterol biosynthetic protein 28	
+P40030	UniProtKB	Topological domain	1	25	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40030	UniProtKB	Transmembrane	26	46	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40030	UniProtKB	Topological domain	47	92	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40030	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40030	UniProtKB	Topological domain	114	120	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40030	UniProtKB	Transmembrane	121	136	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40030	UniProtKB	Topological domain	137	148	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03103 1 563
+Q03103	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03103	UniProtKB	Chain	19	563	.	.	.	ID=PRO_0000008429;Note=Endoplasmic oxidoreductin-1	
+Q03103	UniProtKB	Active site	352	352	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Active site	355	355	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Binding site	187	187	.	.	.	Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Binding site	189	189	.	.	.	Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Binding site	200	200	.	.	.	Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Binding site	228	228	.	.	.	Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Binding site	231	231	.	.	.	Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Binding site	260	260	.	.	.	Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Glycosylation	21	21	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03103	UniProtKB	Glycosylation	35	35	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03103	UniProtKB	Glycosylation	53	53	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03103	UniProtKB	Glycosylation	130	130	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03103	UniProtKB	Glycosylation	342	342	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03103	UniProtKB	Glycosylation	425	425	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03103	UniProtKB	Glycosylation	458	458	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03103	UniProtKB	Glycosylation	468	468	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03103	UniProtKB	Glycosylation	491	491	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03103	UniProtKB	Disulfide bond	90	349	.	.	.	Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1RP4,ECO:0000244|PDB:1RQ1,ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Disulfide bond	100	105	.	.	.	Note=Redox-active;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1RP4,ECO:0000244|PDB:1RQ1,ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Disulfide bond	143	166	.	.	.	Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1RP4,ECO:0000244|PDB:1RQ1,ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Disulfide bond	150	295	.	.	.	Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1RP4,ECO:0000244|PDB:1RQ1,ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Disulfide bond	352	355	.	.	.	Note=Redox-active;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1RP4,ECO:0000244|PDB:1RQ1,ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Mutagenesis	90	90	.	.	.	Note=No effect. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10982384,ECO:0000269|PubMed:17448992;Dbxref=PMID:10982384,PMID:17448992	
+Q03103	UniProtKB	Mutagenesis	100	100	.	.	.	Note=Impairs the capture of mixed-disulfide with PDI1 thereby blocking its function. Loss of activity%3B when associated with A-105. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10982384,ECO:0000269|PubMed:17448992;Dbxref=PMID:10982384,PMID:17448992	
+Q03103	UniProtKB	Mutagenesis	105	105	.	.	.	Note=Loss of activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10982384,ECO:0000269|PubMed:17448992;Dbxref=PMID:10982384,PMID:17448992	
+Q03103	UniProtKB	Mutagenesis	143	143	.	.	.	Note=No effect%3B when associated with A-166. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17448992;Dbxref=PMID:17448992	
+Q03103	UniProtKB	Mutagenesis	150	150	.	.	.	Note=Loss of regulatory disulfide bond and strongly increased activity towards PDI%3B when associated with A-295. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17448992;Dbxref=PMID:17448992	
+Q03103	UniProtKB	Mutagenesis	166	166	.	.	.	Note=No effect%3B when associated with A-143. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17448992;Dbxref=PMID:17448992	
+Q03103	UniProtKB	Mutagenesis	208	208	.	.	.	Note=No effect. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10982384;Dbxref=PMID:10982384	
+Q03103	UniProtKB	Mutagenesis	229	229	.	.	.	Note=In ERO1-1%3B induces defective folding of disulfide proteins. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408	
+Q03103	UniProtKB	Mutagenesis	231	231	.	.	.	Note=In ERO1-2%3B induces defective folding of disulfide proteins. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9659914;Dbxref=PMID:9659914	
+Q03103	UniProtKB	Mutagenesis	295	295	.	.	.	Note=Loss of regulatory disulfide bond and strongly increased activity towards PDI%3B when associated with A-150. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17448992;Dbxref=PMID:17448992	
+Q03103	UniProtKB	Mutagenesis	349	349	.	.	.	Note=Does not affect activity but increases by twofold the amount of protein found in mixed disulfide with PDI1 or MPD2. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10982384;Dbxref=PMID:10982384	
+Q03103	UniProtKB	Mutagenesis	352	352	.	.	.	Note=Loss of activity. Prevents its reoxidation thereby blocking its function. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10982384,ECO:0000269|PubMed:17448992;Dbxref=PMID:10982384,PMID:17448992	
+Q03103	UniProtKB	Mutagenesis	355	355	.	.	.	Note=Loss of activity. Prevents its reoxidation thereby blocking its function. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10982384,ECO:0000269|PubMed:17448992;Dbxref=PMID:10982384,PMID:17448992	
+Q03103	UniProtKB	Sequence conflict	555	555	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03103	UniProtKB	Helix	56	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Turn	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Beta strand	80	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Beta strand	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Beta strand	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RP4	
+Q03103	UniProtKB	Turn	102	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Beta strand	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NVJ	
+Q03103	UniProtKB	Helix	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RP4	
+Q03103	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	122	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Turn	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Beta strand	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RQ1	
+Q03103	UniProtKB	Beta strand	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RQ1	
+Q03103	UniProtKB	Helix	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Turn	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RP4	
+Q03103	UniProtKB	Beta strand	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RP4	
+Q03103	UniProtKB	Helix	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Beta strand	176	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	193	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	216	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Beta strand	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Turn	245	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	254	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Turn	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	265	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	297	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	316	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Turn	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	330	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	347	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	353	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	381	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+Q03103	UniProtKB	Helix	393	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31	
+##sequence-region P39704 1 215
+P39704	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39704	UniProtKB	Chain	26	215	.	.	.	ID=PRO_0000010409;Note=Protein ERP2	
+P39704	UniProtKB	Topological domain	26	182	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39704	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39704	UniProtKB	Topological domain	204	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39704	UniProtKB	Domain	41	123	.	.	.	Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096	
+##sequence-region P17261 1 260
+P17261	UniProtKB	Chain	1	260	.	.	.	ID=PRO_0000205519;Note=Cystine transporter	
+P17261	UniProtKB	Transmembrane	7	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17261	UniProtKB	Transmembrane	40	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17261	UniProtKB	Transmembrane	81	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17261	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17261	UniProtKB	Transmembrane	151	175	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17261	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17261	UniProtKB	Transmembrane	227	247	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17261	UniProtKB	Domain	1	67	.	.	.	Note=PQ-loop 1	
+P17261	UniProtKB	Domain	162	212	.	.	.	Note=PQ-loop 2	
+P17261	UniProtKB	Glycosylation	177	177	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53173 1 138
+P53173	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9732282;Dbxref=PMID:9732282	
+P53173	UniProtKB	Chain	2	138	.	.	.	ID=PRO_0000122236;Note=ER-derived vesicles protein ERV14	
+P53173	UniProtKB	Topological domain	2	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53173	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53173	UniProtKB	Topological domain	28	52	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53173	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53173	UniProtKB	Topological domain	74	111	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53173	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53173	UniProtKB	Topological domain	133	138	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03661 1 1658
+Q03661	UniProtKB	Chain	1	1658	.	.	.	ID=PRO_0000203333;Note=Silent chromatin protein ESC1	
+Q03661	UniProtKB	Modified residue	500	500	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03661	UniProtKB	Modified residue	532	532	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03661	UniProtKB	Modified residue	579	579	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03661	UniProtKB	Modified residue	583	583	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	608	608	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	662	662	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03661	UniProtKB	Modified residue	865	865	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03661	UniProtKB	Modified residue	866	866	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03661	UniProtKB	Modified residue	888	888	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03661	UniProtKB	Modified residue	911	911	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03661	UniProtKB	Modified residue	937	937	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1092	1092	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1096	1096	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1098	1098	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1166	1166	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03661	UniProtKB	Modified residue	1176	1176	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1178	1178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1214	1214	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1254	1254	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03661	UniProtKB	Modified residue	1290	1290	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1326	1326	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03661	UniProtKB	Modified residue	1332	1332	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1403	1403	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1409	1409	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1450	1450	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1454	1454	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1539	1539	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1590	1590	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03661	UniProtKB	Modified residue	1591	1591	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53743 1 316
+P53743	UniProtKB	Chain	1	316	.	.	.	ID=PRO_0000203480;Note=Pre-rRNA-processing protein ESF2	
+P53743	UniProtKB	Domain	114	204	.	.	.	Note=RRM	
+P53743	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53743	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53743	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P42940 1 261
+P42940	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P42940	UniProtKB	Chain	2	261	.	.	.	ID=PRO_0000167874;Note=Probable electron transfer flavoprotein subunit beta	
+P42940	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q08421 1 412
+Q08421	UniProtKB	Chain	1	412	.	.	.	ID=PRO_0000245279;Note=Enhancer of translation termination 1	
+Q08421	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08421	UniProtKB	Sequence conflict	338	338	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39875 1 702
+P39875	UniProtKB	Chain	1	702	.	.	.	ID=PRO_0000154045;Note=Exodeoxyribonuclease 1	
+P39875	UniProtKB	Region	1	96	.	.	.	Note=N-domain	
+P39875	UniProtKB	Region	114	247	.	.	.	Note=I-domain	
+P39875	UniProtKB	Compositional bias	501	520	.	.	.	Note=Asp/Glu-rich (acidic)	
+P39875	UniProtKB	Compositional bias	537	553	.	.	.	Note=Asp/Glu-rich (acidic)	
+P39875	UniProtKB	Compositional bias	618	625	.	.	.	Note=Asp-rich (acidic)	
+P39875	UniProtKB	Metal binding	30	30	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39875	UniProtKB	Metal binding	78	78	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39875	UniProtKB	Metal binding	150	150	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39875	UniProtKB	Metal binding	152	152	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39875	UniProtKB	Metal binding	171	171	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39875	UniProtKB	Metal binding	173	173	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39875	UniProtKB	Metal binding	227	227	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39875	UniProtKB	Modified residue	372	372	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38289 1 585
+P38289	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38289	UniProtKB	Chain	27	585	.	.	.	ID=PRO_0000202501;Note=Exonuclease V%2C mitochondrial	
+P38289	UniProtKB	Metal binding	141	141	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38289	UniProtKB	Metal binding	549	549	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38289	UniProtKB	Metal binding	552	552	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38289	UniProtKB	Metal binding	558	558	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38289	UniProtKB	Mutagenesis	270	270	.	.	.	Note=Impairs exonuclease activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20086101;Dbxref=PMID:20086101	
+P38289	UniProtKB	Mutagenesis	320	320	.	.	.	Note=Impairs exonuclease activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20086101;Dbxref=PMID:20086101	
+##sequence-region P38261 1 753
+P38261	UniProtKB	Chain	1	753	.	.	.	ID=PRO_0000118987;Note=Exocyst complex component EXO84	
+P38261	UniProtKB	Coiled coil	227	279	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38261	UniProtKB	Coiled coil	531	585	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38261	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38261	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38261	UniProtKB	Modified residue	482	482	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38261	UniProtKB	Cross-link	219	219	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P38261	UniProtKB	Helix	528	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S	
+P38261	UniProtKB	Helix	552	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S	
+P38261	UniProtKB	Helix	579	604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S	
+P38261	UniProtKB	Helix	609	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S	
+P38261	UniProtKB	Helix	625	645	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S	
+P38261	UniProtKB	Helix	653	678	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S	
+P38261	UniProtKB	Helix	684	708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S	
+P38261	UniProtKB	Helix	717	728	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S	
+P38261	UniProtKB	Helix	729	733	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S	
+P38261	UniProtKB	Helix	738	746	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S	
+P38261	UniProtKB	Helix	747	751	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S	
+##sequence-region P09201 1 348
+P09201	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3008716;Dbxref=PMID:3008716	
+P09201	UniProtKB	Chain	2	348	.	.	.	ID=PRO_0000200511;Note=Fructose-1%2C6-bisphosphatase	
+P09201	UniProtKB	Nucleotide binding	38	42	.	.	.	Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Nucleotide binding	122	123	.	.	.	Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Region	131	134	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Metal binding	79	79	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Metal binding	108	108	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Metal binding	108	108	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Metal binding	128	128	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Metal binding	128	128	.	.	.	Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Metal binding	130	130	.	.	.	Note=Magnesium 2%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Metal binding	131	131	.	.	.	Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Metal binding	292	292	.	.	.	Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Binding site	222	222	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Binding site	256	256	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Binding site	276	276	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Binding site	286	286	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09201	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P09201	UniProtKB	Sequence conflict	278	278	.	.	.	Note=C->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P34756 1 2278
+P34756	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P34756	UniProtKB	Chain	2	2278	.	.	.	ID=PRO_0000185451;Note=1-phosphatidylinositol 3-phosphate 5-kinase FAB1	
+P34756	UniProtKB	Domain	1932	2266	.	.	.	Note=PIPK;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00781	
+P34756	UniProtKB	Zinc finger	240	299	.	.	.	Note=FYVE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
+P34756	UniProtKB	Region	2	676	.	.	.	Note=Required for localization to the vacuole membrane	
+P34756	UniProtKB	Region	800	1500	.	.	.	Note=Mediates interaction with VAC14 and FIG4	
+P34756	UniProtKB	Compositional bias	393	397	.	.	.	Note=Poly-Pro	
+P34756	UniProtKB	Compositional bias	571	590	.	.	.	Note=Poly-Asn	
+P34756	UniProtKB	Compositional bias	1808	1811	.	.	.	Note=Poly-Thr	
+P34756	UniProtKB	Compositional bias	1891	1897	.	.	.	Note=Poly-Gln	
+P34756	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P34756	UniProtKB	Modified residue	186	186	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34756	UniProtKB	Modified residue	1627	1627	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34756	UniProtKB	Modified residue	1630	1630	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34756	UniProtKB	Modified residue	1938	1938	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34756	UniProtKB	Modified residue	1953	1953	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34756	UniProtKB	Mutagenesis	262	262	.	.	.	Note=Cells show growth at 38 degrees Celsius. Failure to localize to the vacuole membrane. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18653468;Dbxref=PMID:18653468	
+P34756	UniProtKB	Mutagenesis	864	864	.	.	.	Note=Loss of interaction with VAC14. Failure to localize to the vacuole membrane. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19037259;Dbxref=PMID:19037259	
+P34756	UniProtKB	Mutagenesis	1017	1017	.	.	.	Note=Cells are defective for growth at 38 degrees Celsius. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18653468;Dbxref=PMID:18653468	
+P34756	UniProtKB	Mutagenesis	1243	1243	.	.	.	Note=Cells are defective for growth at 38 degrees Celsius and show single-lobed%2C enlarged vacuoles. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18653468;Dbxref=PMID:18653468	
+P34756	UniProtKB	Mutagenesis	2134	2134	.	.	.	Note=Cells are defective for growth at 38 degrees Celsius. PtdIns(3%2C5)P2 levels are severely reduced. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18653468;Dbxref=PMID:18653468	
+P34756	UniProtKB	Sequence conflict	2275	2275	.	.	.	Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32771 1 386
+P32771	UniProtKB	Chain	1	386	.	.	.	ID=PRO_0000160785;Note=S-(hydroxymethyl)glutathione dehydrogenase	
+P32771	UniProtKB	Metal binding	49	49	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32771	UniProtKB	Metal binding	71	71	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32771	UniProtKB	Metal binding	101	101	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32771	UniProtKB	Metal binding	104	104	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32771	UniProtKB	Metal binding	107	107	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32771	UniProtKB	Metal binding	115	115	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32771	UniProtKB	Metal binding	179	179	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P32604 1 452
+P32604	UniProtKB	Chain	1	452	.	.	.	ID=PRO_0000179975;Note=Fructose-2%2C6-bisphosphatase	
+P32604	UniProtKB	Nucleotide binding	20	28	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Nucleotide binding	143	148	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Nucleotide binding	324	327	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953	
+P32604	UniProtKB	Nucleotide binding	368	372	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953	
+P32604	UniProtKB	Region	1	223	.	.	.	Note=6-phosphofructo-2-kinase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32604	UniProtKB	Region	224	452	.	.	.	Note=Fructose-2%2C6-bisphosphatase	
+P32604	UniProtKB	Active site	104	104	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32604	UniProtKB	Active site	232	232	.	.	.	Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Active site	302	302	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	53	53	.	.	.	Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	78	78	.	.	.	Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	106	106	.	.	.	Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	112	112	.	.	.	Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	169	169	.	.	.	Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	173	173	.	.	.	Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	231	231	.	.	.	Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	238	238	.	.	.	Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	244	244	.	.	.	Note=Fructose 2%2C6-bisphosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	313	313	.	.	.	Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	327	327	.	.	.	Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	331	331	.	.	.	Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	342	342	.	.	.	Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	368	368	.	.	.	Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Binding site	372	372	.	.	.	Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953	
+P32604	UniProtKB	Binding site	404	404	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Site	231	231	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Site	238	238	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Site	367	367	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875	
+P32604	UniProtKB	Modified residue	435	435	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32604	UniProtKB	Modified residue	446	446	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32604	UniProtKB	Sequence conflict	199	199	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32604	UniProtKB	Sequence conflict	362	362	.	.	.	Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32604	UniProtKB	Sequence conflict	448	449	.	.	.	Note=LE->FQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12099 1 399
+Q12099	UniProtKB	Chain	1	399	.	.	.	ID=PRO_0000054975;Note=ATP-dependent RNA helicase FAL1	
+Q12099	UniProtKB	Domain	54	227	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q12099	UniProtKB	Domain	238	399	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q12099	UniProtKB	Nucleotide binding	67	74	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q12099	UniProtKB	Motif	23	51	.	.	.	Note=Q motif	
+Q12099	UniProtKB	Motif	173	176	.	.	.	Note=DEAD box	
+Q12099	UniProtKB	Mutagenesis	85	85	.	.	.	Note=Decreases the amount of 40S ribosomal subunit%3B when associated with R-144%3B A-244 and A-246. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372960;Dbxref=PMID:9372960	
+Q12099	UniProtKB	Mutagenesis	144	144	.	.	.	Note=Decreases the amount of 40S ribosomal subunit%3B when associated with T-85%3B A-244 and A-246. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372960;Dbxref=PMID:9372960	
+Q12099	UniProtKB	Mutagenesis	244	244	.	.	.	Note=Decreases the amount of 40S ribosomal subunit%3B when associated with T-85%3B R-144 and A-246. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372960;Dbxref=PMID:9372960	
+Q12099	UniProtKB	Mutagenesis	246	246	.	.	.	Note=Decreases the amount of 40S ribosomal subunit%3B when associated with T-85%3B R-144 and A-244. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372960;Dbxref=PMID:9372960	
+##sequence-region Q04952 1 1785
+Q04952	UniProtKB	Chain	1	1785	.	.	.	ID=PRO_0000121727;Note=1%2C3-beta-glucan synthase component FKS3	
+Q04952	UniProtKB	Transmembrane	337	357	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	375	395	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	415	435	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	444	464	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	508	528	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	547	567	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	572	592	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	712	732	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	1215	1235	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	1268	1288	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	1303	1323	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	1370	1390	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	1394	1414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	1475	1495	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	1514	1534	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	1549	1569	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	1585	1605	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	1655	1675	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Transmembrane	1713	1733	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Glycosylation	844	844	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Glycosylation	874	874	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Glycosylation	955	955	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Glycosylation	1002	1002	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Glycosylation	1170	1170	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Glycosylation	1360	1360	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Glycosylation	1579	1579	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04952	UniProtKB	Glycosylation	1761	1761	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36170 1 1169
+P36170	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Chain	25	1146	.	.	.	ID=PRO_0000014336;Note=Flocculation protein FLO10	
+P36170	UniProtKB	Propeptide	1147	1169	.	.	.	ID=PRO_0000372449;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Domain	111	271	.	.	.	Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164	
+P36170	UniProtKB	Repeat	303	326	.	.	.	Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P36170	UniProtKB	Repeat	330	356	.	.	.	Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P36170	UniProtKB	Repeat	357	383	.	.	.	Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P36170	UniProtKB	Repeat	384	419	.	.	.	Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P36170	UniProtKB	Repeat	420	446	.	.	.	Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P36170	UniProtKB	Repeat	447	482	.	.	.	Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P36170	UniProtKB	Repeat	483	509	.	.	.	Note=1-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P36170	UniProtKB	Repeat	510	545	.	.	.	Note=2-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P36170	UniProtKB	Repeat	546	572	.	.	.	Note=1-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P36170	UniProtKB	Repeat	573	608	.	.	.	Note=2-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P36170	UniProtKB	Region	303	572	.	.	.	Note=6 X 27 AA approximate repeats%2C Ser/Thr-rich	
+P36170	UniProtKB	Region	384	608	.	.	.	Note=4 X 36 AA approximate repeats%2C Ser/Thr-rich	
+P36170	UniProtKB	Compositional bias	299	1143	.	.	.	Note=Ser/Thr-rich	
+P36170	UniProtKB	Lipidation	1146	1146	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	122	122	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	157	157	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	279	279	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	389	389	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	452	452	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	515	515	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	578	578	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	656	656	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	686	686	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	879	879	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	1092	1092	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36170	UniProtKB	Glycosylation	1099	1099	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P08640 1 1367
+P08640	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08640	UniProtKB	Chain	22	1346	.	.	.	ID=PRO_0000019586;Note=Flocculation protein FLO11	
+P08640	UniProtKB	Propeptide	1347	1367	.	.	.	ID=PRO_0000019587;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08640	UniProtKB	Domain	31	207	.	.	.	Note=Flo11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01168	
+P08640	UniProtKB	Repeat	210	219	.	.	.	Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	220	229	.	.	.	Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	230	239	.	.	.	Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	240	249	.	.	.	Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	262	274	.	.	.	Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	275	287	.	.	.	Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	313	327	.	.	.	Note=3-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	328	342	.	.	.	Note=3-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	343	354	.	.	.	Note=4-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	355	369	.	.	.	Note=3-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	370	381	.	.	.	Note=4-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	382	393	.	.	.	Note=4-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	394	408	.	.	.	Note=3-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	409	420	.	.	.	Note=4-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	421	432	.	.	.	Note=4-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	433	444	.	.	.	Note=4-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	445	456	.	.	.	Note=4-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	457	471	.	.	.	Note=3-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	472	483	.	.	.	Note=4-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	484	498	.	.	.	Note=3-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	499	510	.	.	.	Note=4-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	511	525	.	.	.	Note=3-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	526	540	.	.	.	Note=3-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	541	552	.	.	.	Note=4-10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	568	579	.	.	.	Note=4-11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	580	594	.	.	.	Note=3-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	595	609	.	.	.	Note=3-10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	610	625	.	.	.	Note=3-11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	625	636	.	.	.	Note=4-12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	637	651	.	.	.	Note=3-12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	652	666	.	.	.	Note=3-13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	667	681	.	.	.	Note=3-14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	682	693	.	.	.	Note=4-13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	694	705	.	.	.	Note=4-14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	706	720	.	.	.	Note=3-15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	721	735	.	.	.	Note=3-16;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	736	750	.	.	.	Note=3-17;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	751	762	.	.	.	Note=4-15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	763	777	.	.	.	Note=3-18;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	778	792	.	.	.	Note=3-19;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	808	822	.	.	.	Note=3-21;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	838	852	.	.	.	Note=3-20;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	865	879	.	.	.	Note=3-22;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	937	968	.	.	.	Note=5-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	981	1012	.	.	.	Note=5-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Repeat	1088	1119	.	.	.	Note=5-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P08640	UniProtKB	Region	22	209	.	.	.	Note=Involved in homotypic binding;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08640	UniProtKB	Region	210	249	.	.	.	Note=4 X 10 AA repeats%2C Ser/Thr-rich	
+P08640	UniProtKB	Region	262	287	.	.	.	Note=2 X 13 AA repeats%2C Thr-rich	
+P08640	UniProtKB	Region	313	852	.	.	.	Note=22 X 15 AA approximate repeats%2C Ser-rich	
+P08640	UniProtKB	Region	343	762	.	.	.	Note=15 X 12 AA repeats%2C Ser/Thr-rich	
+P08640	UniProtKB	Region	937	1119	.	.	.	Note=3 X 32 AA tandem repeats%2C Thr-rich	
+P08640	UniProtKB	Lipidation	1346	1346	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08640	UniProtKB	Glycosylation	817	817	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08640	UniProtKB	Glycosylation	874	874	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08640	UniProtKB	Mutagenesis	1340	1367	.	.	.	Note=Increased shedding%2C associated with loss of GPI-anchor site. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20619652;Dbxref=PMID:20619652	
+P08640	UniProtKB	Beta strand	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Helix	50	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Turn	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	61	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	75	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Helix	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	93	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	108	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Turn	113	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	125	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	136	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	149	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Helix	157	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	171	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	186	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Beta strand	195	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+P08640	UniProtKB	Helix	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR	
+##sequence-region P32768 1 1537
+P32768	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Chain	25	1514	.	.	.	ID=PRO_0000021273;Note=Flocculation protein FLO1	
+P32768	UniProtKB	Propeptide	1515	1537	.	.	.	ID=PRO_0000021274;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Domain	74	249	.	.	.	Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164	
+P32768	UniProtKB	Repeat	278	322	.	.	.	Note=1-1	
+P32768	UniProtKB	Repeat	323	367	.	.	.	Note=1-2	
+P32768	UniProtKB	Repeat	368	412	.	.	.	Note=1-3	
+P32768	UniProtKB	Repeat	413	457	.	.	.	Note=1-4	
+P32768	UniProtKB	Repeat	458	502	.	.	.	Note=1-5	
+P32768	UniProtKB	Repeat	503	547	.	.	.	Note=1-6	
+P32768	UniProtKB	Repeat	548	592	.	.	.	Note=1-7	
+P32768	UniProtKB	Repeat	593	637	.	.	.	Note=1-8	
+P32768	UniProtKB	Repeat	638	682	.	.	.	Note=1-9	
+P32768	UniProtKB	Repeat	683	727	.	.	.	Note=1-10	
+P32768	UniProtKB	Repeat	728	772	.	.	.	Note=1-11	
+P32768	UniProtKB	Repeat	773	817	.	.	.	Note=1-12	
+P32768	UniProtKB	Repeat	818	862	.	.	.	Note=1-13	
+P32768	UniProtKB	Repeat	863	907	.	.	.	Note=1-14	
+P32768	UniProtKB	Repeat	908	952	.	.	.	Note=1-15	
+P32768	UniProtKB	Repeat	953	997	.	.	.	Note=1-16	
+P32768	UniProtKB	Repeat	998	1042	.	.	.	Note=1-17	
+P32768	UniProtKB	Repeat	1043	1087	.	.	.	Note=1-18	
+P32768	UniProtKB	Repeat	1118	1137	.	.	.	Note=2-1	
+P32768	UniProtKB	Repeat	1138	1157	.	.	.	Note=2-2	
+P32768	UniProtKB	Repeat	1226	1276	.	.	.	Note=3-1	
+P32768	UniProtKB	Repeat	1291	1341	.	.	.	Note=3-2	
+P32768	UniProtKB	Repeat	1342	1392	.	.	.	Note=3-3	
+P32768	UniProtKB	Repeat	1408	1416	.	.	.	Note=4-1	
+P32768	UniProtKB	Repeat	1417	1425	.	.	.	Note=4-2	
+P32768	UniProtKB	Repeat	1426	1434	.	.	.	Note=4-3	
+P32768	UniProtKB	Region	197	240	.	.	.	Note=Sugar recognition	
+P32768	UniProtKB	Region	278	1087	.	.	.	Note=18 X 45 AA approximate tandem repeats%2C Thr-rich	
+P32768	UniProtKB	Region	1118	1157	.	.	.	Note=2 X 20 AA approximate tandem repeats%2C Ser/Thr-rich	
+P32768	UniProtKB	Region	1226	1392	.	.	.	Note=3 X 51 AA approximate repeats%2C Ser/Thr-rich	
+P32768	UniProtKB	Region	1408	1434	.	.	.	Note=3 X 9 AA approximate tandem repeats%2C Thr-rich	
+P32768	UniProtKB	Lipidation	1514	1514	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	135	135	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	187	187	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	262	262	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	329	329	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	374	374	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	419	419	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	464	464	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	509	509	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	554	554	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	599	599	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	644	644	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	689	689	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	734	734	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Glycosylation	1114	1114	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32768	UniProtKB	Natural variant	303	797	.	.	.	Note=In strain: S288c / KV295. Missing	
+P32768	UniProtKB	Natural variant	317	946	.	.	.	Note=In strain: S288c / KV333. Missing	
+P32768	UniProtKB	Natural variant	317	901	.	.	.	Note=In strain: S288c / KV291. Missing	
+P32768	UniProtKB	Sequence conflict	330	330	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	349	349	.	.	.	Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	375	375	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	384	384	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	416	422	.	.	.	Note=QPWNDTF->HHGTTLL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	429	429	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	429	429	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	436	436	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	464	464	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	469	469	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	474	474	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	519	519	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	550	550	.	.	.	Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	609	609	.	.	.	Note=M->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	637	637	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	699	699	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	706	706	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	926	926	.	.	.	Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	926	926	.	.	.	Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	926	926	.	.	.	Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Sequence conflict	926	926	.	.	.	Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32768	UniProtKB	Beta strand	35	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Helix	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Helix	57	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Helix	63	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	69	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	86	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Helix	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Turn	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Turn	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Turn	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	135	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	147	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	160	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Turn	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	189	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	204	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	215	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	233	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	242	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Turn	248	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	251	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Beta strand	264	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+P32768	UniProtKB	Helix	268	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL	
+##sequence-region Q08023 1 583
+Q08023	UniProtKB	Transit peptide	1	25	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08023	UniProtKB	Chain	26	583	.	.	.	ID=PRO_0000247338;Note=Protein FMP25%2C mitochondrial	
+Q08023	UniProtKB	Transmembrane	83	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08023	UniProtKB	Repeat	332	389	.	.	.	Note=RCC1 1	
+Q08023	UniProtKB	Repeat	390	452	.	.	.	Note=RCC1 2	
+Q08023	UniProtKB	Repeat	459	510	.	.	.	Note=RCC1 3	
+Q08023	UniProtKB	Repeat	512	569	.	.	.	Note=RCC1 4	
+Q08023	UniProtKB	Sequence conflict	160	160	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43557 1 207
+P43557	UniProtKB	Transmembrane	184	206	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43557	UniProtKB	Coiled coil	100	136	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53233 1 369
+P53233	UniProtKB	Chain	1	369	.	.	.	ID=PRO_0000086113;Note=Probable serine/threonine-protein kinase FMP48	
+P53233	UniProtKB	Domain	2	369	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53233	UniProtKB	Nucleotide binding	8	16	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53233	UniProtKB	Active site	133	133	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P53233	UniProtKB	Binding site	31	31	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region P50264 1 508
+P50264	UniProtKB	Chain	1	508	.	.	.	ID=PRO_0000087317;Note=Polyamine oxidase FMS1	
+P50264	UniProtKB	Beta strand	7	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	18	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	34	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	40	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	58	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Turn	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	73	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ECH	
+P50264	UniProtKB	Beta strand	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Turn	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Turn	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	115	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Turn	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BNM	
+P50264	UniProtKB	Helix	141	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	158	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	172	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Turn	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	184	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	196	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	201	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	217	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BNU	
+P50264	UniProtKB	Beta strand	223	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GDP	
+P50264	UniProtKB	Beta strand	234	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	243	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	255	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	263	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CNT	
+P50264	UniProtKB	Beta strand	268	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CND	
+P50264	UniProtKB	Beta strand	273	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	280	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GDP	
+P50264	UniProtKB	Beta strand	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BI4	
+P50264	UniProtKB	Beta strand	295	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	311	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	321	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	333	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	353	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ECH	
+P50264	UniProtKB	Beta strand	358	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	363	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	370	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	380	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Turn	387	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	391	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	420	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GDP	
+P50264	UniProtKB	Helix	424	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CN8	
+P50264	UniProtKB	Beta strand	431	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Turn	440	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Turn	444	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	461	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Beta strand	470	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+P50264	UniProtKB	Helix	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BI4	
+P50264	UniProtKB	Turn	484	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GDP	
+P50264	UniProtKB	Helix	489	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG	
+##sequence-region P40546 1 346
+P40546	UniProtKB	Chain	1	346	.	.	.	ID=PRO_0000087172;Note=Protein FAF1	
+P40546	UniProtKB	Helix	146	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+##sequence-region P46671 1 204
+P46671	UniProtKB	Chain	1	204	.	.	.	ID=PRO_0000087191;Note=Factor arrest protein 3	
+P46671	UniProtKB	Sequence conflict	6	6	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46671	UniProtKB	Sequence conflict	131	131	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05040 1 523
+Q05040	UniProtKB	Chain	1	523	.	.	.	ID=PRO_0000087193;Note=Factor arrest protein 8	
+Q05040	UniProtKB	Coiled coil	26	76	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05040	UniProtKB	Modified residue	115	115	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q05040	UniProtKB	Modified residue	132	132	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P38137 1 543
+P38137	UniProtKB	Chain	1	543	.	.	.	ID=PRO_0000193182;Note=Peroxisomal-coenzyme A synthetase	
+P38137	UniProtKB	Nucleotide binding	190	207	.	.	.	Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38137	UniProtKB	Motif	541	543	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12178 1 158
+Q12178	UniProtKB	Chain	1	158	.	.	.	ID=PRO_0000171702;Note=Cytosine deaminase	
+Q12178	UniProtKB	Domain	9	129	.	.	.	Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083	
+Q12178	UniProtKB	Compositional bias	129	132	.	.	.	Note=Poly-Val	
+Q12178	UniProtKB	Active site	64	64	.	.	.	Note=Proton donor	
+Q12178	UniProtKB	Metal binding	62	62	.	.	.	Note=Zinc%3B catalytic	
+Q12178	UniProtKB	Metal binding	91	91	.	.	.	Note=Zinc%3B catalytic	
+Q12178	UniProtKB	Metal binding	94	94	.	.	.	Note=Zinc%3B catalytic	
+Q12178	UniProtKB	Binding site	51	51	.	.	.	Note=Substrate	
+Q12178	UniProtKB	Binding site	155	155	.	.	.	Note=Substrate	
+Q12178	UniProtKB	Helix	11	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Beta strand	34	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Turn	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Beta strand	45	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Helix	53	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Helix	63	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Helix	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Beta strand	82	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Helix	92	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Beta strand	105	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Helix	118	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Beta strand	128	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Helix	135	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+Q12178	UniProtKB	Helix	149	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O	
+##sequence-region P25621 1 512
+P25621	UniProtKB	Chain	1	512	.	.	.	ID=PRO_0000121367;Note=Pantothenate transporter FEN2	
+P25621	UniProtKB	Topological domain	1	27	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	28	48	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	49	79	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	101	102	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	103	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	124	132	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	133	153	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	154	164	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	165	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	186	198	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	220	271	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	272	292	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	293	312	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	313	333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	334	342	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	343	363	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	364	372	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	394	401	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	402	422	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	423	434	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Transmembrane	435	455	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25621	UniProtKB	Topological domain	456	512	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08907 1 204
+Q08907	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08907	UniProtKB	Chain	19	182	.	.	.	ID=PRO_0000021269;Note=Facilitator of iron transport 3	
+Q08907	UniProtKB	Propeptide	183	204	.	.	.	ID=PRO_0000372453;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08907	UniProtKB	Compositional bias	22	191	.	.	.	Note=Ser/Thr-rich	
+Q08907	UniProtKB	Lipidation	182	182	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P19658 1 623
+P19658	UniProtKB	Chain	1	623	.	.	.	ID=PRO_0000118975;Note=Exocyst complex component EXO70	
+P19658	UniProtKB	Sequence conflict	497	497	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19658	UniProtKB	Helix	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	74	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	97	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Beta strand	116	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PFV	
+P19658	UniProtKB	Turn	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7M	
+P19658	UniProtKB	Helix	125	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	161	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	176	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	195	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Turn	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PFV	
+P19658	UniProtKB	Helix	239	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	268	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	298	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PFV	
+P19658	UniProtKB	Helix	304	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Turn	319	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	327	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	370	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	383	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	386	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Turn	393	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	398	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	408	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	423	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	469	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	492	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Turn	496	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	499	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Beta strand	535	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	542	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	571	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	597	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Beta strand	600	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	603	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+P19658	UniProtKB	Helix	611	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E	
+##sequence-region P53971 1 965
+P53971	UniProtKB	Chain	1	965	.	.	.	ID=PRO_0000056343;Note=FKBP12-associated protein 1	
+P53971	UniProtKB	Domain	733	796	.	.	.	Note=R3H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00382	
+P53971	UniProtKB	Zinc finger	68	118	.	.	.	Note=RING-type%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P53971	UniProtKB	Zinc finger	159	177	.	.	.	Note=NF-X1-type 1	
+P53971	UniProtKB	Zinc finger	216	235	.	.	.	Note=NF-X1-type 2	
+P53971	UniProtKB	Zinc finger	362	382	.	.	.	Note=NF-X1-type 3	
+P53971	UniProtKB	Zinc finger	468	487	.	.	.	Note=NF-X1-type 4	
+P53971	UniProtKB	Zinc finger	586	606	.	.	.	Note=NF-X1-type 5	
+P53971	UniProtKB	Modified residue	951	951	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53971	UniProtKB	Modified residue	958	958	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q05498 1 189
+Q05498	UniProtKB	Chain	1	189	.	.	.	ID=PRO_0000253818;Note=rRNA-processing protein FCF1	
+Q05498	UniProtKB	Domain	63	162	.	.	.	Note=PINc	
+##sequence-region Q03254 1 732
+Q03254	UniProtKB	Chain	1	732	.	.	.	ID=PRO_0000212568;Note=RNA polymerase II subunit A C-terminal domain phosphatase	
+Q03254	UniProtKB	Domain	170	363	.	.	.	Note=FCP1 homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00336	
+Q03254	UniProtKB	Domain	499	593	.	.	.	Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+Q03254	UniProtKB	Modified residue	701	701	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03254	UniProtKB	Modified residue	718	718	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03254	UniProtKB	Modified residue	720	720	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03254	UniProtKB	Cross-link	74	74	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q12119 1 530
+Q12119	UniProtKB	Chain	1	530	.	.	.	ID=PRO_0000197922;Note=Purine-cytosine permease FCY22	
+Q12119	UniProtKB	Transmembrane	96	116	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Transmembrane	162	182	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Transmembrane	197	217	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Transmembrane	220	240	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Transmembrane	263	283	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Transmembrane	298	318	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Transmembrane	345	365	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Transmembrane	396	416	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Transmembrane	418	438	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Transmembrane	463	483	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12119	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P40039	
+##sequence-region Q06001 1 478
+Q06001	UniProtKB	Chain	1	478	.	.	.	ID=PRO_0000087189;Note=Factor arrest protein 10	
+Q06001	UniProtKB	Topological domain	1	454	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06001	UniProtKB	Transmembrane	455	475	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06001	UniProtKB	Topological domain	476	478	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06001	UniProtKB	Domain	116	176	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+Q06001	UniProtKB	Coiled coil	342	426	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06001	UniProtKB	Compositional bias	108	115	.	.	.	Note=Poly-Ser	
+##sequence-region P17064 1 533
+P17064	UniProtKB	Chain	1	533	.	.	.	ID=PRO_0000197920;Note=Purine-cytosine permease FCY2	
+P17064	UniProtKB	Topological domain	1	98	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Topological domain	120	121	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Transmembrane	122	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Topological domain	142	198	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Transmembrane	199	218	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Topological domain	219	256	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Transmembrane	257	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Topological domain	277	300	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Transmembrane	301	320	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Topological domain	321	347	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Transmembrane	348	367	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Topological domain	368	398	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Transmembrane	399	418	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Topological domain	419	465	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Transmembrane	466	485	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Topological domain	486	533	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Region	165	184	.	.	.	Note=Surface seeking;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17064	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P17064	UniProtKB	Cross-link	16	16	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P17064	UniProtKB	Sequence conflict	192	192	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17064	UniProtKB	Sequence conflict	261	261	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17064	UniProtKB	Sequence conflict	459	459	.	.	.	Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CF35 1 236
+P0CF35	UniProtKB	Chain	1	236	.	.	.	ID=PRO_0000223648;Note=Truncated formate dehydrogenase 2	
+P0CF35	UniProtKB	Nucleotide binding	36	37	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160	
+P0CF35	UniProtKB	Nucleotide binding	104	108	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160	
+P0CF35	UniProtKB	Nucleotide binding	185	188	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160	
+P0CF35	UniProtKB	Binding site	57	57	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160	
+P0CF35	UniProtKB	Binding site	130	130	.	.	.	Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160	
+P0CF35	UniProtKB	Binding site	156	156	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160	
+P0CF35	UniProtKB	Site	132	132	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160	
+P0CF35	UniProtKB	Site	185	185	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160	
+##sequence-region P39676 1 399
+P39676	UniProtKB	Chain	1	399	.	.	.	ID=PRO_0000052458;Note=Flavohemoprotein	
+P39676	UniProtKB	Domain	147	264	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+P39676	UniProtKB	Nucleotide binding	207	210	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39676	UniProtKB	Nucleotide binding	281	286	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39676	UniProtKB	Nucleotide binding	389	392	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39676	UniProtKB	Region	1	138	.	.	.	Note=Globin	
+P39676	UniProtKB	Region	146	399	.	.	.	Note=Reductase	
+P39676	UniProtKB	Region	272	399	.	.	.	Note=NAD or NADP-binding	
+P39676	UniProtKB	Active site	95	95	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39676	UniProtKB	Active site	137	137	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39676	UniProtKB	Metal binding	85	85	.	.	.	Note=Iron (heme proximal ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00238	
+P39676	UniProtKB	Binding site	189	189	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39676	UniProtKB	Site	29	29	.	.	.	Note=Involved in heme-bound ligand stabilization and O-O bond activation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39676	UniProtKB	Site	84	84	.	.	.	Note=Influences the redox potential of the prosthetic heme and FAD groups;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39676	UniProtKB	Site	388	388	.	.	.	Note=Influences the redox potential of the prosthetic heme and FAD groups;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39676	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39676	UniProtKB	Natural variant	153	153	.	.	.	Note=In strain: JM43. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1594608;Dbxref=PMID:1594608	
+P39676	UniProtKB	Natural variant	345	345	.	.	.	Note=In strain: JM43. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1594608;Dbxref=PMID:1594608	
+P39676	UniProtKB	Natural variant	365	365	.	.	.	Note=In strain: JM43. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1594608;Dbxref=PMID:1594608	
+##sequence-region P07149 1 2051
+P07149	UniProtKB	Chain	1	2051	.	.	.	ID=PRO_0000180282;Note=Fatty acid synthase subunit beta	
+P07149	UniProtKB	Domain	1523	1648	.	.	.	Note=MaoC-like	
+P07149	UniProtKB	Region	1	468	.	.	.	Note=Acetyltransferase	
+P07149	UniProtKB	Region	480	868	.	.	.	Note=Enoyl reductase	
+P07149	UniProtKB	Region	1144	1626	.	.	.	Note=Dehydratase	
+P07149	UniProtKB	Region	1627	1845	.	.	.	Note=Malonyl/palmitoyl transferase	
+P07149	UniProtKB	Active site	274	274	.	.	.	Note=For acetyltransferase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07149	UniProtKB	Active site	1808	1808	.	.	.	Note=For malonyltransferase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07149	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07149	UniProtKB	Modified residue	733	733	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07149	UniProtKB	Modified residue	1121	1121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P07149	UniProtKB	Cross-link	1364	1364	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P07149	UniProtKB	Sequence conflict	191	191	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	191	191	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	212	212	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	403	403	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1039	1039	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1039	1039	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1149	1149	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1184	1184	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1184	1184	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1290	1292	.	.	.	Note=FEI->SET;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1331	1333	.	.	.	Note=WRA->LRG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1331	1333	.	.	.	Note=WRA->LRG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1407	1411	.	.	.	Note=TSSFF->IFLFL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1559	1559	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1559	1559	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1576	1576	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1587	1587	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1631	1631	.	.	.	Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1647	1647	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1661	1661	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1661	1661	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1876	1876	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Sequence conflict	1980	1980	.	.	.	Note=Y->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07149	UniProtKB	Beta strand	10	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	16	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	27	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	57	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	81	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	101	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	116	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	144	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	156	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	169	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	181	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	215	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	228	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	234	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	260	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	267	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	277	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	289	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	321	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	337	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	346	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	367	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	377	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	383	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	404	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	417	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	430	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	433	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	445	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	452	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	462	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	466	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	475	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	490	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	499	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	505	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	508	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	512	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	526	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	540	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	544	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	552	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	561	564	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	568	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	577	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	582	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	591	594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	598	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	604	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	616	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	621	623	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	627	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	647	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	658	671	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	675	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	688	697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	703	705	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	710	722	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	728	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	738	740	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	748	757	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	766	770	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	774	777	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	778	780	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	781	783	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	785	787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	788	790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	803	805	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	815	822	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	829	836	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	841	847	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	853	857	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	860	870	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	871	874	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	877	879	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	880	885	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	888	898	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	914	916	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	919	930	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	933	936	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	937	939	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	941	958	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	970	974	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	976	986	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	988	991	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	997	1006	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1010	1012	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1016	1018	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1025	1030	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1035	1038	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1040	1042	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1048	1050	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	1057	1062	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1070	1090	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1094	1096	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1125	1128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1135	1143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1149	1155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1158	1161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1164	1167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1169	1174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1181	1186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1190	1192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1194	1201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1204	1214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	1215	1217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1218	1225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1229	1232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1234	1241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1258	1270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1294	1304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1323	1325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1326	1335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1336	1338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1341	1343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1347	1349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1350	1359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1367	1369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1375	1383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1385	1398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1401	1414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1419	1421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1423	1434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1438	1446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1450	1454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1463	1474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1476	1478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1480	1492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1498	1510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1515	1522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1524	1527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1529	1545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1551	1557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1562	1564	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1567	1572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1576	1578	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1582	1597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1602	1604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1605	1612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1621	1632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1635	1643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1649	1658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1662	1666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	1674	1677	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1678	1683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1685	1702	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1706	1711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1715	1720	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1724	1734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1749	1754	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1761	1765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1770	1772	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1774	1794	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1803	1806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1810	1819	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1824	1840	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1850	1857	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1859	1862	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1868	1882	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1886	1893	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	1894	1896	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1897	1903	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1904	1919	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1924	1930	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1933	1952	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	1964	1968	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1979	1981	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1988	1993	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	1998	2000	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	2003	2006	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	2007	2009	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Beta strand	2013	2015	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	2023	2033	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Helix	2036	2043	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+P07149	UniProtKB	Turn	2044	2048	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8	
+##sequence-region P40039 1 528
+P40039	UniProtKB	Chain	1	528	.	.	.	ID=PRO_0000197921;Note=Purine-cytosine permease FCY21	
+P40039	UniProtKB	Topological domain	1	90	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	112	118	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	140	161	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	162	182	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	183	198	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	220	221	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	222	242	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	243	260	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	261	281	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	282	295	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	296	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	317	340	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	341	361	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	362	393	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	394	414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	415	416	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	417	437	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	438	460	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	461	481	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	482	493	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Transmembrane	494	514	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Topological domain	515	528	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40039	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40039	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q08991 1 375
+Q08991	UniProtKB	Chain	1	375	.	.	.	ID=PRO_0000255979;Note=Fluoride export protein 2	
+Q08991	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913	
+Q08991	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08991	UniProtKB	Topological domain	33	34	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913	
+Q08991	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08991	UniProtKB	Topological domain	56	79	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:Q08913,ECO:0000305	
+Q08991	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08991	UniProtKB	Topological domain	101	127	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913	
+Q08991	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08991	UniProtKB	Topological domain	149	213	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913	
+Q08991	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08991	UniProtKB	Topological domain	235	241	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913	
+Q08991	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08991	UniProtKB	Topological domain	263	268	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913	
+Q08991	UniProtKB	Transmembrane	269	289	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08991	UniProtKB	Topological domain	290	310	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913	
+Q08991	UniProtKB	Transmembrane	311	331	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08991	UniProtKB	Topological domain	332	338	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913	
+Q08991	UniProtKB	Transmembrane	339	359	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08991	UniProtKB	Topological domain	360	375	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913	
+Q08991	UniProtKB	Glycosylation	109	109	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q08991	UniProtKB	Glycosylation	117	117	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q08991	UniProtKB	Glycosylation	235	235	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+##sequence-region P25653 1 1609
+P25653	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Chain	23	1588	.	.	.	ID=PRO_0000021264;Note=Factor-induced gene 2 protein	
+P25653	UniProtKB	Propeptide	1589	1609	.	.	.	ID=PRO_0000372452;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Compositional bias	30	1366	.	.	.	Note=Ser-rich	
+P25653	UniProtKB	Compositional bias	529	1554	.	.	.	Note=Thr-rich	
+P25653	UniProtKB	Lipidation	1588	1588	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	29	29	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	231	231	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	298	298	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	347	347	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	386	386	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	426	426	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	495	495	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	535	535	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	661	661	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	674	674	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	713	713	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	889	889	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	907	907	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	1079	1079	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25653	UniProtKB	Glycosylation	1400	1400	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P42837 1 879
+P42837	UniProtKB	Chain	1	879	.	.	.	ID=PRO_0000209742;Note=Polyphosphoinositide phosphatase	
+P42837	UniProtKB	Domain	166	528	.	.	.	Note=SAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00183	
+P42837	UniProtKB	Region	761	879	.	.	.	Note=Required for vacuolar localization	
+P42837	UniProtKB	Modified residue	829	829	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P42837	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Defective activation of FAB1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17572665;Dbxref=PMID:17572665	
+P42837	UniProtKB	Mutagenesis	469	469	.	.	.	Note=Partially defective in both hyperosmotic shock-induced PtdIns(3%2C5)P2 elevation and turnover. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492811;Dbxref=PMID:16492811	
+P42837	UniProtKB	Mutagenesis	519	519	.	.	.	Note=In FIG4-1%3B loss of catalytic activity in vitro. Almost 3-fold increase in PtdIns(3%2C5)P2 level in vivo. Partially defective in both hyperosmotic shock-induced PtdIns(3%2C5)P2 elevation and turnover. G->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11950935,ECO:0000269|PubMed:14528018,ECO:0000269|PubMed:16492811;Dbxref=PMID:11950935,PMID:14528018,PMID:16492811	
+##sequence-region P38911 1 411
+P38911	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38911	UniProtKB	Chain	2	411	.	.	.	ID=PRO_0000075313;Note=FK506-binding nuclear protein	
+P38911	UniProtKB	Domain	324	411	.	.	.	Note=PPIase FKBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00277	
+P38911	UniProtKB	Motif	256	271	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38911	UniProtKB	Compositional bias	60	87	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P38911	UniProtKB	Compositional bias	88	99	.	.	.	Note=Lys-rich (highly basic)	
+P38911	UniProtKB	Compositional bias	101	119	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P38911	UniProtKB	Compositional bias	173	248	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P38911	UniProtKB	Compositional bias	250	298	.	.	.	Note=Lys-rich (highly basic)	
+P38911	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38911	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38911	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38911	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38911	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphotyrosine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9148902;Dbxref=PMID:9148902	
+P38911	UniProtKB	Modified residue	186	186	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9148902;Dbxref=PMID:9148902	
+P38911	UniProtKB	Sequence conflict	122	122	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38911	UniProtKB	Sequence conflict	240	240	.	.	.	Note=E->EEE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38911	UniProtKB	Sequence conflict	335	335	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P20081 1 114
+P20081	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P20081	UniProtKB	Chain	2	114	.	.	.	ID=PRO_0000075305;Note=FK506-binding protein 1	
+P20081	UniProtKB	Domain	26	114	.	.	.	Note=PPIase FKBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00277	
+P20081	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P20081	UniProtKB	Modified residue	51	51	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P20081	UniProtKB	Mutagenesis	43	43	.	.	.	Note=Reduces interaction with FAP1. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178	
+P20081	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Abrogates interaction with FAP1. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178	
+P20081	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Abrogates interaction with FAP1. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178	
+P20081	UniProtKB	Mutagenesis	49	49	.	.	.	Note=Abrogates interaction with FAP1. R->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178	
+P20081	UniProtKB	Mutagenesis	94	94	.	.	.	Note=Abrogates interaction with FAP1. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178	
+P20081	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Reduces interaction with FAP1. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178	
+P20081	UniProtKB	Helix	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Beta strand	10	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Beta strand	28	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Beta strand	42	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Turn	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Beta strand	53	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Beta strand	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Helix	64	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Helix	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Beta strand	78	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Helix	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Turn	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Turn	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+P20081	UniProtKB	Beta strand	104	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT	
+##sequence-region P38631 1 1876
+P38631	UniProtKB	Chain	1	1876	.	.	.	ID=PRO_0000121725;Note=1%2C3-beta-glucan synthase component FKS1	
+P38631	UniProtKB	Topological domain	1	454	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	455	475	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	476	492	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	493	513	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	514	531	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	532	552	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	553	563	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	564	584	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	585	621	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	622	642	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	643	678	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	679	699	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	700	1358	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	1359	1379	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	1380	1444	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	1445	1465	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	1466	1469	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	1470	1490	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	1491	1560	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	1561	1581	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	1582	1601	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	1602	1622	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	1623	1643	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	1644	1664	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	1665	1672	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	1673	1695	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	1696	1802	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Transmembrane	1803	1823	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Topological domain	1824	1876	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38631	UniProtKB	Modified residue	269	269	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38631	UniProtKB	Modified residue	272	272	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38631	UniProtKB	Cross-link	259	259	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38631	UniProtKB	Cross-link	275	275	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38631	UniProtKB	Cross-link	386	386	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38631	UniProtKB	Cross-link	910	910	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38631	UniProtKB	Cross-link	915	915	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38631	UniProtKB	Cross-link	1539	1539	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38631	UniProtKB	Cross-link	1547	1547	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38631	UniProtKB	Mutagenesis	146	146	.	.	.	Note=In 1132%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with N-329%3B N-335 and DEL-GSC2. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	302	302	.	.	.	Note=In 1082%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with DEL-GSC2. V->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	329	329	.	.	.	Note=In 1132%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with V-146%3B N-335 and DEL-GSC2. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	335	335	.	.	.	Note=In 1132%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with V-146%3B N-329 and DEL-GSC2. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	470	470	.	.	.	Note=In ACR79-5%3B selectively resistant to antibiotic arborcandin C. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14693557;Dbxref=PMID:14693557	
+P38631	UniProtKB	Mutagenesis	605	605	.	.	.	Note=In 1093%3B temperature-sensitive mutant%3B higher beta-glucan content of cells%3B when associated with T-761 and DEL-GSC2. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	642	642	.	.	.	Note=In ACR1A3%3B selectively resistant to antibiotic arborcandin C. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14693557;Dbxref=PMID:14693557	
+P38631	UniProtKB	Mutagenesis	713	713	.	.	.	Note=In 1163%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with V-722 and DEL-GSC2. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	722	722	.	.	.	Note=In 1163%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with L-713 and DEL-GSC2. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	761	761	.	.	.	Note=In 1093%3B temperature-sensitive mutant%3B higher beta-glucan content of cells%3B when associated with I-605 and DEL-GSC2. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	823	823	.	.	.	Note=In 1104%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with E-920 and DEL-GSC2. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	828	828	.	.	.	Note=In 1014%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B partially K1 killer toxin-sensitive%3B when associated with DEL-GSC2. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	853	853	.	.	.	Note=In 1114%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with G-932%3B D-934%3B Y-1020%3B N-1047 and DEL-GSC2. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	855	855	.	.	.	Note=In A6%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with DEL-GSC2. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	872	872	.	.	.	Note=In 1144%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with K-907%3B S-982 and DEL-GSC2. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	877	877	.	.	.	Note=In 1154%3B temperature-sensitive mutant which is able to grow at 25 degrees Celsius but fails to grow at temperatures above 35 degrees Celsius%3B defective in 1%2C3-beta-glucan synthesis and thus has lower beta-glucan content%3B hypersensitive to echinocandin B and to a chitin-binding reagent%2C Calcofluor white%3B fails to grow in a low glucose medium%3B when associated with S-899%3B P-977 and DEL-GSC2. K->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12185837,ECO:0000269|PubMed:12399379;Dbxref=PMID:12185837,PMID:12399379	
+P38631	UniProtKB	Mutagenesis	899	899	.	.	.	Note=In 1154%3B temperature-sensitive mutant which is able to grow at 25 degrees Celsius but fails to grow at temperatures above 35 degrees Celsius%3B defective in 1%2C3-beta-glucan synthesis and thus has lower beta-glucan content%3B hypersensitive to echinocandin B and to a chitin-binding reagent%2C Calcofluor white%3B fails to grow in a low glucose medium%3B when associated with N-877%3B P-977 and DEL-GSC2. A->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12185837,ECO:0000269|PubMed:12399379;Dbxref=PMID:12185837,PMID:12399379	
+P38631	UniProtKB	Mutagenesis	907	907	.	.	.	Note=In 1144%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with F-872%3B S-982 and DEL-GSC2. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	920	920	.	.	.	Note=In 1104%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with V-823 and DEL-GSC2. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	932	932	.	.	.	Note=In 1114%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with T-853%3B D-934%3B Y-1020%3B N-1047 and DEL-GSC2. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	934	934	.	.	.	Note=In 1114%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with T-853%3B G-932%3B Y-1020%3B N-1047 and DEL-GSC2. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	977	977	.	.	.	Note=In 1154%3B temperature-sensitive mutant which is able to grow at 25 degrees Celsius but fails to grow at temperatures above 35 degrees Celsius%3B defective in 1%2C3-beta-glucan synthesis and thus has lower beta-glucan content%3B hypersensitive to echinocandin B and to a chitin-binding reagent%2C Calcofluor white%3B fails to grow in a low glucose medium%3B when associated with N-877%3B S-899 and DEL-GSC2. Q->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12185837,ECO:0000269|PubMed:12399379;Dbxref=PMID:12185837,PMID:12399379	
+P38631	UniProtKB	Mutagenesis	982	982	.	.	.	Note=In 1144%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with F-872%3B K-907 and DEL-GSC2. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	1020	1020	.	.	.	Note=In 1114%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with T-853%3B G-932%3B D-934%3B N-1047 and DEL-GSC2. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	1047	1047	.	.	.	Note=In 1114%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with T-853%3B G-932%3B D-934%3B Y-1020 and DEL-GSC2. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	1111	1111	.	.	.	Note=In F4%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with DEL-GSC2. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	1258	1258	.	.	.	Note=In 1125%3B temperature-sensitive mutant%3B lower beta-glucan content of cells and partially K1 killer toxin-resistant%3B when associated with D-1520 and DEL-GSC2. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Mutagenesis	1520	1520	.	.	.	Note=In 1125%3B temperature-sensitive mutant%3B lower beta-glucan content of cells and partial K1 killer toxin-resistant phenotype%3B when associated with Y-1258 and DEL-GSC2. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837	
+P38631	UniProtKB	Sequence conflict	19	19	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	19	19	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	19	19	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	19	19	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	19	19	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	113	113	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	113	113	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	113	113	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	113	113	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	113	113	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	236	236	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	236	236	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	236	236	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	236	236	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	236	236	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	373	373	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	373	373	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	373	373	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	373	373	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	373	373	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	437	437	.	.	.	Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	470	470	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	492	492	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	492	492	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	492	492	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	492	492	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	492	492	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	642	642	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1341	1341	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1341	1341	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1341	1341	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1341	1341	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1341	1341	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1457	1457	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1457	1457	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1457	1457	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1457	1457	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1457	1457	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1790	1790	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1790	1790	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1790	1790	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1790	1790	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1790	1790	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1827	1828	.	.	.	Note=KH->DQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1827	1828	.	.	.	Note=KH->DQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1827	1828	.	.	.	Note=KH->DQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1827	1828	.	.	.	Note=KH->DQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1827	1828	.	.	.	Note=KH->DQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1834	1834	.	.	.	Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1834	1834	.	.	.	Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1834	1834	.	.	.	Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1834	1834	.	.	.	Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1834	1834	.	.	.	Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1844	1844	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1844	1844	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1844	1844	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1844	1844	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1844	1844	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1853	1853	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1853	1853	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1853	1853	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1853	1853	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38631	UniProtKB	Sequence conflict	1853	1853	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40068 1 799
+P40068	UniProtKB	Chain	1	799	.	.	.	ID=PRO_0000087303;Note=Transcriptional activator FLO8	
+P40068	UniProtKB	Domain	73	105	.	.	.	Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126	
+P40068	UniProtKB	Compositional bias	41	55	.	.	.	Note=Poly-Gln	
+P40068	UniProtKB	Natural variant	54	54	.	.	.	Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. Q->QQQ	
+P40068	UniProtKB	Natural variant	112	112	.	.	.	Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. V->I	
+P40068	UniProtKB	Natural variant	115	115	.	.	.	Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. P->S	
+P40068	UniProtKB	Natural variant	383	383	.	.	.	Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. C->G	
+P40068	UniProtKB	Natural variant	441	441	.	.	.	Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. A->T	
+P40068	UniProtKB	Natural variant	447	447	.	.	.	Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. A->V	
+P40068	UniProtKB	Natural variant	598	598	.	.	.	Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. R->P	
+##sequence-region P53279 1 174
+P53279	UniProtKB	Chain	1	174	.	.	.	ID=PRO_0000202823;Note=Non-classical export protein 2 homolog 1	
+P53279	UniProtKB	Topological domain	1	7	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53279	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53279	UniProtKB	Topological domain	29	41	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53279	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53279	UniProtKB	Topological domain	63	69	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53279	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53279	UniProtKB	Topological domain	91	122	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53279	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53279	UniProtKB	Topological domain	144	174	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08645 1 548
+Q08645	UniProtKB	Chain	1	548	.	.	.	ID=PRO_0000168312;Note=Folylpolyglutamate synthase	
+Q08645	UniProtKB	Nucleotide binding	130	133	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+Q08645	UniProtKB	Metal binding	157	157	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+Q08645	UniProtKB	Metal binding	234	234	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+Q08645	UniProtKB	Metal binding	262	262	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+Q08645	UniProtKB	Binding site	382	382	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+Q08645	UniProtKB	Binding site	396	396	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+##sequence-region P08524 1 352
+P08524	UniProtKB	Chain	1	352	.	.	.	ID=PRO_0000123952;Note=Farnesyl pyrophosphate synthase	
+P08524	UniProtKB	Metal binding	100	100	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Metal binding	100	100	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Metal binding	104	104	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Metal binding	104	104	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Metal binding	240	240	.	.	.	Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Binding site	52	52	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Binding site	55	55	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Binding site	93	93	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Binding site	109	109	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Binding site	110	110	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Binding site	197	197	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Binding site	198	198	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Binding site	237	237	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Binding site	254	254	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Binding site	263	263	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08524	UniProtKB	Mutagenesis	197	197	.	.	.	Note=In ERG20-2%3B 14-fold decrease in FPPS activity. K->E	
+##sequence-region Q07825 1 749
+Q07825	UniProtKB	Chain	1	749	.	.	.	ID=PRO_0000185086;Note=Putative Xaa-Pro aminopeptidase FRA1	
+Q07825	UniProtKB	Metal binding	551	551	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07825	UniProtKB	Metal binding	562	562	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07825	UniProtKB	Metal binding	562	562	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07825	UniProtKB	Metal binding	660	660	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07825	UniProtKB	Metal binding	674	674	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07825	UniProtKB	Metal binding	674	674	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07825	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07825	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07825	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P32791 1 686
+P32791	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Chain	23	686	.	.	.	ID=PRO_0000010137;Note=Ferric/cupric reductase transmembrane component 1	
+P32791	UniProtKB	Topological domain	23	148	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Transmembrane	149	169	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Topological domain	170	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Topological domain	237	259	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Transmembrane	260	280	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Topological domain	281	296	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Transmembrane	297	317	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Topological domain	318	328	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Transmembrane	329	349	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Topological domain	350	358	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Transmembrane	359	378	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Topological domain	379	383	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Transmembrane	384	401	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Topological domain	402	686	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Domain	258	398	.	.	.	Note=Ferric oxidoreductase;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Domain	399	522	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+P32791	UniProtKB	Nucleotide binding	462	468	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Nucleotide binding	514	517	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Nucleotide binding	652	653	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Metal binding	294	294	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093	
+P32791	UniProtKB	Metal binding	308	308	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093	
+P32791	UniProtKB	Metal binding	364	364	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093	
+P32791	UniProtKB	Metal binding	378	378	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093	
+P32791	UniProtKB	Glycosylation	69	69	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Glycosylation	100	100	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Glycosylation	124	124	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32791	UniProtKB	Mutagenesis	294	294	.	.	.	Note=Impairs heme binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093	
+P32791	UniProtKB	Mutagenesis	308	308	.	.	.	Note=Impairs heme binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093	
+P32791	UniProtKB	Mutagenesis	364	364	.	.	.	Note=Impairs heme binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093	
+P32791	UniProtKB	Mutagenesis	378	378	.	.	.	Note=Impairs heme binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093	
+##sequence-region P53746 1 719
+P53746	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Chain	19	719	.	.	.	ID=PRO_0000010140;Note=Ferric reductase transmembrane component 4	
+P53746	UniProtKB	Topological domain	19	156	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Topological domain	178	228	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Transmembrane	229	249	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Topological domain	250	267	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Transmembrane	268	288	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Topological domain	289	304	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Transmembrane	305	325	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Topological domain	326	346	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Transmembrane	347	367	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Topological domain	368	373	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Transmembrane	374	394	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Topological domain	395	395	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Transmembrane	396	416	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Topological domain	417	719	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Domain	273	407	.	.	.	Note=Ferric oxidoreductase	
+P53746	UniProtKB	Domain	408	527	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+P53746	UniProtKB	Nucleotide binding	472	478	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Nucleotide binding	519	522	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Nucleotide binding	685	686	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Metal binding	309	309	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Metal binding	323	323	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Metal binding	379	379	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Metal binding	393	393	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53746	UniProtKB	Glycosylation	51	51	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Glycosylation	80	80	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Glycosylation	101	101	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Glycosylation	113	113	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Glycosylation	127	127	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53746	UniProtKB	Glycosylation	135	135	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P08417 1 488
+P08417	UniProtKB	Region	164	166	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08417	UniProtKB	Binding site	126	126	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08417	UniProtKB	Modified residue	428	428	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P08417	UniProtKB	Sequence conflict	173	173	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08417	UniProtKB	Sequence conflict	289	289	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08417	UniProtKB	Sequence conflict	392	392	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08417	UniProtKB	Beta strand	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Beta strand	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Beta strand	38	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	48	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	68	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	93	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Beta strand	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	126	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	155	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Turn	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	165	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	185	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Turn	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Beta strand	207	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Beta strand	215	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	222	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Turn	255	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	267	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	289	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	297	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Beta strand	327	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	353	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	387	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	413	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	420	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	432	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Turn	435	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	438	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	443	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	460	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	472	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+P08417	UniProtKB	Helix	481	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM	
+##sequence-region P28003 1 413
+P28003	UniProtKB	Chain	1	413	.	.	.	ID=PRO_0000202417;Note=SWIRM domain-containing protein FUN19	
+P28003	UniProtKB	Domain	316	413	.	.	.	Note=SWIRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00247	
+P28003	UniProtKB	Compositional bias	31	76	.	.	.	Note=Asn-rich	
+P28003	UniProtKB	Modified residue	194	194	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P28003	UniProtKB	Modified residue	207	207	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P28003	UniProtKB	Modified residue	211	211	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P28003	UniProtKB	Sequence conflict	255	255	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28003	UniProtKB	Sequence conflict	369	369	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11412 1 505
+P11412	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2040308,ECO:0000269|PubMed:2387402;Dbxref=PMID:2040308,PMID:2387402	
+P11412	UniProtKB	Chain	2	505	.	.	.	ID=PRO_0000068107;Note=Glucose-6-phosphate 1-dehydrogenase	
+P11412	UniProtKB	Nucleotide binding	18	25	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11412	UniProtKB	Region	187	191	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11412	UniProtKB	Active site	249	249	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11412	UniProtKB	Binding site	52	52	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11412	UniProtKB	Binding site	157	157	.	.	.	Note=NADP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11412	UniProtKB	Binding site	157	157	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11412	UniProtKB	Binding site	225	225	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11412	UniProtKB	Binding site	244	244	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11412	UniProtKB	Binding site	343	343	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11412	UniProtKB	Binding site	377	377	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11412	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2040308,ECO:0000269|PubMed:2387402;Dbxref=PMID:2040308,PMID:2387402	
+P11412	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P11412	UniProtKB	Modified residue	145	145	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P11412	UniProtKB	Sequence conflict	59	59	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11412	UniProtKB	Sequence conflict	80	80	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11412	UniProtKB	Sequence conflict	175	175	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P04385 1 528
+P04385	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:200486;Dbxref=PMID:200486	
+P04385	UniProtKB	Chain	2	528	.	.	.	ID=PRO_0000184657;Note=Galactokinase	
+P04385	UniProtKB	Nucleotide binding	163	173	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04385	UniProtKB	Active site	217	217	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04385	UniProtKB	Site	53	53	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04385	UniProtKB	Modified residue	381	381	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04385	UniProtKB	Sequence conflict	6	6	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04385	UniProtKB	Sequence conflict	162	162	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04385	UniProtKB	Sequence conflict	206	239	.	.	.	Note=EHYVGVNNGGMDQAASVCGEEDHALYVEFKPQLK->DIMLVLTMAVWIRLPLFAVRKIMLYTLSSNAVE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04385	UniProtKB	Sequence conflict	297	297	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04385	UniProtKB	Sequence conflict	428	428	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04385	UniProtKB	Sequence conflict	483	483	.	.	.	Note=N->NN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04385	UniProtKB	Helix	23	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	45	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	68	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	90	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	123	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	143	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	153	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	170	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	195	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	203	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	216	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	229	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	239	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	252	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Turn	266	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	274	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	310	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	332	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	351	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	359	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	370	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	379	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	390	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	419	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	446	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	461	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	470	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	486	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	498	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Helix	507	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	514	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+P04385	UniProtKB	Beta strand	523	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4	
+##sequence-region P04386 1 881
+P04386	UniProtKB	Chain	1	881	.	.	.	ID=PRO_0000114951;Note=Regulatory protein GAL4	
+P04386	UniProtKB	DNA binding	11	38	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P04386	UniProtKB	Motif	862	870	.	.	.	Note=9aaTAD	
+P04386	UniProtKB	Metal binding	11	11	.	.	.	Note=Zinc 1	
+P04386	UniProtKB	Metal binding	11	11	.	.	.	Note=Zinc 2	
+P04386	UniProtKB	Metal binding	14	14	.	.	.	Note=Zinc 1	
+P04386	UniProtKB	Metal binding	21	21	.	.	.	Note=Zinc 1	
+P04386	UniProtKB	Metal binding	28	28	.	.	.	Note=Zinc 1	
+P04386	UniProtKB	Metal binding	28	28	.	.	.	Note=Zinc 2	
+P04386	UniProtKB	Metal binding	31	31	.	.	.	Note=Zinc 2	
+P04386	UniProtKB	Metal binding	38	38	.	.	.	Note=Zinc 2	
+P04386	UniProtKB	Modified residue	694	694	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04386	UniProtKB	Modified residue	696	696	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04386	UniProtKB	Modified residue	699	699	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04386	UniProtKB	Modified residue	703	703	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04386	UniProtKB	Modified residue	712	712	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04386	UniProtKB	Mutagenesis	26	26	.	.	.	Note=Loss of DNA-binding. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3299106;Dbxref=PMID:3299106	
+P04386	UniProtKB	Helix	12	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ	
+P04386	UniProtKB	Beta strand	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ	
+P04386	UniProtKB	Helix	29	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ	
+P04386	UniProtKB	Helix	51	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ	
+P04386	UniProtKB	Beta strand	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ	
+P04386	UniProtKB	Helix	77	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ	
+P04386	UniProtKB	Helix	86	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ	
+##sequence-region Q04739 1 417
+Q04739	UniProtKB	Chain	1	417	.	.	.	ID=PRO_0000204373;Note=SNF1 protein kinase subunit beta-3	
+Q04739	UniProtKB	Region	152	342	.	.	.	Note=Kinase-interacting sequence (KIS)%3B required for interaction with SNF1	
+Q04739	UniProtKB	Region	343	417	.	.	.	Note=Association with SNF1 kinase complex (ASC) domain%3B required for interaction with SNF4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9121458;Dbxref=PMID:9121458	
+Q04739	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q04739	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04739	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04739	UniProtKB	Modified residue	135	135	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04739	UniProtKB	Modified residue	276	276	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q04739	UniProtKB	Modified residue	279	279	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P39719 1 783
+P39719	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Chain	23	783	.	.	.	ID=PRO_0000202424;Note=Flavin carrier protein 2	
+P39719	UniProtKB	Topological domain	23	182	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Topological domain	204	211	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Transmembrane	212	232	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Topological domain	233	347	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Transmembrane	348	368	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Topological domain	369	402	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Transmembrane	403	423	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Topological domain	424	430	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Transmembrane	431	451	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Topological domain	452	492	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Transmembrane	493	513	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Topological domain	514	521	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Transmembrane	522	542	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Topological domain	543	547	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Transmembrane	548	568	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Topological domain	569	581	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Transmembrane	582	602	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Topological domain	603	783	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Glycosylation	65	65	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Glycosylation	81	81	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Glycosylation	156	156	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Glycosylation	323	323	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39719	UniProtKB	Sequence conflict	111	111	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39719	UniProtKB	Sequence conflict	312	312	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39719	UniProtKB	Sequence conflict	641	643	.	.	.	Note=NDS->IDP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32785 1 401
+P32785	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32785	UniProtKB	Chain	27	401	.	.	.	ID=PRO_0000010096;Note=Methionyl-tRNA formyltransferase%2C mitochondrial	
+P32785	UniProtKB	Region	159	162	.	.	.	Note=Tetrahydrofolate (THF) binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q02207 1 900
+Q02207	UniProtKB	Chain	1	900	.	.	.	ID=PRO_0000054700;Note=Peroxisomal hydratase-dehydrogenase-epimerase	
+Q02207	UniProtKB	Domain	775	887	.	.	.	Note=MaoC-like	
+Q02207	UniProtKB	Nucleotide binding	13	37	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Nucleotide binding	75	76	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Nucleotide binding	165	169	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Nucleotide binding	197	200	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Nucleotide binding	326	350	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Region	6	230	.	.	.	Note=Short-chain dehydrogenase like 1	
+Q02207	UniProtKB	Region	319	535	.	.	.	Note=Short-chain dehydrogenase like 2	
+Q02207	UniProtKB	Region	689	690	.	.	.	Note=(3R)-3-hydroxydecanoyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Region	803	808	.	.	.	Note=(3R)-3-hydroxydecanoyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Motif	898	900	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02207	UniProtKB	Active site	165	165	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001	
+Q02207	UniProtKB	Active site	469	469	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001	
+Q02207	UniProtKB	Binding site	21	21	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Binding site	40	40	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Binding site	100	100	.	.	.	Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Binding site	152	152	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Binding site	456	456	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Binding site	719	719	.	.	.	Note=(3R)-3-hydroxydecanoyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Binding site	826	826	.	.	.	Note=(3R)-3-hydroxydecanoyl-CoA%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02207	UniProtKB	Binding site	851	851	.	.	.	Note=(3R)-3-hydroxydecanoyl-CoA%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P36033 1 711
+P36033	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Chain	24	711	.	.	.	ID=PRO_0000010138;Note=Ferric/cupric reductase transmembrane component 2	
+P36033	UniProtKB	Topological domain	24	164	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Transmembrane	165	185	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Topological domain	186	235	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Transmembrane	236	256	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Topological domain	257	280	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Transmembrane	281	301	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Topological domain	302	317	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Transmembrane	318	340	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Topological domain	341	353	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Transmembrane	354	374	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Topological domain	375	377	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Transmembrane	378	398	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Topological domain	399	400	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Transmembrane	401	423	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Topological domain	424	711	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Domain	280	414	.	.	.	Note=Ferric oxidoreductase	
+P36033	UniProtKB	Domain	415	534	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+P36033	UniProtKB	Nucleotide binding	479	485	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Nucleotide binding	526	529	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Nucleotide binding	677	678	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Metal binding	316	316	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36033	UniProtKB	Metal binding	330	330	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36033	UniProtKB	Metal binding	386	386	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36033	UniProtKB	Metal binding	400	400	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36033	UniProtKB	Glycosylation	85	85	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Glycosylation	108	108	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Glycosylation	120	120	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Glycosylation	134	134	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36033	UniProtKB	Glycosylation	341	341	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12473 1 712
+Q12473	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Chain	18	712	.	.	.	ID=PRO_0000010142;Note=Ferric reductase transmembrane component 6	
+Q12473	UniProtKB	Topological domain	18	167	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Topological domain	189	244	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Transmembrane	245	265	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Topological domain	266	287	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Transmembrane	288	308	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Topological domain	309	328	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Transmembrane	329	349	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Topological domain	350	360	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Transmembrane	361	381	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Topological domain	382	387	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Transmembrane	388	408	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Topological domain	409	416	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Transmembrane	417	437	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Topological domain	438	712	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Domain	287	411	.	.	.	Note=Ferric oxidoreductase	
+Q12473	UniProtKB	Domain	412	546	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+Q12473	UniProtKB	Nucleotide binding	493	499	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Nucleotide binding	538	541	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Nucleotide binding	678	679	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Compositional bias	553	556	.	.	.	Note=Poly-Leu	
+Q12473	UniProtKB	Metal binding	323	323	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12473	UniProtKB	Metal binding	337	337	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12473	UniProtKB	Metal binding	393	393	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12473	UniProtKB	Metal binding	407	407	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12473	UniProtKB	Glycosylation	89	89	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Glycosylation	112	112	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Glycosylation	124	124	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12473	UniProtKB	Mutagenesis	493	496	.	.	.	Note=Loss of function. HPFT->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17553781;Dbxref=PMID:17553781	
+##sequence-region Q12333 1 620
+Q12333	UniProtKB	Chain	1	620	.	.	.	ID=PRO_0000210150;Note=Ferric/cupric reductase transmembrane component 7	
+Q12333	UniProtKB	Topological domain	1	45	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12333	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12333	UniProtKB	Topological domain	67	107	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12333	UniProtKB	Transmembrane	108	128	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12333	UniProtKB	Topological domain	129	167	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12333	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12333	UniProtKB	Topological domain	189	194	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12333	UniProtKB	Transmembrane	195	215	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12333	UniProtKB	Topological domain	216	237	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12333	UniProtKB	Transmembrane	238	258	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12333	UniProtKB	Topological domain	259	265	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12333	UniProtKB	Transmembrane	266	286	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12333	UniProtKB	Topological domain	287	292	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12333	UniProtKB	Transmembrane	293	313	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12333	UniProtKB	Topological domain	314	620	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12333	UniProtKB	Domain	161	320	.	.	.	Note=Ferric oxidoreductase	
+Q12333	UniProtKB	Domain	321	419	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+Q12333	UniProtKB	Nucleotide binding	369	375	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12333	UniProtKB	Nucleotide binding	411	414	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12333	UniProtKB	Nucleotide binding	578	579	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12333	UniProtKB	Metal binding	197	197	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12333	UniProtKB	Metal binding	211	211	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12333	UniProtKB	Metal binding	271	271	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12333	UniProtKB	Metal binding	285	285	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P12709 1 554
+P12709	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P12709	UniProtKB	Chain	2	554	.	.	.	ID=PRO_0000180578;Note=Glucose-6-phosphate isomerase	
+P12709	UniProtKB	Active site	367	367	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12709	UniProtKB	Active site	398	398	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12709	UniProtKB	Active site	520	520	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12709	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P12709	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P12709	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P17649 1 471
+P17649	UniProtKB	Chain	1	471	.	.	.	ID=PRO_0000120382;Note=4-aminobutyrate aminotransferase	
+P17649	UniProtKB	Region	135	136	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80147	
+P17649	UniProtKB	Binding site	192	192	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80147	
+P17649	UniProtKB	Binding site	351	351	.	.	.	Note=Pyridoxal phosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80147	
+P17649	UniProtKB	Modified residue	326	326	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80147	
+P17649	UniProtKB	Sequence conflict	240	240	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17649	UniProtKB	Sequence conflict	240	240	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38225 1 669
+P38225	UniProtKB	Chain	1	669	.	.	.	ID=PRO_0000193181;Note=Very long-chain fatty acid transport protein	
+P38225	UniProtKB	Transmembrane	6	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38225	UniProtKB	Transmembrane	54	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38225	UniProtKB	Transmembrane	149	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38225	UniProtKB	Transmembrane	293	313	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38225	UniProtKB	Glycosylation	184	184	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38225	UniProtKB	Glycosylation	289	289	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38225	UniProtKB	Glycosylation	534	534	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38225	UniProtKB	Glycosylation	591	591	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38993 1 636
+P38993	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38993	UniProtKB	Chain	22	636	.	.	.	ID=PRO_0000002959;Note=Iron transport multicopper oxidase FET3	
+P38993	UniProtKB	Topological domain	22	559	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38993	UniProtKB	Transmembrane	560	584	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38993	UniProtKB	Topological domain	585	636	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38993	UniProtKB	Domain	73	144	.	.	.	Note=Plastocyanin-like 1	
+P38993	UniProtKB	Domain	190	300	.	.	.	Note=Plastocyanin-like 2	
+P38993	UniProtKB	Domain	382	500	.	.	.	Note=Plastocyanin-like 3	
+P38993	UniProtKB	Metal binding	81	81	.	.	.	Note=Copper 1%3B type 2	
+P38993	UniProtKB	Metal binding	83	83	.	.	.	Note=Copper 2%3B type 3	
+P38993	UniProtKB	Metal binding	126	126	.	.	.	Note=Copper 2%3B type 3	
+P38993	UniProtKB	Metal binding	128	128	.	.	.	Note=Copper 3%3B type 3	
+P38993	UniProtKB	Metal binding	413	413	.	.	.	Note=Copper 4%3B type 1	
+P38993	UniProtKB	Metal binding	416	416	.	.	.	Note=Copper 1%3B type 2	
+P38993	UniProtKB	Metal binding	418	418	.	.	.	Note=Copper 3%3B type 3	
+P38993	UniProtKB	Metal binding	483	483	.	.	.	Note=Copper 3%3B type 3	
+P38993	UniProtKB	Metal binding	484	484	.	.	.	Note=Copper 4%3B type 1	
+P38993	UniProtKB	Metal binding	485	485	.	.	.	Note=Copper 2%3B type 3	
+P38993	UniProtKB	Metal binding	489	489	.	.	.	Note=Copper 4%3B type 1	
+P38993	UniProtKB	Glycosylation	27	27	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618	
+P38993	UniProtKB	Glycosylation	74	74	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38993	UniProtKB	Glycosylation	77	77	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618	
+P38993	UniProtKB	Glycosylation	88	88	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618	
+P38993	UniProtKB	Glycosylation	113	113	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618	
+P38993	UniProtKB	Glycosylation	194	194	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618	
+P38993	UniProtKB	Glycosylation	198	198	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618	
+P38993	UniProtKB	Glycosylation	244	244	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618	
+P38993	UniProtKB	Glycosylation	265	265	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38993	UniProtKB	Glycosylation	292	292	.	.	.	Note=N-linked (GlcNAc...) asparagine	
+P38993	UniProtKB	Glycosylation	300	300	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618	
+P38993	UniProtKB	Glycosylation	359	359	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618	
+P38993	UniProtKB	Glycosylation	381	381	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618	
+P38993	UniProtKB	Beta strand	23	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	37	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	43	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	64	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Turn	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	109	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	121	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	132	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	138	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	153	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	168	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	189	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	208	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	222	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	231	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	239	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	249	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	256	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	271	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	282	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	292	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	336	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	353	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	369	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	383	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	388	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	392	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	400	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	413	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	422	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	433	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	455	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	467	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	478	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	487	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	495	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	502	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	509	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Helix	515	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	529	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+P38993	UniProtKB	Beta strand	535	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU	
+##sequence-region Q08913 1 375
+Q08913	UniProtKB	Chain	1	375	.	.	.	ID=PRO_0000241699;Note=Fluoride export protein 1	
+Q08913	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26055717;Dbxref=PMID:26055717	
+Q08913	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08913	UniProtKB	Topological domain	33	34	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26055717;Dbxref=PMID:26055717	
+Q08913	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08913	UniProtKB	Topological domain	56	79	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26055717;Dbxref=PMID:26055717	
+Q08913	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08913	UniProtKB	Topological domain	101	127	.	.	.	Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26055717;Dbxref=PMID:26055717	
+Q08913	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08913	UniProtKB	Topological domain	149	213	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26055717;Dbxref=PMID:26055717	
+Q08913	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08913	UniProtKB	Topological domain	235	241	.	.	.	Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26055717;Dbxref=PMID:26055717	
+Q08913	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08913	UniProtKB	Topological domain	263	268	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26055717;Dbxref=PMID:26055717	
+Q08913	UniProtKB	Transmembrane	269	289	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08913	UniProtKB	Topological domain	290	310	.	.	.	Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26055717;Dbxref=PMID:26055717	
+Q08913	UniProtKB	Transmembrane	311	331	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08913	UniProtKB	Topological domain	332	338	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26055717;Dbxref=PMID:26055717	
+Q08913	UniProtKB	Transmembrane	339	359	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08913	UniProtKB	Topological domain	360	375	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26055717;Dbxref=PMID:26055717	
+Q08913	UniProtKB	Glycosylation	109	109	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q08913	UniProtKB	Glycosylation	117	117	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q08913	UniProtKB	Glycosylation	235	235	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+##sequence-region P39521 1 936
+P39521	UniProtKB	Chain	1	936	.	.	.	ID=PRO_0000091901;Note=Pre-rRNA-processing protein FHL1	
+P39521	UniProtKB	Domain	300	357	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+P39521	UniProtKB	DNA binding	460	552	.	.	.	Note=Fork-head;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00089	
+P39521	UniProtKB	Compositional bias	816	862	.	.	.	Note=Ser-rich	
+P39521	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950	
+P39521	UniProtKB	Modified residue	228	228	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39521	UniProtKB	Modified residue	230	230	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39521	UniProtKB	Modified residue	247	247	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39521	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P32472 1 135
+P32472	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32472	UniProtKB	Chain	18	135	.	.	.	ID=PRO_0000025512;Note=Peptidyl-prolyl cis-trans isomerase FPR2	
+P32472	UniProtKB	Domain	43	132	.	.	.	Note=PPIase FKBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00277	
+##sequence-region P53121 1 802
+P53121	UniProtKB	Signal peptide	1	28	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Chain	29	802	.	.	.	ID=PRO_0000202738;Note=Putative flavin carrier protein 3	
+P53121	UniProtKB	Topological domain	29	169	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Transmembrane	170	190	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Topological domain	191	200	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Transmembrane	201	221	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Topological domain	222	229	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Transmembrane	230	250	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Topological domain	251	255	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Transmembrane	256	278	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Topological domain	279	323	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Transmembrane	324	344	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Topological domain	345	377	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Transmembrane	378	398	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Topological domain	399	405	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Transmembrane	406	426	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Topological domain	427	467	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Transmembrane	468	488	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Topological domain	489	495	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Transmembrane	496	516	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Topological domain	517	525	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Transmembrane	526	546	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Topological domain	547	557	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Transmembrane	558	578	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Topological domain	579	802	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Modified residue	616	616	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53121	UniProtKB	Modified residue	635	635	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53121	UniProtKB	Modified residue	779	779	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53121	UniProtKB	Modified residue	782	782	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53121	UniProtKB	Glycosylation	149	149	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Glycosylation	321	321	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53121	UniProtKB	Glycosylation	547	547	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40491 1 155
+##sequence-region Q12497 1 93
+Q12497	UniProtKB	Transit peptide	1	25	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12497	UniProtKB	Chain	26	93	.	.	.	ID=PRO_0000244462;Note=Protein FMP16%2C mitochondrial	
+##sequence-region P40008 1 231
+P40008	UniProtKB	Transit peptide	1	44	.	.	.	Note=Mitochondrion	
+P40008	UniProtKB	Chain	45	231	.	.	.	ID=PRO_0000202620;Note=Protein FMP52%2C mitochondrial	
+##sequence-region P22007 1 431
+P22007	UniProtKB	Chain	1	431	.	.	.	ID=PRO_0000119768;Note=Protein farnesyltransferase subunit beta	
+P22007	UniProtKB	Repeat	130	171	.	.	.	Note=PFTB 1	
+P22007	UniProtKB	Repeat	182	224	.	.	.	Note=PFTB 2	
+P22007	UniProtKB	Repeat	231	273	.	.	.	Note=PFTB 3	
+P22007	UniProtKB	Repeat	280	322	.	.	.	Note=PFTB 4	
+P22007	UniProtKB	Repeat	332	375	.	.	.	Note=PFTB 5	
+P22007	UniProtKB	Region	258	261	.	.	.	Note=Farnesyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22007	UniProtKB	Region	301	304	.	.	.	Note=Farnesyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22007	UniProtKB	Region	310	313	.	.	.	Note=Farnesyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22007	UniProtKB	Metal binding	307	307	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22007	UniProtKB	Metal binding	309	309	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22007	UniProtKB	Metal binding	363	363	.	.	.	Note=Zinc%3B via tele nitrogen%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22007	UniProtKB	Site	108	108	.	.	.	Note=Important for selectivity against geranylgeranyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22007	UniProtKB	Sequence conflict	47	47	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region O13329 1 566
+O13329	UniProtKB	Chain	1	566	.	.	.	ID=PRO_0000087323;Note=DNA replication fork-blocking protein FOB1	
+O13329	UniProtKB	Zinc finger	159	196	.	.	.	Note=C2H2-type;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14645529;Dbxref=PMID:14645529	
+O13329	UniProtKB	Mutagenesis	159	159	.	.	.	Note=Abolishes RFB-binding%2C replication fork blocking activity and reduces recombination rate. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14645529;Dbxref=PMID:14645529	
+O13329	UniProtKB	Mutagenesis	164	164	.	.	.	Note=Abolishes RFB-binding%2C replication fork blocking activity and reduces recombination rate. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14645529;Dbxref=PMID:14645529	
+O13329	UniProtKB	Mutagenesis	193	193	.	.	.	Note=Abolishes RFB-binding%2C replication fork blocking activity and reduces recombination rate. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14645529;Dbxref=PMID:14645529	
+O13329	UniProtKB	Mutagenesis	196	196	.	.	.	Note=Abolishes RFB-binding%2C replication fork blocking activity and reduces recombination rate. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14645529;Dbxref=PMID:14645529	
+O13329	UniProtKB	Mutagenesis	291	291	.	.	.	Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14645529;Dbxref=PMID:14645529	
+O13329	UniProtKB	Sequence conflict	103	103	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08911 1 376
+Q08911	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000223647;Note=Formate dehydrogenase 1	
+Q08911	UniProtKB	Nucleotide binding	176	177	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Nucleotide binding	244	248	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Nucleotide binding	325	328	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Region	5	121	.	.	.	Note=Catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Region	122	326	.	.	.	Note=Coenzyme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Region	327	372	.	.	.	Note=Catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Binding site	97	97	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Binding site	121	121	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Binding site	197	197	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Binding site	270	270	.	.	.	Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Binding site	296	296	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Site	272	272	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Site	325	325	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210	
+Q08911	UniProtKB	Mutagenesis	197	198	.	.	.	Note=Shifts the coenzyme preference of the enzyme from NAD(+) to NADP(+). DY->AR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12144528;Dbxref=PMID:12144528	
+##sequence-region P40466 1 484
+P40466	UniProtKB	Chain	1	484	.	.	.	ID=PRO_0000091903;Note=Fork head protein homolog 1	
+P40466	UniProtKB	Domain	76	142	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+P40466	UniProtKB	DNA binding	302	393	.	.	.	Note=Fork-head;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00089	
+##sequence-region Q08967 1 793
+Q08967	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Chain	22	793	.	.	.	ID=PRO_0000252267;Note=Flavin carrier protein 1	
+Q08967	UniProtKB	Topological domain	22	163	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Topological domain	185	194	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Transmembrane	195	215	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Topological domain	216	223	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Transmembrane	224	244	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Topological domain	245	249	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Transmembrane	250	272	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Topological domain	273	317	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Transmembrane	318	338	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Topological domain	339	372	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Topological domain	394	397	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Transmembrane	398	418	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Topological domain	419	461	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Transmembrane	462	482	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Topological domain	483	484	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Transmembrane	485	505	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Topological domain	506	516	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Transmembrane	517	537	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Topological domain	538	551	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Transmembrane	552	572	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Topological domain	573	793	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Modified residue	610	610	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53121	
+Q08967	UniProtKB	Modified residue	626	626	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08967	UniProtKB	Modified residue	771	771	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+Q08967	UniProtKB	Modified residue	774	774	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08967	UniProtKB	Glycosylation	143	143	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08967	UniProtKB	Glycosylation	281	281	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53739 1 893
+P53739	UniProtKB	Chain	1	893	.	.	.	ID=PRO_0000086154;Note=Flippase kinase 1	
+P53739	UniProtKB	Domain	496	777	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53739	UniProtKB	Domain	778	861	.	.	.	Note=AGC-kinase C-terminal	
+P53739	UniProtKB	Nucleotide binding	502	510	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53739	UniProtKB	Active site	621	621	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P53739	UniProtKB	Binding site	525	525	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53739	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53739	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53739	UniProtKB	Modified residue	171	171	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53739	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53739	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53739	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53739	UniProtKB	Modified residue	414	414	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53739	UniProtKB	Modified residue	462	462	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P23900 1 669
+P23900	UniProtKB	Chain	1	669	.	.	.	ID=PRO_0000064098;Note=Glycerol uptake/efflux facilitator protein	
+P23900	UniProtKB	Topological domain	1	254	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23900	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23900	UniProtKB	Topological domain	276	325	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23900	UniProtKB	Transmembrane	326	346	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23900	UniProtKB	Topological domain	347	369	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23900	UniProtKB	Transmembrane	370	390	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23900	UniProtKB	Topological domain	391	446	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23900	UniProtKB	Transmembrane	447	467	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23900	UniProtKB	Topological domain	468	506	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23900	UniProtKB	Transmembrane	507	527	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23900	UniProtKB	Topological domain	528	669	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23900	UniProtKB	Motif	352	354	.	.	.	Note=NPA 1	
+P23900	UniProtKB	Motif	480	482	.	.	.	Note=NPA 2	
+P23900	UniProtKB	Compositional bias	50	69	.	.	.	Note=Asn-rich	
+P23900	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P23900	UniProtKB	Modified residue	168	168	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P23900	UniProtKB	Modified residue	209	209	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23900	UniProtKB	Modified residue	212	212	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P23900	UniProtKB	Sequence conflict	640	640	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05015 1 223
+Q05015	UniProtKB	Chain	1	223	.	.	.	ID=PRO_0000212581;Note=Family of serine hydrolases 2	
+Q05015	UniProtKB	Active site	110	110	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05015	UniProtKB	Active site	174	174	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05015	UniProtKB	Active site	203	203	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q99369 1 266
+Q99369	UniProtKB	Chain	1	266	.	.	.	ID=PRO_0000212582;Note=Family of serine hydrolases 3	
+Q99369	UniProtKB	Active site	117	117	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99369	UniProtKB	Active site	180	180	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99369	UniProtKB	Active site	209	209	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38310 1 465
+P38310	UniProtKB	Chain	1	465	.	.	.	ID=PRO_0000159650;Note=Iron transporter FTH1	
+P38310	UniProtKB	Topological domain	1	11	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38310	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38310	UniProtKB	Topological domain	33	135	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38310	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38310	UniProtKB	Topological domain	157	170	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38310	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38310	UniProtKB	Topological domain	192	289	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38310	UniProtKB	Transmembrane	290	310	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38310	UniProtKB	Topological domain	311	358	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38310	UniProtKB	Transmembrane	359	379	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38310	UniProtKB	Topological domain	380	465	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38310	UniProtKB	Modified residue	449	449	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P38310	UniProtKB	Modified residue	453	453	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38310	UniProtKB	Sequence conflict	18	18	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	18	18	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	36	36	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	36	36	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	228	228	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	228	228	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	249	250	.	.	.	Note=VF->YS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	249	250	.	.	.	Note=VF->YS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	334	334	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	334	334	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	389	390	.	.	.	Note=IC->KY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	389	390	.	.	.	Note=IC->KY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	399	401	.	.	.	Note=EKY->GKC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38310	UniProtKB	Sequence conflict	399	401	.	.	.	Note=EKY->GKC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12247 1 151
+Q12247	UniProtKB	Chain	1	151	.	.	.	ID=PRO_0000087404;Note=rRNA-processing protein FYV7	
+Q12247	UniProtKB	Coiled coil	70	113	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32805 1 299
+P32805	UniProtKB	Chain	1	299	.	.	.	ID=PRO_0000046805;Note=Zinc finger protein FZF1	
+P32805	UniProtKB	Zinc finger	12	36	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P32805	UniProtKB	Zinc finger	42	66	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P32805	UniProtKB	Zinc finger	72	94	.	.	.	Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P32805	UniProtKB	Zinc finger	155	179	.	.	.	Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P32805	UniProtKB	Zinc finger	246	271	.	.	.	Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P32805	UniProtKB	Motif	96	107	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32805	UniProtKB	Natural variant	110	110	.	.	.	Note=In strain: Sgu52E and Sgu52F. G->E	
+P32805	UniProtKB	Natural variant	120	120	.	.	.	Note=In strain: MMW1-15h2%2C MMW1-2h2%2C Sgu52E and Sgu52F. N->D	
+P32805	UniProtKB	Natural variant	228	228	.	.	.	Note=In strain: MMW1-15h2%2C MMW1-2h2%2C Sgu52E and Sgu52F. V->I	
+P32805	UniProtKB	Natural variant	238	238	.	.	.	Note=In strain: MMW1-15h2 and MMW1-2h2. D->N	
+P32805	UniProtKB	Sequence conflict	180	180	.	.	.	Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32805	UniProtKB	Sequence conflict	235	235	.	.	.	Note=T->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32805	UniProtKB	Sequence conflict	246	246	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00358 1 332
+P00358	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6	
+P00358	UniProtKB	Chain	2	332	.	.	.	ID=PRO_0000145590;Note=Glyceraldehyde-3-phosphate dehydrogenase 2	
+P00358	UniProtKB	Nucleotide binding	11	12	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00358	UniProtKB	Region	149	151	.	.	.	Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00358	UniProtKB	Region	209	210	.	.	.	Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00358	UniProtKB	Active site	150	150	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10009	
+P00358	UniProtKB	Binding site	33	33	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00358	UniProtKB	Binding site	78	78	.	.	.	Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00358	UniProtKB	Binding site	180	180	.	.	.	Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00358	UniProtKB	Binding site	232	232	.	.	.	Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00358	UniProtKB	Binding site	314	314	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00358	UniProtKB	Site	177	177	.	.	.	Note=Activates thiol group during catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00358	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00359	
+P00358	UniProtKB	Cross-link	46	46	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00359	
+P00358	UniProtKB	Cross-link	63	63	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00358	UniProtKB	Sequence conflict	77	77	.	.	.	Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00359 1 332
+P00359	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11946592;Dbxref=PMID:11946592	
+P00359	UniProtKB	Chain	2	332	.	.	.	ID=PRO_0000145591;Note=Glyceraldehyde-3-phosphate dehydrogenase 3	
+P00359	UniProtKB	Nucleotide binding	11	12	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00359	UniProtKB	Region	149	151	.	.	.	Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00359	UniProtKB	Region	209	210	.	.	.	Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00359	UniProtKB	Active site	150	150	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10009	
+P00359	UniProtKB	Binding site	33	33	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00359	UniProtKB	Binding site	78	78	.	.	.	Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00359	UniProtKB	Binding site	180	180	.	.	.	Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00359	UniProtKB	Binding site	232	232	.	.	.	Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00359	UniProtKB	Binding site	314	314	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00359	UniProtKB	Site	177	177	.	.	.	Note=Activates thiol group during catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00359	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00359	UniProtKB	Cross-link	46	46	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00359	UniProtKB	Cross-link	63	63	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00359	UniProtKB	Sequence conflict	136	136	.	.	.	Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00359	UniProtKB	Sequence conflict	136	136	.	.	.	Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00359	UniProtKB	Sequence conflict	248	248	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00359	UniProtKB	Sequence conflict	248	248	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00359	UniProtKB	Sequence conflict	287	287	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00359	UniProtKB	Sequence conflict	329	329	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00359	UniProtKB	Sequence conflict	329	329	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00359	UniProtKB	Beta strand	3	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	11	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	27	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	38	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Turn	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	62	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	70	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Turn	85	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	91	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	103	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	115	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Turn	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	150	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	168	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	183	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	211	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	225	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	239	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	253	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Turn	266	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	272	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	281	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	290	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	295	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	299	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Beta strand	305	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+P00359	UniProtKB	Helix	316	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM	
+##sequence-region P40569 1 121
+P40569	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000083487;Note=Protein GAT4	
+P40569	UniProtKB	Zinc finger	53	79	.	.	.	Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094	
+##sequence-region P38260 1 290
+P38260	UniProtKB	Chain	1	290	.	.	.	ID=PRO_0000202485;Note=Hsp70 nucleotide exchange factor FES1	
+P38260	UniProtKB	Repeat	13	57	.	.	.	Note=ARM 1	
+P38260	UniProtKB	Repeat	76	116	.	.	.	Note=ARM 2	
+P38260	UniProtKB	Repeat	120	161	.	.	.	Note=ARM 3	
+P38260	UniProtKB	Repeat	164	205	.	.	.	Note=ARM 4	
+P38260	UniProtKB	Repeat	211	251	.	.	.	Note=ARM 5	
+P38260	UniProtKB	Repeat	253	290	.	.	.	Note=ARM 6	
+P38260	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P43561 1 622
+P43561	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Chain	19	622	.	.	.	ID=PRO_0000002960;Note=Iron transport multicopper oxidase FET5	
+P43561	UniProtKB	Topological domain	19	573	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Transmembrane	574	594	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Topological domain	595	622	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Domain	43	146	.	.	.	Note=Plastocyanin-like 1	
+P43561	UniProtKB	Domain	192	301	.	.	.	Note=Plastocyanin-like 2	
+P43561	UniProtKB	Domain	392	514	.	.	.	Note=Plastocyanin-like 3	
+P43561	UniProtKB	Metal binding	79	79	.	.	.	Note=Copper 1%3B type 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43561	UniProtKB	Metal binding	81	81	.	.	.	Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43561	UniProtKB	Metal binding	128	128	.	.	.	Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43561	UniProtKB	Metal binding	130	130	.	.	.	Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43561	UniProtKB	Metal binding	418	418	.	.	.	Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43561	UniProtKB	Metal binding	421	421	.	.	.	Note=Copper 1%3B type 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43561	UniProtKB	Metal binding	423	423	.	.	.	Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43561	UniProtKB	Metal binding	496	496	.	.	.	Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43561	UniProtKB	Metal binding	497	497	.	.	.	Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43561	UniProtKB	Metal binding	498	498	.	.	.	Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43561	UniProtKB	Metal binding	502	502	.	.	.	Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43561	UniProtKB	Glycosylation	24	24	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Glycosylation	86	86	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Glycosylation	196	196	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Glycosylation	200	200	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Glycosylation	246	246	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Glycosylation	295	295	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Glycosylation	364	364	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43561	UniProtKB	Glycosylation	455	455	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P41813 1 862
+P41813	UniProtKB	Chain	1	862	.	.	.	ID=PRO_0000091904;Note=Fork head protein homolog 2	
+P41813	UniProtKB	Domain	83	152	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+P41813	UniProtKB	DNA binding	339	430	.	.	.	Note=Fork-head;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00089	
+P41813	UniProtKB	Modified residue	708	708	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41813	UniProtKB	Modified residue	832	832	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P41813	UniProtKB	Modified residue	833	833	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P40989 1 1895
+P40989	UniProtKB	Chain	1	1895	.	.	.	ID=PRO_0000121726;Note=1%2C3-beta-glucan synthase component GSC2	
+P40989	UniProtKB	Topological domain	1	473	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Transmembrane	474	494	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Topological domain	495	511	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Transmembrane	512	532	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Topological domain	533	550	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Transmembrane	551	571	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Topological domain	572	582	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Transmembrane	583	603	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Topological domain	604	1579	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Transmembrane	1580	1600	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Topological domain	1601	1620	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Transmembrane	1621	1641	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Topological domain	1642	1758	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Transmembrane	1759	1779	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Topological domain	1780	1821	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Transmembrane	1822	1842	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Topological domain	1843	1895	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40989	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631	
+P40989	UniProtKB	Modified residue	291	291	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631	
+P40989	UniProtKB	Cross-link	278	278	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631	
+P40989	UniProtKB	Cross-link	405	405	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631	
+P40989	UniProtKB	Cross-link	929	929	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631	
+P40989	UniProtKB	Cross-link	934	934	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631	
+P40989	UniProtKB	Cross-link	1558	1558	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631	
+P40989	UniProtKB	Cross-link	1566	1566	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631	
+P40989	UniProtKB	Natural variant	1059	1059	.	.	.	Note=In strain: SK1. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40989	UniProtKB	Natural variant	1853	1854	.	.	.	Note=In strain: SK1. TG->KD	
+P40989	UniProtKB	Sequence conflict	137	137	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40989	UniProtKB	Sequence conflict	261	261	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40989	UniProtKB	Sequence conflict	275	275	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12676 1 427
+Q12676	UniProtKB	Chain	1	427	.	.	.	ID=PRO_0000168308;Note=Dihydrofolate synthetase	
+Q12676	UniProtKB	Nucleotide binding	34	37	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+Q12676	UniProtKB	Metal binding	123	123	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+Q12676	UniProtKB	Metal binding	153	153	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+Q12676	UniProtKB	Binding site	275	275	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+Q12676	UniProtKB	Binding site	296	296	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+##sequence-region Q08905 1 711
+Q08905	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Chain	21	711	.	.	.	ID=PRO_0000010139;Note=Ferric reductase transmembrane component 3	
+Q08905	UniProtKB	Topological domain	21	166	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Transmembrane	167	187	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Topological domain	188	237	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Transmembrane	238	258	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Topological domain	259	280	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Transmembrane	281	301	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Topological domain	302	321	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Transmembrane	322	341	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Topological domain	342	353	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Transmembrane	354	374	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Topological domain	375	376	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Transmembrane	377	397	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Topological domain	398	398	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Transmembrane	399	419	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Topological domain	420	711	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Domain	280	414	.	.	.	Note=Ferric oxidoreductase	
+Q08905	UniProtKB	Domain	415	534	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+Q08905	UniProtKB	Nucleotide binding	479	485	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Nucleotide binding	526	529	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Nucleotide binding	677	678	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Metal binding	316	316	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08905	UniProtKB	Metal binding	330	330	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08905	UniProtKB	Metal binding	386	386	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08905	UniProtKB	Metal binding	400	400	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08905	UniProtKB	Glycosylation	85	85	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Glycosylation	108	108	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Glycosylation	120	120	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08905	UniProtKB	Glycosylation	134	134	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08908 1 694
+Q08908	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08908	UniProtKB	Chain	20	694	.	.	.	ID=PRO_0000010141;Note=Ferric reductase transmembrane component 5	
+Q08908	UniProtKB	Topological domain	20	163	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08908	UniProtKB	Topological domain	185	222	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Transmembrane	223	243	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08908	UniProtKB	Topological domain	244	267	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Transmembrane	268	288	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08908	UniProtKB	Topological domain	289	311	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Transmembrane	312	334	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08908	UniProtKB	Topological domain	335	347	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Transmembrane	348	368	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08908	UniProtKB	Topological domain	369	371	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08908	UniProtKB	Topological domain	393	403	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Transmembrane	404	424	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08908	UniProtKB	Topological domain	425	694	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Domain	274	408	.	.	.	Note=Ferric oxidoreductase	
+Q08908	UniProtKB	Domain	409	528	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+Q08908	UniProtKB	Nucleotide binding	473	479	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08908	UniProtKB	Nucleotide binding	520	523	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08908	UniProtKB	Nucleotide binding	660	661	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08908	UniProtKB	Compositional bias	362	368	.	.	.	Note=Poly-Phe	
+Q08908	UniProtKB	Metal binding	310	310	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Metal binding	324	324	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Metal binding	380	380	.	.	.	Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Metal binding	394	394	.	.	.	Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08908	UniProtKB	Glycosylation	117	117	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12209 1 686
+Q12209	UniProtKB	Chain	1	686	.	.	.	ID=PRO_0000239647;Note=Probable ferric reductase transmembrane component 8	
+Q12209	UniProtKB	Topological domain	1	35	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Transmembrane	36	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Topological domain	57	89	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Topological domain	111	128	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Transmembrane	129	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Topological domain	150	157	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Transmembrane	158	178	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Topological domain	179	186	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Topological domain	208	216	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Topological domain	238	267	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Transmembrane	268	288	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Topological domain	289	402	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Transmembrane	403	423	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Topological domain	424	686	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Domain	119	666	.	.	.	Note=Ferric oxidoreductase	
+Q12209	UniProtKB	Nucleotide binding	320	326	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Nucleotide binding	442	450	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Glycosylation	371	371	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Glycosylation	383	383	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12209	UniProtKB	Glycosylation	384	384	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03002 1 865
+Q03002	UniProtKB	Chain	1	865	.	.	.	ID=PRO_0000234367;Note=Fatty acyl-CoA synthetase and RNA processing-associated kinase 1	
+Q03002	UniProtKB	Domain	41	313	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03002	UniProtKB	Nucleotide binding	47	55	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03002	UniProtKB	Active site	175	175	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q03002	UniProtKB	Binding site	80	80	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03002	UniProtKB	Modified residue	441	441	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P37261 1 193
+P37261	UniProtKB	Chain	1	193	.	.	.	ID=PRO_0000087340;Note=Fatty acid repression mutant protein 2	
+P37261	UniProtKB	Helix	7	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Helix	31	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Helix	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Beta strand	55	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Helix	60	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Turn	81	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Beta strand	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Beta strand	91	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Helix	100	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Helix	117	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Beta strand	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Helix	149	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Beta strand	158	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Beta strand	164	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+P37261	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP	
+##sequence-region P32599 1 642
+P32599	UniProtKB	Chain	1	642	.	.	.	ID=PRO_0000073757;Note=Fimbrin	
+P32599	UniProtKB	Domain	16	50	.	.	.	Note=EF-hand 1	
+P32599	UniProtKB	Domain	51	86	.	.	.	Note=EF-hand 2	
+P32599	UniProtKB	Domain	139	259	.	.	.	Note=Calponin-homology (CH) 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044	
+P32599	UniProtKB	Domain	287	390	.	.	.	Note=Calponin-homology (CH) 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044	
+P32599	UniProtKB	Domain	411	521	.	.	.	Note=Calponin-homology (CH) 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044	
+P32599	UniProtKB	Domain	534	642	.	.	.	Note=Calponin-homology (CH) 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044	
+P32599	UniProtKB	Calcium binding	29	40	.	.	.	Note=1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32599	UniProtKB	Calcium binding	64	75	.	.	.	Note=2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32599	UniProtKB	Region	125	394	.	.	.	Note=Actin-binding 1	
+P32599	UniProtKB	Region	395	642	.	.	.	Note=Actin-binding 2	
+##sequence-region Q03898 1 291
+Q03898	UniProtKB	Chain	1	291	.	.	.	ID=PRO_0000087257;Note=Filament protein FIN1	
+Q03898	UniProtKB	Coiled coil	254	284	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03898	UniProtKB	Compositional bias	153	158	.	.	.	Note=Poly-Gln	
+Q03898	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q03898	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q03898	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+Q03898	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q04433 1 528
+Q04433	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04433	UniProtKB	Chain	19	506	.	.	.	ID=PRO_0000021265;Note=Facilitator of iron transport 1	
+Q04433	UniProtKB	Propeptide	507	528	.	.	.	ID=PRO_0000021266;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04433	UniProtKB	Repeat	20	98	.	.	.	Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	99	168	.	.	.	Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	169	233	.	.	.	Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	234	274	.	.	.	Note=1-4%3B truncated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	289	294	.	.	.	Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	295	300	.	.	.	Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	301	306	.	.	.	Note=2-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	307	312	.	.	.	Note=2-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	313	318	.	.	.	Note=2-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	319	324	.	.	.	Note=2-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	325	330	.	.	.	Note=2-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	331	336	.	.	.	Note=2-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	337	342	.	.	.	Note=2-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	343	348	.	.	.	Note=2-10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	349	353	.	.	.	Note=2-11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Repeat	354	359	.	.	.	Note=2-12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q04433	UniProtKB	Nucleotide binding	488	495	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04433	UniProtKB	Region	20	274	.	.	.	Note=4 X approximate tandem repeats	
+Q04433	UniProtKB	Region	289	359	.	.	.	Note=12 X 6 AA approximate tandem repeats%2C Ser/Thr-rich	
+Q04433	UniProtKB	Compositional bias	22	498	.	.	.	Note=Thr-rich	
+Q04433	UniProtKB	Compositional bias	275	478	.	.	.	Note=Ser-rich	
+Q04433	UniProtKB	Lipidation	506	506	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04433	UniProtKB	Glycosylation	412	412	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04433	UniProtKB	Glycosylation	464	464	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04433	UniProtKB	Glycosylation	503	503	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39712 1 1322
+P39712	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Chain	25	1299	.	.	.	ID=PRO_0000021277;Note=Flocculation protein FLO9	
+P39712	UniProtKB	Propeptide	1300	1322	.	.	.	ID=PRO_0000372454;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Domain	74	249	.	.	.	Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164	
+P39712	UniProtKB	Repeat	278	322	.	.	.	Note=1-1	
+P39712	UniProtKB	Repeat	323	367	.	.	.	Note=1-2	
+P39712	UniProtKB	Repeat	368	412	.	.	.	Note=1-3	
+P39712	UniProtKB	Repeat	413	457	.	.	.	Note=1-4	
+P39712	UniProtKB	Repeat	458	502	.	.	.	Note=1-5	
+P39712	UniProtKB	Repeat	503	547	.	.	.	Note=1-6	
+P39712	UniProtKB	Repeat	548	592	.	.	.	Note=1-7	
+P39712	UniProtKB	Repeat	593	637	.	.	.	Note=1-8	
+P39712	UniProtKB	Repeat	638	682	.	.	.	Note=1-9	
+P39712	UniProtKB	Repeat	683	727	.	.	.	Note=1-10	
+P39712	UniProtKB	Repeat	728	772	.	.	.	Note=1-11	
+P39712	UniProtKB	Repeat	773	817	.	.	.	Note=1-12	
+P39712	UniProtKB	Repeat	818	862	.	.	.	Note=1-13	
+P39712	UniProtKB	Repeat	892	906	.	.	.	Note=2-1	
+P39712	UniProtKB	Repeat	907	921	.	.	.	Note=2-2	
+P39712	UniProtKB	Repeat	922	936	.	.	.	Note=2-3	
+P39712	UniProtKB	Repeat	1013	1063	.	.	.	Note=3-1	
+P39712	UniProtKB	Repeat	1085	1135	.	.	.	Note=3-2	
+P39712	UniProtKB	Repeat	1136	1186	.	.	.	Note=3-3	
+P39712	UniProtKB	Region	197	240	.	.	.	Note=Sugar recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39712	UniProtKB	Region	278	862	.	.	.	Note=13 X 45 AA approximate tandem repeats%2C Thr-rich	
+P39712	UniProtKB	Region	892	936	.	.	.	Note=3 X 15 AA approximate repeats%2C Ser-rich	
+P39712	UniProtKB	Region	1013	1186	.	.	.	Note=3 X 51 AA approximate repeats%2C Thr-rich	
+P39712	UniProtKB	Lipidation	1299	1299	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	135	135	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	187	187	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	203	203	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	257	257	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	262	262	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	270	270	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	329	329	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	419	419	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	464	464	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	509	509	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	554	554	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	599	599	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	644	644	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	689	689	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	734	734	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39712	UniProtKB	Glycosylation	888	888	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P03870 1 423
+P03870	UniProtKB	Chain	1	423	.	.	.	ID=PRO_0000197567;Note=Site-specific recombinase Flp	
+P03870	UniProtKB	Active site	343	343	.	.	.	Note=O-(3'-phospho-DNA)-tyrosine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2211714;Dbxref=PMID:2211714	
+P03870	UniProtKB	Mutagenesis	305	305	.	.	.	Note=Inactive and weakened DNA binding. H->L%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2974924;Dbxref=PMID:2974924	
+P03870	UniProtKB	Mutagenesis	305	305	.	.	.	Note=Reduced activity. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2974924;Dbxref=PMID:2974924	
+P03870	UniProtKB	Mutagenesis	308	308	.	.	.	Note=Inactive and weakened DNA binding. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2974924;Dbxref=PMID:2974924	
+P03870	UniProtKB	Mutagenesis	343	343	.	.	.	Note=No strand cleavage or recombination. Y->F%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3104911;Dbxref=PMID:3104911	
+P03870	UniProtKB	Sequence conflict	5	5	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03870	UniProtKB	Sequence conflict	5	5	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03870	UniProtKB	Helix	3	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	12	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	35	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	54	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Turn	72	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Beta strand	76	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	86	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Beta strand	101	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	116	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	138	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Beta strand	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M6X	
+P03870	UniProtKB	Helix	154	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Turn	164	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	172	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	192	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Beta strand	199	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Turn	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Beta strand	214	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Beta strand	228	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Beta strand	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	241	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Beta strand	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P4E	
+P03870	UniProtKB	Beta strand	272	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	279	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	294	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	306	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	324	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	337	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Turn	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P4E	
+P03870	UniProtKB	Helix	352	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Beta strand	361	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Turn	366	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Beta strand	370	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	380	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	395	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Helix	401	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+P03870	UniProtKB	Turn	404	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P4E	
+P03870	UniProtKB	Helix	409	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO	
+##sequence-region P38124 1 548
+P38124	UniProtKB	Chain	1	548	.	.	.	ID=PRO_0000173435;Note=Fluconazole resistance protein 1	
+P38124	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38124	UniProtKB	Transmembrane	139	159	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38124	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38124	UniProtKB	Transmembrane	203	223	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38124	UniProtKB	Transmembrane	230	250	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38124	UniProtKB	Transmembrane	261	281	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38124	UniProtKB	Transmembrane	347	367	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38124	UniProtKB	Transmembrane	376	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38124	UniProtKB	Transmembrane	416	436	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38124	UniProtKB	Transmembrane	440	460	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38124	UniProtKB	Transmembrane	476	496	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38124	UniProtKB	Transmembrane	511	531	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06179 1 2628
+##sequence-region P46998 1 180
+P46998	UniProtKB	Chain	1	180	.	.	.	ID=PRO_0000203028;Note=Mitochondrial membrane protein FMP33	
+P46998	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46998	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46998	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53889 1 259
+P53889	UniProtKB	Chain	1	259	.	.	.	ID=PRO_0000156843;Note=Uncharacterized mitochondrial hydrolase FMP41	
+P53889	UniProtKB	Metal binding	87	87	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53889	UniProtKB	Metal binding	89	89	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53889	UniProtKB	Metal binding	121	121	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53889	UniProtKB	Helix	4	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	12	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Helix	23	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	88	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Helix	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Helix	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	113	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Helix	125	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Helix	139	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Helix	156	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Turn	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	170	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	179	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Helix	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Helix	193	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	228	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+P53889	UniProtKB	Beta strand	238	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ	
+##sequence-region Q07651 1 309
+Q07651	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000202591;Note=SUR7 family protein FMP45	
+Q07651	UniProtKB	Topological domain	1	5	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07651	UniProtKB	Transmembrane	6	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07651	UniProtKB	Topological domain	27	116	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07651	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07651	UniProtKB	Topological domain	138	140	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07651	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07651	UniProtKB	Topological domain	162	188	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07651	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07651	UniProtKB	Topological domain	210	309	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07651	UniProtKB	Modified residue	230	230	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07651	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07651	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07651	UniProtKB	Glycosylation	73	73	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P31380 1 1131
+P31380	UniProtKB	Chain	1	1131	.	.	.	ID=PRO_0000074384;Note=ATP-dependent helicase FUN30	
+P31380	UniProtKB	Domain	584	752	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P31380	UniProtKB	Domain	953	1108	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P31380	UniProtKB	Nucleotide binding	597	604	.	.	.	Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31380	UniProtKB	Region	76	111	.	.	.	Note=CUE-like region	
+P31380	UniProtKB	Motif	703	706	.	.	.	Note=DEGH box	
+P31380	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P31380	UniProtKB	Modified residue	369	369	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P31380	UniProtKB	Modified residue	451	451	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P31380	UniProtKB	Mutagenesis	603	603	.	.	.	Note=Abolishes both the silencing function and the ability to promote DNA end resection of double-strand breaks (DSBs). K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22960744;Dbxref=PMID:22960744	
+P31380	UniProtKB	Beta strand	813	820	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	824	846	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	853	858	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	859	861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	864	874	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	878	880	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Beta strand	883	885	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	887	897	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	901	904	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	909	917	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	921	930	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	932	935	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	936	938	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	944	946	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	949	962	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Beta strand	969	974	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	976	988	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Beta strand	993	996	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Turn	1002	1004	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	1005	1014	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Beta strand	1020	1024	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	1025	1029	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Beta strand	1039	1044	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	1049	1056	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Turn	1057	1059	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Beta strand	1068	1075	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	1079	1086	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	1094	1096	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+P31380	UniProtKB	Helix	1109	1122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1	
+##sequence-region Q12035 1 217
+Q12035	UniProtKB	Chain	1	217	.	.	.	ID=PRO_0000253819;Note=rRNA-processing protein FCF2	
+Q12035	UniProtKB	Compositional bias	75	79	.	.	.	Note=Poly-Lys	
+Q12035	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q06205 1 392
+Q06205	UniProtKB	Chain	1	392	.	.	.	ID=PRO_0000075314;Note=FK506-binding protein 4	
+Q06205	UniProtKB	Domain	306	392	.	.	.	Note=PPIase FKBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00277	
+Q06205	UniProtKB	Compositional bias	191	199	.	.	.	Note=Poly-Glu	
+Q06205	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06205	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06205	UniProtKB	Beta strand	282	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8	
+Q06205	UniProtKB	Beta strand	291	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8	
+Q06205	UniProtKB	Beta strand	308	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8	
+Q06205	UniProtKB	Beta strand	322	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8	
+Q06205	UniProtKB	Beta strand	332	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8	
+Q06205	UniProtKB	Beta strand	339	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8	
+Q06205	UniProtKB	Helix	343	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8	
+Q06205	UniProtKB	Beta strand	357	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8	
+Q06205	UniProtKB	Helix	364	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8	
+Q06205	UniProtKB	Turn	367	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8	
+Q06205	UniProtKB	Beta strand	382	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8	
+##sequence-region P38866 1 432
+P38866	UniProtKB	Chain	1	432	.	.	.	ID=PRO_0000147670;Note=Thiol-specific monooxygenase	
+##sequence-region Q08968 1 688
+Q08968	UniProtKB	Chain	1	688	.	.	.	ID=PRO_0000121401;Note=UPF0061 protein FMP40	
+##sequence-region Q04991 1 504
+Q04991	UniProtKB	Chain	1	504	.	.	.	ID=PRO_0000218642;Note=Protein FMP42	
+Q04991	UniProtKB	Topological domain	1	11	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Topological domain	33	64	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Topological domain	86	91	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Topological domain	113	119	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Topological domain	141	150	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Transmembrane	151	171	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Topological domain	172	186	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Topological domain	208	302	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Transmembrane	303	323	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Topological domain	324	344	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Transmembrane	345	365	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Topological domain	366	385	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Transmembrane	386	406	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Topological domain	407	421	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Transmembrane	422	442	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Topological domain	443	462	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Transmembrane	463	483	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Topological domain	484	504	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04991	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q04991	UniProtKB	Modified residue	249	249	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04991	UniProtKB	Modified residue	269	269	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P29703 1 316
+P29703	UniProtKB	Chain	1	316	.	.	.	ID=PRO_0000119754;Note=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha	
+P29703	UniProtKB	Repeat	47	81	.	.	.	Note=PFTA 1	
+P29703	UniProtKB	Repeat	89	123	.	.	.	Note=PFTA 2	
+P29703	UniProtKB	Repeat	125	159	.	.	.	Note=PFTA 3	
+P29703	UniProtKB	Repeat	160	193	.	.	.	Note=PFTA 4	
+P29703	UniProtKB	Repeat	199	233	.	.	.	Note=PFTA 5	
+##sequence-region P53848 1 824
+P53848	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53848	UniProtKB	Chain	2	824	.	.	.	ID=PRO_0000168243;Note=Folic acid synthesis protein FOL1	
+P53848	UniProtKB	Domain	504	814	.	.	.	Note=Pterin-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00334	
+P53848	UniProtKB	Region	22	144	.	.	.	Note=DHNA 1	
+P53848	UniProtKB	Region	147	284	.	.	.	Note=DHNA 2	
+P53848	UniProtKB	Region	295	466	.	.	.	Note=HPPK	
+P53848	UniProtKB	Region	506	824	.	.	.	Note=DHPS	
+P53848	UniProtKB	Region	802	804	.	.	.	Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate binding;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PDB:2BMB,ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662	
+P53848	UniProtKB	Metal binding	511	511	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WND1	
+P53848	UniProtKB	Binding site	558	558	.	.	.	Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PDB:2BMB,ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662	
+P53848	UniProtKB	Binding site	596	596	.	.	.	Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662	
+P53848	UniProtKB	Binding site	615	615	.	.	.	Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PDB:2BMB,ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662	
+P53848	UniProtKB	Binding site	715	715	.	.	.	Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PDB:2BMB,ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662	
+P53848	UniProtKB	Binding site	767	767	.	.	.	Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PDB:2BMB,ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662	
+P53848	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53848	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53848	UniProtKB	Beta strand	298	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	308	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	311	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	328	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	336	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	350	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	363	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	392	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	420	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	424	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Turn	431	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Turn	441	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	447	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	460	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	464	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	479	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	498	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	505	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Turn	517	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	527	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	548	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	566	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	584	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	588	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	591	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	600	608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	613	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Turn	617	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	626	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	636	641	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Turn	647	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	650	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Turn	660	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	665	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	675	677	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	681	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	686	704	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	709	711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	712	715	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	724	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	734	737	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	740	746	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	749	754	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	760	762	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	768	774	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	779	782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	783	795	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Beta strand	799	804	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+P53848	UniProtKB	Helix	806	821	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB	
+##sequence-region P38894 1 1075
+P38894	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38894	UniProtKB	Chain	25	1052	.	.	.	ID=PRO_0000021275;Note=Flocculation protein FLO5	
+P38894	UniProtKB	Propeptide	1053	1075	.	.	.	ID=PRO_0000021276;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38894	UniProtKB	Domain	74	249	.	.	.	Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164	
+P38894	UniProtKB	Repeat	278	322	.	.	.	Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	323	367	.	.	.	Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	368	412	.	.	.	Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	413	457	.	.	.	Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	458	502	.	.	.	Note=1-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	503	547	.	.	.	Note=1-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	548	592	.	.	.	Note=1-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	593	637	.	.	.	Note=1-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	667	686	.	.	.	Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	687	706	.	.	.	Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	775	825	.	.	.	Note=3-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	847	897	.	.	.	Note=3-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Repeat	898	948	.	.	.	Note=3-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P38894	UniProtKB	Region	197	240	.	.	.	Note=Sugar recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38894	UniProtKB	Region	278	637	.	.	.	Note=8 X 45 AA approximate tandem repeats%2C Thr-rich	
+P38894	UniProtKB	Region	667	706	.	.	.	Note=2 X 20 AA approximate tandem repeats%2C Ser-rich	
+P38894	UniProtKB	Region	775	948	.	.	.	Note=3 X 51 AA approximate repeats%2C Ser/Thr-rich	
+P38894	UniProtKB	Lipidation	1052	1052	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38894	UniProtKB	Glycosylation	135	135	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38894	UniProtKB	Glycosylation	187	187	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38894	UniProtKB	Glycosylation	203	203	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38894	UniProtKB	Glycosylation	262	262	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38894	UniProtKB	Glycosylation	663	663	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38894	UniProtKB	Glycosylation	749	749	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38894	UniProtKB	Beta strand	36	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Helix	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Helix	57	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Helix	63	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	69	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	86	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Helix	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Turn	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Turn	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Turn	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	135	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	147	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	160	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Turn	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	189	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AHW	
+P38894	UniProtKB	Beta strand	205	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	215	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	233	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	242	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Turn	248	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	251	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Beta strand	264	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+P38894	UniProtKB	Turn	268	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP	
+##sequence-region P40464 1 311
+P40464	UniProtKB	Chain	1	311	.	.	.	ID=PRO_0000090682;Note=Mitochondrial FAD carrier protein FLX1	
+P40464	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40464	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40464	UniProtKB	Transmembrane	129	149	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40464	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40464	UniProtKB	Transmembrane	230	250	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40464	UniProtKB	Transmembrane	266	286	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40464	UniProtKB	Repeat	7	101	.	.	.	Note=Solcar 1	
+P40464	UniProtKB	Repeat	123	210	.	.	.	Note=Solcar 2	
+P40464	UniProtKB	Repeat	224	310	.	.	.	Note=Solcar 3	
+##sequence-region P38231 1 175
+P38231	UniProtKB	Transit peptide	1	38	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38231	UniProtKB	Chain	39	175	.	.	.	ID=PRO_0000202474;Note=Protein FMP23%2C mitochondrial	
+##sequence-region Q02883 1 468
+Q02883	UniProtKB	Transit peptide	1	39	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02883	UniProtKB	Chain	40	468	.	.	.	ID=PRO_0000238633;Note=N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D%2C mitochondrial	
+Q02883	UniProtKB	Transmembrane	54	76	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02883	UniProtKB	Metal binding	265	265	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02883	UniProtKB	Metal binding	267	267	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02883	UniProtKB	Metal binding	269	269	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02883	UniProtKB	Metal binding	270	270	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02883	UniProtKB	Metal binding	332	332	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02883	UniProtKB	Metal binding	425	425	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZB3 1 126
+A0A023PZB3	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000430968;Note=Protein FMP49%2C mitochondrial	
+##sequence-region Q12029 1 327
+Q12029	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12029	UniProtKB	Chain	2	327	.	.	.	ID=PRO_0000237642;Note=Probable mitochondrial transport protein FSF1	
+Q12029	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12029	UniProtKB	Transmembrane	143	163	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12029	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12029	UniProtKB	Transmembrane	272	292	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12029	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P25659 1 250
+P25659	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000202574;Note=Silencing boundary-establishment protein FUB1	
+P25659	UniProtKB	Compositional bias	228	248	.	.	.	Note=Gly/Ser-rich	
+##sequence-region P16892 1 353
+P16892	UniProtKB	Chain	1	353	.	.	.	ID=PRO_0000186326;Note=Mitogen-activated protein kinase FUS3	
+P16892	UniProtKB	Domain	13	309	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P16892	UniProtKB	Nucleotide binding	19	27	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P16892	UniProtKB	Motif	180	182	.	.	.	Note=TXY	
+P16892	UniProtKB	Active site	137	137	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P16892	UniProtKB	Binding site	42	42	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P16892	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1628831;Dbxref=PMID:1628831	
+P16892	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1628831;Dbxref=PMID:1628831	
+P16892	UniProtKB	Cross-link	345	345	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P16892	UniProtKB	Sequence conflict	334	334	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16892	UniProtKB	Beta strand	4	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F49	
+P16892	UniProtKB	Beta strand	13	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Beta strand	23	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Turn	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Beta strand	38	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	50	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Beta strand	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Turn	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9F	
+P16892	UniProtKB	Beta strand	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Beta strand	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	111	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Beta strand	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9F	
+P16892	UniProtKB	Beta strand	182	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F49	
+P16892	UniProtKB	Helix	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	191	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	202	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	228	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Turn	245	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	254	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	271	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	280	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	294	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	300	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Turn	310	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	326	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+P16892	UniProtKB	Helix	340	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H	
+##sequence-region P38783 1 130
+P38783	UniProtKB	Transit peptide	1	27	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38783	UniProtKB	Chain	28	130	.	.	.	ID=PRO_0000202897;Note=Protein FYV4%2C mitochondrial	
+##sequence-region P53913 1 173
+P53913	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53913	UniProtKB	Chain	2	173	.	.	.	ID=PRO_0000203427;Note=Protein FYV6	
+P53913	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P45976 1 327
+P45976	UniProtKB	Chain	1	327	.	.	.	ID=PRO_0000215042;Note=Pre-mRNA polyadenylation factor FIP1	
+P45976	UniProtKB	Compositional bias	61	80	.	.	.	Note=Asp-rich (acidic)	
+P45976	UniProtKB	Compositional bias	258	266	.	.	.	Note=Poly-Asn	
+P45976	UniProtKB	Compositional bias	284	318	.	.	.	Note=Pro-rich	
+P45976	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P45976	UniProtKB	Beta strand	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C66	
+P45976	UniProtKB	Beta strand	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C66	
+P45976	UniProtKB	Beta strand	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C66	
+P45976	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C66	
+P45976	UniProtKB	Helix	99	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C66	
+##sequence-region P40515 1 155
+P40515	UniProtKB	Chain	1	155	.	.	.	ID=PRO_0000202982;Note=Mitochondrial fission 1 protein	
+P40515	UniProtKB	Topological domain	1	131	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40515	UniProtKB	Transmembrane	132	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40515	UniProtKB	Topological domain	150	155	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40515	UniProtKB	Mutagenesis	80	80	.	.	.	Note=In fis1-L80P%3B no interaction with MDV1%3B mitochondrial fission is blocked%3B DNM1 assembly at punctate structures normal as in wild-type. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163467;Dbxref=PMID:12163467	
+P40515	UniProtKB	Helix	12	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48	
+P40515	UniProtKB	Helix	19	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48	
+P40515	UniProtKB	Helix	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48	
+P40515	UniProtKB	Helix	39	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48	
+P40515	UniProtKB	Beta strand	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y8M	
+P40515	UniProtKB	Helix	55	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48	
+P40515	UniProtKB	Helix	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48	
+P40515	UniProtKB	Helix	76	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48	
+P40515	UniProtKB	Helix	93	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48	
+P40515	UniProtKB	Helix	111	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48	
+##sequence-region P40098 1 244
+P40098	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000202660;Note=Uncharacterized mitochondrial membrane protein FMP10	
+P40098	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40098	UniProtKB	Transmembrane	139	159	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36141 1 133
+P36141	UniProtKB	Transit peptide	1	21	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36141	UniProtKB	Chain	22	133	.	.	.	ID=PRO_0000203215;Note=Putative redox protein FMP46%2C mitochondrial	
+P36141	UniProtKB	Active site	97	97	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36141	UniProtKB	Beta strand	13	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Beta strand	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Helix	27	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Turn	32	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Beta strand	41	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Helix	53	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Beta strand	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Helix	66	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Helix	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Turn	81	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Helix	86	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Helix	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Beta strand	109	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Beta strand	118	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+P36141	UniProtKB	Helix	123	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI	
+##sequence-region P36001 1 430
+P36001	UniProtKB	Chain	1	430	.	.	.	ID=PRO_0000168307;Note=Probable folylpolyglutamate synthase	
+P36001	UniProtKB	Nucleotide binding	37	40	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+P36001	UniProtKB	Metal binding	132	132	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+P36001	UniProtKB	Binding site	300	300	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192	
+##sequence-region P40099 1 211
+P40099	UniProtKB	Chain	1	211	.	.	.	ID=PRO_0000200280;Note=5-formyltetrahydrofolate cyclo-ligase	
+P40099	UniProtKB	Nucleotide binding	4	8	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40099	UniProtKB	Nucleotide binding	151	158	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40099	UniProtKB	Region	152	156	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40099	UniProtKB	Binding site	56	56	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40099	UniProtKB	Binding site	194	194	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P04397 1 699
+P04397	UniProtKB	Chain	1	699	.	.	.	ID=PRO_0000197442;Note=Bifunctional protein GAL10	
+P04397	UniProtKB	Nucleotide binding	13	44	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04397	UniProtKB	Region	1	357	.	.	.	Note=Galactowaldenase	
+P04397	UniProtKB	Region	358	699	.	.	.	Note=Mutarotase	
+P04397	UniProtKB	Active site	537	537	.	.	.	Note=For mutarotase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04397	UniProtKB	Modified residue	562	562	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04397	UniProtKB	Sequence conflict	302	306	.	.	.	Note=DLPYK->WSSVR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04397	UniProtKB	Sequence conflict	464	464	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04397	UniProtKB	Sequence conflict	479	480	.	.	.	Note=KD->NY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04397	UniProtKB	Sequence conflict	498	498	.	.	.	Note=P->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04397	UniProtKB	Sequence conflict	518	518	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04397	UniProtKB	Sequence conflict	667	667	.	.	.	Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04397	UniProtKB	Sequence conflict	694	695	.	.	.	Note=IV->TL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04397	UniProtKB	Beta strand	13	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Turn	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	22	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	37	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	50	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	73	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	97	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	104	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	129	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	136	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	162	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	186	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	215	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	226	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	248	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	251	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	274	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	288	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	323	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	337	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	360	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	373	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	382	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	395	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	412	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	432	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	435	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	438	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	444	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	455	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	460	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	464	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	470	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	481	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	492	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	495	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Turn	511	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	515	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Turn	542	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	548	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	553	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	561	565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	571	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	585	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	589	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	599	604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	621	627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Turn	629	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	634	647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	662	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	672	674	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Turn	676	678	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Helix	679	682	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	683	685	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+P04397	UniProtKB	Beta strand	689	699	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45	
+##sequence-region P13181 1 574
+P13181	UniProtKB	Chain	1	574	.	.	.	ID=PRO_0000050416;Note=Galactose transporter	
+P13181	UniProtKB	Topological domain	1	70	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	92	121	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	143	149	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	171	175	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	176	196	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	197	207	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	229	242	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	264	342	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	343	362	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	363	366	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	367	387	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	388	394	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	395	415	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	416	435	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	436	456	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	457	472	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	473	493	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	494	499	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Transmembrane	500	520	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Topological domain	521	574	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13181	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13181	UniProtKB	Modified residue	35	35	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13181	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13181	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13181	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13181	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13181	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13181	UniProtKB	Sequence conflict	50	50	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13181	UniProtKB	Sequence conflict	50	50	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13181	UniProtKB	Sequence conflict	79	79	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13181	UniProtKB	Sequence conflict	90	90	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13181	UniProtKB	Sequence conflict	90	90	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13181	UniProtKB	Sequence conflict	392	392	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13181	UniProtKB	Sequence conflict	392	392	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P13045 1 520
+P13045	UniProtKB	Chain	1	520	.	.	.	ID=PRO_0000184658;Note=Protein GAL3	
+P13045	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P13045	UniProtKB	Sequence conflict	37	45	.	.	.	Note=KPDFIARSP->NLILSLGLL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13045	UniProtKB	Sequence conflict	170	171	.	.	.	Note=AA->GR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13045	UniProtKB	Sequence conflict	192	211	.	.	.	Note=RITAVAEHYVGVNNGGMDQA->ASQRLRSTMLESIMVVWIKQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13045	UniProtKB	Sequence conflict	227	241	.	.	.	Note=RPKLKATPFKFPQLK->MAKTKWPHFQVSSIE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13045	UniProtKB	Sequence conflict	251	294	.	.	.	Note=NTLVKSNKFETAPTNYNLRVIEVTVAANALATRYSVALPSHKDN->ILCTRSNNRTLLHISLSCSLLTLLYISTFAREPCGPDTLGLTISQGQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13045	UniProtKB	Sequence conflict	303	338	.	.	.	Note=RDFMDAYYARYENQAQPWNGDIGTGIERLLKMLQLV->EIYGCLLRPDTKTKPNHGMEISELVLNVYSRCYNWY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13045	UniProtKB	Sequence conflict	407	425	.	.	.	Note=TFHTDEDFFTDFGRLMNES->IFTRTRFLYRFWPTNE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13045	UniProtKB	Beta strand	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V2U	
+P13045	UniProtKB	Helix	20	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	39	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	62	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	84	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	119	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	137	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	148	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	162	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	187	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	198	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	208	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	220	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	231	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	244	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	258	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V2U	
+P13045	UniProtKB	Turn	263	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	266	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	296	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	302	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	324	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	351	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	362	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	370	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	382	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	411	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	438	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	453	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	478	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	490	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Helix	499	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	506	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+P13045	UniProtKB	Beta strand	515	519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R	
+##sequence-region P43574 1 510
+P43574	UniProtKB	Chain	1	510	.	.	.	ID=PRO_0000083484;Note=Transcriptional regulatory protein GAT1	
+P43574	UniProtKB	Zinc finger	310	334	.	.	.	Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094	
+P43574	UniProtKB	Compositional bias	151	158	.	.	.	Note=Poly-Asp	
+P43574	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43574	UniProtKB	Modified residue	262	262	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P43574	UniProtKB	Modified residue	270	270	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P43574	UniProtKB	Modified residue	369	369	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43574	UniProtKB	Modified residue	399	399	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P43574	UniProtKB	Modified residue	418	418	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region P39012 1 614
+P39012	UniProtKB	Chain	1	614	.	.	.	ID=PRO_0000087417;Note=GPI transamidase component GAA1	
+P39012	UniProtKB	Topological domain	1	19	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Topological domain	41	356	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Transmembrane	357	377	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Topological domain	378	394	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Transmembrane	395	415	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Topological domain	416	464	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Transmembrane	465	485	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Topological domain	486	535	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Transmembrane	536	556	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Topological domain	557	577	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Transmembrane	578	598	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Topological domain	599	614	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Motif	610	614	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39012	UniProtKB	Glycosylation	87	87	.	.	.	Note=N-linked (GlcNAc...) asparagine	
+P39012	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Loss of N-glycosylation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7730400;Dbxref=PMID:7730400	
+##sequence-region P28006 1 793
+P28006	UniProtKB	Chain	1	793	.	.	.	ID=PRO_0000071518;Note=Serine/threonine-protein phosphatase 1 regulatory subunit GAC1	
+P28006	UniProtKB	Domain	235	360	.	.	.	Note=CBM21;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00491	
+P28006	UniProtKB	Compositional bias	500	523	.	.	.	Note=Ser-rich	
+P28006	UniProtKB	Modified residue	415	415	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P28006	UniProtKB	Modified residue	424	424	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P28006	UniProtKB	Sequence conflict	228	228	.	.	.	Note=S->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P41913 1 522
+P41913	UniProtKB	Chain	1	522	.	.	.	ID=PRO_0000087453;Note=Protein GDS1	
+##sequence-region Q08622 1 556
+Q08622	UniProtKB	Transit peptide	1	21	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08622	UniProtKB	Chain	22	556	.	.	.	ID=PRO_0000237640;Note=Genetic interactor of prohibitins 3%2C mitochondrial	
+Q08622	UniProtKB	Domain	113	305	.	.	.	Note=CP-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01058	
+##sequence-region P40056 1 285
+P40056	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40056	UniProtKB	Chain	2	285	.	.	.	ID=PRO_0000097362;Note=Golgi to ER traffic protein 2	
+P40056	UniProtKB	Topological domain	2	148	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114	
+P40056	UniProtKB	Transmembrane	149	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114	
+P40056	UniProtKB	Topological domain	170	196	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114	
+P40056	UniProtKB	Transmembrane	197	216	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114	
+P40056	UniProtKB	Topological domain	217	263	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114	
+P40056	UniProtKB	Transmembrane	264	284	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114	
+P40056	UniProtKB	Topological domain	285	285	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114	
+P40056	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40056	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40056	UniProtKB	Glycosylation	173	173	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114	
+P40056	UniProtKB	Glycosylation	196	196	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114	
+P40056	UniProtKB	Helix	6	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZS9	
+P40056	UniProtKB	Turn	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZS9	
+P40056	UniProtKB	Helix	25	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZS9	
+##sequence-region P14742 1 717
+P14742	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15699032;Dbxref=PMID:15699032	
+P14742	UniProtKB	Chain	2	717	.	.	.	ID=PRO_0000135289;Note=Glutamine--fructose-6-phosphate aminotransferase [isomerizing]	
+P14742	UniProtKB	Domain	2	318	.	.	.	Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609	
+P14742	UniProtKB	Domain	390	529	.	.	.	Note=SIS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00797	
+P14742	UniProtKB	Domain	562	707	.	.	.	Note=SIS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00797	
+P14742	UniProtKB	Active site	2	2	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15699032;Dbxref=PMID:15699032	
+P14742	UniProtKB	Modified residue	253	253	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14742	UniProtKB	Modified residue	334	334	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14742	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14742	UniProtKB	Sequence conflict	453	454	.	.	.	Note=QS->HC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14742	UniProtKB	Sequence conflict	534	534	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40036 1 548
+P40036	UniProtKB	Chain	1	548	.	.	.	ID=PRO_0000071521;Note=GLC7-interacting protein 2	
+P40036	UniProtKB	Domain	419	534	.	.	.	Note=CBM21;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00491	
+P40036	UniProtKB	Modified residue	51	51	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40036	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40036	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40036	UniProtKB	Modified residue	221	221	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P40036	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P39732 1 760
+P39732	UniProtKB	Chain	1	760	.	.	.	ID=PRO_0000202416;Note=GLC7-interacting protein 4	
+P39732	UniProtKB	Modified residue	497	497	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P39732	UniProtKB	Modified residue	501	501	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P39732	UniProtKB	Modified residue	609	609	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P53849 1 153
+P53849	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000087496;Note=Zinc finger protein GIS2	
+P53849	UniProtKB	Zinc finger	4	21	.	.	.	Note=CCHC-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+P53849	UniProtKB	Zinc finger	23	40	.	.	.	Note=CCHC-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+P53849	UniProtKB	Zinc finger	47	64	.	.	.	Note=CCHC-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+P53849	UniProtKB	Zinc finger	65	82	.	.	.	Note=CCHC-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+P53849	UniProtKB	Zinc finger	92	109	.	.	.	Note=CCHC-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+P53849	UniProtKB	Zinc finger	116	133	.	.	.	Note=CCHC-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+P53849	UniProtKB	Zinc finger	135	152	.	.	.	Note=CCHC-type 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+##sequence-region P25346 1 518
+P25346	UniProtKB	Chain	1	518	.	.	.	ID=PRO_0000050459;Note=Glycerophosphoinositol transporter 1	
+P25346	UniProtKB	Topological domain	1	44	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	66	91	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	113	114	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	115	136	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	137	138	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	139	159	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	160	184	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	206	216	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	238	268	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	269	289	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	290	306	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	307	327	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	328	335	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	336	356	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	357	360	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	361	381	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	382	399	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	400	420	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	421	430	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Transmembrane	431	451	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Topological domain	452	518	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25346	UniProtKB	Glycosylation	80	80	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12315 1 538
+Q12315	UniProtKB	Chain	1	538	.	.	.	ID=PRO_0000204820;Note=Nucleoporin GLE1	
+Q12315	UniProtKB	Region	257	538	.	.	.	Note=Interactions with NUP42%2C DBP5 and GFD1	
+Q12315	UniProtKB	Coiled coil	131	244	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12315	UniProtKB	Motif	154	170	.	.	.	Note=Bipartite nuclear localization signal 1	
+Q12315	UniProtKB	Motif	272	288	.	.	.	Note=Bipartite nuclear localization signal 2	
+Q12315	UniProtKB	Compositional bias	157	229	.	.	.	Note=Glu-rich	
+Q12315	UniProtKB	Compositional bias	161	273	.	.	.	Note=Lys-rich	
+Q12315	UniProtKB	Compositional bias	164	167	.	.	.	Note=Poly-Glu	
+Q12315	UniProtKB	Mutagenesis	351	351	.	.	.	Note=Partial loss of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8848052;Dbxref=PMID:8848052	
+Q12315	UniProtKB	Mutagenesis	353	353	.	.	.	Note=Partial loss of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8848052;Dbxref=PMID:8848052	
+Q12315	UniProtKB	Mutagenesis	356	356	.	.	.	Note=Temperature-sensitive. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8848052;Dbxref=PMID:8848052	
+Q12315	UniProtKB	Mutagenesis	358	358	.	.	.	Note=Partial loss of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8848052;Dbxref=PMID:8848052	
+Q12315	UniProtKB	Helix	245	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	268	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	276	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	292	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	300	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Turn	316	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	321	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	347	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	350	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	367	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	380	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	392	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	411	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Turn	435	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	448	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	462	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	467	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	490	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	502	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	508	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+Q12315	UniProtKB	Helix	513	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV	
+##sequence-region P36143 1 616
+P36143	UniProtKB	Chain	1	616	.	.	.	ID=PRO_0000215181;Note=Glycogenin-1	
+P36143	UniProtKB	Glycosylation	230	230	.	.	.	Note=O-linked (Glc...) tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36143	UniProtKB	Glycosylation	598	598	.	.	.	Note=O-linked (Glc...) tyrosine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36143	UniProtKB	Mutagenesis	230	230	.	.	.	Note=Eliminates glycogen accumulation%3B when associated with F-598. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8900126;Dbxref=PMID:8900126	
+P36143	UniProtKB	Mutagenesis	598	598	.	.	.	Note=Eliminates glycogen accumulation%3B when associated with F-230. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8900126;Dbxref=PMID:8900126	
+##sequence-region P38777 1 243
+P38777	UniProtKB	Chain	1	243	.	.	.	ID=PRO_0000212580;Note=Family of serine hydrolases 1	
+P38777	UniProtKB	Active site	110	110	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15802654;Dbxref=PMID:15802654	
+P38777	UniProtKB	Active site	183	183	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15802654;Dbxref=PMID:15802654	
+P38777	UniProtKB	Active site	218	218	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15802654;Dbxref=PMID:15802654	
+P38777	UniProtKB	Beta strand	7	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Helix	18	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Helix	26	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Beta strand	38	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Beta strand	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Helix	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Helix	59	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Beta strand	72	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Helix	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Helix	87	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Beta strand	104	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Helix	111	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Beta strand	134	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Beta strand	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Beta strand	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Helix	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Turn	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Beta strand	174	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Beta strand	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Helix	188	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Turn	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Turn	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Beta strand	209	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+P38777	UniProtKB	Helix	224	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD	
+##sequence-region P05316 1 633
+P05316	UniProtKB	Chain	1	633	.	.	.	ID=PRO_0000197925;Note=Uracil permease	
+P05316	UniProtKB	Transmembrane	143	163	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Transmembrane	197	217	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Transmembrane	268	288	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Transmembrane	310	330	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Transmembrane	350	370	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Transmembrane	400	420	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Transmembrane	442	462	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Transmembrane	465	485	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Transmembrane	521	541	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Transmembrane	559	579	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05316	UniProtKB	Sequence conflict	217	217	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05316	UniProtKB	Sequence conflict	229	229	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05316	UniProtKB	Sequence conflict	320	320	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05670 1 677
+Q05670	UniProtKB	Chain	1	677	.	.	.	ID=PRO_0000080954;Note=Nuclear fusion protein FUS2	
+Q05670	UniProtKB	Domain	112	326	.	.	.	Note=DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00062	
+Q05670	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q05670	UniProtKB	Modified residue	67	67	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q05670	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q05670	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q05670	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q05670	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q05670	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q05670	UniProtKB	Sequence conflict	185	185	.	.	.	Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q05670	UniProtKB	Sequence conflict	203	203	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q05670	UniProtKB	Sequence conflict	543	546	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q05670	UniProtKB	Sequence conflict	589	677	.	.	.	Note=HDTIECILLNYIKVFLKYLEIIAGGKKYLQKDLENMSLNDSIATGQIKNLDILQCYSKSRYMTKRMVRKDWPFPGDPSGSRVVRKLFEL->PRYYRMYLVELYQSLLKIFGNHCWWKKIPAKRS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08559 1 129
+Q08559	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000239648;Note=Protein FYV12	
+Q08559	UniProtKB	Transmembrane	109	128	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08559	UniProtKB	Glycosylation	91	91	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25585 1 152
+P25585	UniProtKB	Chain	1	152	.	.	.	ID=PRO_0000202552;Note=Protein FYV5	
+P25585	UniProtKB	Transmembrane	26	46	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25585	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25585	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25585	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25585	UniProtKB	Transmembrane	127	147	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46949 1 817
+P46949	UniProtKB	Chain	1	817	.	.	.	ID=PRO_0000202842;Note=Protein FYV8	
+P46949	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46949	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P46949	UniProtKB	Modified residue	134	134	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46949	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46949	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46949	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46949	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46949	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46949	UniProtKB	Modified residue	532	532	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P00360 1 332
+P00360	UniProtKB	Chain	1	332	.	.	.	ID=PRO_0000145589;Note=Glyceraldehyde-3-phosphate dehydrogenase 1	
+P00360	UniProtKB	Nucleotide binding	11	12	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00360	UniProtKB	Region	149	151	.	.	.	Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00360	UniProtKB	Region	209	210	.	.	.	Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00360	UniProtKB	Active site	150	150	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10009	
+P00360	UniProtKB	Binding site	33	33	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00360	UniProtKB	Binding site	78	78	.	.	.	Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00360	UniProtKB	Binding site	180	180	.	.	.	Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00360	UniProtKB	Binding site	232	232	.	.	.	Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00360	UniProtKB	Binding site	314	314	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00360	UniProtKB	Site	177	177	.	.	.	Note=Activates thiol group during catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00360	UniProtKB	Sequence conflict	248	248	.	.	.	Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P08431 1 366
+P08431	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6324089;Dbxref=PMID:6324089	
+P08431	UniProtKB	Chain	2	366	.	.	.	ID=PRO_0000169893;Note=Galactose-1-phosphate uridylyltransferase	
+P08431	UniProtKB	Region	79	80	.	.	.	Note=UDP-alpha-D-glucose binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902	
+P08431	UniProtKB	Region	329	332	.	.	.	Note=UDP-alpha-D-glucose binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902	
+P08431	UniProtKB	Region	334	335	.	.	.	Note=UDP-alpha-D-glucose binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902	
+P08431	UniProtKB	Active site	182	182	.	.	.	Note=Tele-UMP-histidine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10033	
+P08431	UniProtKB	Metal binding	54	54	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10033	
+P08431	UniProtKB	Metal binding	57	57	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10033	
+P08431	UniProtKB	Metal binding	124	124	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10033	
+P08431	UniProtKB	Metal binding	180	180	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10033	
+P08431	UniProtKB	Metal binding	198	198	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09148	
+P08431	UniProtKB	Metal binding	297	297	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09148	
+P08431	UniProtKB	Metal binding	314	314	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09148	
+P08431	UniProtKB	Metal binding	316	316	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09148	
+P08431	UniProtKB	Binding site	63	63	.	.	.	Note=UDP-alpha-D-glucose%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902	
+P08431	UniProtKB	Binding site	169	169	.	.	.	Note=UDP-alpha-D-glucose%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902	
+P08431	UniProtKB	Binding site	184	184	.	.	.	Note=UDP-alpha-D-glucose;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902	
+P08431	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08431	UniProtKB	Sequence conflict	11	11	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08431	UniProtKB	Sequence conflict	58	58	.	.	.	Note=P->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08431	UniProtKB	Sequence conflict	85	86	.	.	.	Note=RL->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08431	UniProtKB	Sequence conflict	267	267	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08431	UniProtKB	Sequence conflict	345	345	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P04387 1 435
+P04387	UniProtKB	Chain	1	435	.	.	.	ID=PRO_0000087427;Note=Galactose/lactose metabolism regulatory protein GAL80	
+P04387	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1985957;Dbxref=PMID:1985957	
+P04387	UniProtKB	Sequence conflict	101	101	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04387	UniProtKB	Beta strand	18	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Turn	32	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	36	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Turn	43	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	47	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	57	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	73	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V2U	
+P04387	UniProtKB	Helix	78	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	99	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	118	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	129	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	145	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	151	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	156	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Turn	167	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	172	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	183	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	195	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Turn	206	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	210	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	226	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	238	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	245	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTS	
+P04387	UniProtKB	Beta strand	249	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	260	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Turn	269	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	273	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	287	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V2U	
+P04387	UniProtKB	Beta strand	291	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	302	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V2U	
+P04387	UniProtKB	Beta strand	316	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	348	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	360	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Turn	377	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Beta strand	396	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Helix	402	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+P04387	UniProtKB	Turn	428	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV	
+##sequence-region P25555 1 427
+P25555	UniProtKB	Chain	1	427	.	.	.	ID=PRO_0000081596;Note=Single-strand telomeric DNA-binding protein GBP2	
+P25555	UniProtKB	Domain	122	198	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P25555	UniProtKB	Domain	219	296	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P25555	UniProtKB	Domain	349	426	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P25555	UniProtKB	Modified residue	130	130	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25555	UniProtKB	Helix	332	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ	
+P25555	UniProtKB	Turn	337	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ	
+P25555	UniProtKB	Beta strand	349	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ	
+P25555	UniProtKB	Helix	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ	
+P25555	UniProtKB	Helix	365	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ	
+P25555	UniProtKB	Turn	370	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ	
+P25555	UniProtKB	Beta strand	375	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ	
+P25555	UniProtKB	Beta strand	390	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ	
+P25555	UniProtKB	Helix	399	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ	
+P25555	UniProtKB	Beta strand	420	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ	
+##sequence-region P51601 1 243
+P51601	UniProtKB	Chain	1	243	.	.	.	ID=PRO_0000119489;Note=GTP cyclohydrolase 1	
+P51601	UniProtKB	Metal binding	132	132	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P51601	UniProtKB	Metal binding	135	135	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P51601	UniProtKB	Metal binding	203	203	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P51601	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P51601	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P51601	UniProtKB	Sequence conflict	159	160	.	.	.	Note=LA->QG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P51601	UniProtKB	Sequence conflict	206	206	.	.	.	Note=S->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P51601	UniProtKB	Sequence conflict	217	217	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07928 1 141
+Q07928	UniProtKB	Chain	1	141	.	.	.	ID=PRO_0000083486;Note=Protein GAT3	
+Q07928	UniProtKB	Zinc finger	72	98	.	.	.	Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094	
+##sequence-region P33893 1 541
+P33893	UniProtKB	Chain	1	541	.	.	.	ID=PRO_0000010712;Note=Glutamyl-tRNA(Gln) amidotransferase subunit B%2C mitochondrial	
+P33893	UniProtKB	Sequence conflict	415	415	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33893	UniProtKB	Sequence conflict	415	415	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33893	UniProtKB	Beta strand	29	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Turn	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Turn	66	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Helix	80	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	104	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	116	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	131	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Helix	136	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	142	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	161	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	172	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	183	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Helix	196	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Turn	220	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	224	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Helix	247	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	277	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	304	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P33893	UniProtKB	Beta strand	309	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0I	
+P33893	UniProtKB	Helix	313	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+##sequence-region P43535 1 752
+P43535	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P43535	UniProtKB	Chain	2	752	.	.	.	ID=PRO_0000093461;Note=Protein GCN20	
+P43535	UniProtKB	Domain	199	464	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P43535	UniProtKB	Domain	532	748	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P43535	UniProtKB	Nucleotide binding	232	239	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P43535	UniProtKB	Nucleotide binding	565	572	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P43535	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P53171 1 287
+P53171	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53171	UniProtKB	Chain	25	287	.	.	.	ID=PRO_0000202766;Note=Genetic interactor of prohibitin 7%2C mitochondrial	
+P53171	UniProtKB	Transmembrane	250	266	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53192 1 235
+P53192	UniProtKB	Chain	1	235	.	.	.	ID=PRO_0000414847;Note=Golgi to ER traffic protein 1	
+P53192	UniProtKB	Topological domain	1	1	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113	
+P53192	UniProtKB	Transmembrane	2	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113	
+P53192	UniProtKB	Topological domain	22	104	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113	
+P53192	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113	
+P53192	UniProtKB	Topological domain	126	181	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113	
+P53192	UniProtKB	Transmembrane	182	198	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113	
+P53192	UniProtKB	Topological domain	199	235	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113	
+P53192	UniProtKB	Coiled coil	68	104	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113	
+P53192	UniProtKB	Helix	40	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E	
+P53192	UniProtKB	Turn	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E	
+P53192	UniProtKB	Helix	65	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E	
+P53192	UniProtKB	Turn	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E	
+P53192	UniProtKB	Helix	85	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E	
+P53192	UniProtKB	Turn	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E	
+P53192	UniProtKB	Turn	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E	
+P53192	UniProtKB	Helix	100	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SJB	
+##sequence-region Q12154 1 354
+Q12154	UniProtKB	Chain	1	354	.	.	.	ID=PRO_0000152256;Note=ATPase GET3	
+Q12154	UniProtKB	Nucleotide binding	26	33	.	.	.	Note=ATP	
+Q12154	UniProtKB	Nucleotide binding	315	322	.	.	.	Note=ATP	
+Q12154	UniProtKB	Active site	57	57	.	.	.	.	
+Q12154	UniProtKB	Metal binding	285	285	.	.	.	Note=Zinc%3B shared with dimeric partner;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03112,ECO:0000269|PubMed:19675567;Dbxref=PMID:19675567	
+Q12154	UniProtKB	Metal binding	288	288	.	.	.	Note=Zinc%3B shared with dimeric partner;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03112,ECO:0000269|PubMed:19675567;Dbxref=PMID:19675567	
+Q12154	UniProtKB	Binding site	245	245	.	.	.	Note=ATP	
+Q12154	UniProtKB	Binding site	272	272	.	.	.	Note=ATP	
+Q12154	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Abolishes ATPase activity%2C leading to secretion of resident ER proteins. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12680698,ECO:0000269|PubMed:19706470;Dbxref=PMID:12680698,PMID:19706470	
+Q12154	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Abolishes ATP hydrolysis. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19675567;Dbxref=PMID:19675567	
+Q12154	UniProtKB	Mutagenesis	285	285	.	.	.	Note=Prevents dimerization%3B when associated with S-288. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19675567;Dbxref=PMID:19675567	
+Q12154	UniProtKB	Mutagenesis	288	288	.	.	.	Note=Prevents dimerization%3B when associated with S-285. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19675567;Dbxref=PMID:19675567	
+Q12154	UniProtKB	Sequence conflict	43	43	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12154	UniProtKB	Beta strand	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XWO	
+Q12154	UniProtKB	Helix	10	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Beta strand	20	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Beta strand	27	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84	
+Q12154	UniProtKB	Helix	31	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E	
+Q12154	UniProtKB	Beta strand	51	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Beta strand	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XVU	
+Q12154	UniProtKB	Helix	62	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Beta strand	81	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Helix	90	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Turn	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E	
+Q12154	UniProtKB	Beta strand	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84	
+Q12154	UniProtKB	Helix	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84	
+Q12154	UniProtKB	Helix	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84	
+Q12154	UniProtKB	Helix	125	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Helix	136	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Beta strand	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84	
+Q12154	UniProtKB	Beta strand	161	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Helix	170	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Helix	179	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Helix	191	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84	
+Q12154	UniProtKB	Beta strand	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E	
+Q12154	UniProtKB	Helix	200	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84	
+Q12154	UniProtKB	Turn	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84	
+Q12154	UniProtKB	Helix	213	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Turn	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Beta strand	236	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Helix	246	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Beta strand	268	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Turn	277	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84	
+Q12154	UniProtKB	Helix	286	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Turn	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Beta strand	309	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Helix	323	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Helix	340	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+Q12154	UniProtKB	Helix	344	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ	
+##sequence-region Q04839 1 188
+Q04839	UniProtKB	Chain	1	188	.	.	.	ID=PRO_0000087477;Note=mRNA transport factor GFD1	
+Q04839	UniProtKB	Coiled coil	119	164	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04839	UniProtKB	Compositional bias	17	136	.	.	.	Note=Lys-rich	
+Q04839	UniProtKB	Compositional bias	152	155	.	.	.	Note=Poly-Gln	
+Q04839	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956	
+Q04839	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q04839	UniProtKB	Modified residue	111	111	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q04839	UniProtKB	Helix	127	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LCN	
+##sequence-region P22146 1 559
+P22146	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1824714;Dbxref=PMID:1824714	
+P22146	UniProtKB	Chain	23	528	.	.	.	ID=PRO_0000010473;Note=1%2C3-beta-glucanosyltransferase GAS1	
+P22146	UniProtKB	Propeptide	529	559	.	.	.	ID=PRO_0000010474;Note=Removed in mature form	
+P22146	UniProtKB	Region	119	127	.	.	.	Note=Donor substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Compositional bias	438	525	.	.	.	Note=Ser-rich	
+P22146	UniProtKB	Active site	161	161	.	.	.	Note=Proton donor	
+P22146	UniProtKB	Active site	262	262	.	.	.	Note=Nucleophile	
+P22146	UniProtKB	Binding site	92	92	.	.	.	Note=Donor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Binding site	160	160	.	.	.	Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Binding site	161	161	.	.	.	Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Binding site	202	202	.	.	.	Note=Acceptor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Binding site	207	207	.	.	.	Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Binding site	294	294	.	.	.	Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Lipidation	528	528	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1824714;Dbxref=PMID:1824714	
+P22146	UniProtKB	Glycosylation	40	40	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22146	UniProtKB	Glycosylation	57	57	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22146	UniProtKB	Glycosylation	95	95	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22146	UniProtKB	Glycosylation	149	149	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22146	UniProtKB	Glycosylation	165	165	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22146	UniProtKB	Glycosylation	253	253	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22146	UniProtKB	Glycosylation	283	283	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22146	UniProtKB	Glycosylation	321	321	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22146	UniProtKB	Glycosylation	409	409	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22146	UniProtKB	Glycosylation	495	495	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22146	UniProtKB	Disulfide bond	74	103	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Disulfide bond	216	348	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Disulfide bond	234	265	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Disulfide bond	370	421	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Disulfide bond	372	462	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Disulfide bond	379	445	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Disulfide bond	398	403	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22146	UniProtKB	Mutagenesis	74	74	.	.	.	Note=Impairs the folding and stability of the protein. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355340;Dbxref=PMID:15355340	
+P22146	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Partially impairs the folding and stability of the protein. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355340;Dbxref=PMID:15355340	
+P22146	UniProtKB	Mutagenesis	161	161	.	.	.	Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355340;Dbxref=PMID:15355340	
+P22146	UniProtKB	Mutagenesis	262	262	.	.	.	Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355340;Dbxref=PMID:15355340	
+P22146	UniProtKB	Mutagenesis	265	265	.	.	.	Note=Partially impairs the folding and stability of the protein. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355340;Dbxref=PMID:15355340	
+P22146	UniProtKB	Mutagenesis	348	348	.	.	.	Note=Impairs the folding and stability of the protein. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18468997;Dbxref=PMID:18468997	
+P22146	UniProtKB	Sequence conflict	211	211	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06135 1 555
+Q06135	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06135	UniProtKB	Chain	25	531	.	.	.	ID=PRO_0000010475;Note=1%2C3-beta-glucanosyltransferase GAS2	
+Q06135	UniProtKB	Propeptide	532	555	.	.	.	ID=PRO_0000010476;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06135	UniProtKB	Region	134	142	.	.	.	Note=Donor substrate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Active site	176	176	.	.	.	Note=Proton donor	
+Q06135	UniProtKB	Active site	275	275	.	.	.	Note=Nucleophile	
+Q06135	UniProtKB	Binding site	107	107	.	.	.	Note=Donor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Binding site	175	175	.	.	.	Note=Donor substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Binding site	176	176	.	.	.	Note=Acceptor substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Binding site	217	217	.	.	.	Note=Acceptor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Binding site	222	222	.	.	.	Note=Acceptor substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Binding site	307	307	.	.	.	Note=Donor substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Lipidation	531	531	.	.	.	Note=GPI-anchor amidated aspartate;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06135	UniProtKB	Glycosylation	498	498	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06135	UniProtKB	Disulfide bond	89	118	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997	
+Q06135	UniProtKB	Disulfide bond	231	367	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997	
+Q06135	UniProtKB	Disulfide bond	247	278	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997	
+Q06135	UniProtKB	Disulfide bond	390	442	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997	
+Q06135	UniProtKB	Disulfide bond	392	489	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997	
+Q06135	UniProtKB	Disulfide bond	399	466	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997	
+Q06135	UniProtKB	Disulfide bond	419	424	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997	
+Q06135	UniProtKB	Mutagenesis	62	62	.	.	.	Note=Slightly reduces catalytic activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Mutagenesis	107	107	.	.	.	Note=Slightly reduces catalytic activity. Y->F%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Mutagenesis	132	132	.	.	.	Note=Slightly reduces catalytic activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Mutagenesis	175	175	.	.	.	Note=Abolishes catalytic activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Abolishes catalytic activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Mutagenesis	244	244	.	.	.	Note=Moderately reduces hydrolysis%2C and causes a 10-fold reduction in transglycosylation activity. Y->F%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Mutagenesis	275	275	.	.	.	Note=Abolishes catalytic activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Mutagenesis	307	307	.	.	.	Note=Moderately reduces catalytic activity. Y->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Mutagenesis	404	404	.	.	.	Note=Slightly reduces catalytic activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Mutagenesis	474	474	.	.	.	Note=No effect. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997	
+Q06135	UniProtKB	Beta strand	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Turn	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	54	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Turn	72	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	86	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	102	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	116	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	128	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FIH	
+Q06135	UniProtKB	Helix	149	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	168	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	187	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	211	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Turn	219	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	222	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	239	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	252	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	257	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	271	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	280	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	288	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	295	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	303	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	313	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W62	
+Q06135	UniProtKB	Beta strand	318	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	327	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	331	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	350	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Turn	372	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	387	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	398	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	408	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	411	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Turn	419	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	424	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Turn	431	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Turn	438	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	444	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Beta strand	473	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	477	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+Q06135	UniProtKB	Helix	490	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61	
+##sequence-region P18851 1 423
+P18851	UniProtKB	Chain	1	423	.	.	.	ID=PRO_0000127720;Note=Guanine nucleotide-binding protein subunit beta	
+P18851	UniProtKB	Repeat	90	120	.	.	.	Note=WD 1	
+P18851	UniProtKB	Repeat	132	162	.	.	.	Note=WD 2	
+P18851	UniProtKB	Repeat	179	208	.	.	.	Note=WD 3	
+P18851	UniProtKB	Repeat	220	256	.	.	.	Note=WD 4	
+P18851	UniProtKB	Repeat	268	298	.	.	.	Note=WD 5	
+P18851	UniProtKB	Repeat	348	377	.	.	.	Note=WD 6	
+P18851	UniProtKB	Repeat	389	419	.	.	.	Note=WD 7	
+P18851	UniProtKB	Sequence conflict	33	33	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18851	UniProtKB	Sequence conflict	236	236	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39993 1 1459
+P39993	UniProtKB	Chain	1	1459	.	.	.	ID=PRO_0000120213;Note=ARF guanine-nucleotide exchange factor 2	
+P39993	UniProtKB	Domain	570	714	.	.	.	Note=SEC7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00189	
+P39993	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39993	UniProtKB	Modified residue	284	284	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39993	UniProtKB	Helix	558	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	574	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Beta strand	586	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	592	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Turn	602	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	608	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	618	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	621	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	638	645	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Turn	646	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	655	671	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	677	679	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	688	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	695	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	723	729	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Turn	730	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+P39993	UniProtKB	Helix	741	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1	
+##sequence-region P25370 1 566
+P25370	UniProtKB	Chain	1	566	.	.	.	ID=PRO_0000202543;Note=Good for full DBP5 activity protein 2	
+##sequence-region Q12051 1 335
+Q12051	UniProtKB	Chain	1	335	.	.	.	ID=PRO_0000228139;Note=Geranylgeranyl pyrophosphate synthase	
+Q12051	UniProtKB	Metal binding	75	75	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16554305,ECO:0000269|PubMed:17535895;Dbxref=PMID:16554305,PMID:17535895	
+Q12051	UniProtKB	Metal binding	75	75	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16554305,ECO:0000269|PubMed:17535895;Dbxref=PMID:16554305,PMID:17535895	
+Q12051	UniProtKB	Metal binding	79	79	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16554305,ECO:0000269|PubMed:17535895;Dbxref=PMID:16554305,PMID:17535895	
+Q12051	UniProtKB	Metal binding	79	79	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16554305,ECO:0000269|PubMed:17535895;Dbxref=PMID:16554305,PMID:17535895	
+Q12051	UniProtKB	Metal binding	209	209	.	.	.	Note=Magnesium 3;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16554305,ECO:0000269|PubMed:17535895;Dbxref=PMID:16554305,PMID:17535895	
+Q12051	UniProtKB	Binding site	36	36	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895	
+Q12051	UniProtKB	Binding site	39	39	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895	
+Q12051	UniProtKB	Binding site	68	68	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895	
+Q12051	UniProtKB	Binding site	84	84	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895	
+Q12051	UniProtKB	Binding site	85	85	.	.	.	Note=Isopentenyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895	
+Q12051	UniProtKB	Binding site	169	169	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895	
+Q12051	UniProtKB	Binding site	170	170	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895	
+Q12051	UniProtKB	Binding site	206	206	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895	
+Q12051	UniProtKB	Binding site	213	213	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895	
+Q12051	UniProtKB	Binding site	223	223	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12051	UniProtKB	Binding site	233	233	.	.	.	Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895	
+Q12051	UniProtKB	Site	107	107	.	.	.	Note=Important for determining product chain length	
+Q12051	UniProtKB	Mutagenesis	7	7	.	.	.	Note=No effect. Monomer%3B when associated with G-8. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19245203;Dbxref=PMID:19245203	
+Q12051	UniProtKB	Mutagenesis	8	8	.	.	.	Note=Monomer and homodimer. Monomer%3B when associated with G-7. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19245203;Dbxref=PMID:19245203	
+Q12051	UniProtKB	Mutagenesis	9	9	.	.	.	Note=Mostly monomer. Exclusively monomer%3B when associated with G-8. Reduces enzyme activity 1000-fold. I->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19245203;Dbxref=PMID:19245203	
+Q12051	UniProtKB	Mutagenesis	107	107	.	.	.	Note=Reduced affinity for isopentenyl diphosphate (IPP). Y->A	
+Q12051	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Reduced affinity for isopentenyl diphosphate (IPP). F->A	
+Q12051	UniProtKB	Mutagenesis	139	139	.	.	.	Note=Reduced affinity for isopentenyl diphosphate (IPP). H->A	
+Q12051	UniProtKB	Helix	1	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	17	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Beta strand	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8X	
+Q12051	UniProtKB	Helix	38	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	54	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Beta strand	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	90	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	96	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	114	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	121	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Turn	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4V	
+Q12051	UniProtKB	Helix	159	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	171	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	195	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Turn	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DH4	
+Q12051	UniProtKB	Helix	227	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	236	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	251	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	268	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	284	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V	
+Q12051	UniProtKB	Helix	325	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4V	
+Q12051	UniProtKB	Turn	331	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4V	
+##sequence-region Q06648 1 383
+Q06648	UniProtKB	Chain	1	383	.	.	.	ID=PRO_0000212660;Note=GTPase-interacting component 2	
+Q06648	UniProtKB	Domain	134	147	.	.	.	Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057	
+Q06648	UniProtKB	Compositional bias	74	102	.	.	.	Note=Ser-rich	
+Q06648	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06648	UniProtKB	Modified residue	258	258	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06648	UniProtKB	Modified residue	337	337	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06648	UniProtKB	Modified residue	345	345	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+Q06648	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q03833 1 894
+Q03833	UniProtKB	Chain	1	894	.	.	.	ID=PRO_0000046806;Note=Transcriptional activator/repressor GIS1	
+Q03833	UniProtKB	Domain	12	53	.	.	.	Note=JmjN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00537	
+Q03833	UniProtKB	Domain	170	324	.	.	.	Note=JmjC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538	
+Q03833	UniProtKB	Zinc finger	828	851	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q03833	UniProtKB	Zinc finger	857	882	.	.	.	Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q03833	UniProtKB	Coiled coil	90	110	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03833	UniProtKB	Coiled coil	361	385	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03833	UniProtKB	Motif	316	332	.	.	.	Note=Bipartite nuclear localization signal	
+Q03833	UniProtKB	Compositional bias	462	806	.	.	.	Note=Asn-rich	
+Q03833	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03833	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03833	UniProtKB	Modified residue	690	690	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03833	UniProtKB	Modified residue	694	694	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03833	UniProtKB	Modified residue	696	696	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03833	UniProtKB	Modified residue	734	734	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03833	UniProtKB	Modified residue	747	747	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38196 1 639
+P38196	UniProtKB	Chain	1	639	.	.	.	ID=PRO_0000197923;Note=Uridine permease	
+P38196	UniProtKB	Topological domain	1	162	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Transmembrane	163	180	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Topological domain	181	200	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Transmembrane	201	225	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Topological domain	226	259	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Transmembrane	260	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Topological domain	277	283	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Transmembrane	284	305	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Topological domain	306	367	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Transmembrane	368	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Topological domain	393	416	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Transmembrane	417	435	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Topological domain	436	460	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Transmembrane	461	477	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Topological domain	478	483	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Transmembrane	484	507	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Topological domain	508	537	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Transmembrane	538	562	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Topological domain	563	572	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Transmembrane	573	590	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Topological domain	591	639	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38196	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38196	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38196	UniProtKB	Cross-link	635	635	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P11710 1 512
+P11710	UniProtKB	Chain	1	512	.	.	.	ID=PRO_0000087384;Note=Nuclear fusion protein FUS1	
+P11710	UniProtKB	Transmembrane	72	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P11710	UniProtKB	Domain	436	512	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P11710	UniProtKB	Region	97	512	.	.	.	Note=Hydrophilic	
+P11710	UniProtKB	Compositional bias	1	71	.	.	.	Note=Ser/Thr-rich	
+P11710	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P11710	UniProtKB	Modified residue	190	190	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P11710	UniProtKB	Modified residue	256	256	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P11710	UniProtKB	Modified residue	281	281	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P11710	UniProtKB	Modified residue	424	424	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P40492 1 516
+P40492	UniProtKB	Chain	1	516	.	.	.	ID=PRO_0000202970;Note=Protein FYV10	
+P40492	UniProtKB	Domain	187	245	.	.	.	Note=CTLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00058	
+##sequence-region Q99341 1 161
+Q99341	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000299774;Note=Putative uncharacterized protein FYV1	
+##sequence-region P38297 1 855
+P38297	UniProtKB	Chain	1	855	.	.	.	ID=PRO_0000127682;Note=Mitofusin FZO1	
+P38297	UniProtKB	Topological domain	1	705	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11266460;Dbxref=PMID:11266460	
+P38297	UniProtKB	Transmembrane	706	726	.	.	.	Note=Helical%3B Name%3D1	
+P38297	UniProtKB	Topological domain	727	736	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11266460;Dbxref=PMID:11266460	
+P38297	UniProtKB	Transmembrane	737	757	.	.	.	Note=Helical%3B Name%3D2	
+P38297	UniProtKB	Topological domain	758	855	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11266460;Dbxref=PMID:11266460	
+P38297	UniProtKB	Domain	184	467	.	.	.	Note=Dynamin-type G	
+P38297	UniProtKB	Nucleotide binding	197	202	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IWA4	
+P38297	UniProtKB	Nucleotide binding	370	373	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IWA4	
+P38297	UniProtKB	Region	91	190	.	.	.	Note=HRN	
+P38297	UniProtKB	Region	484	547	.	.	.	Note=HR1	
+P38297	UniProtKB	Region	630	843	.	.	.	Note=Required for interaction with UGO1	
+P38297	UniProtKB	Region	769	831	.	.	.	Note=HR2	
+P38297	UniProtKB	Coiled coil	798	825	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38297	UniProtKB	Binding site	408	408	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IWA4	
+P38297	UniProtKB	Cross-link	398	398	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23317502;Dbxref=PMID:23317502	
+P38297	UniProtKB	Cross-link	464	464	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23317502;Dbxref=PMID:23317502	
+P38297	UniProtKB	Mutagenesis	172	172	.	.	.	Note=Abolishes fusion function. V->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808	
+P38297	UniProtKB	Mutagenesis	195	195	.	.	.	Note=Abolishes fusion function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21385840;Dbxref=PMID:21385840	
+P38297	UniProtKB	Mutagenesis	196	196	.	.	.	Note=Leads to an unusual intermediate mitochondrial morphology described as disorganized tubules in which mitochondria are tubular%2C distorted%2C less branched%2C and poorly distributed throughout the cell. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19812251;Dbxref=PMID:19812251	
+P38297	UniProtKB	Mutagenesis	197	197	.	.	.	Note=Abolishes fusion function. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21385840;Dbxref=PMID:21385840	
+P38297	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Abolishes fusion function%2C MDM30-binding and MDM30-dependent ubiquitination. No effect on localization or interaction with UGO1. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16624808,ECO:0000269|PubMed:21385840,ECO:0000269|PubMed:21502136,ECO:0000269|PubMed:9786948;Dbxref=PMID:16624808,PMID:21385840,PMID:21502136,PMID:9786948	
+P38297	UniProtKB	Mutagenesis	201	201	.	.	.	Note=Abolishes fusion function%2C MDM30-binding and MDM30-dependent ubiquitination%2C but not localization to mitochondrial outer membrane. S->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16624808,ECO:0000269|PubMed:21385840,ECO:0000269|PubMed:21502136,ECO:0000269|PubMed:9786948;Dbxref=PMID:16624808,PMID:21385840,PMID:21502136,PMID:9786948	
+P38297	UniProtKB	Mutagenesis	221	221	.	.	.	Note=Abolishes fusion function%2C MDM30-binding and MDM30-dependent ubiquitination%2C but not localization to mitochondrial outer membrane. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16624808,ECO:0000269|PubMed:21385840,ECO:0000269|PubMed:21502136,ECO:0000269|PubMed:9786948;Dbxref=PMID:16624808,PMID:21385840,PMID:21502136,PMID:9786948	
+P38297	UniProtKB	Mutagenesis	320	320	.	.	.	Note=Loss of mitochondrial fusion. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21385840;Dbxref=PMID:21385840	
+P38297	UniProtKB	Mutagenesis	327	327	.	.	.	Note=Impairs GTP Hydrolysis and abolishes fusion function. V->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19812251;Dbxref=PMID:19812251	
+P38297	UniProtKB	Mutagenesis	371	371	.	.	.	Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9786948;Dbxref=PMID:9786948	
+P38297	UniProtKB	Mutagenesis	398	398	.	.	.	Note=Leads to accelerated proteolysis. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23317502;Dbxref=PMID:23317502	
+P38297	UniProtKB	Mutagenesis	464	464	.	.	.	Note=Abolishes fusion function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23317502;Dbxref=PMID:23317502	
+P38297	UniProtKB	Mutagenesis	490	490	.	.	.	Note=Abolishes fusion function. Y->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808	
+P38297	UniProtKB	Mutagenesis	501	501	.	.	.	Note=Abolishes fusion function%3B when associated with Ala-504. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808	
+P38297	UniProtKB	Mutagenesis	504	504	.	.	.	Note=Abolishes fusion function%3B when associated with Ala-501. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808	
+P38297	UniProtKB	Mutagenesis	518	518	.	.	.	Note=Abolishes fusion function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808	
+P38297	UniProtKB	Mutagenesis	538	538	.	.	.	Note=Abolishes fusion function. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808	
+P38297	UniProtKB	Mutagenesis	769	769	.	.	.	Note=Abolishes fusion function. Y->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808	
+P38297	UniProtKB	Mutagenesis	773	773	.	.	.	Note=Abolishes fusion function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808	
+P38297	UniProtKB	Mutagenesis	819	819	.	.	.	Note=Abolishes fusion function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808	
+##sequence-region P53260 1 183
+P53260	UniProtKB	Chain	1	183	.	.	.	ID=PRO_0000202811;Note=Glutamyl-tRNA(Gln) amidotransferase subunit F%2C mitochondrial	
+P53260	UniProtKB	Sequence conflict	9	9	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53260	UniProtKB	Helix	39	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P53260	UniProtKB	Helix	53	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P53260	UniProtKB	Helix	71	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P53260	UniProtKB	Helix	90	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P53260	UniProtKB	Helix	105	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P53260	UniProtKB	Helix	135	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P53260	UniProtKB	Helix	149	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P53260	UniProtKB	Turn	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+P53260	UniProtKB	Beta strand	171	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+##sequence-region P18852 1 110
+P18852	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000194812;Note=Guanine nucleotide-binding protein subunit gamma	
+P18852	UniProtKB	Propeptide	108	110	.	.	.	ID=PRO_0000396775;Note=Removed in mature form	
+P18852	UniProtKB	Compositional bias	11	22	.	.	.	Note=Gln-rich	
+P18852	UniProtKB	Compositional bias	96	104	.	.	.	Note=Asn/Ser-rich	
+P18852	UniProtKB	Modified residue	107	107	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523659;Dbxref=PMID:10523659	
+P18852	UniProtKB	Lipidation	106	106	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10523659,ECO:0000269|PubMed:10712512;Dbxref=PMID:10523659,PMID:10712512	
+P18852	UniProtKB	Lipidation	107	107	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10523659,ECO:0000269|PubMed:10712512;Dbxref=PMID:10523659,PMID:10712512	
+P18852	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Partial loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523659;Dbxref=PMID:10523659	
+P18852	UniProtKB	Mutagenesis	107	107	.	.	.	Note=Loss of function. C->X;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7982577;Dbxref=PMID:7982577	
+##sequence-region P38301 1 280
+P38301	UniProtKB	Chain	1	280	.	.	.	ID=PRO_0000212467;Note=GCR1-dependent translation factor 1	
+P38301	UniProtKB	Topological domain	1	3	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Transmembrane	4	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Topological domain	25	45	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Topological domain	67	71	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Topological domain	93	104	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Topological domain	126	183	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Transmembrane	184	204	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Topological domain	205	222	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Transmembrane	223	243	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Topological domain	244	255	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Transmembrane	256	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Topological domain	277	280	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38301	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Loss of function in calcium homeostasis. R->C%2CH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23575229;Dbxref=PMID:23575229	
+P38301	UniProtKB	Sequence conflict	158	158	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47102 1 1408
+P47102	UniProtKB	Chain	1	1408	.	.	.	ID=PRO_0000120212;Note=ARF guanine-nucleotide exchange factor 1	
+P47102	UniProtKB	Domain	552	706	.	.	.	Note=SEC7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00189	
+P47102	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P39993	
+P47102	UniProtKB	Mutagenesis	862	862	.	.	.	Note=Abolishes interaction with GMH1. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808035;Dbxref=PMID:12808035	
+P47102	UniProtKB	Helix	540	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	556	565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Beta strand	568	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	574	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	585	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	590	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	600	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	603	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	620	627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	637	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	687	705	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	715	721	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Turn	722	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	733	745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+P47102	UniProtKB	Helix	751	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0	
+##sequence-region P38988 1 300
+P38988	UniProtKB	Chain	1	300	.	.	.	ID=PRO_0000090687;Note=Mitochondrial GTP/GDP carrier protein 1	
+P38988	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38988	UniProtKB	Transmembrane	85	101	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38988	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38988	UniProtKB	Transmembrane	173	189	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38988	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38988	UniProtKB	Transmembrane	268	285	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38988	UniProtKB	Repeat	8	108	.	.	.	Note=Solcar 1	
+P38988	UniProtKB	Repeat	117	198	.	.	.	Note=Solcar 2	
+P38988	UniProtKB	Repeat	208	293	.	.	.	Note=Solcar 3	
+##sequence-region Q04233 1 774
+Q04233	UniProtKB	Chain	1	774	.	.	.	ID=PRO_0000087498;Note=Protein GIS4	
+Q04233	UniProtKB	Compositional bias	147	152	.	.	.	Note=Poly-Asn	
+Q04233	UniProtKB	Compositional bias	183	203	.	.	.	Note=Thr-rich	
+Q04233	UniProtKB	Compositional bias	329	358	.	.	.	Note=Ser-rich	
+Q04233	UniProtKB	Compositional bias	340	349	.	.	.	Note=Poly-Ser	
+Q04233	UniProtKB	Compositional bias	353	358	.	.	.	Note=Poly-Ser	
+Q04233	UniProtKB	Compositional bias	576	589	.	.	.	Note=Asp-rich	
+Q04233	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04233	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04233	UniProtKB	Modified residue	616	616	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04233	UniProtKB	Modified residue	622	622	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q04233	UniProtKB	Modified residue	707	707	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q04233	UniProtKB	Modified residue	720	720	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q07540 1 174
+Q07540	UniProtKB	Transit peptide	1	21	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q07540	UniProtKB	Chain	22	174	.	.	.	ID=PRO_0000010135;Note=Frataxin homolog intermediate form	
+Q07540	UniProtKB	Chain	52	174	.	.	.	ID=PRO_0000010136;Note=Frataxin homolog%2C mitochondrial	
+Q07540	UniProtKB	Mutagenesis	79	79	.	.	.	Note=Nearly abolishes ferroxidase activity%2C slows down oligomerization%2C impairs resistance to iron-catalyzed oxidative stress%2C no effect on Fe(2+) delivery and cell growth%3B when associated with A-82. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422	
+Q07540	UniProtKB	Mutagenesis	82	82	.	.	.	Note=Nearly abolishes ferroxidase activity%2C slows down oligomerization%2C impairs resistance to iron-catalyzed oxidative stress%2C no effect on Fe(2+) delivery and cell growth%3B when associated with A-79. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422	
+Q07540	UniProtKB	Mutagenesis	93	93	.	.	.	Note=Impairs oligomerization and iron mineralization. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422	
+Q07540	UniProtKB	Mutagenesis	93	93	.	.	.	Note=Impairs resistance to iron-catalyzed oxidative stress%2C no effect on Fe(2+) delivery and cell growth%3B when associated with A-97 and A-103. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422	
+Q07540	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Impairs resistance to iron-catalyzed oxidative stress%2C no effect on Fe(2+) delivery and cell growth%3B when associated with A-93 and A-103. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422	
+Q07540	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Impairs resistance to iron-catalyzed oxidative stress%2C no effect on Fe(2+) delivery and cell growth%3B when associated with A-93 and A-97. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422	
+Q07540	UniProtKB	Mutagenesis	122	124	.	.	.	Note=Impairs cell growth%2C lowers activity of motochondrial iron-sulfur cluster-containing enzymes%2C no effect on iron binding and oligomerization. NKQ->ATA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18319250;Dbxref=PMID:18319250	
+Q07540	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Impairs cell growth and lowers aconitase activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19884169;Dbxref=PMID:19884169	
+Q07540	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Impairs cell growth and lowers aconitase activity. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19884169;Dbxref=PMID:19884169	
+Q07540	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Impairs cell growth%2C lowers aconitase activity and strongly decreases interaction with ISU1. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19884169;Dbxref=PMID:19884169	
+Q07540	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Lowers aconitase activity and no effexct on interaction with ISU1. W->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19884169;Dbxref=PMID:19884169	
+Q07540	UniProtKB	Mutagenesis	141	141	.	.	.	Note=Impairs cell growth and lowers aconitase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19884169;Dbxref=PMID:19884169	
+Q07540	UniProtKB	Turn	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Helix	76	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Turn	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Beta strand	96	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQL	
+Q07540	UniProtKB	Beta strand	101	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Beta strand	106	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Turn	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Beta strand	119	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Beta strand	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Beta strand	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Turn	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Beta strand	138	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Turn	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+Q07540	UniProtKB	Helix	158	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ	
+##sequence-region P32614 1 470
+P32614	UniProtKB	Chain	1	470	.	.	.	ID=PRO_0000158669;Note=Fumarate reductase 1	
+P32614	UniProtKB	Nucleotide binding	6	20	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32614	UniProtKB	Active site	249	249	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32614	UniProtKB	Active site	272	272	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32614	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32614	UniProtKB	Sequence conflict	285	285	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32614	UniProtKB	Sequence conflict	440	440	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36088 1 180
+P36088	UniProtKB	Chain	1	180	.	.	.	ID=PRO_0000171552;Note=Free methionine-R-sulfoxide reductase	
+P36088	UniProtKB	Domain	99	177	.	.	.	Note=GAF	
+P36088	UniProtKB	Mutagenesis	91	91	.	.	.	Note=Dramatic reduction in enzyme activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19049972;Dbxref=PMID:19049972	
+P36088	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Dramatic reduction in enzyme activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19049972;Dbxref=PMID:19049972	
+P36088	UniProtKB	Mutagenesis	125	125	.	.	.	Note=Dramatic reduction in enzyme activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19049972;Dbxref=PMID:19049972	
+P36088	UniProtKB	Helix	9	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Helix	21	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Helix	42	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Beta strand	64	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Beta strand	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Beta strand	79	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Beta strand	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Helix	99	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Beta strand	111	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Helix	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Beta strand	131	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Beta strand	144	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+P36088	UniProtKB	Helix	160	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M	
+##sequence-region P40088 1 404
+P40088	UniProtKB	Chain	1	404	.	.	.	ID=PRO_0000159649;Note=Plasma membrane iron permease	
+P40088	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40088	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40088	UniProtKB	Transmembrane	87	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40088	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40088	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40088	UniProtKB	Transmembrane	207	227	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40088	UniProtKB	Transmembrane	294	314	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P18411 1 198
+P18411	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000202412;Note=Protein FUN14	
+P18411	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18411	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18411	UniProtKB	Transmembrane	172	192	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P31381 1 517
+P31381	UniProtKB	Chain	1	517	.	.	.	ID=PRO_0000209346;Note=Nucleoside transporter FUN26	
+P31381	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31381	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31381	UniProtKB	Transmembrane	151	171	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31381	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31381	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31381	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31381	UniProtKB	Transmembrane	344	364	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31381	UniProtKB	Transmembrane	367	387	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31381	UniProtKB	Transmembrane	411	431	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31381	UniProtKB	Transmembrane	446	466	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31381	UniProtKB	Transmembrane	492	512	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31381	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P31381	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P19145 1 602
+P19145	UniProtKB	Chain	1	602	.	.	.	ID=PRO_0000054151;Note=General amino-acid permease GAP1	
+P19145	UniProtKB	Topological domain	1	95	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	96	116	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	117	121	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	143	165	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	166	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	186	204	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	205	224	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	225	237	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	238	256	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	257	280	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	281	298	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	299	321	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	322	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	343	376	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	377	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	397	421	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	422	442	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	443	451	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	452	472	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	473	491	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	492	510	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	511	529	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Transmembrane	530	548	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Topological domain	549	602	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19145	UniProtKB	Cross-link	76	76	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12872131,ECO:0000269|PubMed:14557538;Dbxref=PMID:12872131,PMID:14557538	
+P19145	UniProtKB	Mutagenesis	297	297	.	.	.	Note=Impairs basic amino-acids transport and regulation by these amino-acids. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21471002;Dbxref=PMID:21471002	
+P19145	UniProtKB	Sequence conflict	122	122	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19145	UniProtKB	Sequence conflict	189	189	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19145	UniProtKB	Sequence conflict	338	338	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19145	UniProtKB	Sequence conflict	518	518	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P28007 1 205
+P28007	UniProtKB	Chain	1	205	.	.	.	ID=PRO_0000208566;Note=H/ACA ribonucleoprotein complex subunit 1	
+P28007	UniProtKB	Region	4	21	.	.	.	Note=RGG-box 1	
+P28007	UniProtKB	Region	147	205	.	.	.	Note=RGG-box 2	
+P28007	UniProtKB	Modified residue	4	4	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	8	8	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	11	11	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	15	15	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	19	19	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	147	147	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	154	154	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	158	158	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	162	162	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	165	165	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	171	171	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	174	174	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	180	180	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	184	184	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	189	189	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	193	193	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	197	197	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Modified residue	201	201	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P28007	UniProtKB	Cross-link	77	77	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P28007	UniProtKB	Beta strand	37	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P28007	UniProtKB	Beta strand	50	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P28007	UniProtKB	Beta strand	57	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P28007	UniProtKB	Beta strand	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P28007	UniProtKB	Beta strand	74	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P28007	UniProtKB	Beta strand	89	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P28007	UniProtKB	Helix	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P28007	UniProtKB	Beta strand	108	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P28007	UniProtKB	Helix	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+P28007	UniProtKB	Helix	119	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+##sequence-region Q03655 1 524
+Q03655	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03655	UniProtKB	Chain	22	498	.	.	.	ID=PRO_0000010477;Note=Probable 1%2C3-beta-glucanosyltransferase GAS3	
+Q03655	UniProtKB	Propeptide	499	524	.	.	.	ID=PRO_0000010478;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03655	UniProtKB	Compositional bias	458	496	.	.	.	Note=Ser-rich	
+Q03655	UniProtKB	Active site	169	169	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03655	UniProtKB	Active site	283	283	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03655	UniProtKB	Binding site	96	96	.	.	.	Note=Donor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q03655	UniProtKB	Binding site	168	168	.	.	.	Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q03655	UniProtKB	Binding site	169	169	.	.	.	Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q03655	UniProtKB	Binding site	212	212	.	.	.	Note=Acceptor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q03655	UniProtKB	Binding site	217	217	.	.	.	Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q03655	UniProtKB	Binding site	315	315	.	.	.	Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q03655	UniProtKB	Lipidation	498	498	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03655	UniProtKB	Glycosylation	201	201	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03655	UniProtKB	Glycosylation	269	269	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03655	UniProtKB	Glycosylation	350	350	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03655	UniProtKB	Glycosylation	385	385	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03655	UniProtKB	Glycosylation	404	404	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03655	UniProtKB	Glycosylation	422	422	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03655	UniProtKB	Disulfide bond	78	107	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q03655	UniProtKB	Disulfide bond	226	369	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q03655	UniProtKB	Disulfide bond	254	286	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+##sequence-region P40209 1 560
+P40209	UniProtKB	Chain	1	560	.	.	.	ID=PRO_0000083485;Note=Protein GAT2	
+P40209	UniProtKB	Zinc finger	472	497	.	.	.	Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094	
+##sequence-region P39726 1 170
+P39726	UniProtKB	Transit peptide	1	47	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39726	UniProtKB	Chain	48	170	.	.	.	ID=PRO_0000010739;Note=Glycine cleavage system H protein%2C mitochondrial	
+P39726	UniProtKB	Domain	61	143	.	.	.	Note=Lipoyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066	
+P39726	UniProtKB	Modified residue	102	102	.	.	.	Note=N6-lipoyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066	
+P39726	UniProtKB	Sequence conflict	14	14	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39726	UniProtKB	Sequence conflict	73	73	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39726	UniProtKB	Sequence conflict	90	90	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08271 1 471
+Q08271	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08271	UniProtKB	Chain	22	447	.	.	.	ID=PRO_0000010479;Note=1%2C3-beta-glucanosyltransferase GAS4	
+Q08271	UniProtKB	Propeptide	448	471	.	.	.	ID=PRO_0000010480;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08271	UniProtKB	Active site	161	161	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08271	UniProtKB	Active site	266	266	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08271	UniProtKB	Binding site	88	88	.	.	.	Note=Donor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08271	UniProtKB	Binding site	160	160	.	.	.	Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08271	UniProtKB	Binding site	161	161	.	.	.	Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08271	UniProtKB	Binding site	203	203	.	.	.	Note=Acceptor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08271	UniProtKB	Binding site	208	208	.	.	.	Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08271	UniProtKB	Binding site	298	298	.	.	.	Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08271	UniProtKB	Lipidation	447	447	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08271	UniProtKB	Glycosylation	151	151	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08271	UniProtKB	Glycosylation	398	398	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08271	UniProtKB	Disulfide bond	70	99	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08271	UniProtKB	Disulfide bond	217	354	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08271	UniProtKB	Disulfide bond	238	269	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+##sequence-region Q08193 1 484
+Q08193	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08193	UniProtKB	Chain	20	462	.	.	.	ID=PRO_0000010481;Note=1%2C3-beta-glucanosyltransferase GAS5	
+Q08193	UniProtKB	Propeptide	463	484	.	.	.	ID=PRO_0000010482;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08193	UniProtKB	Compositional bias	395	403	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+Q08193	UniProtKB	Compositional bias	405	460	.	.	.	Note=Ser-rich	
+Q08193	UniProtKB	Compositional bias	405	427	.	.	.	Note=Poly-Ser	
+Q08193	UniProtKB	Compositional bias	432	439	.	.	.	Note=Poly-Ser	
+Q08193	UniProtKB	Active site	160	160	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08193	UniProtKB	Active site	262	262	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08193	UniProtKB	Binding site	89	89	.	.	.	Note=Donor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08193	UniProtKB	Binding site	159	159	.	.	.	Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08193	UniProtKB	Binding site	160	160	.	.	.	Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08193	UniProtKB	Binding site	201	201	.	.	.	Note=Acceptor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08193	UniProtKB	Binding site	206	206	.	.	.	Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08193	UniProtKB	Binding site	295	295	.	.	.	Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08193	UniProtKB	Lipidation	462	462	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08193	UniProtKB	Glycosylation	24	24	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08193	UniProtKB	Glycosylation	60	60	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08193	UniProtKB	Glycosylation	166	166	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08193	UniProtKB	Glycosylation	299	299	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08193	UniProtKB	Glycosylation	344	344	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08193	UniProtKB	Glycosylation	359	359	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08193	UniProtKB	Disulfide bond	71	100	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08193	UniProtKB	Disulfide bond	215	348	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+Q08193	UniProtKB	Disulfide bond	234	265	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135	
+##sequence-region Q03557 1 464
+Q03557	UniProtKB	Chain	1	464	.	.	.	ID=PRO_0000001205;Note=Glutamyl-tRNA(Gln) amidotransferase subunit A%2C mitochondrial	
+Q03557	UniProtKB	Active site	52	52	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03150	
+Q03557	UniProtKB	Active site	130	130	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03150	
+Q03557	UniProtKB	Active site	154	154	.	.	.	Note=Acyl-ester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03150	
+Q03557	UniProtKB	Helix	7	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	24	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Turn	43	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	48	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	79	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	90	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	132	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	142	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	156	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	164	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Turn	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	188	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	196	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	219	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	236	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	252	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	269	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	276	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	281	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Turn	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	301	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	313	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	329	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	344	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	369	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Turn	374	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	384	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	400	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	411	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0I	
+Q03557	UniProtKB	Turn	417	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	422	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	431	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Beta strand	443	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+Q03557	UniProtKB	Helix	453	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H	
+##sequence-region P38011 1 319
+P38011	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378	
+P38011	UniProtKB	Chain	2	319	.	.	.	ID=PRO_0000127758;Note=Guanine nucleotide-binding protein subunit beta-like protein	
+P38011	UniProtKB	Repeat	15	55	.	.	.	Note=WD 1	
+P38011	UniProtKB	Repeat	63	102	.	.	.	Note=WD 2	
+P38011	UniProtKB	Repeat	105	145	.	.	.	Note=WD 3	
+P38011	UniProtKB	Repeat	147	191	.	.	.	Note=WD 4	
+P38011	UniProtKB	Repeat	194	233	.	.	.	Note=WD 5	
+P38011	UniProtKB	Repeat	235	275	.	.	.	Note=WD 6	
+P38011	UniProtKB	Repeat	284	319	.	.	.	Note=WD 7	
+P38011	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378	
+P38011	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38011	UniProtKB	Modified residue	168	168	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38011	UniProtKB	Cross-link	46	46	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38011	UniProtKB	Cross-link	53	53	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38011	UniProtKB	Cross-link	107	107	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38011	UniProtKB	Cross-link	137	137	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38011	UniProtKB	Cross-link	161	161	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38011	UniProtKB	Beta strand	5	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	20	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	40	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	53	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	77	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	87	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Turn	94	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	98	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	110	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	121	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	131	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	140	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	151	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	168	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	178	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Turn	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	187	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	199	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	208	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Helix	216	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RFH	
+P38011	UniProtKB	Beta strand	219	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Turn	225	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	229	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	240	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	247	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	259	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Turn	265	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	269	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Helix	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	289	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	298	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+P38011	UniProtKB	Beta strand	310	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX	
+##sequence-region P07261 1 785
+P07261	UniProtKB	Chain	1	785	.	.	.	ID=PRO_0000087445;Note=Glycolytic genes transcriptional activator GCR1	
+P07261	UniProtKB	Region	267	299	.	.	.	Note=Leucine-zipper	
+P07261	UniProtKB	Region	632	785	.	.	.	Note=DNA-binding	
+P07261	UniProtKB	Compositional bias	412	618	.	.	.	Note=Pro/Ser-rich	
+P07261	UniProtKB	Modified residue	447	447	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07261	UniProtKB	Modified residue	449	449	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07261	UniProtKB	Modified residue	482	482	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07261	UniProtKB	Modified residue	489	489	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07261	UniProtKB	Modified residue	538	538	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07261	UniProtKB	Sequence conflict	399	399	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P14065 1 312
+P14065	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000124611;Note=Glycerol 2-dehydrogenase (NADP(+))	
+P14065	UniProtKB	Nucleotide binding	220	274	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14065	UniProtKB	Active site	56	56	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14065	UniProtKB	Binding site	112	112	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14065	UniProtKB	Site	81	81	.	.	.	Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14065	UniProtKB	Modified residue	306	306	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14065	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Decreases catalytic activity. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23770562;Dbxref=PMID:23770562	
+P14065	UniProtKB	Mutagenesis	56	56	.	.	.	Note=Loss of catalytic activity. Y->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17140678;Dbxref=PMID:17140678	
+P14065	UniProtKB	Mutagenesis	264	264	.	.	.	Note=Decreases catalytic activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23770562;Dbxref=PMID:23770562	
+P14065	UniProtKB	Mutagenesis	267	267	.	.	.	Note=Decreases catalytic activity. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23770562;Dbxref=PMID:23770562	
+P14065	UniProtKB	Mutagenesis	270	270	.	.	.	Note=Decreases catalytic activity. R->H%2CY%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23770562;Dbxref=PMID:23770562	
+##sequence-region P32775 1 704
+P32775	UniProtKB	Chain	1	704	.	.	.	ID=PRO_0000188786;Note=1%2C4-alpha-glucan-branching enzyme	
+P32775	UniProtKB	Active site	356	356	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32775	UniProtKB	Active site	417	417	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32775	UniProtKB	Modified residue	190	190	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32775	UniProtKB	Sequence conflict	564	564	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P17695 1 143
+P17695	UniProtKB	Transit peptide	1	35	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2189409;Dbxref=PMID:2189409	
+P17695	UniProtKB	Chain	36	143	.	.	.	ID=PRO_0000141612;Note=Glutaredoxin-2%2C mitochondrial	
+P17695	UniProtKB	Domain	41	143	.	.	.	Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686	
+P17695	UniProtKB	Region	58	63	.	.	.	Note=Glutathione binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757	
+P17695	UniProtKB	Region	122	123	.	.	.	Note=Glutathione binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757	
+P17695	UniProtKB	Binding site	109	109	.	.	.	Note=Glutathione%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757	
+P17695	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P17695	UniProtKB	Modified residue	61	61	.	.	.	Note=S-glutathionyl cysteine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757	
+P17695	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P17695	UniProtKB	Disulfide bond	61	64	.	.	.	Note=Redox-active%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20417731;Dbxref=PMID:20417731	
+P17695	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Leads to 30 percent decreased oxidoreductase activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757	
+P17695	UniProtKB	Mutagenesis	123	123	.	.	.	Note=Leads to decreased oxidoreductase activity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20417731;Dbxref=PMID:20417731	
+P17695	UniProtKB	Helix	38	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+P17695	UniProtKB	Beta strand	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+P17695	UniProtKB	Helix	62	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+P17695	UniProtKB	Helix	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+P17695	UniProtKB	Beta strand	82	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+P17695	UniProtKB	Helix	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+P17695	UniProtKB	Helix	93	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+P17695	UniProtKB	Beta strand	111	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+P17695	UniProtKB	Beta strand	117	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+P17695	UniProtKB	Helix	122	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+P17695	UniProtKB	Helix	133	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+P17695	UniProtKB	Turn	138	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG	
+##sequence-region P37303 1 387
+P37303	UniProtKB	Chain	1	387	.	.	.	ID=PRO_0000121572;Note=Low specificity L-threonine aldolase	
+P37303	UniProtKB	Modified residue	213	213	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P37303	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P37303	UniProtKB	Modified residue	369	369	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P37303	UniProtKB	Modified residue	370	370	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P37303	UniProtKB	Cross-link	228	228	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P37303	UniProtKB	Sequence conflict	253	253	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32191 1 649
+P32191	UniProtKB	Nucleotide binding	69	97	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32191	UniProtKB	Sequence conflict	1	51	.	.	.	Note=MFSVTRRRAAGAAAAMATATGTLYWMTSQGDRPLVHNDPSYMVQFPTAAPP->MTRATWCNSPPPLHR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32191	UniProtKB	Sequence conflict	63	63	.	.	.	Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32191	UniProtKB	Sequence conflict	182	182	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32191	UniProtKB	Sequence conflict	234	234	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32191	UniProtKB	Sequence conflict	243	243	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32191	UniProtKB	Sequence conflict	249	249	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32191	UniProtKB	Sequence conflict	320	320	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32191	UniProtKB	Sequence conflict	342	342	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32191	UniProtKB	Sequence conflict	645	646	.	.	.	Note=KT->QGR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38875 1 610
+P38875	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38875	UniProtKB	Chain	20	610	.	.	.	ID=PRO_0000024110;Note=GPI transamidase component GPI16	
+P38875	UniProtKB	Topological domain	20	551	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38875	UniProtKB	Transmembrane	552	572	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38875	UniProtKB	Topological domain	573	610	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38875	UniProtKB	Glycosylation	184	184	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11598210;Dbxref=PMID:11598210	
+P38875	UniProtKB	Disulfide bond	202	202	.	.	.	Note=Interchain (with C-85 in GPI8);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P46961 1 280
+P46961	UniProtKB	Chain	1	280	.	.	.	ID=PRO_0000087558;Note=Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit	
+P46961	UniProtKB	Topological domain	1	53	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Topological domain	75	75	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Topological domain	97	108	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Topological domain	130	135	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Topological domain	157	189	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Transmembrane	190	210	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Topological domain	211	220	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Transmembrane	221	241	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Topological domain	242	280	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46961	UniProtKB	Sequence conflict	48	48	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46961	UniProtKB	Sequence conflict	239	280	.	.	.	Note=IFFASVFYITVLPKWFIYWKINYHKRDNDLLSTWDARTPILD->FSLLQYFILQFYLSGSSTGKSIIINGITIY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40106 1 250
+P40106	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000087561;Note=Glycerol-1-phosphate phosphohydrolase 2	
+P40106	UniProtKB	Active site	18	18	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40106	UniProtKB	Active site	20	20	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40106	UniProtKB	Metal binding	18	18	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40106	UniProtKB	Metal binding	20	20	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40106	UniProtKB	Metal binding	179	179	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40106	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41277	
+P40106	UniProtKB	Cross-link	64	64	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41277	
+P40106	UniProtKB	Cross-link	144	144	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41277	
+##sequence-region P35197 1 352
+P35197	UniProtKB	Chain	1	352	.	.	.	ID=PRO_0000074224;Note=ADP-ribosylation factor GTPase-activating protein GCS1	
+P35197	UniProtKB	Domain	11	127	.	.	.	Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+P35197	UniProtKB	Zinc finger	26	49	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+P35197	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35197	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P35197	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P35197	UniProtKB	Modified residue	168	168	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35197	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35197	UniProtKB	Modified residue	260	260	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P35197	UniProtKB	Natural variant	27	27	.	.	.	Note=M->I	
+P35197	UniProtKB	Mutagenesis	29	29	.	.	.	Note=In GCS1-1%3B severely affect the function. C->Y	
+##sequence-region Q12393 1 293
+Q12393	UniProtKB	Chain	1	293	.	.	.	ID=PRO_0000247349;Note=Genetic interactor of prohibitin 5%2C mitochondrial	
+##sequence-region P25596 1 615
+P25596	UniProtKB	Chain	1	615	.	.	.	ID=PRO_0000202557;Note=Glutathione exchanger 1	
+P25596	UniProtKB	Topological domain	1	58	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	80	120	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	142	152	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	174	186	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	208	216	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	238	275	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	276	296	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	297	306	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	307	327	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	328	343	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	344	364	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	365	383	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	384	404	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	405	407	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	408	428	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	429	440	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	441	461	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	462	547	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Transmembrane	548	568	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25596	UniProtKB	Topological domain	569	615	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03016 1 1276
+Q03016	UniProtKB	Chain	1	1276	.	.	.	ID=PRO_0000238623;Note=GLC7-interacting protein 3	
+Q03016	UniProtKB	Compositional bias	28	214	.	.	.	Note=Ser-rich	
+Q03016	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q03016	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03016	UniProtKB	Modified residue	103	103	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03016	UniProtKB	Modified residue	143	143	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q03016	UniProtKB	Modified residue	260	260	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q03016	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q03016	UniProtKB	Modified residue	269	269	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q05926 1 109
+Q05926	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000268192;Note=Glutaredoxin-8	
+Q05926	UniProtKB	Domain	5	109	.	.	.	Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686	
+Q05926	UniProtKB	Disulfide bond	25	28	.	.	.	Note=Redox-active;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q05926	UniProtKB	Mutagenesis	25	25	.	.	.	Note=Impairs activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19166312;Dbxref=PMID:19166312	
+Q05926	UniProtKB	Mutagenesis	28	28	.	.	.	Note=Impairs activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19166312;Dbxref=PMID:19166312	
+Q05926	UniProtKB	Helix	5	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80	
+Q05926	UniProtKB	Beta strand	17	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80	
+Q05926	UniProtKB	Helix	28	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80	
+Q05926	UniProtKB	Turn	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80	
+Q05926	UniProtKB	Beta strand	44	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80	
+Q05926	UniProtKB	Helix	54	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80	
+Q05926	UniProtKB	Beta strand	72	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80	
+Q05926	UniProtKB	Beta strand	81	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80	
+Q05926	UniProtKB	Helix	86	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80	
+Q05926	UniProtKB	Helix	98	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80	
+##sequence-region P03069 1 281
+P03069	UniProtKB	Chain	1	281	.	.	.	ID=PRO_0000076490;Note=General control protein GCN4	
+P03069	UniProtKB	Domain	225	281	.	.	.	Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P03069	UniProtKB	Region	89	100	.	.	.	Note=Required for transcriptional activation	
+P03069	UniProtKB	Region	106	125	.	.	.	Note=Required for transcriptional activation	
+P03069	UniProtKB	Region	231	251	.	.	.	Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P03069	UniProtKB	Region	253	274	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P03069	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P03069	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12101234;Dbxref=PMID:12101234	
+P03069	UniProtKB	Modified residue	218	218	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P03069	UniProtKB	Natural variant	24	24	.	.	.	Note=In strain: CLIB 219. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P03069	UniProtKB	Natural variant	62	62	.	.	.	Note=In strain: CLIB 630 haplotype Ha2. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P03069	UniProtKB	Natural variant	82	82	.	.	.	Note=In strain: CLIB 556 haplotype Ha1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P03069	UniProtKB	Natural variant	91	91	.	.	.	Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13 haplotype Ha2%2C Sigma 1278B haplotype Ha1%2C YIIc12 and YIIc17. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P03069	UniProtKB	Natural variant	125	125	.	.	.	Note=In strain: CLIB 556 haplotype Ha1. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P03069	UniProtKB	Natural variant	196	196	.	.	.	Note=In strain: CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 630 haplotype Ha1%2C K1%2C YIIc12 haplotype Ha2 and YIIc17 haplotype Ha1. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P03069	UniProtKB	Mutagenesis	97	98	.	.	.	Note=Reduces transcriptional activation activity%3B when associated with A-107%3B A-110%3B A-113%3B A-120%3B A-123 and A-124. FF->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7862116;Dbxref=PMID:7862116	
+P03069	UniProtKB	Mutagenesis	107	107	.	.	.	Note=Reduces transcriptional activation activity%3B when associated with A-97%3B A-98%3B A-110%3B A-113%3B A-120%3B A-123 and A-124. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7862116;Dbxref=PMID:7862116	
+P03069	UniProtKB	Mutagenesis	110	110	.	.	.	Note=Reduces transcriptional activation activity%3B when associated with A-97%3B A-98%3B A-107%3B A-113%3B A-120%3B A-123 and A-124. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7862116;Dbxref=PMID:7862116	
+P03069	UniProtKB	Mutagenesis	113	113	.	.	.	Note=Reduces transcriptional activation activity%3B when associated with A-97%3B A-98%3B A-107%3B A-110%3B A-120%3B A-123 and A-124. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7862116;Dbxref=PMID:7862116	
+P03069	UniProtKB	Mutagenesis	120	124	.	.	.	Note=Reduces transcriptional activation activity%3B when associated with A-97%3B A-98%3B A-107%3B A-110 and A-113. WTSLF->ATSAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7862116;Dbxref=PMID:7862116	
+P03069	UniProtKB	Sequence conflict	239	281	.	.	.	Note=ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER->PGVLVRESCKE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03069	UniProtKB	Helix	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB	
+P03069	UniProtKB	Helix	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB	
+P03069	UniProtKB	Helix	250	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TL1	
+P03069	UniProtKB	Turn	264	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AZD	
+P03069	UniProtKB	Helix	268	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AZD	
+P03069	UniProtKB	Turn	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AZD	
+##sequence-region Q03330 1 439
+Q03330	UniProtKB	Chain	1	439	.	.	.	ID=PRO_0000211201;Note=Histone acetyltransferase GCN5	
+Q03330	UniProtKB	Domain	100	255	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+Q03330	UniProtKB	Domain	344	414	.	.	.	Note=Bromo;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+Q03330	UniProtKB	Region	177	179	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92830	
+Q03330	UniProtKB	Region	184	190	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92830	
+Q03330	UniProtKB	Region	216	219	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92830	
+Q03330	UniProtKB	Active site	173	173	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92830	
+Q03330	UniProtKB	Site	173	173	.	.	.	Note=Important for catalytic activity	
+Q03330	UniProtKB	Sequence conflict	187	187	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03330	UniProtKB	Beta strand	100	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Helix	111	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Helix	133	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Beta strand	146	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Turn	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Beta strand	156	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Helix	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Beta strand	171	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Helix	188	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Beta strand	208	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Helix	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Helix	218	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Beta strand	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Helix	234	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Beta strand	248	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH	
+Q03330	UniProtKB	Helix	333	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I	
+Q03330	UniProtKB	Helix	350	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I	
+Q03330	UniProtKB	Turn	358	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I	
+Q03330	UniProtKB	Helix	364	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I	
+Q03330	UniProtKB	Helix	374	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I	
+Q03330	UniProtKB	Helix	389	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I	
+Q03330	UniProtKB	Helix	412	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I	
+Q03330	UniProtKB	Helix	432	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I	
+##sequence-region Q01722 1 534
+Q01722	UniProtKB	Chain	1	534	.	.	.	ID=PRO_0000087446;Note=Glycolytic genes transcriptional activator GCR2	
+Q01722	UniProtKB	Region	497	534	.	.	.	Note=Leucine-zipper	
+Q01722	UniProtKB	Motif	281	288	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01722	UniProtKB	Compositional bias	255	283	.	.	.	Note=Asn-rich	
+Q01722	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q01722	UniProtKB	Modified residue	406	406	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q01722	UniProtKB	Modified residue	409	409	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32621 1 518
+P32621	UniProtKB	Chain	1	518	.	.	.	ID=PRO_0000209919;Note=Guanosine-diphosphatase	
+P32621	UniProtKB	Topological domain	1	9	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32621	UniProtKB	Transmembrane	10	24	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32621	UniProtKB	Topological domain	25	518	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32621	UniProtKB	Active site	216	216	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32621	UniProtKB	Glycosylation	41	41	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32621	UniProtKB	Glycosylation	280	280	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32621	UniProtKB	Glycosylation	335	335	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q02979 1 1223
+Q02979	UniProtKB	Chain	1	1223	.	.	.	ID=PRO_0000233009;Note=Glycerophosphocholine phosphodiesterase GDE1	
+Q02979	UniProtKB	Domain	1	213	.	.	.	Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714	
+Q02979	UniProtKB	Repeat	427	456	.	.	.	Note=ANK 1	
+Q02979	UniProtKB	Repeat	472	502	.	.	.	Note=ANK 2	
+Q02979	UniProtKB	Repeat	504	533	.	.	.	Note=ANK 3	
+Q02979	UniProtKB	Repeat	538	567	.	.	.	Note=ANK 4	
+Q02979	UniProtKB	Repeat	572	601	.	.	.	Note=ANK 5	
+Q02979	UniProtKB	Repeat	605	634	.	.	.	Note=ANK 6	
+Q02979	UniProtKB	Domain	872	1217	.	.	.	Note=GP-PDE	
+Q02979	UniProtKB	Modified residue	653	653	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02979	UniProtKB	Modified residue	983	983	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q99339 1 116
+Q99339	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000211376;Note=Putative UPF0320 protein YLL065W	
+##sequence-region P38229 1 639
+P38229	UniProtKB	Chain	1	639	.	.	.	ID=PRO_0000071520;Note=GLC7-interacting protein 1	
+##sequence-region Q03768 1 265
+Q03768	UniProtKB	Chain	1	265	.	.	.	ID=PRO_0000087495;Note=Protein GIR2	
+Q03768	UniProtKB	Domain	9	159	.	.	.	Note=RWD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00179	
+##sequence-region P38068 1 203
+P38068	UniProtKB	Signal peptide	1	32	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38068	UniProtKB	Chain	33	203	.	.	.	ID=PRO_0000042989;Note=Monothiol glutaredoxin-7	
+P38068	UniProtKB	Domain	88	191	.	.	.	Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686	
+P38068	UniProtKB	Metal binding	108	108	.	.	.	Note=Iron-sulfur (2Fe-2S)%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P37291 1 469
+P37291	UniProtKB	Chain	1	469	.	.	.	ID=PRO_0000113516;Note=Serine hydroxymethyltransferase%2C cytosolic	
+P37291	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P37291	UniProtKB	Modified residue	26	26	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P37291	UniProtKB	Modified residue	248	248	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P37291	UniProtKB	Modified residue	429	429	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P37291	UniProtKB	Cross-link	456	456	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P37291	UniProtKB	Sequence conflict	429	429	.	.	.	Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40107 1 337
+P40107	UniProtKB	Chain	1	337	.	.	.	ID=PRO_0000213398;Note=GDP-mannose transporter 1	
+P40107	UniProtKB	Topological domain	1	16	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Topological domain	38	51	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Topological domain	73	92	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Topological domain	114	119	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Topological domain	141	144	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Topological domain	166	180	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Transmembrane	181	201	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Topological domain	202	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Topological domain	237	252	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Transmembrane	253	273	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Topological domain	274	279	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Transmembrane	280	300	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Topological domain	301	304	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Transmembrane	305	325	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Topological domain	326	337	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Region	279	291	.	.	.	Note=GDP-mannose-binding	
+P40107	UniProtKB	Region	326	337	.	.	.	Note=RET2-binding	
+P40107	UniProtKB	Glycosylation	119	119	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Glycosylation	242	242	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Glycosylation	246	246	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Glycosylation	249	249	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40107	UniProtKB	Mutagenesis	278	278	.	.	.	Note=In VIG4-2%3B increases drug sensitivity and decreases protein glycolysis. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10570930;Dbxref=PMID:10570930	
+P40107	UniProtKB	Mutagenesis	280	280	.	.	.	Note=Decreases transport activity and GDP-mannose-binding. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855	
+P40107	UniProtKB	Mutagenesis	282	282	.	.	.	Note=Decreases transport activity and GDP-mannose-binding. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855	
+P40107	UniProtKB	Mutagenesis	285	285	.	.	.	Note=Decreases transport activity and GDP-mannose-binding. G->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855	
+P40107	UniProtKB	Mutagenesis	286	286	.	.	.	Note=In VIG4-1%3B increases drug sensitivity and decreases protein glycolysis. A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10570930,ECO:0000269|PubMed:11067855;Dbxref=PMID:10570930,PMID:11067855	
+P40107	UniProtKB	Mutagenesis	287	287	.	.	.	Note=Decreases transport activity and GDP-mannose-binding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855	
+P40107	UniProtKB	Mutagenesis	288	288	.	.	.	Note=Decreases transport activity and GDP-mannose-binding. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855	
+P40107	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Decreases transport activity and GDP-mannose-binding. K->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855	
+P40107	UniProtKB	Mutagenesis	291	291	.	.	.	Note=Decreases transport activity and GDP-mannose-binding. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855	
+##sequence-region P0CE11 1 249
+P0CE11	UniProtKB	Chain	1	249	.	.	.	ID=PRO_0000202628;Note=Probable GDP-mannose transporter 2	
+P0CE11	UniProtKB	Topological domain	1	15	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Topological domain	37	47	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Topological domain	69	84	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Topological domain	106	122	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Topological domain	144	159	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Transmembrane	160	180	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Topological domain	181	186	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Topological domain	208	211	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Transmembrane	212	232	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Topological domain	233	249	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Glycosylation	149	149	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE11	UniProtKB	Glycosylation	153	153	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43577 1 159
+P43577	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P43577	UniProtKB	Chain	2	159	.	.	.	ID=PRO_0000074552;Note=Glucosamine 6-phosphate N-acetyltransferase	
+P43577	UniProtKB	Domain	28	159	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+P43577	UniProtKB	Region	86	89	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591	
+P43577	UniProtKB	Region	98	100	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591	
+P43577	UniProtKB	Region	100	102	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1I12,ECO:0000269|PubMed:11278591;Dbxref=PMID:11278591	
+P43577	UniProtKB	Region	108	113	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1I12,ECO:0000269|PubMed:11278591;Dbxref=PMID:11278591	
+P43577	UniProtKB	Region	129	130	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591	
+P43577	UniProtKB	Region	143	145	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1I12,ECO:0000269|PubMed:11278591;Dbxref=PMID:11278591	
+P43577	UniProtKB	Binding site	28	28	.	.	.	Note=Substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591	
+P43577	UniProtKB	Binding site	134	134	.	.	.	Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591	
+P43577	UniProtKB	Binding site	158	158	.	.	.	Note=Substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591	
+P43577	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P43577	UniProtKB	Sequence conflict	112	159	.	.	.	Note=GKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVEMQIRK->ASS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43577	UniProtKB	Turn	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I21	
+P43577	UniProtKB	Beta strand	7	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Helix	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Helix	17	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Turn	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Helix	35	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Beta strand	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Beta strand	65	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Turn	70	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Beta strand	74	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Helix	88	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Beta strand	93	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Helix	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Helix	111	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Beta strand	129	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Helix	140	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+P43577	UniProtKB	Beta strand	149	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12	
+##sequence-region Q03554 1 138
+Q03554	UniProtKB	Chain	1	138	.	.	.	ID=PRO_0000218586;Note=Protein transport protein GOT1	
+Q03554	UniProtKB	Topological domain	1	8	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03554	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03554	UniProtKB	Topological domain	30	31	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03554	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03554	UniProtKB	Topological domain	53	67	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03554	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03554	UniProtKB	Topological domain	89	112	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03554	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03554	UniProtKB	Topological domain	134	138	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03554	UniProtKB	Mutagenesis	73	73	.	.	.	Note=In got1-1%3B loss of function. ER-Golgi transport defect when associated with lack of SFT2. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10406798;Dbxref=PMID:10406798	
+##sequence-region P10823 1 449
+P10823	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+P10823	UniProtKB	Chain	2	449	.	.	.	ID=PRO_0000203617;Note=Guanine nucleotide-binding protein alpha-2 subunit	
+P10823	UniProtKB	Nucleotide binding	130	137	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P10823	UniProtKB	Nucleotide binding	270	276	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P10823	UniProtKB	Nucleotide binding	296	300	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P10823	UniProtKB	Nucleotide binding	365	368	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P10823	UniProtKB	Metal binding	137	137	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P10823	UniProtKB	Metal binding	276	276	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P10823	UniProtKB	Binding site	420	420	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P10823	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250	
+P10823	UniProtKB	Lipidation	4	4	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250	
+P10823	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Abolishes both palmitoylation and N-myristoylation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250	
+P10823	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Abolishes palmitoylation but not N-myristoylation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250	
+P10823	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Abolishes both palmitoylation and N-myristoylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250	
+P10823	UniProtKB	Mutagenesis	132	132	.	.	.	Note=Locks GPA2 in its activated GTP-bound form and abrogates the negative control by RGS2. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10523302,ECO:0000269|PubMed:12150916;Dbxref=PMID:10523302,PMID:12150916	
+P10823	UniProtKB	Mutagenesis	299	299	.	.	.	Note=Dominant negativ allele unable to undergo the GTP-induced conformational change. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12150916,ECO:0000269|PubMed:16030250;Dbxref=PMID:12150916,PMID:16030250	
+P10823	UniProtKB	Mutagenesis	300	300	.	.	.	Note=Dominant active allele that abolishes intrinsic GTPase activity. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12150916;Dbxref=PMID:12150916	
+P10823	UniProtKB	Sequence conflict	375	375	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08886 1 897
+Q08886	UniProtKB	Chain	1	897	.	.	.	ID=PRO_0000239649;Note=Guanine nucleotide-binding protein subunit beta 1	
+Q08886	UniProtKB	Repeat	304	352	.	.	.	Note=Kelch 1	
+Q08886	UniProtKB	Repeat	390	438	.	.	.	Note=Kelch 2	
+Q08886	UniProtKB	Repeat	543	589	.	.	.	Note=Kelch 3	
+Q08886	UniProtKB	Repeat	715	761	.	.	.	Note=Kelch 4	
+Q08886	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08886	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P40066 1 365
+P40066	UniProtKB	Chain	1	365	.	.	.	ID=PRO_0000051007;Note=Nucleoporin GLE2	
+P40066	UniProtKB	Repeat	34	74	.	.	.	Note=WD 1	
+P40066	UniProtKB	Repeat	78	117	.	.	.	Note=WD 2	
+P40066	UniProtKB	Repeat	119	162	.	.	.	Note=WD 3	
+P40066	UniProtKB	Repeat	267	306	.	.	.	Note=WD 4	
+##sequence-region Q05584 1 274
+Q05584	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000192346;Note=Hydroxyacylglutathione hydrolase%2C cytoplasmic isozyme	
+Q05584	UniProtKB	Region	188	190	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q05584	UniProtKB	Region	268	271	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q05584	UniProtKB	Metal binding	59	59	.	.	.	Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q05584	UniProtKB	Metal binding	61	61	.	.	.	Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q05584	UniProtKB	Metal binding	63	63	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q05584	UniProtKB	Metal binding	64	64	.	.	.	Note=Zinc 2%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q05584	UniProtKB	Metal binding	121	121	.	.	.	Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q05584	UniProtKB	Metal binding	144	144	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q05584	UniProtKB	Metal binding	144	144	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q05584	UniProtKB	Metal binding	188	188	.	.	.	Note=Zinc 2%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q05584	UniProtKB	Binding site	153	153	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05584	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q05584	UniProtKB	Sequence conflict	222	222	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38682 1 493
+P38682	UniProtKB	Chain	1	493	.	.	.	ID=PRO_0000074225;Note=ADP-ribosylation factor GTPase-activating protein GLO3	
+P38682	UniProtKB	Domain	16	137	.	.	.	Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+P38682	UniProtKB	Zinc finger	31	54	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+P38682	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38682	UniProtKB	Modified residue	306	306	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38682	UniProtKB	Modified residue	389	389	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38682	UniProtKB	Modified residue	398	398	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38682	UniProtKB	Sequence conflict	222	222	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38682	UniProtKB	Sequence conflict	406	493	.	.	.	Note=EAHDKLKTFDNATSISSSSYFGEDKEVDEFGNPINSSGSGAGNFDGRNSNNGFIDFNASADDELQMLRDVVEQGAEKLGSYLRDYLRK->GSA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32190 1 709
+P32190	UniProtKB	Chain	1	709	.	.	.	ID=PRO_0000059542;Note=Glycerol kinase	
+P32190	UniProtKB	Nucleotide binding	584	588	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32190	UniProtKB	Binding site	56	56	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32190	UniProtKB	Binding site	60	60	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32190	UniProtKB	Binding site	201	201	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32190	UniProtKB	Binding site	258	258	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32190	UniProtKB	Binding site	386	386	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32190	UniProtKB	Binding site	408	408	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32190	UniProtKB	Binding site	463	463	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12438 1 231
+Q12438	UniProtKB	Signal peptide	1	29	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12438	UniProtKB	Chain	30	231	.	.	.	ID=PRO_0000042988;Note=Monothiol glutaredoxin-6	
+Q12438	UniProtKB	Domain	116	219	.	.	.	Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686	
+Q12438	UniProtKB	Metal binding	136	136	.	.	.	Note=Iron-sulfur (2Fe-2S)%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12438	UniProtKB	Helix	115	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N	
+Q12438	UniProtKB	Beta strand	127	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N	
+Q12438	UniProtKB	Helix	137	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N	
+Q12438	UniProtKB	Beta strand	150	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N	
+Q12438	UniProtKB	Beta strand	157	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N	
+Q12438	UniProtKB	Helix	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N	
+Q12438	UniProtKB	Helix	167	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N	
+Q12438	UniProtKB	Beta strand	185	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N	
+Q12438	UniProtKB	Helix	196	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N	
+Q12438	UniProtKB	Helix	208	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N	
+Q12438	UniProtKB	Beta strand	221	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N	
+##sequence-region P48813 1 663
+P48813	UniProtKB	Chain	1	663	.	.	.	ID=PRO_0000054152;Note=High-affinity glutamine permease	
+P48813	UniProtKB	Topological domain	1	154	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	155	175	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	176	177	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	178	198	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	199	219	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	220	240	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	241	264	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	265	285	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	286	289	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	290	310	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	311	342	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	343	363	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	364	381	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	382	402	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	403	432	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	433	453	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	454	481	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	482	502	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	503	506	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	507	527	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	528	560	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	561	581	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	582	590	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Transmembrane	591	611	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Topological domain	612	663	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48813	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48813	UniProtKB	Modified residue	113	113	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48813	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P48813	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P48813	UniProtKB	Cross-link	34	34	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P48813	UniProtKB	Cross-link	39	39	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P48813	UniProtKB	Cross-link	41	41	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P48813	UniProtKB	Cross-link	61	61	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P48813	UniProtKB	Cross-link	132	132	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P48813	UniProtKB	Sequence conflict	319	319	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53839 1 350
+P53839	UniProtKB	Chain	1	350	.	.	.	ID=PRO_0000076040;Note=Glyoxylate reductase 1	
+P53839	UniProtKB	Nucleotide binding	173	174	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53839	UniProtKB	Nucleotide binding	252	254	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53839	UniProtKB	Nucleotide binding	301	304	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53839	UniProtKB	Active site	254	254	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53839	UniProtKB	Active site	283	283	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53839	UniProtKB	Active site	301	301	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53839	UniProtKB	Binding site	278	278	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53839	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q00055 1 391
+Q00055	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.9	
+Q00055	UniProtKB	Chain	2	391	.	.	.	ID=PRO_0000138100;Note=Glycerol-3-phosphate dehydrogenase [NAD(+)] 1	
+Q00055	UniProtKB	Nucleotide binding	41	46	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00055	UniProtKB	Region	310	311	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00055	UniProtKB	Active site	245	245	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00055	UniProtKB	Binding site	129	129	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00055	UniProtKB	Binding site	152	152	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00055	UniProtKB	Binding site	152	152	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00055	UniProtKB	Binding site	185	185	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00055	UniProtKB	Binding site	310	310	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00055	UniProtKB	Binding site	339	339	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00055	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.9	
+Q00055	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q00055	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+Q00055	UniProtKB	Natural variant	16	16	.	.	.	Note=In strain: WFB. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+Q00055	UniProtKB	Natural variant	143	143	.	.	.	Note=In strain: WFB. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+Q00055	UniProtKB	Natural variant	164	164	.	.	.	Note=In strain: WFB. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+Q00055	UniProtKB	Natural variant	183	183	.	.	.	Note=In strain: WFB. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+Q00055	UniProtKB	Natural variant	225	225	.	.	.	Note=In strain: WFB. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+Q00055	UniProtKB	Natural variant	256	256	.	.	.	Note=In strain: WFB. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+Q00055	UniProtKB	Sequence conflict	103	107	.	.	.	Note=DNLVA->TIWLL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00055	UniProtKB	Beta strand	35	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	44	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Turn	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Beta strand	64	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Beta strand	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	82	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Turn	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Beta strand	103	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	111	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Beta strand	119	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	130	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Turn	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Beta strand	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Beta strand	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Beta strand	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	164	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Beta strand	175	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	185	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Beta strand	194	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Beta strand	209	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	215	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Beta strand	227	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	235	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	261	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	289	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Turn	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	299	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	310	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	325	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	340	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	361	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+Q00055	UniProtKB	Helix	379	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW	
+##sequence-region Q06636 1 219
+Q06636	UniProtKB	Chain	1	219	.	.	.	ID=PRO_0000191771;Note=Glycosylphosphatidylinositol anchor biosynthesis protein 11	
+Q06636	UniProtKB	Topological domain	1	45	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Topological domain	67	67	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Topological domain	89	108	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Topological domain	130	135	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Topological domain	157	170	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Topological domain	192	198	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Transmembrane	199	217	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Topological domain	218	219	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06636	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P47088 1 403
+P47088	UniProtKB	Chain	1	403	.	.	.	ID=PRO_0000203084;Note=GPI mannosyltransferase 1	
+P47088	UniProtKB	Topological domain	1	4	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Transmembrane	5	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Topological domain	26	78	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Transmembrane	79	99	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Topological domain	100	110	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Topological domain	132	132	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Transmembrane	133	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Topological domain	150	160	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Topological domain	182	193	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Transmembrane	194	214	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Topological domain	215	266	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Topological domain	288	310	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Transmembrane	311	331	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Topological domain	332	334	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Transmembrane	335	355	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Topological domain	356	361	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Transmembrane	362	382	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47088	UniProtKB	Topological domain	383	403	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04082 1 140
+Q04082	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000240380;Note=Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19	
+Q04082	UniProtKB	Topological domain	1	12	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16278447;Dbxref=PMID:16278447	
+Q04082	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04082	UniProtKB	Topological domain	34	52	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16278447;Dbxref=PMID:16278447	
+Q04082	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04082	UniProtKB	Topological domain	74	140	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16278447;Dbxref=PMID:16278447	
+##sequence-region P32363 1 452
+P32363	UniProtKB	Chain	1	452	.	.	.	ID=PRO_0000080325;Note=Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit	
+P32363	UniProtKB	Transmembrane	407	427	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32363	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Severe growth defect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279	
+P32363	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Reduces the transferase reaction 12-fold. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279	
+P32363	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Lethal. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279	
+P32363	UniProtKB	Mutagenesis	297	297	.	.	.	Note=Lethal. E->A%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279	
+P32363	UniProtKB	Mutagenesis	297	297	.	.	.	Note=No transferase activity. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279	
+P32363	UniProtKB	Mutagenesis	301	301	.	.	.	Note=Reduces the transferase reaction 5-fold. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279	
+##sequence-region Q08726 1 347
+Q08726	UniProtKB	Chain	1	347	.	.	.	ID=PRO_0000245255;Note=GPN-loop GTPase 2	
+Q08726	UniProtKB	Nucleotide binding	12	17	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+Q08726	UniProtKB	Nucleotide binding	175	178	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+Q08726	UniProtKB	Motif	69	71	.	.	.	Note=Gly-Pro-Asn (GPN)-loop%3B involved in dimer interface;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+Q08726	UniProtKB	Site	71	71	.	.	.	Note=Stabilizes the phosphate intermediate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+Q08726	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Impairs heterodimer formation with NPA3/GPN1. E->K%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23324351;Dbxref=PMID:23324351	
+##sequence-region P40581 1 163
+P40581	UniProtKB	Chain	1	163	.	.	.	ID=PRO_0000066643;Note=Glutathione peroxidase-like peroxiredoxin HYR1	
+P40581	UniProtKB	Active site	36	36	.	.	.	Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:17720812,ECO:0000305|PubMed:18767166;Dbxref=PMID:17720812,PMID:18767166	
+P40581	UniProtKB	Disulfide bond	36	82	.	.	.	Note=Redox-active;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:18767166;Dbxref=PMID:18767166	
+P40581	UniProtKB	Disulfide bond	36	36	.	.	.	Note=Interchain (with C-598 in YAP1)%3B transient;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12437921,ECO:0000269|PubMed:17720812;Dbxref=PMID:12437921,PMID:17720812	
+P40581	UniProtKB	Mutagenesis	82	82	.	.	.	Note=Loss of enzyme activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18767166;Dbxref=PMID:18767166	
+P40581	UniProtKB	Helix	3	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Helix	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Beta strand	26	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Helix	39	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Helix	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Beta strand	57	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Beta strand	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Helix	105	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Beta strand	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Beta strand	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Beta strand	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Beta strand	138	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Helix	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+P40581	UniProtKB	Helix	152	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI	
+##sequence-region P33892 1 2672
+P33892	UniProtKB	Chain	1	2672	.	.	.	ID=PRO_0000087444;Note=eIF-2-alpha kinase activator GCN1	
+P33892	UniProtKB	Repeat	5	42	.	.	.	Note=HEAT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	79	117	.	.	.	Note=HEAT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	174	211	.	.	.	Note=HEAT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	227	267	.	.	.	Note=HEAT 4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	329	366	.	.	.	Note=HEAT 5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	372	410	.	.	.	Note=HEAT 6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	509	549	.	.	.	Note=HEAT 7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	611	648	.	.	.	Note=HEAT 8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	706	745	.	.	.	Note=HEAT 9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	902	932	.	.	.	Note=HEAT 10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	933	970	.	.	.	Note=HEAT 11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	975	994	.	.	.	Note=HEAT 12%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	995	1030	.	.	.	Note=HEAT 13%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1031	1067	.	.	.	Note=HEAT 14;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1099	1138	.	.	.	Note=HEAT 15;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1185	1224	.	.	.	Note=HEAT 16;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1243	1281	.	.	.	Note=HEAT 17;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1284	1321	.	.	.	Note=HEAT 18;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1363	1401	.	.	.	Note=HEAT 19;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1405	1442	.	.	.	Note=HEAT 20;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1444	1480	.	.	.	Note=HEAT 21;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1484	1521	.	.	.	Note=HEAT 22;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1523	1559	.	.	.	Note=HEAT 23;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1561	1598	.	.	.	Note=HEAT 24;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1603	1640	.	.	.	Note=HEAT 25;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1641	1679	.	.	.	Note=HEAT 26;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1681	1717	.	.	.	Note=HEAT 27;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1721	1758	.	.	.	Note=HEAT 28;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1760	1796	.	.	.	Note=HEAT 29;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1825	1862	.	.	.	Note=HEAT 30;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1863	1903	.	.	.	Note=HEAT 31;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1905	1942	.	.	.	Note=HEAT 32;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1947	1984	.	.	.	Note=HEAT 33;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	1985	2024	.	.	.	Note=HEAT 34;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	2026	2055	.	.	.	Note=HEAT 35;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	2057	2095	.	.	.	Note=HEAT 36;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	2097	2134	.	.	.	Note=HEAT 37;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	2138	2175	.	.	.	Note=HEAT 38;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	2206	2243	.	.	.	Note=HEAT 39;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	2250	2286	.	.	.	Note=HEAT 40;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	2290	2328	.	.	.	Note=HEAT 41;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	2347	2384	.	.	.	Note=HEAT 42;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	2392	2429	.	.	.	Note=HEAT 43;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	2450	2487	.	.	.	Note=HEAT 44;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Repeat	2506	2546	.	.	.	Note=HEAT 45;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33892	UniProtKB	Region	1330	1641	.	.	.	Note=EF3-like region;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9234705;Dbxref=PMID:9234705	
+P33892	UniProtKB	Mutagenesis	757	758	.	.	.	Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-762%3B A-765%3B A-775%3B 777-A-A-778%3B 782-A-A-783%3B 786-A-A-787 and A-790. KK->AA%2CDD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004	
+P33892	UniProtKB	Mutagenesis	762	762	.	.	.	Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-765%3B A-775%3B 777-A-A-778%3B 782-A-A-783%3B 786-A-A-787 and A-790. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004	
+P33892	UniProtKB	Mutagenesis	765	765	.	.	.	Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-775%3B 777-A-A-778%3B 782-A-A-783%3B 786-A-A-787 and A-790. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004	
+P33892	UniProtKB	Mutagenesis	775	775	.	.	.	Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-765%3B 777-A-A-778%3B 782-A-A-783%3B 786-A-A-787 and A-790. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004	
+P33892	UniProtKB	Mutagenesis	777	778	.	.	.	Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-765%3B A-775%3B 782-A-A-783%3B 786-A-A-787 and A-790. RK->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004	
+P33892	UniProtKB	Mutagenesis	782	783	.	.	.	Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-765%3B A-775%3B 777-A-A-778%3B 786-A-A-787 and A-790. KK->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004	
+P33892	UniProtKB	Mutagenesis	786	787	.	.	.	Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-765%3B A-775%3B 777-A-A-778%3B 782-A-A-783 and A-790. KK->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004	
+P33892	UniProtKB	Mutagenesis	790	790	.	.	.	Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-765%3B A-775%3B 777-A-A-778%3B 782-A-A-783 and 786-A-A-787. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004	
+P33892	UniProtKB	Mutagenesis	1444	1444	.	.	.	Note=Decreases interaction with GCN20 and polysomal association. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234705;Dbxref=PMID:9234705	
+P33892	UniProtKB	Mutagenesis	1458	1458	.	.	.	Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20 and strongly impairs eIF-2-alpha phosphorylation%3B when associated with 1461-A--A-1465. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15722345;Dbxref=PMID:15722345	
+P33892	UniProtKB	Mutagenesis	1461	1465	.	.	.	Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20 and strongly impairs eIF-2-alpha phosphorylation%3B when associated with A-1458. WRTKR->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15722345;Dbxref=PMID:15722345	
+P33892	UniProtKB	Mutagenesis	2259	2259	.	.	.	Note=Decreases interaction with GCN2 and YIH1 but not with GCN20 and ribosomes. R->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11101534,ECO:0000269|PubMed:15126500,ECO:0000269|PubMed:21239490;Dbxref=PMID:11101534,PMID:15126500,PMID:21239490	
+P33892	UniProtKB	Mutagenesis	2291	2291	.	.	.	Note=Does not interact with GCN2%2C impairs eIF-2-alpha phosphorylation and fails to derepress GCN4 translation in amino acid-starved cells. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350982;Dbxref=PMID:11350982	
+P33892	UniProtKB	Mutagenesis	2304	2304	.	.	.	Note=Does not interact with GCN2. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350982;Dbxref=PMID:11350982	
+P33892	UniProtKB	Mutagenesis	2353	2353	.	.	.	Note=Does not interact with GCN2. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350982;Dbxref=PMID:11350982	
+##sequence-region P49095 1 1034
+P49095	UniProtKB	Modified residue	773	773	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P37020 1 779
+P37020	UniProtKB	Chain	1	779	.	.	.	ID=PRO_0000094472;Note=Anion/proton exchange transporter GEF1	
+P37020	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000419270;Note=GEF1 N-terminal	
+P37020	UniProtKB	Chain	137	779	.	.	.	ID=PRO_0000419271;Note=GEF1 C-terminal	
+P37020	UniProtKB	Topological domain	1	75	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	97	154	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	155	175	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	176	177	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	178	198	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	199	203	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	225	264	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	265	285	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	286	296	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	297	319	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	320	336	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	337	357	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	358	369	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	370	390	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	391	436	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	437	457	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	458	465	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	466	486	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	487	500	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	501	523	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	524	529	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Transmembrane	530	552	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Topological domain	553	779	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37020	UniProtKB	Domain	591	659	.	.	.	Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P37020	UniProtKB	Domain	688	744	.	.	.	Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P37020	UniProtKB	Site	136	137	.	.	.	Note=Cleavage%3B by KEX2	
+P37020	UniProtKB	Site	230	230	.	.	.	Note=Mediates proton transfer from the outer aqueous phase to the interior of the protein%3B involved in linking H(+) and Cl(-) transport;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P37020	UniProtKB	Site	287	287	.	.	.	Note=Mediates proton transfer from the protein to the inner aqueous phase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P37020	UniProtKB	Sequence conflict	13	13	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37020	UniProtKB	Sequence conflict	207	207	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37020	UniProtKB	Sequence conflict	257	257	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37020	UniProtKB	Sequence conflict	262	262	.	.	.	Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37020	UniProtKB	Sequence conflict	497	497	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38812 1 185
+P38812	UniProtKB	Chain	1	185	.	.	.	ID=PRO_0000202908;Note=Phosphatidylglycerophosphatase GEP4%2C mitochondrial	
+P38812	UniProtKB	Motif	45	49	.	.	.	Note=Phosphoryl acceptor	
+P38812	UniProtKB	Mutagenesis	45	45	.	.	.	Note=Abolishes phosphatase activity and impairs cardiolipin biosynthesis. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485265;Dbxref=PMID:20485265	
+P38812	UniProtKB	Mutagenesis	47	47	.	.	.	Note=Abolishes phosphatase activity and impairs cardiolipin biosynthesis. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485265;Dbxref=PMID:20485265	
+##sequence-region Q12125 1 312
+Q12125	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000228107;Note=Golgi to ER traffic protein 4	
+Q12125	UniProtKB	Helix	13	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	29	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	49	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	69	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	92	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	112	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	134	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	150	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	162	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	184	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	204	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Beta strand	226	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Beta strand	234	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	243	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	260	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	271	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12125	UniProtKB	Helix	278	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+##sequence-region P36173 1 615
+P36173	UniProtKB	Chain	1	615	.	.	.	ID=PRO_0000203231;Note=Glutathione exchanger 2	
+P36173	UniProtKB	Topological domain	1	58	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	80	120	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	142	152	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	174	216	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	238	275	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	276	296	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	297	307	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	308	328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	329	343	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	344	364	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	365	383	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	384	404	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	405	407	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	408	428	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	429	440	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	441	461	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	462	471	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	472	492	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	493	548	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Transmembrane	549	569	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36173	UniProtKB	Topological domain	570	615	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06336 1 557
+Q06336	UniProtKB	Chain	1	557	.	.	.	ID=PRO_0000212686;Note=ADP-ribosylation factor-binding protein GGA1	
+Q06336	UniProtKB	Domain	29	165	.	.	.	Note=VHS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00218	
+Q06336	UniProtKB	Domain	192	317	.	.	.	Note=GAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00373	
+Q06336	UniProtKB	Domain	440	556	.	.	.	Note=GAE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00093	
+Q06336	UniProtKB	Modified residue	348	348	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06336	UniProtKB	Modified residue	353	353	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06336	UniProtKB	Modified residue	357	357	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q06336	UniProtKB	Modified residue	378	378	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06336	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06336	UniProtKB	Beta strand	445	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2	
+Q06336	UniProtKB	Beta strand	451	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2	
+Q06336	UniProtKB	Beta strand	463	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2	
+Q06336	UniProtKB	Beta strand	477	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2	
+Q06336	UniProtKB	Beta strand	481	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2	
+Q06336	UniProtKB	Beta strand	495	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2	
+Q06336	UniProtKB	Beta strand	510	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2	
+Q06336	UniProtKB	Helix	523	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2	
+Q06336	UniProtKB	Beta strand	531	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2	
+Q06336	UniProtKB	Beta strand	544	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2	
+##sequence-region P38817 1 585
+P38817	UniProtKB	Chain	1	585	.	.	.	ID=PRO_0000212687;Note=ADP-ribosylation factor-binding protein GGA2	
+P38817	UniProtKB	Domain	33	169	.	.	.	Note=VHS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00218	
+P38817	UniProtKB	Domain	196	321	.	.	.	Note=GAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00373	
+P38817	UniProtKB	Domain	466	581	.	.	.	Note=GAE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00093	
+P38817	UniProtKB	Cross-link	180	180	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38817	UniProtKB	Cross-link	287	287	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38817	UniProtKB	Mutagenesis	560	560	.	.	.	Note=Reduced binding to ENT3. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220	
+P38817	UniProtKB	Mutagenesis	563	563	.	.	.	Note=Reduced binding to ENT3 and ENT5. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220	
+P38817	UniProtKB	Mutagenesis	564	564	.	.	.	Note=Reduced binding to ENT3 and ENT5. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220	
+P38817	UniProtKB	Beta strand	472	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM	
+P38817	UniProtKB	Beta strand	479	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM	
+P38817	UniProtKB	Beta strand	491	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM	
+P38817	UniProtKB	Beta strand	495	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM	
+P38817	UniProtKB	Beta strand	505	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM	
+P38817	UniProtKB	Beta strand	509	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM	
+P38817	UniProtKB	Beta strand	522	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM	
+P38817	UniProtKB	Beta strand	542	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM	
+P38817	UniProtKB	Beta strand	560	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM	
+P38817	UniProtKB	Beta strand	572	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM	
+##sequence-region P25569 1 745
+P25569	UniProtKB	Chain	1	745	.	.	.	ID=PRO_0000051006;Note=Glucose-induced degradation protein 7	
+P25569	UniProtKB	Repeat	167	209	.	.	.	Note=WD 1	
+P25569	UniProtKB	Repeat	322	365	.	.	.	Note=WD 2	
+P25569	UniProtKB	Repeat	369	408	.	.	.	Note=WD 3	
+P25569	UniProtKB	Repeat	540	579	.	.	.	Note=WD 4	
+P25569	UniProtKB	Repeat	613	652	.	.	.	Note=WD 5	
+P25569	UniProtKB	Repeat	657	696	.	.	.	Note=WD 6	
+P25569	UniProtKB	Repeat	710	745	.	.	.	Note=WD 7	
+##sequence-region P32642 1 244
+P32642	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000102250;Note=Monothiol glutaredoxin-4	
+P32642	UniProtKB	Domain	3	110	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P32642	UniProtKB	Domain	146	244	.	.	.	Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686	
+P32642	UniProtKB	Region	225	226	.	.	.	Note=Glutathione binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32642	UniProtKB	Metal binding	171	171	.	.	.	Note=Iron-sulfur (2Fe-2S)%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32642	UniProtKB	Binding site	163	163	.	.	.	Note=Glutathione;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32642	UniProtKB	Binding site	200	200	.	.	.	Note=Glutathione;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32642	UniProtKB	Binding site	212	212	.	.	.	Note=Glutathione%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38138 1 954
+P38138	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38138	UniProtKB	Chain	23	954	.	.	.	ID=PRO_0000185370;Note=Glucosidase 2 subunit alpha	
+P38138	UniProtKB	Active site	537	537	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10066	
+P38138	UniProtKB	Active site	540	540	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38138	UniProtKB	Active site	614	614	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38138	UniProtKB	Glycosylation	114	114	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38138	UniProtKB	Glycosylation	126	126	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38138	UniProtKB	Glycosylation	142	142	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38138	UniProtKB	Glycosylation	173	173	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38138	UniProtKB	Glycosylation	345	345	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38138	UniProtKB	Glycosylation	783	783	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38138	UniProtKB	Glycosylation	791	791	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38138	UniProtKB	Glycosylation	867	867	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38138	UniProtKB	Glycosylation	880	880	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38138	UniProtKB	Glycosylation	907	907	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38138	UniProtKB	Glycosylation	941	941	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04924 1 702
+Q04924	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04924	UniProtKB	Chain	21	702	.	.	.	ID=PRO_0000245572;Note=Glucosidase 2 subunit beta	
+Q04924	UniProtKB	Coiled coil	163	228	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04924	UniProtKB	Coiled coil	478	517	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04924	UniProtKB	Glycosylation	145	145	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04924	UniProtKB	Glycosylation	240	240	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04924	UniProtKB	Glycosylation	358	358	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04924	UniProtKB	Glycosylation	520	520	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04924	UniProtKB	Glycosylation	525	525	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04924	UniProtKB	Glycosylation	688	688	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04924	UniProtKB	Glycosylation	699	699	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P48015 1 400
+P48015	UniProtKB	Binding site	221	221	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48015	UniProtKB	Binding site	250	250	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48015	UniProtKB	Binding site	397	397	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48015	UniProtKB	Sequence conflict	122	122	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06625 1 1536
+Q06625	UniProtKB	Chain	1	1536	.	.	.	ID=PRO_0000087452;Note=Glycogen debranching enzyme	
+Q06625	UniProtKB	Active site	535	535	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06625	UniProtKB	Active site	538	538	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06625	UniProtKB	Active site	670	670	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06625	UniProtKB	Sequence conflict	368	368	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06625	UniProtKB	Sequence conflict	536	536	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06625	UniProtKB	Sequence conflict	774	774	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06625	UniProtKB	Sequence conflict	1180	1180	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06625	UniProtKB	Sequence conflict	1289	1289	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06625	UniProtKB	Sequence conflict	1489	1489	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39958 1 451
+P39958	UniProtKB	Chain	1	451	.	.	.	ID=PRO_0000056684;Note=Rab GDP-dissociation inhibitor	
+P39958	UniProtKB	Region	106	112	.	.	.	Note=Interaction with YPT1	
+P39958	UniProtKB	Region	234	259	.	.	.	Note=Interaction with YPT1	
+P39958	UniProtKB	Beta strand	11	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	19	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	40	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	53	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	67	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	94	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	116	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	123	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	131	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ	
+P39958	UniProtKB	Helix	142	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Turn	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	176	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	187	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	211	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	231	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	241	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	265	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Turn	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	275	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	283	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	294	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	301	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPI	
+P39958	UniProtKB	Beta strand	326	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	343	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	350	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	360	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	373	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	378	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	382	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	388	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Turn	405	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	408	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Beta strand	419	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+P39958	UniProtKB	Helix	422	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG	
+##sequence-region Q12434 1 202
+Q12434	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12434	UniProtKB	Chain	2	202	.	.	.	ID=PRO_0000219022;Note=Rho GDP-dissociation inhibitor	
+Q12434	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12434	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+Q12434	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P39722 1 662
+P39722	UniProtKB	Chain	1	662	.	.	.	ID=PRO_0000202422;Note=Mitochondrial Rho GTPase 1	
+P39722	UniProtKB	Topological domain	1	634	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39722	UniProtKB	Transmembrane	635	655	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39722	UniProtKB	Topological domain	656	662	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39722	UniProtKB	Domain	1	140	.	.	.	Note=Miro 1	
+P39722	UniProtKB	Domain	201	236	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P39722	UniProtKB	Domain	330	365	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P39722	UniProtKB	Domain	442	662	.	.	.	Note=Miro 2	
+P39722	UniProtKB	Nucleotide binding	12	19	.	.	.	Note=GTP 1;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39722	UniProtKB	Nucleotide binding	62	64	.	.	.	Note=GTP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39722	UniProtKB	Nucleotide binding	116	119	.	.	.	Note=GTP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39722	UniProtKB	Calcium binding	214	225	.	.	.	Note=1;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39722	UniProtKB	Calcium binding	343	354	.	.	.	Note=2;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39722	UniProtKB	Nucleotide binding	455	462	.	.	.	Note=GTP 2;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39722	UniProtKB	Nucleotide binding	491	495	.	.	.	Note=GTP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39722	UniProtKB	Nucleotide binding	560	563	.	.	.	Note=GTP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39722	UniProtKB	Mutagenesis	18	18	.	.	.	Note=Loss of function. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738	
+P39722	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Loss of function. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738	
+P39722	UniProtKB	Mutagenesis	33	33	.	.	.	Note=No effect. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738	
+P39722	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Induces collapsed%2C globular or grape-like mitochondria%3B when associated with A-354. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738	
+P39722	UniProtKB	Mutagenesis	354	354	.	.	.	Note=Induces collapsed%2C globular or grape-like mitochondria%3B when associated with A-225. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738	
+P39722	UniProtKB	Mutagenesis	461	461	.	.	.	Note=Induces collapsed%2C globular or grape-like mitochondria. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738	
+P39722	UniProtKB	Mutagenesis	462	462	.	.	.	Note=Induces collapsed%2C globular or grape-like mitochondria. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738	
+P39722	UniProtKB	Mutagenesis	480	480	.	.	.	Note=Induces collapsed%2C globular or grape-like mitochondria. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738	
+##sequence-region P38785 1 314
+P38785	UniProtKB	Chain	1	314	.	.	.	ID=PRO_0000212659;Note=GTPase-interacting component 1	
+P38785	UniProtKB	Domain	126	139	.	.	.	Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057	
+##sequence-region Q12418 1 502
+Q12418	UniProtKB	Chain	1	502	.	.	.	ID=PRO_0000087497;Note=Protein GIS3	
+##sequence-region P41818 1 229
+P41818	UniProtKB	Chain	1	229	.	.	.	ID=PRO_0000071517;Note=Protein GLC8	
+P41818	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198	
+P41818	UniProtKB	Modified residue	118	118	.	.	.	Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12407105;Dbxref=PMID:12407105	
+P41818	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P41818	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P47011 1 380
+P47011	UniProtKB	Chain	1	380	.	.	.	ID=PRO_0000215182;Note=Glycogenin-2	
+P47011	UniProtKB	Glycosylation	230	230	.	.	.	Note=O-linked (Glc...) tyrosine	
+P47011	UniProtKB	Glycosylation	232	232	.	.	.	Note=O-linked (Glc...) tyrosine	
+P47011	UniProtKB	Glycosylation	367	367	.	.	.	Note=O-linked (Glc...) tyrosine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47011	UniProtKB	Mutagenesis	230	230	.	.	.	Note=Eliminates glycogen accumulation%3B when associated with F-232 and F-367. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8900126;Dbxref=PMID:8900126	
+P47011	UniProtKB	Mutagenesis	232	232	.	.	.	Note=Eliminates glycogen accumulation%3B when associated with F-230 and F-367. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8900126;Dbxref=PMID:8900126	
+P47011	UniProtKB	Mutagenesis	367	367	.	.	.	Note=Eliminates glycogen accumulation%3B when associated with F-230 and F-232. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8900126;Dbxref=PMID:8900126	
+P47011	UniProtKB	Sequence conflict	241	241	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38263 1 362
+P38263	UniProtKB	Chain	1	362	.	.	.	ID=PRO_0000065826;Note=Vacuolar import and degradation protein 24	
+P38263	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38263	UniProtKB	Cross-link	20	20	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P40208 1 455
+P40208	UniProtKB	Chain	1	455	.	.	.	ID=PRO_0000087486;Note=Glucose-induced degradation protein 8	
+P40208	UniProtKB	Domain	85	116	.	.	.	Note=LisH	
+P40208	UniProtKB	Domain	130	213	.	.	.	Note=CTLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00058	
+P40208	UniProtKB	Compositional bias	179	186	.	.	.	Note=Poly-Gln	
+##sequence-region Q12263 1 1142
+Q12263	UniProtKB	Chain	1	1142	.	.	.	ID=PRO_0000085964;Note=Serine/threonine-protein kinase GIN4	
+Q12263	UniProtKB	Domain	19	289	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12263	UniProtKB	Nucleotide binding	25	33	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12263	UniProtKB	Active site	156	156	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q12263	UniProtKB	Binding site	48	48	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12263	UniProtKB	Modified residue	406	406	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12263	UniProtKB	Modified residue	465	465	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12263	UniProtKB	Modified residue	471	471	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12263	UniProtKB	Modified residue	617	617	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12263	UniProtKB	Modified residue	689	689	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q12263	UniProtKB	Modified residue	719	719	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12263	UniProtKB	Modified residue	805	805	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q12263	UniProtKB	Modified residue	807	807	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q12263	UniProtKB	Modified residue	883	883	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12263	UniProtKB	Modified residue	884	884	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12263	UniProtKB	Modified residue	930	930	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P32288 1 370
+P32288	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:2891705,ECO:0000269|PubMed:9298649;Dbxref=PMID:15665377,PMID:22814378,PMID:2891705,PMID:9298649	
+P32288	UniProtKB	Chain	2	370	.	.	.	ID=PRO_0000153166;Note=Glutamine synthetase	
+P32288	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:15665377,PMID:22814378,PMID:9298649	
+P32288	UniProtKB	Modified residue	5	5	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P32288	UniProtKB	Cross-link	283	283	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32288	UniProtKB	Cross-link	324	324	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32288	UniProtKB	Cross-link	363	363	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32288	UniProtKB	Sequence conflict	165	165	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32288	UniProtKB	Sequence conflict	172	172	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32288	UniProtKB	Sequence conflict	251	251	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32288	UniProtKB	Sequence conflict	251	251	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32288	UniProtKB	Sequence conflict	264	264	.	.	.	Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32288	UniProtKB	Sequence conflict	264	264	.	.	.	Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32288	UniProtKB	Beta strand	24	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	37	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Helix	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Turn	61	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	74	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Turn	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	92	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Helix	111	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Helix	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	127	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Turn	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Helix	170	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	187	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	198	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Helix	209	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Turn	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	232	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	239	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	248	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Helix	256	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Helix	264	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Helix	278	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Helix	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	307	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	314	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Helix	320	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Beta strand	330	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Helix	341	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+P32288	UniProtKB	Turn	361	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY	
+##sequence-region Q12320 1 285
+Q12320	UniProtKB	Metal binding	69	69	.	.	.	Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q12320	UniProtKB	Metal binding	71	71	.	.	.	Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q12320	UniProtKB	Metal binding	73	73	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q12320	UniProtKB	Metal binding	74	74	.	.	.	Note=Zinc 2%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q12320	UniProtKB	Metal binding	131	131	.	.	.	Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q12320	UniProtKB	Metal binding	154	154	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q12320	UniProtKB	Metal binding	154	154	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+Q12320	UniProtKB	Metal binding	198	198	.	.	.	Note=Zinc 2%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775	
+##sequence-region P25373 1 110
+P25373	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000141613;Note=Glutaredoxin-1	
+P25373	UniProtKB	Domain	7	110	.	.	.	Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686	
+P25373	UniProtKB	Region	24	29	.	.	.	Note=Glutathione binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17327665,ECO:0000269|PubMed:18473363;Dbxref=PMID:17327665,PMID:18473363	
+P25373	UniProtKB	Region	88	89	.	.	.	Note=Glutathione binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17327665,ECO:0000269|PubMed:18473363;Dbxref=PMID:17327665,PMID:18473363	
+P25373	UniProtKB	Binding site	63	63	.	.	.	Note=Glutathione;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17327665,ECO:0000269|PubMed:18473363;Dbxref=PMID:17327665,PMID:18473363	
+P25373	UniProtKB	Binding site	75	75	.	.	.	Note=Glutathione%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17327665,ECO:0000269|PubMed:18473363;Dbxref=PMID:17327665,PMID:18473363	
+P25373	UniProtKB	Modified residue	27	27	.	.	.	Note=S-glutathionyl cysteine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17327665,ECO:0000269|PubMed:18473363;Dbxref=PMID:17327665,PMID:18473363	
+P25373	UniProtKB	Disulfide bond	27	30	.	.	.	Note=Redox-active%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18473363;Dbxref=PMID:18473363	
+P25373	UniProtKB	Cross-link	11	11	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25373	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Leads to increased oxidoreductase activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757	
+P25373	UniProtKB	Mutagenesis	89	89	.	.	.	Note=Leads to increased oxidoreductase activity. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20417731;Dbxref=PMID:20417731	
+P25373	UniProtKB	Helix	4	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R	
+P25373	UniProtKB	Beta strand	17	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R	
+P25373	UniProtKB	Helix	28	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R	
+P25373	UniProtKB	Turn	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JAD	
+P25373	UniProtKB	Helix	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R	
+P25373	UniProtKB	Beta strand	48	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R	
+P25373	UniProtKB	Helix	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R	
+P25373	UniProtKB	Helix	59	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R	
+P25373	UniProtKB	Beta strand	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R	
+P25373	UniProtKB	Beta strand	83	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R	
+P25373	UniProtKB	Helix	88	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R	
+P25373	UniProtKB	Helix	99	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R	
+##sequence-region Q12680 1 2145
+Q12680	UniProtKB	Propeptide	1	53	.	.	.	ID=PRO_0000011612;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7836314;Dbxref=PMID:7836314	
+Q12680	UniProtKB	Chain	54	2145	.	.	.	ID=PRO_0000011613;Note=Glutamate synthase [NADH]	
+Q12680	UniProtKB	Domain	54	455	.	.	.	Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609	
+Q12680	UniProtKB	Nucleotide binding	1132	1189	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12680	UniProtKB	Nucleotide binding	1928	1942	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12680	UniProtKB	Coiled coil	1551	1600	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12680	UniProtKB	Active site	54	54	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12680	UniProtKB	Metal binding	1185	1185	.	.	.	Note=Iron-sulfur (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12680	UniProtKB	Metal binding	1191	1191	.	.	.	Note=Iron-sulfur (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12680	UniProtKB	Metal binding	1196	1196	.	.	.	Note=Iron-sulfur (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12680	UniProtKB	Modified residue	2070	2070	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12680	UniProtKB	Sequence conflict	166	173	.	.	.	Note=NVPVDSTI->TSRRFYY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12680	UniProtKB	Sequence conflict	450	452	.	.	.	Note=FLV->IPS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12680	UniProtKB	Sequence conflict	1753	1753	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P37292 1 490
+P37292	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37292	UniProtKB	Chain	21	490	.	.	.	ID=PRO_0000032568;Note=Serine hydroxymethyltransferase%2C mitochondrial	
+P37292	UniProtKB	Modified residue	265	265	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P37292	UniProtKB	Sequence conflict	72	72	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03786 1 193
+Q03786	UniProtKB	Chain	1	193	.	.	.	ID=PRO_0000253810;Note=Probable gluconokinase	
+Q03786	UniProtKB	Nucleotide binding	18	25	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P30777 1 616
+P30777	UniProtKB	Chain	1	616	.	.	.	ID=PRO_0000202736;Note=GPI mannosyltransferase 3	
+P30777	UniProtKB	Topological domain	1	16	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Topological domain	38	86	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Transmembrane	87	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Topological domain	108	136	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Transmembrane	137	157	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Topological domain	158	188	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Topological domain	210	240	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Topological domain	262	278	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Transmembrane	279	299	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Topological domain	300	338	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Transmembrane	339	359	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Topological domain	360	392	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Transmembrane	393	413	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Topological domain	414	423	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Transmembrane	424	444	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Topological domain	445	616	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30777	UniProtKB	Mutagenesis	48	48	.	.	.	Note=In gpi10-1%3B accumulate M2%2C an abnormal GPI-anchor intermediate due to the absence of third mannose. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9639537;Dbxref=PMID:9639537	
+P30777	UniProtKB	Sequence conflict	339	339	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07830 1 1017
+Q07830	UniProtKB	Chain	1	1017	.	.	.	ID=PRO_0000240363;Note=GPI ethanolamine phosphate transferase 3	
+Q07830	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	347	367	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	457	477	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	484	504	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	515	535	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	558	578	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	582	602	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	644	664	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	685	705	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	715	735	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	765	785	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	806	826	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	829	849	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	903	923	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	947	967	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Transmembrane	981	1001	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Glycosylation	66	66	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Glycosylation	71	71	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Glycosylation	100	100	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Glycosylation	182	182	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Glycosylation	203	203	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Glycosylation	411	411	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Glycosylation	681	681	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Glycosylation	682	682	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Glycosylation	707	707	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Glycosylation	742	742	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07830	UniProtKB	Mutagenesis	198	198	.	.	.	Note=In MCP1-5%3B impairs growth at 36 degrees Celsius%3B when associated with S-231 and T-411. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642	
+Q07830	UniProtKB	Mutagenesis	231	231	.	.	.	Note=In MCP1-5%3B impairs growth at 36 degrees Celsius%3B when associated with R-198 and T-411. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642	
+Q07830	UniProtKB	Mutagenesis	367	367	.	.	.	Note=In MCP1-4%3B impairs growth at 36 degrees Celsius%3B when associated with P-556%3B G-887 and A-901. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642	
+Q07830	UniProtKB	Mutagenesis	411	411	.	.	.	Note=In MCP1-5%3B impairs growth at 36 degrees Celsius%3B when associated with R-198 and S-231. N->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642	
+Q07830	UniProtKB	Mutagenesis	556	556	.	.	.	Note=In MCP1-4%3B impairs growth at 36 degrees Celsius%3B when associated with T-367%3B G-887 and A-901. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642	
+Q07830	UniProtKB	Mutagenesis	887	887	.	.	.	Note=In MCP1-4%3B impairs growth at 36 degrees Celsius%3B when associated with T-367%3B P-556 and A-901. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642	
+Q07830	UniProtKB	Mutagenesis	901	901	.	.	.	Note=In MCP1-4%3B impairs growth at 36 degrees Celsius%3B when associated with T-367%3B P-556 and G-887. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642	
+##sequence-region P53306 1 609
+P53306	UniProtKB	Chain	1	609	.	.	.	ID=PRO_0000215666;Note=Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1	
+P53306	UniProtKB	Topological domain	1	186	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53306	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53306	UniProtKB	Topological domain	208	280	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53306	UniProtKB	Transmembrane	281	301	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53306	UniProtKB	Topological domain	302	380	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53306	UniProtKB	Transmembrane	381	401	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53306	UniProtKB	Topological domain	402	451	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53306	UniProtKB	Transmembrane	452	472	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53306	UniProtKB	Topological domain	473	485	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53306	UniProtKB	Transmembrane	486	506	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53306	UniProtKB	Topological domain	507	609	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06543 1 272
+Q06543	UniProtKB	Chain	1	272	.	.	.	ID=PRO_0000255597;Note=GPN-loop GTPase 3	
+Q06543	UniProtKB	Nucleotide binding	13	18	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+Q06543	UniProtKB	Nucleotide binding	173	176	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+Q06543	UniProtKB	Motif	70	72	.	.	.	Note=Gly-Pro-Asn (GPN)-loop%3B involved in dimer interface;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+Q06543	UniProtKB	Site	72	72	.	.	.	Note=Stabilizes the phosphate intermediate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+Q06543	UniProtKB	Mutagenesis	110	110	.	.	.	Note=Impairs heterodimer formation with NPA3/GPN1. E->K%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23324351;Dbxref=PMID:23324351	
+##sequence-region P41277 1 250
+P41277	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9038161;Dbxref=PMID:9038161	
+P41277	UniProtKB	Chain	2	250	.	.	.	ID=PRO_0000087560;Note=Glycerol-1-phosphate phosphohydrolase 1	
+P41277	UniProtKB	Active site	18	18	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41277	UniProtKB	Active site	20	20	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41277	UniProtKB	Metal binding	18	18	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41277	UniProtKB	Metal binding	20	20	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41277	UniProtKB	Metal binding	179	179	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41277	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41277	UniProtKB	Cross-link	64	64	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219	
+P41277	UniProtKB	Cross-link	64	64	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P41277	UniProtKB	Cross-link	144	144	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P41277	UniProtKB	Sequence conflict	91	91	.	.	.	Note=I->IK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41277	UniProtKB	Beta strand	6	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Turn	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	27	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	46	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	58	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	72	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	82	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	96	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Beta strand	111	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	119	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Beta strand	135	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	151	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Beta strand	174	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	181	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Beta strand	193	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	203	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Beta strand	212	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Helix	218	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Beta strand	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Turn	228	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Beta strand	232	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Beta strand	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+P41277	UniProtKB	Turn	245	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT	
+##sequence-region P18494 1 730
+P18494	UniProtKB	Chain	1	730	.	.	.	ID=PRO_0000083477;Note=Nitrogen regulatory protein GLN3	
+P18494	UniProtKB	Zinc finger	306	330	.	.	.	Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094	
+P18494	UniProtKB	Motif	129	137	.	.	.	Note=9aaTAD	
+P18494	UniProtKB	Compositional bias	351	361	.	.	.	Note=Arg/Lys-rich (basic)	
+P18494	UniProtKB	Modified residue	251	251	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P18494	UniProtKB	Modified residue	267	267	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P18494	UniProtKB	Modified residue	285	285	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P18494	UniProtKB	Modified residue	469	469	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P18494	UniProtKB	Modified residue	552	552	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P18494	UniProtKB	Modified residue	562	562	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P18494	UniProtKB	Sequence conflict	474	474	.	.	.	Note=P->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03835 1 250
+Q03835	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000102249;Note=Monothiol glutaredoxin-3	
+Q03835	UniProtKB	Domain	1	110	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+Q03835	UniProtKB	Domain	151	250	.	.	.	Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686	
+Q03835	UniProtKB	Metal binding	176	176	.	.	.	Note=Iron-sulfur (2Fe-2S)%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03835	UniProtKB	Beta strand	3	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+Q03835	UniProtKB	Helix	9	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+Q03835	UniProtKB	Turn	17	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+Q03835	UniProtKB	Beta strand	25	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+Q03835	UniProtKB	Helix	37	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+Q03835	UniProtKB	Helix	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+Q03835	UniProtKB	Beta strand	56	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+Q03835	UniProtKB	Turn	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+Q03835	UniProtKB	Helix	67	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+Q03835	UniProtKB	Beta strand	77	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+Q03835	UniProtKB	Beta strand	88	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+Q03835	UniProtKB	Helix	98	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I	
+##sequence-region Q02784 1 150
+Q02784	UniProtKB	Transit peptide	1	29	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11950925;Dbxref=PMID:11950925	
+Q02784	UniProtKB	Chain	30	150	.	.	.	ID=PRO_0000011632;Note=Monothiol glutaredoxin-5%2C mitochondrial	
+Q02784	UniProtKB	Domain	35	140	.	.	.	Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686	
+Q02784	UniProtKB	Region	92	96	.	.	.	Note=Glutathione binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02784	UniProtKB	Region	117	118	.	.	.	Note=Glutathione binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02784	UniProtKB	Metal binding	60	60	.	.	.	Note=Iron-sulfur (2Fe-2S)%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02784	UniProtKB	Binding site	52	52	.	.	.	Note=Glutathione;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02784	UniProtKB	Binding site	104	104	.	.	.	Note=Glutathione%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02784	UniProtKB	Helix	32	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8	
+Q02784	UniProtKB	Beta strand	46	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8	
+Q02784	UniProtKB	Beta strand	55	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8	
+Q02784	UniProtKB	Helix	62	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8	
+Q02784	UniProtKB	Helix	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8	
+Q02784	UniProtKB	Beta strand	80	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8	
+Q02784	UniProtKB	Helix	89	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8	
+Q02784	UniProtKB	Beta strand	106	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8	
+Q02784	UniProtKB	Beta strand	112	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8	
+Q02784	UniProtKB	Helix	117	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8	
+Q02784	UniProtKB	Helix	128	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8	
+##sequence-region P32784 1 759
+P32784	UniProtKB	Chain	1	759	.	.	.	ID=PRO_0000195257;Note=Glycerol-3-phosphate O-acyltransferase 1	
+P32784	UniProtKB	Transmembrane	49	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32784	UniProtKB	Transmembrane	123	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32784	UniProtKB	Transmembrane	260	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32784	UniProtKB	Transmembrane	440	463	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32784	UniProtKB	Transmembrane	494	516	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32784	UniProtKB	Transmembrane	524	545	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32784	UniProtKB	Motif	414	419	.	.	.	Note=HXXXXD motif	
+P32784	UniProtKB	Compositional bias	736	753	.	.	.	Note=Poly-Glu	
+P32784	UniProtKB	Sequence conflict	10	10	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32784	UniProtKB	Sequence conflict	10	10	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32784	UniProtKB	Sequence conflict	30	38	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32784	UniProtKB	Sequence conflict	88	88	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32784	UniProtKB	Sequence conflict	125	125	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32784	UniProtKB	Sequence conflict	278	278	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32784	UniProtKB	Sequence conflict	324	324	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32784	UniProtKB	Sequence conflict	574	574	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32784	UniProtKB	Sequence conflict	730	730	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07286 1 448
+P07286	UniProtKB	Chain	1	448	.	.	.	ID=PRO_0000108765;Note=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase	
+P07286	UniProtKB	Transmembrane	24	44	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07286	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07286	UniProtKB	Transmembrane	129	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07286	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07286	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07286	UniProtKB	Transmembrane	231	251	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07286	UniProtKB	Transmembrane	256	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07286	UniProtKB	Transmembrane	283	303	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07286	UniProtKB	Transmembrane	309	329	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07286	UniProtKB	Transmembrane	387	407	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07286	UniProtKB	Transmembrane	419	439	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07286	UniProtKB	Motif	81	93	.	.	.	Note=Dolichol recognition	
+P07286	UniProtKB	Motif	257	269	.	.	.	Note=Dolichol recognition	
+##sequence-region P36148 1 743
+P36148	UniProtKB	Chain	1	743	.	.	.	ID=PRO_0000195258;Note=Glycerol-3-phosphate O-acyltransferase 2	
+P36148	UniProtKB	Topological domain	1	30	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36148	UniProtKB	Transmembrane	31	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36148	UniProtKB	Topological domain	56	68	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36148	UniProtKB	Transmembrane	69	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36148	UniProtKB	Topological domain	86	501	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36148	UniProtKB	Transmembrane	502	524	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36148	UniProtKB	Topological domain	525	538	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36148	UniProtKB	Transmembrane	539	555	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36148	UniProtKB	Topological domain	556	743	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36148	UniProtKB	Modified residue	632	632	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36148	UniProtKB	Modified residue	637	637	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36148	UniProtKB	Modified residue	647	647	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36148	UniProtKB	Modified residue	651	651	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36148	UniProtKB	Modified residue	654	654	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36148	UniProtKB	Modified residue	657	657	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36148	UniProtKB	Modified residue	664	664	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36148	UniProtKB	Modified residue	668	668	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36148	UniProtKB	Modified residue	671	671	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36148	UniProtKB	Modified residue	673	673	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36148	UniProtKB	Modified residue	688	688	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36148	UniProtKB	Modified residue	692	692	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36148	UniProtKB	Modified residue	693	693	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q04410 1 372
+Q04410	UniProtKB	Chain	1	372	.	.	.	ID=PRO_0000270975;Note=GRASP65 homolog protein 1	
+Q04410	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17261844;Dbxref=PMID:17261844	
+Q04410	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04410	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Abolishes acetylation and association with cis-Golgi. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17261844;Dbxref=PMID:17261844	
+##sequence-region Q08929 1 609
+Q08929	UniProtKB	Chain	1	609	.	.	.	ID=PRO_0000213133;Note=Glycerol uptake protein 2	
+Q08929	UniProtKB	Transmembrane	76	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08929	UniProtKB	Transmembrane	129	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08929	UniProtKB	Transmembrane	164	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08929	UniProtKB	Transmembrane	201	218	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08929	UniProtKB	Transmembrane	323	345	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08929	UniProtKB	Transmembrane	365	387	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08929	UniProtKB	Transmembrane	408	427	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08929	UniProtKB	Transmembrane	501	523	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08929	UniProtKB	Transmembrane	535	557	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08929	UniProtKB	Transmembrane	577	594	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08929	UniProtKB	Active site	496	496	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04322 1 720
+Q04322	UniProtKB	Chain	1	720	.	.	.	ID=PRO_0000208062;Note=Probable GTPase-activating protein GYL1	
+Q04322	UniProtKB	Domain	297	477	.	.	.	Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163	
+Q04322	UniProtKB	Coiled coil	572	696	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04322	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04322	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q04322	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q04322	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04322	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04322	UniProtKB	Cross-link	498	498	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542864;Dbxref=PMID:15542864	
+##sequence-region P48365 1 746
+P48365	UniProtKB	Chain	1	746	.	.	.	ID=PRO_0000208017;Note=GTPase-activating protein GYP7	
+P48365	UniProtKB	Domain	385	633	.	.	.	Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163	
+P48365	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48365	UniProtKB	Modified residue	339	339	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P23337 1 708
+P23337	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2123485;Dbxref=PMID:2123485	
+P23337	UniProtKB	Chain	2	708	.	.	.	ID=PRO_0000194773;Note=Glycogen [starch] synthase isoform 1	
+P23337	UniProtKB	Binding site	20	20	.	.	.	Note=UDP-glucose;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23337	UniProtKB	Modified residue	159	159	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23337	UniProtKB	Modified residue	363	363	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23337	UniProtKB	Modified residue	560	560	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23337	UniProtKB	Modified residue	651	651	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P23337	UniProtKB	Modified residue	655	655	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P23337	UniProtKB	Modified residue	660	660	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23337	UniProtKB	Modified residue	662	662	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23337	UniProtKB	Modified residue	667	667	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27472	
+##sequence-region P04911 1 132
+P04911	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12915400;Dbxref=PMID:12915400	
+P04911	UniProtKB	Chain	2	132	.	.	.	ID=PRO_0000055326;Note=Histone H2A.1	
+P04911	UniProtKB	Motif	129	130	.	.	.	Note=[ST]-Q motif	
+P04911	UniProtKB	Site	120	120	.	.	.	Note=Not ubiquitinated;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642555,ECO:0000269|PubMed:2201907;Dbxref=PMID:10642555,PMID:2201907	
+P04911	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12915400;Dbxref=PMID:12915400	
+P04911	UniProtKB	Modified residue	5	5	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10082517;Dbxref=PMID:10082517	
+P04911	UniProtKB	Modified residue	8	8	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10082517,ECO:0000269|PubMed:11545749;Dbxref=PMID:10082517,PMID:11545749	
+P04911	UniProtKB	Modified residue	106	106	.	.	.	Note=N5-methylglutamine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239	
+P04911	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636	
+P04911	UniProtKB	Cross-link	127	127	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
+P04911	UniProtKB	Mutagenesis	120	121	.	.	.	Note=No effect. No effect%3B when associated with R-124 and R-127. KK->RR;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642555,ECO:0000269|PubMed:2201907;Dbxref=PMID:10642555,PMID:2201907	
+P04911	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Causes hypersensitivity to DNA-damage-inducing agents and impairs sporulation. S->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781691;Dbxref=PMID:15781691	
+P04911	UniProtKB	Mutagenesis	124	124	.	.	.	Note=No effect%3B when associated with R-120%3B R-121 and R-127. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10642555;Dbxref=PMID:10642555	
+P04911	UniProtKB	Mutagenesis	127	127	.	.	.	Note=No effect%3B when associated with R-120%3B R-121 and R-124. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10642555;Dbxref=PMID:10642555	
+P04911	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Causes hypersensitivity to DNA-damage-inducing agents. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636	
+P04911	UniProtKB	Mutagenesis	129	129	.	.	.	Note=No effect. S->E%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636	
+P04911	UniProtKB	Helix	19	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN	
+P04911	UniProtKB	Helix	29	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN	
+P04911	UniProtKB	Beta strand	41	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN	
+P04911	UniProtKB	Helix	48	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN	
+P04911	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN	
+P04911	UniProtKB	Helix	82	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN	
+P04911	UniProtKB	Helix	93	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN	
+P04911	UniProtKB	Beta strand	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ID3	
+P04911	UniProtKB	Helix	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ID3	
+##sequence-region P02294 1 131
+P02294	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02294	UniProtKB	Chain	2	131	.	.	.	ID=PRO_0000071939;Note=Histone H2B.2	
+P02294	UniProtKB	Modified residue	7	7	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039	
+P02294	UniProtKB	Modified residue	8	8	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039	
+P02294	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15652479,ECO:0000269|PubMed:15970663;Dbxref=PMID:15652479,PMID:15970663	
+P02294	UniProtKB	Modified residue	12	12	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:15186774;Dbxref=PMID:11545749,PMID:15186774	
+P02294	UniProtKB	Modified residue	17	17	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:15186774,ECO:0000269|PubMed:16598039;Dbxref=PMID:11545749,PMID:15186774,PMID:16598039	
+P02294	UniProtKB	Cross-link	7	7	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate	
+P02294	UniProtKB	Cross-link	8	8	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate	
+P02294	UniProtKB	Cross-link	17	17	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02294	UniProtKB	Cross-link	18	18	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02294	UniProtKB	Cross-link	124	124	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12535538,ECO:0000269|PubMed:12535539,ECO:0000269|PubMed:14660635,ECO:0000269|PubMed:15280549;Dbxref=PMID:12535538,PMID:12535539,PMID:14660635,PMID:15280549	
+P02294	UniProtKB	Mutagenesis	7	8	.	.	.	Note=Reduces sumoylation. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039	
+P02294	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Desensitizes cells to H(2)O(2) treatment. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652479;Dbxref=PMID:15652479	
+P02294	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Induces apoptotic-like features including chromatin condensation. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652479;Dbxref=PMID:15652479	
+P02294	UniProtKB	Mutagenesis	17	18	.	.	.	Note=Reduces sumoylation. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039	
+P02294	UniProtKB	Mutagenesis	124	124	.	.	.	Note=Impairs ubiquitin conjugation%2C DNA double-strand breaks formation during meiosis and histone H3-K79 methylation. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:14660635,ECO:0000269|PubMed:15280549;Dbxref=PMID:12152067,PMID:14660635,PMID:15280549	
+P02294	UniProtKB	Helix	42	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P02294	UniProtKB	Turn	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P02294	UniProtKB	Helix	60	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P02294	UniProtKB	Beta strand	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P02294	UniProtKB	Helix	95	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P02294	UniProtKB	Helix	109	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+##sequence-region P40857 1 217
+P40857	UniProtKB	Chain	1	217	.	.	.	ID=PRO_0000203047;Note=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1	
+P40857	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Transmembrane	12	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Topological domain	30	47	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Transmembrane	48	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Topological domain	67	76	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Transmembrane	77	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Topological domain	95	99	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Transmembrane	100	117	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Topological domain	118	142	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Transmembrane	143	160	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Topological domain	161	178	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Transmembrane	179	196	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Topological domain	197	217	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40857	UniProtKB	Motif	214	217	.	.	.	Note=Endoplasmic reticulum retention signal	
+P40857	UniProtKB	Active site	149	149	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:18272525;Dbxref=PMID:18272525	
+P40857	UniProtKB	Active site	156	156	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:18272525;Dbxref=PMID:18272525	
+P40857	UniProtKB	Mutagenesis	149	149	.	.	.	Note=No catalytic activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18272525;Dbxref=PMID:18272525	
+P40857	UniProtKB	Mutagenesis	156	156	.	.	.	Note=No catalytic activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18272525;Dbxref=PMID:18272525	
+##sequence-region P25333 1 603
+P25333	UniProtKB	Chain	1	603	.	.	.	ID=PRO_0000085987;Note=Serine/threonine-protein kinase HAL4/SAT4	
+P25333	UniProtKB	Domain	316	590	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P25333	UniProtKB	Nucleotide binding	322	330	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P25333	UniProtKB	Compositional bias	99	111	.	.	.	Note=Ser-rich	
+P25333	UniProtKB	Active site	449	449	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P25333	UniProtKB	Binding site	353	353	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region Q04399 1 608
+Q04399	UniProtKB	Chain	1	608	.	.	.	ID=PRO_0000085585;Note=Putative multicopper oxidase GMC1	
+Q04399	UniProtKB	Domain	51	163	.	.	.	Note=Plastocyanin-like 1	
+Q04399	UniProtKB	Domain	243	374	.	.	.	Note=Plastocyanin-like 2	
+Q04399	UniProtKB	Domain	421	548	.	.	.	Note=Plastocyanin-like 3	
+Q04399	UniProtKB	Metal binding	100	100	.	.	.	Note=Copper 1%3B type 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04399	UniProtKB	Metal binding	102	102	.	.	.	Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04399	UniProtKB	Metal binding	145	145	.	.	.	Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04399	UniProtKB	Metal binding	147	147	.	.	.	Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04399	UniProtKB	Metal binding	452	452	.	.	.	Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04399	UniProtKB	Metal binding	455	455	.	.	.	Note=Copper 1%3B type 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04399	UniProtKB	Metal binding	457	457	.	.	.	Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04399	UniProtKB	Metal binding	530	530	.	.	.	Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04399	UniProtKB	Metal binding	531	531	.	.	.	Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04399	UniProtKB	Metal binding	532	532	.	.	.	Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04399	UniProtKB	Metal binding	536	536	.	.	.	Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38736 1 223
+P38736	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38736	UniProtKB	Chain	2	223	.	.	.	ID=PRO_0000212557;Note=Golgi SNAP receptor complex member 1	
+P38736	UniProtKB	Topological domain	2	204	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38736	UniProtKB	Transmembrane	205	222	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38736	UniProtKB	Topological domain	223	223	.	.	.	Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38736	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38736	UniProtKB	Modified residue	164	164	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P39717 1 880
+P39717	UniProtKB	Chain	1	880	.	.	.	ID=PRO_0000119071;Note=Guanine nucleotide-binding protein subunit beta 2	
+P39717	UniProtKB	Repeat	291	339	.	.	.	Note=Kelch 1	
+P39717	UniProtKB	Repeat	377	425	.	.	.	Note=Kelch 2	
+P39717	UniProtKB	Repeat	501	552	.	.	.	Note=Kelch 3	
+P39717	UniProtKB	Repeat	691	738	.	.	.	Note=Kelch 4	
+P39717	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39717	UniProtKB	Natural variant	215	215	.	.	.	Note=In strain: Sigma 1278B. Y->H	
+P39717	UniProtKB	Natural variant	221	221	.	.	.	Note=In strain: Sigma 1278B. L->P	
+P39717	UniProtKB	Natural variant	552	552	.	.	.	Note=In strain: Sigma 1278B. S->R	
+P39717	UniProtKB	Natural variant	674	674	.	.	.	Note=In strain: Sigma 1278B. A->T	
+P39717	UniProtKB	Natural variant	777	777	.	.	.	Note=In strain: Sigma 1278B. P->S	
+P39717	UniProtKB	Sequence conflict	661	661	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39717	UniProtKB	Sequence conflict	802	802	.	.	.	Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39717	UniProtKB	Sequence conflict	814	815	.	.	.	Note=ED->AA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08969 1 168
+Q08969	UniProtKB	Chain	1	168	.	.	.	ID=PRO_0000083846;Note=Protein GRE1	
+Q08969	UniProtKB	Compositional bias	28	139	.	.	.	Note=Gln-rich	
+##sequence-region P38715 1 327
+P38715	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7747971;Dbxref=PMID:7747971	
+P38715	UniProtKB	Chain	2	327	.	.	.	ID=PRO_0000124678;Note=NADPH-dependent aldose reductase GRE3	
+P38715	UniProtKB	Nucleotide binding	219	286	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38715	UniProtKB	Active site	49	49	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38715	UniProtKB	Binding site	111	111	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38715	UniProtKB	Site	78	78	.	.	.	Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53154 1 560
+P53154	UniProtKB	Chain	1	560	.	.	.	ID=PRO_0000213132;Note=Glycerol uptake protein 1	
+P53154	UniProtKB	Topological domain	1	43	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Transmembrane	44	64	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Topological domain	65	101	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Transmembrane	102	122	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Topological domain	123	131	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Topological domain	153	276	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Transmembrane	277	297	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Topological domain	298	322	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Transmembrane	323	343	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Topological domain	344	352	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Transmembrane	353	373	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Topological domain	374	432	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Transmembrane	433	449	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Topological domain	450	454	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Transmembrane	455	474	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Topological domain	475	485	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Transmembrane	486	506	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Topological domain	507	526	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Transmembrane	527	547	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Topological domain	548	560	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53154	UniProtKB	Active site	447	447	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40531 1 326
+P40531	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P40531	UniProtKB	Chain	2	326	.	.	.	ID=PRO_0000083881;Note=Protein GVP36	
+P40531	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P40531	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P40531	UniProtKB	Modified residue	319	319	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40531	UniProtKB	Cross-link	13	13	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40531	UniProtKB	Cross-link	305	305	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40531	UniProtKB	Cross-link	313	313	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q08484 1 637
+Q08484	UniProtKB	Chain	1	637	.	.	.	ID=PRO_0000208010;Note=GTPase-activating protein GYP1	
+Q08484	UniProtKB	Domain	280	508	.	.	.	Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163	
+Q08484	UniProtKB	Compositional bias	117	129	.	.	.	Note=His-rich	
+Q08484	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08484	UniProtKB	Modified residue	250	250	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08484	UniProtKB	Helix	251	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	270	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	286	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	304	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Beta strand	323	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	330	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	349	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	354	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Turn	372	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	380	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	393	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	398	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Turn	404	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	415	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	434	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	445	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	463	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	477	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Turn	486	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	489	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	494	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	571	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	587	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	595	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+Q08484	UniProtKB	Helix	612	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM	
+##sequence-region P48566 1 633
+P48566	UniProtKB	Chain	1	633	.	.	.	ID=PRO_0000208012;Note=GTPase-activating protein GYP3	
+P48566	UniProtKB	Domain	223	456	.	.	.	Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163	
+P48566	UniProtKB	Modified residue	147	147	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48566	UniProtKB	Modified residue	484	484	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48566	UniProtKB	Mutagenesis	282	282	.	.	.	Note=Reduced GAP activity. R->F%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12913108;Dbxref=PMID:12913108	
+##sequence-region Q12753 1 694
+Q12753	UniProtKB	Chain	1	694	.	.	.	ID=PRO_0000194933;Note=Transcriptional activator HAA1	
+Q12753	UniProtKB	DNA binding	1	40	.	.	.	Note=Copper-fist;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+Q12753	UniProtKB	Metal binding	11	11	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+Q12753	UniProtKB	Metal binding	14	14	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+Q12753	UniProtKB	Metal binding	23	23	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+Q12753	UniProtKB	Metal binding	25	25	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+Q12753	UniProtKB	Modified residue	125	125	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12753	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12753	UniProtKB	Modified residue	241	241	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956	
+Q12753	UniProtKB	Modified residue	291	291	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P41546 1 238
+P41546	UniProtKB	Chain	1	238	.	.	.	ID=PRO_0000076518;Note=Transcriptional activator HAC1	
+P41546	UniProtKB	Domain	39	102	.	.	.	Note=bZIP	
+P41546	UniProtKB	Region	41	61	.	.	.	Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41546	UniProtKB	Region	67	74	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41546	UniProtKB	Alternative sequence	221	238	.	.	.	ID=VSP_020905;Note=In isoform U. EAQSGLNSFELNDFFITS->AVITMTRKLQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41546	UniProtKB	Sequence conflict	181	181	.	.	.	Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P42950 1 618
+P42950	UniProtKB	Chain	1	618	.	.	.	ID=PRO_0000114998;Note=Glucose starvation modulator protein 1	
+P42950	UniProtKB	Domain	466	538	.	.	.	Note=PAS	
+P42950	UniProtKB	DNA binding	20	48	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P42950	UniProtKB	Sequence conflict	611	611	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32835 1 219
+P32835	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P32835	UniProtKB	Chain	2	219	.	.	.	ID=PRO_0000208733;Note=GTP-binding nuclear protein GSP1/CNR1	
+P32835	UniProtKB	Nucleotide binding	20	27	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825	
+P32835	UniProtKB	Nucleotide binding	124	127	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825	
+P32835	UniProtKB	Nucleotide binding	152	154	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825	
+P32835	UniProtKB	Binding site	70	70	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825	
+P32835	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P32835	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P32835	UniProtKB	Beta strand	12	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Helix	25	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Beta strand	46	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Beta strand	59	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Helix	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Helix	78	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Beta strand	87	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Helix	97	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Helix	103	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Beta strand	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICQ	
+P32835	UniProtKB	Beta strand	119	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Helix	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Helix	141	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Beta strand	147	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Turn	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Turn	157	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Helix	161	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Helix	200	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+P32835	UniProtKB	Turn	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I	
+##sequence-region Q07729 1 489
+Q07729	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000122302;Note=Probable guanine deaminase	
+Q07729	UniProtKB	Region	102	105	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3	
+Q07729	UniProtKB	Region	231	232	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3	
+Q07729	UniProtKB	Region	258	261	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3	
+Q07729	UniProtKB	Metal binding	100	100	.	.	.	Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3	
+Q07729	UniProtKB	Metal binding	102	102	.	.	.	Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3	
+Q07729	UniProtKB	Metal binding	258	258	.	.	.	Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3	
+Q07729	UniProtKB	Metal binding	348	348	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3	
+Q07729	UniProtKB	Binding site	348	348	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3	
+##sequence-region P53551 1 258
+P53551	UniProtKB	Chain	1	258	.	.	.	ID=PRO_0000196001;Note=Histone H1	
+P53551	UniProtKB	Domain	43	117	.	.	.	Note=H15 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00837	
+P53551	UniProtKB	Domain	176	251	.	.	.	Note=H15 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00837	
+P53551	UniProtKB	Modified residue	174	174	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53551	UniProtKB	Sequence conflict	8	8	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53551	UniProtKB	Helix	47	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM	
+P53551	UniProtKB	Helix	66	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM	
+P53551	UniProtKB	Turn	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM	
+P53551	UniProtKB	Beta strand	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM	
+P53551	UniProtKB	Helix	86	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM	
+P53551	UniProtKB	Beta strand	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM	
+P53551	UniProtKB	Beta strand	112	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM	
+P53551	UniProtKB	Helix	180	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS	
+P53551	UniProtKB	Helix	191	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YQA	
+P53551	UniProtKB	Helix	199	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS	
+P53551	UniProtKB	Turn	210	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS	
+P53551	UniProtKB	Helix	220	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS	
+P53551	UniProtKB	Beta strand	235	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS	
+P53551	UniProtKB	Beta strand	243	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YQA	
+P53551	UniProtKB	Beta strand	247	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS	
+##sequence-region P14064 1 554
+P14064	UniProtKB	Chain	1	554	.	.	.	ID=PRO_0000083900;Note=Transcriptional activator HAP4	
+P14064	UniProtKB	Region	1	327	.	.	.	Note=Probably encodes all the information necessary to anchor HAP4 to HAP2/3	
+P14064	UniProtKB	Region	124	300	.	.	.	Note=Activation domain 1	
+P14064	UniProtKB	Region	359	476	.	.	.	Note=Activation domain 2	
+P14064	UniProtKB	Compositional bias	54	80	.	.	.	Note=Arg/Lys-rich (basic)	
+P14064	UniProtKB	Compositional bias	90	113	.	.	.	Note=Asn-rich	
+P14064	UniProtKB	Compositional bias	107	113	.	.	.	Note=Poly-Asn	
+P14064	UniProtKB	Compositional bias	424	471	.	.	.	Note=Asp/Glu-rich (acidic)	
+P14064	UniProtKB	Compositional bias	519	549	.	.	.	Note=Asp/Glu-rich (acidic)	
+P14064	UniProtKB	Mutagenesis	148	151	.	.	.	Note=Greatly diminishes transcriptional activation. FLKF->SSKS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264	
+P14064	UniProtKB	Mutagenesis	390	394	.	.	.	Note=Greatly diminishes transcriptional activation. IWNYL->SSNSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264	
+P14064	UniProtKB	Mutagenesis	427	430	.	.	.	Note=Greatly diminishes transcriptional activation. YLFL->SSSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264	
+P14064	UniProtKB	Mutagenesis	456	459	.	.	.	Note=Greatly diminishes transcriptional activation. FSYL->SSSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264	
+P14064	UniProtKB	Mutagenesis	466	467	.	.	.	Note=Abolishes transcriptional activation. LM->SS	
+P14064	UniProtKB	Mutagenesis	466	466	.	.	.	Note=Greatly diminishes transcriptional activation. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264	
+P14064	UniProtKB	Mutagenesis	467	467	.	.	.	Note=Abolishes transcriptional activation. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264	
+P14064	UniProtKB	Sequence conflict	160	160	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12341 1 374
+Q12341	UniProtKB	Chain	1	374	.	.	.	ID=PRO_0000083903;Note=Histone acetyltransferase type B catalytic subunit	
+Q12341	UniProtKB	Domain	135	303	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+Q12341	UniProtKB	Region	42	44	.	.	.	Note=Interaction with histone H4 N-terminus;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250	
+Q12341	UniProtKB	Region	194	196	.	.	.	Note=Interaction with histone H4 N-terminus;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250	
+Q12341	UniProtKB	Region	197	205	.	.	.	Note=Interaction with HAT2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24835250,ECO:0000269|PubMed:8858151;Dbxref=PMID:24835250,PMID:8858151	
+Q12341	UniProtKB	Region	220	222	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24835250,ECO:0000269|PubMed:9727486;Dbxref=PMID:24835250,PMID:9727486	
+Q12341	UniProtKB	Region	227	233	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24835250,ECO:0000269|PubMed:9727486;Dbxref=PMID:24835250,PMID:9727486	
+Q12341	UniProtKB	Compositional bias	314	317	.	.	.	Note=Poly-Leu	
+Q12341	UniProtKB	Active site	255	255	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:24835250;Dbxref=PMID:24835250	
+Q12341	UniProtKB	Binding site	258	258	.	.	.	Note=Acetyl-CoA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24835250,ECO:0000269|PubMed:9727486;Dbxref=PMID:24835250,PMID:9727486	
+Q12341	UniProtKB	Binding site	267	267	.	.	.	Note=Acetyl-CoA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9727486;Dbxref=PMID:9727486	
+Q12341	UniProtKB	Site	174	174	.	.	.	Note=Interaction with histone H4 N-terminus;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250	
+Q12341	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12341	UniProtKB	Mutagenesis	197	197	.	.	.	Note=Abolishes interaction with HAT2. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250	
+Q12341	UniProtKB	Mutagenesis	199	199	.	.	.	Note=Abolishes interaction with HAT2. Y->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250	
+Q12341	UniProtKB	Mutagenesis	202	202	.	.	.	Note=Impairs interaction with HAT2. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250	
+Q12341	UniProtKB	Mutagenesis	205	205	.	.	.	Note=Abolishes interaction with HAT2. F->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250	
+Q12341	UniProtKB	Mutagenesis	214	214	.	.	.	Note=Impairs interaction with HAT2. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250	
+Q12341	UniProtKB	Sequence conflict	87	87	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12341	UniProtKB	Helix	8	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	12	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	19	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	37	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Turn	41	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BOB	
+Q12341	UniProtKB	Beta strand	45	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	53	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Turn	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	65	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	83	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	101	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	121	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	133	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	144	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	155	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	175	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Turn	182	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	187	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	202	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	213	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	231	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Beta strand	249	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	259	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	278	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	290	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+Q12341	UniProtKB	Helix	304	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+##sequence-region P38523 1 228
+##sequence-region P41921 1 483
+P41921	UniProtKB	Chain	1	483	.	.	.	ID=PRO_0000067972;Note=Glutathione reductase	
+P41921	UniProtKB	Nucleotide binding	53	61	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41921	UniProtKB	Active site	472	472	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41921	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P41921	UniProtKB	Disulfide bond	61	66	.	.	.	Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41921	UniProtKB	Alternative sequence	1	16	.	.	.	ID=VSP_058124;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41921	UniProtKB	Sequence conflict	315	315	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41921	UniProtKB	Sequence conflict	428	428	.	.	.	Note=C->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41921	UniProtKB	Beta strand	23	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	33	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	49	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	59	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	66	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Turn	83	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	105	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	132	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	147	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	157	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	187	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	198	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	207	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	222	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	228	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	238	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	261	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	273	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	282	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	295	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	303	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	329	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	333	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	342	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	360	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	374	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	382	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	389	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	398	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	401	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	411	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	422	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Turn	430	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Beta strand	434	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	445	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	462	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+P41921	UniProtKB	Helix	476	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM	
+##sequence-region P32836 1 220
+P32836	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32835	
+P32836	UniProtKB	Chain	2	220	.	.	.	ID=PRO_0000208734;Note=GTP-binding nuclear protein GSP2/CNR2	
+P32836	UniProtKB	Nucleotide binding	21	28	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825	
+P32836	UniProtKB	Nucleotide binding	125	128	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825	
+P32836	UniProtKB	Nucleotide binding	153	155	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825	
+P32836	UniProtKB	Binding site	71	71	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825	
+P32836	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32835	
+P32836	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32835	
+##sequence-region Q00582 1 310
+Q00582	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000122486;Note=GTP-binding protein GTR1	
+Q00582	UniProtKB	Nucleotide binding	13	20	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q00582	UniProtKB	Nucleotide binding	61	65	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00582	UniProtKB	Nucleotide binding	126	129	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00582	UniProtKB	Beta strand	8	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	19	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	33	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Beta strand	43	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Turn	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Beta strand	55	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	66	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Turn	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	77	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Beta strand	85	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	98	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Beta strand	120	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	133	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Turn	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Beta strand	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	170	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	186	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Beta strand	202	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Turn	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Beta strand	215	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	242	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Beta strand	264	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Turn	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Beta strand	273	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Beta strand	282	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Helix	295	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+Q00582	UniProtKB	Turn	302	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+##sequence-region P53290 1 341
+P53290	UniProtKB	Chain	1	341	.	.	.	ID=PRO_0000122487;Note=GTP-binding protein GTR2	
+P53290	UniProtKB	Nucleotide binding	16	23	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53290	UniProtKB	Nucleotide binding	124	127	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53290	UniProtKB	Beta strand	12	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Helix	24	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Helix	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Turn	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ARZ	
+P53290	UniProtKB	Beta strand	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	58	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Helix	74	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	84	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Helix	98	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	118	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Helix	132	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	159	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	166	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Helix	170	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Helix	186	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Helix	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	199	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	216	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Helix	225	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	270	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	280	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Beta strand	287	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+P53290	UniProtKB	Helix	303	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W	
+##sequence-region P39996 1 337
+P39996	UniProtKB	Chain	1	337	.	.	.	ID=PRO_0000202611;Note=Glutathione transferase 3	
+P39996	UniProtKB	Topological domain	1	239	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39996	UniProtKB	Transmembrane	240	260	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39996	UniProtKB	Topological domain	261	313	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39996	UniProtKB	Transmembrane	314	336	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39996	UniProtKB	Topological domain	337	337	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39996	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39996	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39996	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39996	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P38970 1 855
+P38970	UniProtKB	Chain	1	855	.	.	.	ID=PRO_0000085988;Note=Serine/threonine-protein kinase HAL5	
+P38970	UniProtKB	Domain	503	837	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38970	UniProtKB	Nucleotide binding	509	517	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38970	UniProtKB	Compositional bias	369	377	.	.	.	Note=Poly-Gln	
+P38970	UniProtKB	Active site	688	688	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P38970	UniProtKB	Binding site	546	546	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38970	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38970	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38970	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38970	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38970	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38970	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38970	UniProtKB	Modified residue	277	277	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38970	UniProtKB	Modified residue	324	324	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38970	UniProtKB	Modified residue	333	333	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38970	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38970	UniProtKB	Modified residue	358	358	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38970	UniProtKB	Modified residue	391	391	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38970	UniProtKB	Modified residue	395	395	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P53973 1 706
+P53973	UniProtKB	Chain	1	706	.	.	.	ID=PRO_0000114738;Note=Histone deacetylase HDA1	
+P53973	UniProtKB	Region	67	396	.	.	.	Note=Histone deacetylase	
+P53973	UniProtKB	Active site	206	206	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53973	UniProtKB	Helix	457	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Beta strand	483	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Helix	487	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Beta strand	490	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Helix	496	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Beta strand	500	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Beta strand	511	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Turn	518	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Helix	525	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Beta strand	529	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Helix	535	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Turn	543	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Beta strand	547	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Beta strand	558	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Helix	563	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Turn	580	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Beta strand	590	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Helix	596	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Helix	599	608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Turn	612	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Beta strand	615	623	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Helix	637	644	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Beta strand	646	650	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Helix	667	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Beta strand	672	674	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+P53973	UniProtKB	Helix	680	696	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J	
+##sequence-region P38199 1 381
+P38199	UniProtKB	Chain	1	381	.	.	.	ID=PRO_0000050161;Note=Heterogeneous nuclear rnp K-like protein 2	
+P38199	UniProtKB	Domain	43	107	.	.	.	Note=KH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P38199	UniProtKB	Domain	156	221	.	.	.	Note=KH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P38199	UniProtKB	Domain	258	326	.	.	.	Note=KH 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P38199	UniProtKB	Modified residue	358	358	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38199	UniProtKB	Modified residue	360	360	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38199	UniProtKB	Modified residue	362	362	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38199	UniProtKB	Sequence conflict	362	362	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12361 1 961
+Q12361	UniProtKB	Chain	1	961	.	.	.	ID=PRO_0000195084;Note=G protein-coupled receptor GPR1	
+Q12361	UniProtKB	Topological domain	1	56	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Transmembrane	57	79	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Topological domain	80	91	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Transmembrane	92	114	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Topological domain	115	133	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Transmembrane	134	156	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Topological domain	157	178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Transmembrane	179	198	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Topological domain	199	250	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Transmembrane	251	273	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Topological domain	274	619	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Transmembrane	620	642	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Topological domain	643	822	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Transmembrane	823	843	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Topological domain	844	961	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12361	UniProtKB	Compositional bias	501	547	.	.	.	Note=Poly-Asn	
+Q12361	UniProtKB	Modified residue	373	373	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12361	UniProtKB	Modified residue	903	903	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region P24814 1 1151
+P24814	UniProtKB	Chain	1	1151	.	.	.	ID=PRO_0000119968;Note=SCF E3 ubiquitin ligase complex F-box protein GRR1	
+P24814	UniProtKB	Domain	314	361	.	.	.	Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080	
+P24814	UniProtKB	Repeat	399	423	.	.	.	Note=LRR 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	424	449	.	.	.	Note=LRR 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	450	475	.	.	.	Note=LRR 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	476	501	.	.	.	Note=LRR 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	502	527	.	.	.	Note=LRR 5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	528	553	.	.	.	Note=LRR 6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	554	582	.	.	.	Note=LRR 7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	583	608	.	.	.	Note=LRR 8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	609	634	.	.	.	Note=LRR 9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	635	660	.	.	.	Note=LRR 10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	661	685	.	.	.	Note=LRR 11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	686	714	.	.	.	Note=LRR 12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Repeat	715	740	.	.	.	Note=LRR 13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034	
+P24814	UniProtKB	Compositional bias	38	49	.	.	.	Note=Poly-Asn	
+P24814	UniProtKB	Compositional bias	1045	1124	.	.	.	Note=Asn-rich	
+P24814	UniProtKB	Modified residue	199	199	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P24814	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q04697 1 403
+Q04697	UniProtKB	Chain	1	403	.	.	.	ID=PRO_0000083865;Note=Glucose-signaling factor 2	
+Q04697	UniProtKB	Topological domain	1	177	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04697	UniProtKB	Transmembrane	178	198	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04697	UniProtKB	Topological domain	199	403	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04697	UniProtKB	Coiled coil	330	388	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04697	UniProtKB	Glycosylation	89	89	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04697	UniProtKB	Glycosylation	173	173	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40582 1 234
+P40582	UniProtKB	Chain	1	234	.	.	.	ID=PRO_0000185987;Note=Glutathione S-transferase 1	
+P40582	UniProtKB	Domain	3	90	.	.	.	Note=GST N-terminal	
+P40582	UniProtKB	Domain	96	234	.	.	.	Note=GST C-terminal	
+##sequence-region Q12390 1 233
+Q12390	UniProtKB	Chain	1	233	.	.	.	ID=PRO_0000185988;Note=Glutathione S-transferase 2	
+Q12390	UniProtKB	Domain	17	101	.	.	.	Note=GST N-terminal	
+Q12390	UniProtKB	Domain	106	233	.	.	.	Note=GST C-terminal	
+Q12390	UniProtKB	Region	85	86	.	.	.	Note=Glutathione binding	
+Q12390	UniProtKB	Binding site	29	29	.	.	.	Note=Glutathione%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333	
+Q12390	UniProtKB	Binding site	58	58	.	.	.	Note=Glutathione;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333	
+Q12390	UniProtKB	Binding site	72	72	.	.	.	Note=Glutathione%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333	
+Q12390	UniProtKB	Binding site	133	133	.	.	.	Note=Glutathione;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333	
+Q12390	UniProtKB	Mutagenesis	27	27	.	.	.	Note=Reduced enzyme activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333	
+Q12390	UniProtKB	Mutagenesis	27	27	.	.	.	Note=Loss of enzyme activity. G->C%2CF%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333	
+Q12390	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Reduced enzyme activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333	
+Q12390	UniProtKB	Mutagenesis	133	133	.	.	.	Note=Loss of enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333	
+Q12390	UniProtKB	Beta strand	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	28	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Beta strand	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	61	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Beta strand	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	86	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	107	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	125	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Turn	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	149	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Beta strand	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	183	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	207	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+Q12390	UniProtKB	Helix	220	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH	
+##sequence-region P32806 1 458
+P32806	UniProtKB	Chain	1	458	.	.	.	ID=PRO_0000208013;Note=GTPase-activating protein GYP6	
+P32806	UniProtKB	Domain	33	316	.	.	.	Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163	
+P32806	UniProtKB	Modified residue	436	436	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32806	UniProtKB	Sequence conflict	413	413	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43570 1 497
+P43570	UniProtKB	Chain	1	497	.	.	.	ID=PRO_0000208018;Note=GTPase-activating protein GYP8	
+P43570	UniProtKB	Domain	69	281	.	.	.	Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163	
+##sequence-region Q96VH4 1 193
+Q96VH4	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q96VH4	UniProtKB	Chain	2	193	.	.	.	ID=PRO_0000248448;Note=Putative nitroreductase HBN1	
+Q96VH4	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q12096 1 491
+Q12096	UniProtKB	Chain	1	491	.	.	.	ID=PRO_0000087536;Note=Glucose N-acetyltransferase 1	
+Q12096	UniProtKB	Topological domain	1	10	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12096	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12096	UniProtKB	Topological domain	32	491	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12096	UniProtKB	Motif	198	200	.	.	.	Note=DXD	
+Q12096	UniProtKB	Glycosylation	136	136	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12096	UniProtKB	Glycosylation	177	177	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12096	UniProtKB	Glycosylation	187	187	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12096	UniProtKB	Glycosylation	425	425	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46984 1 123
+P46984	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000203021;Note=EKC/KEOPS complex subunit GON7	
+P46984	UniProtKB	Beta strand	6	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA	
+P46984	UniProtKB	Turn	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA	
+P46984	UniProtKB	Beta strand	14	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA	
+P46984	UniProtKB	Helix	66	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA	
+P46984	UniProtKB	Helix	99	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA	
+##sequence-region P53130 1 126
+P53130	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000202745;Note=Heterotrimeric G protein gamma subunit GPG1	
+##sequence-region P23797 1 304
+P23797	UniProtKB	Chain	1	304	.	.	.	ID=PRO_0000207170;Note=N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase	
+P23797	UniProtKB	Topological domain	1	20	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23797	UniProtKB	Transmembrane	21	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23797	UniProtKB	Topological domain	39	304	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04080 1 534
+Q04080	UniProtKB	Chain	1	534	.	.	.	ID=PRO_0000218608;Note=GPI transamidase component GPI17	
+Q04080	UniProtKB	Topological domain	1	8	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04080	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04080	UniProtKB	Topological domain	30	472	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04080	UniProtKB	Transmembrane	473	493	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04080	UniProtKB	Topological domain	494	534	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04080	UniProtKB	Glycosylation	100	100	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04080	UniProtKB	Glycosylation	170	170	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04080	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04080	UniProtKB	Glycosylation	247	247	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04080	UniProtKB	Glycosylation	299	299	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38211 1 433
+P38211	UniProtKB	Chain	1	433	.	.	.	ID=PRO_0000014309;Note=GPI mannosyltransferase 2	
+P38211	UniProtKB	Topological domain	1	1	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Transmembrane	2	22	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Topological domain	23	109	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Topological domain	131	161	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Transmembrane	162	182	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Topological domain	183	215	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Topological domain	237	243	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Transmembrane	244	264	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Topological domain	265	318	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Transmembrane	319	339	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Topological domain	340	350	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Transmembrane	351	371	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Topological domain	372	409	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Transmembrane	410	430	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Topological domain	431	433	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Glycosylation	69	69	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Glycosylation	101	101	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38211	UniProtKB	Sequence conflict	187	187	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38211	UniProtKB	Sequence conflict	187	187	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40367 1 830
+P40367	UniProtKB	Signal peptide	1	32	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Chain	33	830	.	.	.	ID=PRO_0000203059;Note=GPI ethanolamine phosphate transferase 2	
+P40367	UniProtKB	Topological domain	33	321	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Transmembrane	322	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Topological domain	343	405	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Transmembrane	406	426	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Topological domain	427	439	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Transmembrane	440	460	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Topological domain	461	469	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Transmembrane	470	490	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Topological domain	491	533	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Transmembrane	534	554	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Topological domain	555	598	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Transmembrane	599	619	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Topological domain	620	651	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Transmembrane	652	672	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Topological domain	673	682	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Transmembrane	683	703	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Topological domain	704	724	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Transmembrane	725	745	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Topological domain	746	768	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Transmembrane	769	789	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Topological domain	790	805	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Transmembrane	806	826	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Topological domain	827	830	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Glycosylation	145	145	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Glycosylation	185	185	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Glycosylation	298	298	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Glycosylation	506	506	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40367	UniProtKB	Mutagenesis	153	154	.	.	.	Note=In GPI7-2%3B temperature-sensitive mutant that shows defects in cell separation and a daughter cell-specific growth defect. DD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15452134;Dbxref=PMID:15452134	
+##sequence-region P47122 1 385
+P47122	UniProtKB	Chain	1	385	.	.	.	ID=PRO_0000203101;Note=GPN-loop GTPase 1	
+P47122	UniProtKB	Nucleotide binding	13	18	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+P47122	UniProtKB	Nucleotide binding	173	176	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+P47122	UniProtKB	Motif	70	72	.	.	.	Note=Gly-Pro-Asn (GPN)-loop%3B involved in dimer interface;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+P47122	UniProtKB	Site	72	72	.	.	.	Note=Stabilizes the phosphate intermediate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9	
+P47122	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47122	UniProtKB	Modified residue	308	308	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47122	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47122	UniProtKB	Modified residue	352	352	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47122	UniProtKB	Cross-link	369	369	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P47122	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Impairs nuclear localization of RNAPII. Completely abolishes RNAPII binding. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21844196;Dbxref=PMID:21844196	
+P47122	UniProtKB	Mutagenesis	110	110	.	.	.	Note=Impairs nuclear localization of RNAPII%2C but does not impair RNAPII binding. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21844196;Dbxref=PMID:21844196	
+P47122	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Impairs heterodimer formation with GPN2 and GPN3. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23324351;Dbxref=PMID:23324351	
+P47122	UniProtKB	Beta strand	4	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Helix	16	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Beta strand	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Beta strand	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Turn	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Helix	60	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCI	
+P47122	UniProtKB	Helix	73	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Helix	86	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Turn	96	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Beta strand	101	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Helix	112	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Helix	118	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Beta strand	133	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Helix	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Helix	147	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Beta strand	168	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Helix	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Helix	182	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Helix	216	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Beta strand	232	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Turn	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+P47122	UniProtKB	Helix	245	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN	
+##sequence-region P38143 1 162
+P38143	UniProtKB	Chain	1	162	.	.	.	ID=PRO_0000066642;Note=Glutathione peroxidase-like peroxiredoxin 2	
+P38143	UniProtKB	Active site	37	37	.	.	.	Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16251189;Dbxref=PMID:16251189	
+P38143	UniProtKB	Disulfide bond	37	83	.	.	.	Note=Redox-active;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16251189;Dbxref=PMID:16251189	
+P38143	UniProtKB	Mutagenesis	37	37	.	.	.	Note=Prevents oxidation of the protein. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16251189;Dbxref=PMID:16251189	
+P38143	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Prevents oxidation of the protein. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16251189;Dbxref=PMID:16251189	
+##sequence-region Q12068 1 342
+Q12068	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000215576;Note=NADPH-dependent methylglyoxal reductase GRE2	
+Q12068	UniProtKB	Nucleotide binding	7	12	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127	
+Q12068	UniProtKB	Nucleotide binding	57	58	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127	
+Q12068	UniProtKB	Active site	169	169	.	.	.	Note=Proton donor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24879127;Dbxref=PMID:24879127	
+Q12068	UniProtKB	Binding site	32	32	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127	
+Q12068	UniProtKB	Binding site	36	36	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127	
+Q12068	UniProtKB	Binding site	165	165	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127	
+Q12068	UniProtKB	Binding site	169	169	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127	
+Q12068	UniProtKB	Binding site	199	199	.	.	.	Note=NADP%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127	
+Q12068	UniProtKB	Binding site	216	216	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127	
+Q12068	UniProtKB	Modified residue	333	333	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12068	UniProtKB	Mutagenesis	9	9	.	.	.	Note=Alters cofactor preference of the enzyme to be able to use as well NAD instead of NADP. N->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20480039;Dbxref=PMID:20480039	
+Q12068	UniProtKB	Beta strand	3	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Turn	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	11	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	27	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	34	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	50	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Turn	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	65	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Turn	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	97	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Turn	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	121	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	156	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	161	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Turn	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	190	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	198	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	206	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	215	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	236	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	242	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Turn	257	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	268	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	272	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Turn	284	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Turn	299	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Beta strand	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	311	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+Q12068	UniProtKB	Helix	324	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC	
+##sequence-region Q08220 1 491
+Q08220	UniProtKB	Chain	1	491	.	.	.	ID=PRO_0000211266;Note=Glutathione synthetase	
+Q08220	UniProtKB	Nucleotide binding	382	391	.	.	.	Note=ATP	
+Q08220	UniProtKB	Nucleotide binding	415	418	.	.	.	Note=ATP	
+Q08220	UniProtKB	Region	150	153	.	.	.	Note=Substrate binding	
+Q08220	UniProtKB	Region	228	230	.	.	.	Note=Substrate binding	
+Q08220	UniProtKB	Region	285	288	.	.	.	Note=Substrate binding	
+Q08220	UniProtKB	Region	478	479	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08220	UniProtKB	Metal binding	146	146	.	.	.	Note=Magnesium	
+Q08220	UniProtKB	Metal binding	148	148	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08220	UniProtKB	Metal binding	386	386	.	.	.	Note=Magnesium	
+Q08220	UniProtKB	Binding site	128	128	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12467574;Dbxref=PMID:12467574	
+Q08220	UniProtKB	Binding site	146	146	.	.	.	Note=ATP	
+Q08220	UniProtKB	Binding site	234	234	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12467574;Dbxref=PMID:12467574	
+Q08220	UniProtKB	Binding site	324	324	.	.	.	Note=ATP	
+Q08220	UniProtKB	Binding site	393	393	.	.	.	Note=ATP	
+Q08220	UniProtKB	Binding site	442	442	.	.	.	Note=ATP	
+Q08220	UniProtKB	Binding site	467	467	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08220	UniProtKB	Binding site	469	469	.	.	.	Note=ATP	
+Q08220	UniProtKB	Binding site	475	475	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08220	UniProtKB	Helix	8	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	40	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	55	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	85	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Turn	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	101	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	123	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	139	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	155	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	191	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	219	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	231	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	249	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	254	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Turn	265	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Turn	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	278	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	296	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	308	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	316	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	324	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	333	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Turn	337	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	343	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	356	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	360	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	363	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	376	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	379	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	394	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	397	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Helix	406	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	412	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	428	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	433	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	439	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	456	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	472	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	477	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	483	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+Q08220	UniProtKB	Beta strand	488	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W	
+##sequence-region Q04806 1 366
+Q04806	UniProtKB	Chain	1	366	.	.	.	ID=PRO_0000203338;Note=Glutathione S-transferase omega-like 3	
+Q04806	UniProtKB	Domain	197	349	.	.	.	Note=GST C-terminal	
+Q04806	UniProtKB	Active site	46	46	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P40956 1 396
+P40956	UniProtKB	Chain	1	396	.	.	.	ID=PRO_0000074226;Note=Protein GTS1	
+P40956	UniProtKB	Domain	14	141	.	.	.	Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+P40956	UniProtKB	Domain	193	234	.	.	.	Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
+P40956	UniProtKB	Zinc finger	30	53	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+P40956	UniProtKB	Compositional bias	234	237	.	.	.	Note=Poly-Ser	
+P40956	UniProtKB	Compositional bias	311	396	.	.	.	Note=Gln-rich	
+P40956	UniProtKB	Compositional bias	319	327	.	.	.	Note=Poly-Gln	
+P40956	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40956	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40956	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P40956	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40956	UniProtKB	Modified residue	240	240	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40956	UniProtKB	Modified residue	249	249	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38625 1 525
+P38625	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7483834;Dbxref=PMID:7483834	
+P38625	UniProtKB	Chain	2	525	.	.	.	ID=PRO_0000140258;Note=GMP synthase [glutamine-hydrolyzing]	
+P38625	UniProtKB	Domain	13	202	.	.	.	Note=Glutamine amidotransferase type-1	
+P38625	UniProtKB	Domain	203	400	.	.	.	Note=GMPS ATP-PPase	
+P38625	UniProtKB	Nucleotide binding	231	237	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38625	UniProtKB	Active site	89	89	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38625	UniProtKB	Active site	176	176	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38625	UniProtKB	Active site	178	178	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38625	UniProtKB	Cross-link	241	241	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38625	UniProtKB	Cross-link	426	426	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38625	UniProtKB	Sequence conflict	325	325	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P46943 1 645
+P46943	UniProtKB	Chain	1	645	.	.	.	ID=PRO_0000091560;Note=Translation factor GUF1%2C mitochondrial	
+P46943	UniProtKB	Domain	44	228	.	.	.	Note=tr-type G	
+P46943	UniProtKB	Nucleotide binding	53	60	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03137	
+P46943	UniProtKB	Nucleotide binding	120	124	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03137	
+P46943	UniProtKB	Nucleotide binding	174	177	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03137	
+P46943	UniProtKB	Sequence conflict	260	260	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46943	UniProtKB	Sequence conflict	354	354	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46943	UniProtKB	Sequence conflict	374	374	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46943	UniProtKB	Sequence conflict	559	559	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P42944 1 551
+P42944	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000083488;Note=Protein GZF3	
+P42944	UniProtKB	Zinc finger	131	155	.	.	.	Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094	
+##sequence-region Q12180 1 1030
+Q12180	UniProtKB	Chain	1	1030	.	.	.	ID=PRO_0000233012;Note=Halotolerance protein 9	
+Q12180	UniProtKB	DNA binding	136	166	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+Q12180	UniProtKB	Modified residue	221	221	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12180	UniProtKB	Modified residue	937	937	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q05580 1 639
+Q05580	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q05580	UniProtKB	Chain	2	639	.	.	.	ID=PRO_0000253811;Note=E3 ubiquitin-protein ligase HEL2	
+Q05580	UniProtKB	Domain	222	292	.	.	.	Note=LIM zinc-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125	
+Q05580	UniProtKB	Zinc finger	64	104	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q05580	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q05580	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q05580	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P36014 1 167
+P36014	UniProtKB	Chain	1	167	.	.	.	ID=PRO_0000066641;Note=Glutathione peroxidase-like peroxiredoxin 1	
+P36014	UniProtKB	Active site	36	36	.	.	.	Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:20572871,ECO:0000305|PubMed:22659048;Dbxref=PMID:20572871,PMID:22659048	
+P36014	UniProtKB	Disulfide bond	36	82	.	.	.	Note=Redox-active;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20572871;Dbxref=PMID:20572871	
+P36014	UniProtKB	Mutagenesis	36	36	.	.	.	Note=Prevents oxidation of the protein. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20572871;Dbxref=PMID:20572871	
+##sequence-region Q07845 1 632
+Q07845	UniProtKB	Chain	1	632	.	.	.	ID=PRO_0000087597;Note=Polynucleotide 5'-hydroxyl-kinase GRC3	
+Q07845	UniProtKB	Nucleotide binding	246	253	.	.	.	Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q07845	UniProtKB	Mutagenesis	252	252	.	.	.	Note=Abolishes kinase activity and termination by RNA polymerase I. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20814424;Dbxref=PMID:20814424	
+Q07845	UniProtKB	Mutagenesis	253	253	.	.	.	Note=Abolishes kinase activity and termination by RNA polymerase I. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20814424;Dbxref=PMID:20814424	
+##sequence-region P47026 1 490
+P47026	UniProtKB	Chain	1	490	.	.	.	ID=PRO_0000215188;Note=GPI-anchored wall transfer protein 1	
+P47026	UniProtKB	Topological domain	1	19	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	41	54	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	76	76	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	98	128	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	129	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	150	157	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	158	178	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	179	199	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	221	231	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	253	257	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	258	278	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	279	301	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	302	322	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	323	356	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	357	377	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	378	390	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	391	411	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	412	435	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	436	456	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	457	460	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Transmembrane	461	481	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Topological domain	482	490	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47026	UniProtKB	Mutagenesis	8	8	.	.	.	Note=In gwt1-10%3B impairs the transport of detergent-resistant microdomain-associated membrane proteins TAT2 and FUR4. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16361252;Dbxref=PMID:16361252	
+P47026	UniProtKB	Mutagenesis	63	64	.	.	.	Note=In gwt1-20%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins. WV->RA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589	
+P47026	UniProtKB	Mutagenesis	132	132	.	.	.	Note=Resistant to the drug 1-[4-butylbenzyl]isoquinoline (BIQ). G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12753194;Dbxref=PMID:12753194	
+P47026	UniProtKB	Mutagenesis	209	209	.	.	.	Note=In gwt1-28%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins%3B when associated with D-259. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589	
+P47026	UniProtKB	Mutagenesis	259	259	.	.	.	Note=In gwt1-28%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins%3B when associated with P-209. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589	
+P47026	UniProtKB	Mutagenesis	330	330	.	.	.	Note=In gwt1-16%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins%3B when associated with P-362 and A-479. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589	
+P47026	UniProtKB	Mutagenesis	362	362	.	.	.	Note=In gwt1-16%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins%3B when associated with S-330 and A-479. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589	
+P47026	UniProtKB	Mutagenesis	397	397	.	.	.	Note=Resistant to the drug 1-[4-butylbenzyl]isoquinoline (BIQ). V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12753194;Dbxref=PMID:12753194	
+P47026	UniProtKB	Mutagenesis	479	479	.	.	.	Note=In gwt1-16%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins%3B when associated with S-330 and P-362. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589	
+##sequence-region P53258 1 950
+P53258	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53258	UniProtKB	Chain	2	950	.	.	.	ID=PRO_0000208011;Note=GTPase-activating protein GYP2	
+P53258	UniProtKB	Domain	29	116	.	.	.	Note=GRAM	
+P53258	UniProtKB	Domain	244	432	.	.	.	Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163	
+P53258	UniProtKB	Domain	602	637	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53258	UniProtKB	Domain	638	673	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53258	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53258	UniProtKB	Modified residue	764	764	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53258	UniProtKB	Modified residue	871	871	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region Q12344 1 894
+Q12344	UniProtKB	Chain	1	894	.	.	.	ID=PRO_0000240365;Note=GTPase-activating protein GYP5	
+Q12344	UniProtKB	Domain	451	630	.	.	.	Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163	
+Q12344	UniProtKB	Coiled coil	732	872	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12344	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12344	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12344	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12344	UniProtKB	Modified residue	389	389	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12344	UniProtKB	Mutagenesis	496	496	.	.	.	Note=Loss of GAP activity. R->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12189143;Dbxref=PMID:12189143	
+##sequence-region P27472 1 705
+P27472	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23337	
+P27472	UniProtKB	Chain	2	705	.	.	.	ID=PRO_0000194774;Note=Glycogen [starch] synthase isoform 2	
+P27472	UniProtKB	Binding site	20	20	.	.	.	Note=UDP-glucose;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27472	UniProtKB	Modified residue	159	159	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27472	UniProtKB	Modified residue	363	363	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27472	UniProtKB	Modified residue	467	467	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P27472	UniProtKB	Modified residue	651	651	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P27472	UniProtKB	Modified residue	655	655	.	.	.	Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:9584169;Dbxref=PMID:15665377,PMID:18407956,PMID:9584169	
+P27472	UniProtKB	Modified residue	661	661	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27472	UniProtKB	Modified residue	663	663	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27472	UniProtKB	Modified residue	668	668	.	.	.	Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9584169;Dbxref=PMID:9584169	
+P27472	UniProtKB	Sequence conflict	248	248	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27472	UniProtKB	Sequence conflict	535	535	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27472	UniProtKB	Sequence conflict	622	622	.	.	.	Note=F->FF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27472	UniProtKB	Beta strand	4	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Turn	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	23	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	43	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Turn	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	54	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KQM	
+P27472	UniProtKB	Helix	74	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Turn	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	90	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	102	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	109	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	115	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	135	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	160	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	175	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	187	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	196	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	209	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	218	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	228	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	241	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	249	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	264	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	273	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NCH	
+P27472	UniProtKB	Helix	281	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Turn	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	309	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	312	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Turn	323	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	328	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	350	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	361	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	366	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Turn	400	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KQ2	
+P27472	UniProtKB	Beta strand	407	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	413	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	419	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	442	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	450	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	454	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	471	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	486	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	492	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	500	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	507	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	513	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	525	528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	532	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	543	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	551	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Beta strand	557	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	561	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	580	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	593	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	599	617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	619	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+P27472	UniProtKB	Helix	635	638	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0	
+##sequence-region Q06201 1 188
+Q06201	UniProtKB	Chain	1	188	.	.	.	ID=PRO_0000247355;Note=Grand meiotic recombination cluster protein 2	
+##sequence-region P36125 1 273
+P36125	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36125	UniProtKB	Chain	2	273	.	.	.	ID=PRO_0000203205;Note=Protein GMH1	
+P36125	UniProtKB	Topological domain	2	89	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36125	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36125	UniProtKB	Topological domain	111	134	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36125	UniProtKB	Transmembrane	135	155	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36125	UniProtKB	Topological domain	156	175	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36125	UniProtKB	Transmembrane	176	196	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36125	UniProtKB	Topological domain	197	216	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36125	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36125	UniProtKB	Topological domain	238	242	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36125	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36125	UniProtKB	Topological domain	264	273	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36125	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P41911 1 440
+P41911	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41911	UniProtKB	Chain	17	440	.	.	.	ID=PRO_0000043410;Note=Glycerol-3-phosphate dehydrogenase [NAD(+)] 2%2C mitochondrial	
+P41911	UniProtKB	Nucleotide binding	90	95	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41911	UniProtKB	Region	359	360	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41911	UniProtKB	Active site	294	294	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41911	UniProtKB	Binding site	178	178	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41911	UniProtKB	Binding site	201	201	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41911	UniProtKB	Binding site	201	201	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41911	UniProtKB	Binding site	234	234	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41911	UniProtKB	Binding site	359	359	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41911	UniProtKB	Binding site	388	388	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41911	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P41911	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P41911	UniProtKB	Modified residue	75	75	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P53961 1 229
+P53961	UniProtKB	Chain	1	229	.	.	.	ID=PRO_0000087556;Note=Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15	
+P53961	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53961	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53961	UniProtKB	Sequence conflict	10	10	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P49018 1 411
+P49018	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49018	UniProtKB	Chain	23	411	.	.	.	ID=PRO_0000026532;Note=GPI-anchor transamidase	
+P49018	UniProtKB	Topological domain	23	376	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49018	UniProtKB	Transmembrane	377	397	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49018	UniProtKB	Topological domain	398	411	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49018	UniProtKB	Active site	157	157	.	.	.	.	
+P49018	UniProtKB	Active site	199	199	.	.	.	.	
+P49018	UniProtKB	Glycosylation	256	256	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49018	UniProtKB	Glycosylation	346	346	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49018	UniProtKB	Disulfide bond	85	85	.	.	.	Note=Interchain (with C-194 in GPI16);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49018	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Partial loss of activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10727241;Dbxref=PMID:10727241	
+P49018	UniProtKB	Mutagenesis	60	60	.	.	.	Note=No loss of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10727241;Dbxref=PMID:10727241	
+P49018	UniProtKB	Mutagenesis	60	60	.	.	.	Note=No loss of activity. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10727241;Dbxref=PMID:10727241	
+P49018	UniProtKB	Mutagenesis	85	85	.	.	.	Note=No loss of activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10727241;Dbxref=PMID:10727241	
+P49018	UniProtKB	Mutagenesis	157	157	.	.	.	Note=Loss of activity. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10727241,ECO:0000269|PubMed:10793132;Dbxref=PMID:10727241,PMID:10793132	
+P49018	UniProtKB	Mutagenesis	199	199	.	.	.	Note=Loss of activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10727241,ECO:0000269|PubMed:10793132;Dbxref=PMID:10727241,PMID:10793132	
+##sequence-region P16474 1 682
+P16474	UniProtKB	Signal peptide	1	42	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16474	UniProtKB	Chain	43	682	.	.	.	ID=PRO_0000013587;Note=78 kDa glucose-regulated protein homolog	
+P16474	UniProtKB	Motif	679	682	.	.	.	Note=Prevents secretion from ER	
+P16474	UniProtKB	Beta strand	53	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	59	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	99	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Turn	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	127	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	137	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	146	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	162	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	187	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	198	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	214	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	221	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Turn	229	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	238	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	250	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	261	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	275	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+P16474	UniProtKB	Helix	302	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Turn	319	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	323	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	336	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	344	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	359	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	378	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	384	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	389	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Turn	399	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Turn	410	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Helix	413	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU	
+P16474	UniProtKB	Beta strand	444	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Turn	449	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Beta strand	452	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Beta strand	462	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Beta strand	481	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Helix	493	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Beta strand	496	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Beta strand	517	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Beta strand	527	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Turn	536	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Beta strand	541	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Helix	555	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+P16474	UniProtKB	Helix	569	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X	
+##sequence-region P32477 1 678
+P32477	UniProtKB	Chain	1	678	.	.	.	ID=PRO_0000192572;Note=Glutamate--cysteine ligase	
+P32477	UniProtKB	Sequence conflict	299	299	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32477	UniProtKB	Sequence conflict	492	492	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32477	UniProtKB	Sequence conflict	526	527	.	.	.	Note=IL->MV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32477	UniProtKB	Sequence conflict	542	542	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32477	UniProtKB	Sequence conflict	550	550	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32477	UniProtKB	Helix	12	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	19	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	46	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Turn	60	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Turn	78	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	83	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	91	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	101	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	117	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	149	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Turn	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	168	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Turn	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	196	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	214	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	244	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	252	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	259	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	266	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	276	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	289	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	306	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	314	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Turn	326	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Turn	336	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	348	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	361	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	388	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	404	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	423	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Turn	430	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	435	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	447	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	467	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	480	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Turn	500	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	510	519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	525	528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	530	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	537	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LVV	
+P32477	UniProtKB	Beta strand	545	549	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	550	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Turn	557	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	561	564	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	566	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	580	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Turn	587	589	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LVV	
+P32477	UniProtKB	Helix	590	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	610	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Beta strand	626	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	632	646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+P32477	UniProtKB	Helix	650	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LVV	
+P32477	UniProtKB	Helix	654	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5	
+##sequence-region P48239 1 356
+P48239	UniProtKB	Chain	1	356	.	.	.	ID=PRO_0000202833;Note=Glutathione S-transferase omega-like 1	
+P48239	UniProtKB	Coiled coil	214	257	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48239	UniProtKB	Active site	31	31	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P36156 1 370
+P36156	UniProtKB	Chain	1	370	.	.	.	ID=PRO_0000086922;Note=Glutathione S-transferase omega-like 2	
+P36156	UniProtKB	Domain	201	353	.	.	.	Note=GST C-terminal	
+P36156	UniProtKB	Active site	46	46	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151	
+P36156	UniProtKB	Mutagenesis	46	46	.	.	.	Note=Completely inactive as thiol transferase. No activity recovered against 1-chloro-2%2C4-dinitrobenzene (CDNB). C->S%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151	
+P36156	UniProtKB	Mutagenesis	51	51	.	.	.	Note=No effect on thiol transferase activity. No effect on thiol transferase activity%3B when associated with D-173. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151	
+P36156	UniProtKB	Mutagenesis	173	173	.	.	.	Note=No effect on thiol transferase activity. E->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151	
+P36156	UniProtKB	Mutagenesis	174	174	.	.	.	Note=No effect on thiol transferase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151	
+P36156	UniProtKB	Mutagenesis	246	246	.	.	.	Note=No effect on thiol transferase activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151	
+P36156	UniProtKB	Mutagenesis	280	280	.	.	.	Note=No effect on thiol transferase activity. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151	
+P36156	UniProtKB	Mutagenesis	287	287	.	.	.	Note=Abolishes thiol transferase activity. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151	
+P36156	UniProtKB	Beta strand	37	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	47	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Turn	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Beta strand	65	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Turn	101	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	106	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKD	
+P36156	UniProtKB	Turn	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Turn	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	141	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Beta strand	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Turn	164	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Beta strand	168	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	174	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	184	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	192	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Turn	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	205	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Turn	219	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	222	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	232	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	269	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	285	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Turn	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	301	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	312	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	317	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	331	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Helix	339	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Turn	351	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+P36156	UniProtKB	Beta strand	363	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB	
+##sequence-region P00815 1 799
+P00815	UniProtKB	Chain	1	799	.	.	.	ID=PRO_0000135914;Note=Histidine biosynthesis trifunctional protein	
+P00815	UniProtKB	Region	1	229	.	.	.	Note=Phosphoribosyl-AMP cyclohydrolase	
+P00815	UniProtKB	Region	230	312	.	.	.	Note=Phosphoribosyl-ATP pyrophosphohydrolase	
+P00815	UniProtKB	Region	313	799	.	.	.	Note=Histidinol dehydrogenase	
+P00815	UniProtKB	Active site	687	687	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00815	UniProtKB	Active site	688	688	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00815	UniProtKB	Metal binding	618	618	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00815	UniProtKB	Metal binding	621	621	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00815	UniProtKB	Metal binding	721	721	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00815	UniProtKB	Metal binding	780	780	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00815	UniProtKB	Sequence conflict	53	53	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00815	UniProtKB	Sequence conflict	386	386	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00815	UniProtKB	Sequence conflict	402	403	.	.	.	Note=AL->VF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00815	UniProtKB	Sequence conflict	441	441	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00815	UniProtKB	Sequence conflict	794	794	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53187 1 214
+P53187	UniProtKB	Chain	1	214	.	.	.	ID=PRO_0000084027;Note=Homologous-pairing protein 2	
+P53187	UniProtKB	Coiled coil	97	160	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53187	UniProtKB	Sequence conflict	71	71	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12214 1 470
+Q12214	UniProtKB	Chain	1	470	.	.	.	ID=PRO_0000114726;Note=Histone deacetylase HOS1	
+Q12214	UniProtKB	Region	47	392	.	.	.	Note=Histone deacetylase	
+Q12214	UniProtKB	Active site	211	211	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12214	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q01448 1 625
+Q01448	UniProtKB	Chain	1	625	.	.	.	ID=PRO_0000084039;Note=Histone promoter control protein 2	
+Q01448	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q01448	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q01448	UniProtKB	Modified residue	435	435	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q05905 1 244
+Q05905	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000245329;Note=Protein HRI1	
+Q05905	UniProtKB	Modified residue	143	143	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q05905	UniProtKB	Beta strand	3	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	32	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Turn	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	50	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	61	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	67	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Helix	81	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	95	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	107	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	123	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	155	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	165	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	175	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Helix	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	191	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	204	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Helix	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	229	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+Q05905	UniProtKB	Beta strand	235	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY	
+##sequence-region Q05549 1 1077
+Q05549	UniProtKB	Chain	1	1077	.	.	.	ID=PRO_0000253813;Note=ATP-dependent helicase HRQ1	
+Q05549	UniProtKB	Domain	299	483	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q05549	UniProtKB	Domain	521	678	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q05549	UniProtKB	Nucleotide binding	312	319	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q05549	UniProtKB	Motif	423	426	.	.	.	Note=DEAH box	
+Q05549	UniProtKB	Mutagenesis	318	318	.	.	.	Note=Impairs helicase and ATPase activities. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23026052,ECO:0000269|PubMed:24682993;Dbxref=PMID:23026052,PMID:24682993	
+##sequence-region P09950 1 548
+P09950	UniProtKB	Transit peptide	1	22	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P09950	UniProtKB	Chain	23	548	.	.	.	ID=PRO_0000001245;Note=5-aminolevulinate synthase%2C mitochondrial	
+P09950	UniProtKB	Compositional bias	26	62	.	.	.	Note=Ala-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00001	
+P09950	UniProtKB	Active site	337	337	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079	
+P09950	UniProtKB	Binding site	91	91	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079	
+P09950	UniProtKB	Binding site	204	204	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079	
+P09950	UniProtKB	Binding site	223	223	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079	
+P09950	UniProtKB	Binding site	256	256	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079	
+P09950	UniProtKB	Binding site	284	284	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079	
+P09950	UniProtKB	Binding site	334	334	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079	
+P09950	UniProtKB	Binding site	366	366	.	.	.	Note=Pyridoxal phosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079	
+P09950	UniProtKB	Binding site	367	367	.	.	.	Note=Pyridoxal phosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079	
+P09950	UniProtKB	Binding site	452	452	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079	
+P09950	UniProtKB	Modified residue	337	337	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079	
+P09950	UniProtKB	Mutagenesis	275	275	.	.	.	Note=Lethal in combination with a MCX1 disruption. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25957689;Dbxref=PMID:25957689	
+P09950	UniProtKB	Sequence conflict	181	181	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P28789 1 327
+P28789	UniProtKB	Chain	1	327	.	.	.	ID=PRO_0000143045;Note=Porphobilinogen deaminase	
+P28789	UniProtKB	Modified residue	251	251	.	.	.	Note=S-(dipyrrolylmethanemethyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12276 1 1246
+Q12276	UniProtKB	Chain	1	1246	.	.	.	ID=PRO_0000237668;Note=HMG2-induced ER-remodeling protein 1	
+Q12276	UniProtKB	Compositional bias	139	283	.	.	.	Note=Ser-rich	
+Q12276	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12276	UniProtKB	Modified residue	128	128	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q12276	UniProtKB	Modified residue	277	277	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12276	UniProtKB	Modified residue	1013	1013	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12276	UniProtKB	Modified residue	1130	1130	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12276	UniProtKB	Modified residue	1200	1200	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12276	UniProtKB	Modified residue	1204	1204	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12276	UniProtKB	Modified residue	1207	1207	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P41809 1 1802
+P41809	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41809	UniProtKB	Chain	22	1802	.	.	.	ID=PRO_0000021444;Note=Signaling mucin HKR1	
+P41809	UniProtKB	Topological domain	22	1485	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41809	UniProtKB	Transmembrane	1486	1506	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41809	UniProtKB	Topological domain	1507	1802	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41809	UniProtKB	Repeat	453	480	.	.	.	Note=1%3B approximate	
+P41809	UniProtKB	Repeat	481	508	.	.	.	Note=2	
+P41809	UniProtKB	Repeat	509	536	.	.	.	Note=3	
+P41809	UniProtKB	Repeat	537	564	.	.	.	Note=4	
+P41809	UniProtKB	Repeat	565	592	.	.	.	Note=5	
+P41809	UniProtKB	Repeat	593	620	.	.	.	Note=6	
+P41809	UniProtKB	Repeat	621	648	.	.	.	Note=7	
+P41809	UniProtKB	Repeat	649	676	.	.	.	Note=8	
+P41809	UniProtKB	Repeat	677	704	.	.	.	Note=9	
+P41809	UniProtKB	Repeat	705	732	.	.	.	Note=10	
+P41809	UniProtKB	Repeat	733	760	.	.	.	Note=11	
+P41809	UniProtKB	Repeat	761	788	.	.	.	Note=12	
+P41809	UniProtKB	Region	453	788	.	.	.	Note=12 X 28 AA tandem repeats of S-[AV]-[P]-V-A-V-S-S-T-Y-T-S-S-P-S-A-P-A-A-I-S-S-T-Y-T-S-S-P	
+P41809	UniProtKB	Compositional bias	23	1478	.	.	.	Note=Ser/Thr-rich	
+P41809	UniProtKB	Glycosylation	24	24	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41809	UniProtKB	Glycosylation	1252	1252	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41809	UniProtKB	Glycosylation	1293	1293	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41809	UniProtKB	Glycosylation	1342	1342	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41809	UniProtKB	Glycosylation	1400	1400	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41809	UniProtKB	Sequence conflict	582	582	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41809	UniProtKB	Sequence conflict	594	594	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CY07 1 175
+P0CY07	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000410462;Note=Silenced mating-type protein ALPHA1	
+P0CY07	UniProtKB	DNA binding	88	144	.	.	.	Note=Alpha box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00655	
+##sequence-region P54839 1 491
+P54839	UniProtKB	Chain	1	491	.	.	.	ID=PRO_0000213758;Note=Hydroxymethylglutaryl-CoA synthase	
+P54839	UniProtKB	Active site	127	127	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10116	
+P54839	UniProtKB	Active site	159	159	.	.	.	Note=Acyl-thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10116	
+P54839	UniProtKB	Active site	296	296	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10116	
+P54839	UniProtKB	Modified residue	276	276	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P40480 1 1083
+P40480	UniProtKB	Chain	1	1083	.	.	.	ID=PRO_0000066998;Note=Protein HOS4	
+P40480	UniProtKB	Repeat	329	359	.	.	.	Note=ANK 1	
+P40480	UniProtKB	Repeat	363	392	.	.	.	Note=ANK 2	
+P40480	UniProtKB	Repeat	398	427	.	.	.	Note=ANK 3	
+P40480	UniProtKB	Repeat	532	561	.	.	.	Note=ANK 4	
+P40480	UniProtKB	Repeat	593	622	.	.	.	Note=ANK 5	
+P40480	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40480	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40480	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40480	UniProtKB	Modified residue	67	67	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40480	UniProtKB	Modified residue	290	290	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40480	UniProtKB	Modified residue	507	507	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40480	UniProtKB	Modified residue	698	698	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40480	UniProtKB	Modified residue	700	700	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40480	UniProtKB	Modified residue	778	778	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P48570 1 428
+P48570	UniProtKB	Chain	1	428	.	.	.	ID=PRO_0000140454;Note=Homocitrate synthase%2C cytosolic isozyme	
+P48570	UniProtKB	Domain	23	276	.	.	.	Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151	
+P48570	UniProtKB	Modified residue	385	385	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48570	UniProtKB	Modified residue	396	396	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P48570	UniProtKB	Modified residue	401	401	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P48570	UniProtKB	Modified residue	410	410	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P36078 1 116
+P36078	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000203165;Note=Helper of Tim protein 13	
+P36078	UniProtKB	Zinc finger	10	94	.	.	.	Note=CHY-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00601	
+P36078	UniProtKB	Sequence conflict	71	71	.	.	.	Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99332 1 602
+Q99332	UniProtKB	Chain	1	602	.	.	.	ID=PRO_0000227934;Note=Protein HPH1	
+Q99332	UniProtKB	Transmembrane	575	595	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99332	UniProtKB	Compositional bias	163	420	.	.	.	Note=Ser-rich	
+Q99332	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q99332	UniProtKB	Modified residue	342	342	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P17629 1 752
+P17629	UniProtKB	Chain	1	752	.	.	.	ID=PRO_0000084046;Note=THO complex subunit HPR1	
+P17629	UniProtKB	Modified residue	234	234	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P17629	UniProtKB	Sequence conflict	404	404	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47171 1 1648
+P47171	UniProtKB	Chain	1	1648	.	.	.	ID=PRO_0000203124;Note=Histone transcription regulator 3	
+P47171	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47171	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P48353 1 224
+P48353	UniProtKB	Chain	1	224	.	.	.	ID=PRO_0000071120;Note=Protein HLJ1	
+P48353	UniProtKB	Domain	18	87	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P48353	UniProtKB	Modified residue	109	109	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q04429 1 423
+Q04429	UniProtKB	Chain	1	423	.	.	.	ID=PRO_0000083991;Note=Protein HLR1	
+##sequence-region P12683 1 1054
+P12683	UniProtKB	Chain	1	1054	.	.	.	ID=PRO_0000114456;Note=3-hydroxy-3-methylglutaryl-coenzyme A reductase 1	
+P12683	UniProtKB	Topological domain	1	28	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12683	UniProtKB	Topological domain	50	187	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12683	UniProtKB	Topological domain	209	217	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Transmembrane	218	238	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12683	UniProtKB	Topological domain	239	246	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Transmembrane	247	267	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12683	UniProtKB	Topological domain	268	309	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Transmembrane	310	330	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12683	UniProtKB	Topological domain	331	336	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Transmembrane	337	357	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12683	UniProtKB	Topological domain	358	400	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Transmembrane	401	421	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12683	UniProtKB	Topological domain	422	498	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Transmembrane	499	519	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12683	UniProtKB	Topological domain	520	1054	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Domain	189	357	.	.	.	Note=SSD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00199	
+P12683	UniProtKB	Region	525	617	.	.	.	Note=Linker	
+P12683	UniProtKB	Region	618	1054	.	.	.	Note=Catalytic	
+P12683	UniProtKB	Active site	714	714	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Active site	848	848	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Active site	924	924	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12683	UniProtKB	Active site	1020	1020	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10003	
+P12683	UniProtKB	Modified residue	552	552	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P12683	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12683	UniProtKB	Glycosylation	181	181	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12683	UniProtKB	Glycosylation	452	452	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12683	UniProtKB	Glycosylation	490	490	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CY13 1 119
+P0CY13	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000410463;Note=Silenced mating-type protein A2	
+P0CY13	UniProtKB	DNA binding	38	100	.	.	.	Note=Homeobox%3B TALE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108	
+##sequence-region Q12398 1 434
+Q12398	UniProtKB	Chain	1	434	.	.	.	ID=PRO_0000224147;Note=Probable transcription factor HMS1	
+Q12398	UniProtKB	Domain	266	341	.	.	.	Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981	
+##sequence-region P40545 1 261
+P40545	UniProtKB	Chain	1	261	.	.	.	ID=PRO_0000141963;Note=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase	
+P40545	UniProtKB	Sequence conflict	243	243	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40545	UniProtKB	Beta strand	7	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Helix	41	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Beta strand	57	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Helix	66	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Turn	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Beta strand	80	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Turn	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Helix	91	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Turn	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Helix	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Helix	116	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Helix	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Beta strand	131	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Beta strand	144	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Turn	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Beta strand	154	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Helix	162	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Turn	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Beta strand	173	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Helix	191	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Beta strand	208	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Helix	220	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Beta strand	232	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Helix	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Beta strand	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+P40545	UniProtKB	Helix	250	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK	
+##sequence-region P33734 1 552
+P33734	UniProtKB	Chain	1	552	.	.	.	ID=PRO_0000152476;Note=Imidazole glycerol phosphate synthase hisHF	
+P33734	UniProtKB	Domain	3	218	.	.	.	Note=Glutamine amidotransferase type-1	
+P33734	UniProtKB	Region	236	552	.	.	.	Note=Cyclase	
+P33734	UniProtKB	Region	364	365	.	.	.	Note=PRFAR binding	
+P33734	UniProtKB	Region	402	404	.	.	.	Note=PRFAR binding	
+P33734	UniProtKB	Region	474	475	.	.	.	Note=PRFAR binding	
+P33734	UniProtKB	Region	500	501	.	.	.	Note=PRFAR binding	
+P33734	UniProtKB	Region	523	524	.	.	.	Note=PRFAR binding	
+P33734	UniProtKB	Active site	83	83	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33734	UniProtKB	Active site	193	193	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33734	UniProtKB	Active site	195	195	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33734	UniProtKB	Active site	245	245	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33734	UniProtKB	Active site	404	404	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33734	UniProtKB	Binding site	83	83	.	.	.	Note=Glutamine (covalent)	
+P33734	UniProtKB	Binding site	332	332	.	.	.	Note=Substrate%3B via amide nitrogen	
+P33734	UniProtKB	Binding site	469	469	.	.	.	Note=Substrate	
+P33734	UniProtKB	Mutagenesis	239	239	.	.	.	Note=1000-fold decrease in catalytic efficiency. Uncoupling of glutaminase activity from the cyclase activity. R->A%2CH%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12795596;Dbxref=PMID:12795596	
+P33734	UniProtKB	Mutagenesis	258	258	.	.	.	Note=No activity. Uncoupling of glutaminase activity from the cyclase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12795596;Dbxref=PMID:12795596	
+P33734	UniProtKB	Mutagenesis	258	258	.	.	.	Note=Small reduction of activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12795596;Dbxref=PMID:12795596	
+P33734	UniProtKB	Mutagenesis	360	360	.	.	.	Note=Almost no effect on activity. K->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12795596;Dbxref=PMID:12795596	
+P33734	UniProtKB	Sequence conflict	54	54	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33734	UniProtKB	Beta strand	3	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	15	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	27	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OX6	
+P33734	UniProtKB	Beta strand	45	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	53	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	66	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	79	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	84	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	90	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	104	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Turn	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	119	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	143	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	155	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	167	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	176	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	187	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	198	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	221	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	232	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	240	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OX5	
+P33734	UniProtKB	Beta strand	254	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	277	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	292	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	311	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Turn	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	327	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	346	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	359	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	365	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	386	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	396	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	399	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	405	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	413	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	433	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Turn	441	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	445	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	451	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	465	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	471	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Turn	474	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	482	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	496	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	505	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Beta strand	518	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	524	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+P33734	UniProtKB	Helix	533	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN	
+##sequence-region P38635 1 335
+P38635	UniProtKB	Chain	1	335	.	.	.	ID=PRO_0000122322;Note=Histidinol-phosphatase	
+P38635	UniProtKB	Sequence conflict	30	30	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38635	UniProtKB	Sequence conflict	191	191	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38635	UniProtKB	Sequence conflict	195	195	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03937 1 162
+Q03937	UniProtKB	Chain	1	162	.	.	.	ID=PRO_0000252301;Note=Meiosis-specific protein HED1	
+##sequence-region P51979 1 1187
+P51979	UniProtKB	Chain	1	1187	.	.	.	ID=PRO_0000102090;Note=ATP-dependent DNA helicase MER3	
+P51979	UniProtKB	Domain	148	322	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P51979	UniProtKB	Domain	360	542	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P51979	UniProtKB	Domain	616	922	.	.	.	Note=SEC63	
+P51979	UniProtKB	Nucleotide binding	161	168	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P51979	UniProtKB	Zinc finger	1039	1054	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51979	UniProtKB	Motif	268	271	.	.	.	Note=DEIH box	
+P51979	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Decrease in activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11376001;Dbxref=PMID:11376001	
+P51979	UniProtKB	Sequence conflict	552	552	.	.	.	Note=T->TAA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P06633 1 220
+P06633	UniProtKB	Chain	1	220	.	.	.	ID=PRO_0000158250;Note=Imidazoleglycerol-phosphate dehydratase	
+P06633	UniProtKB	Natural variant	8	8	.	.	.	Note=In strain: CLIB 219. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P06633	UniProtKB	Natural variant	30	30	.	.	.	Note=In strain: CLIB 219%2C CLIB 410%2C CLIB 413 and YIIc17 haplotype Ha2. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P06633	UniProtKB	Natural variant	92	92	.	.	.	Note=In strain: YIIc12 and YIIc17 haplotype Ha1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P06633	UniProtKB	Natural variant	216	216	.	.	.	Note=In strain: YIIc17 haplotype Ha2. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P06633	UniProtKB	Sequence conflict	109	111	.	.	.	Note=GAV->LA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06633	UniProtKB	Sequence conflict	109	111	.	.	.	Note=GAV->LA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P02293 1 131
+P02293	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02293	UniProtKB	Chain	2	131	.	.	.	ID=PRO_0000071938;Note=Histone H2B.1	
+P02293	UniProtKB	Modified residue	7	7	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039	
+P02293	UniProtKB	Modified residue	8	8	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039	
+P02293	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15652479,ECO:0000269|PubMed:15970663;Dbxref=PMID:15652479,PMID:15970663	
+P02293	UniProtKB	Modified residue	12	12	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:15186774;Dbxref=PMID:11545749,PMID:15186774	
+P02293	UniProtKB	Modified residue	17	17	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:15186774,ECO:0000269|PubMed:16598039;Dbxref=PMID:11545749,PMID:15186774,PMID:16598039	
+P02293	UniProtKB	Cross-link	7	7	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate	
+P02293	UniProtKB	Cross-link	8	8	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate	
+P02293	UniProtKB	Cross-link	17	17	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02293	UniProtKB	Cross-link	18	18	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02293	UniProtKB	Cross-link	124	124	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642555,ECO:0000269|PubMed:12535538,ECO:0000269|PubMed:12535539,ECO:0000269|PubMed:14660635,ECO:0000269|PubMed:15280549,ECO:0000269|PubMed:16432255;Dbxref=PMID:10642555,PMID:12535538,PMID:12535539,PMID:14660635,PMID:15280549,PMID:16432255	
+P02293	UniProtKB	Mutagenesis	7	8	.	.	.	Note=Reduces sumoylation. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039	
+P02293	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Desensitizes cells to H(2)O(2) treatment. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652479;Dbxref=PMID:15652479	
+P02293	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Induces apoptotic-like features including chromatin condensation. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652479;Dbxref=PMID:15652479	
+P02293	UniProtKB	Mutagenesis	17	18	.	.	.	Note=Reduces sumoylation. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039	
+P02293	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Confers UV-radiation sensitivity%3B when associated with F-87 and S-88. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11973294;Dbxref=PMID:11973294	
+P02293	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Confers UV-radiation sensitivity%3B when associated with F-48 and S-88. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11973294;Dbxref=PMID:11973294	
+P02293	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Confers UV-radiation sensitivity%3B when associated with F-48 and F-87. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11973294;Dbxref=PMID:11973294	
+P02293	UniProtKB	Mutagenesis	124	124	.	.	.	Note=Impairs ubiquitin conjugation%2C DNA double-strand brakes formation during meiosis and histone H3-K79 methylation. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642555,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:14660635,ECO:0000269|PubMed:15280549,ECO:0000269|PubMed:15632126;Dbxref=PMID:10642555,PMID:12152067,PMID:14660635,PMID:15280549,PMID:15632126	
+P02293	UniProtKB	Helix	42	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+P02293	UniProtKB	Beta strand	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+P02293	UniProtKB	Helix	60	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+P02293	UniProtKB	Beta strand	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+P02293	UniProtKB	Helix	95	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+P02293	UniProtKB	Helix	108	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+##sequence-region P13434 1 144
+P13434	UniProtKB	Chain	1	144	.	.	.	ID=PRO_0000204630;Note=Transcriptional activator HAP3	
+P13434	UniProtKB	DNA binding	42	48	.	.	.	.	
+P13434	UniProtKB	Region	69	80	.	.	.	Note=Subunit association domain (SAD)	
+##sequence-region P32769 1 611
+P32769	UniProtKB	Chain	1	611	.	.	.	ID=PRO_0000091490;Note=Elongation factor 1 alpha-like protein	
+P32769	UniProtKB	Domain	165	390	.	.	.	Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32769	UniProtKB	Nucleotide binding	174	181	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32769	UniProtKB	Nucleotide binding	251	255	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32769	UniProtKB	Nucleotide binding	313	316	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32769	UniProtKB	Region	174	181	.	.	.	Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32769	UniProtKB	Region	230	234	.	.	.	Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32769	UniProtKB	Region	251	254	.	.	.	Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32769	UniProtKB	Region	313	316	.	.	.	Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32769	UniProtKB	Region	352	354	.	.	.	Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32769	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32769	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Loss of function. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11909951;Dbxref=PMID:11909951	
+P32769	UniProtKB	Mutagenesis	255	255	.	.	.	Note=Loss of function. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11909951;Dbxref=PMID:11909951	
+P32769	UniProtKB	Sequence conflict	92	94	.	.	.	Note=NGS->MGV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32769	UniProtKB	Helix	157	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	167	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	180	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	196	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	219	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P27	
+P32769	UniProtKB	Beta strand	237	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	246	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	259	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	270	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	291	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	308	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	315	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	322	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	346	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	353	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	359	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	366	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	377	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	402	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	419	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	435	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Turn	440	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	443	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Turn	453	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	464	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	473	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Helix	483	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	491	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	504	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	524	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	532	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	564	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Turn	583	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Turn	587	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	591	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+P32769	UniProtKB	Beta strand	599	609	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26	
+##sequence-region Q07653 1 1046
+Q07653	UniProtKB	Chain	1	1046	.	.	.	ID=PRO_0000233010;Note=Protein HBT1	
+Q07653	UniProtKB	Compositional bias	151	254	.	.	.	Note=His-rich	
+Q07653	UniProtKB	Compositional bias	967	1001	.	.	.	Note=His-rich	
+Q07653	UniProtKB	Modified residue	41	41	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q07653	UniProtKB	Modified residue	303	303	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07653	UniProtKB	Modified residue	363	363	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07653	UniProtKB	Modified residue	491	491	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07653	UniProtKB	Modified residue	561	561	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07653	UniProtKB	Modified residue	671	671	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07653	UniProtKB	Modified residue	855	855	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07653	UniProtKB	Modified residue	857	857	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07653	UniProtKB	Modified residue	1005	1005	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07653	UniProtKB	Modified residue	1034	1034	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+##sequence-region P25364 1 564
+P25364	UniProtKB	Chain	1	564	.	.	.	ID=PRO_0000091902;Note=Forkhead transcription factor HCM1	
+P25364	UniProtKB	DNA binding	108	199	.	.	.	Note=Fork-head;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00089	
+P25364	UniProtKB	Modified residue	342	342	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25364	UniProtKB	Modified residue	496	496	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25364	UniProtKB	Mutagenesis	155	155	.	.	.	Note=No recognition of DNA-binding site and no suppression of calmodulin mutants%3B when associated with A-159%3B A-162 and A-163. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9920414;Dbxref=PMID:9920414	
+P25364	UniProtKB	Mutagenesis	159	159	.	.	.	Note=No recognition of DNA-binding site and no suppression of calmodulin mutants%3B when associated with A-155%3B A-162 and A-163. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9920414;Dbxref=PMID:9920414	
+P25364	UniProtKB	Mutagenesis	162	162	.	.	.	Note=No recognition of DNA-binding site and no suppression of calmodulin mutants%3B when associated with A-155%3B A-159 and A-163. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9920414;Dbxref=PMID:9920414	
+P25364	UniProtKB	Mutagenesis	163	163	.	.	.	Note=No recognition of DNA-binding site and no suppression of calmodulin mutants%3B when associated with A-155%3B A-159 and A-162. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9920414;Dbxref=PMID:9920414	
+P25364	UniProtKB	Sequence conflict	129	130	.	.	.	Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06623 1 655
+Q06623	UniProtKB	Chain	1	655	.	.	.	ID=PRO_0000083932;Note=HDA1 complex subunit 3	
+Q06623	UniProtKB	Coiled coil	482	632	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06623	UniProtKB	Beta strand	29	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	39	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	53	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Turn	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	68	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	105	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	114	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Beta strand	131	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	141	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Beta strand	156	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Beta strand	175	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Turn	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Beta strand	200	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	214	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Beta strand	235	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	244	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	260	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Turn	282	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	285	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Turn	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	293	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	296	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+Q06623	UniProtKB	Helix	319	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT	
+##sequence-region Q12060 1 488
+Q12060	UniProtKB	Chain	1	488	.	.	.	ID=PRO_0000083959;Note=Transcriptional coactivator HFI1/ADA1	
+Q12060	UniProtKB	Sequence conflict	19	19	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12373 1 385
+Q12373	UniProtKB	Chain	1	385	.	.	.	ID=PRO_0000227731;Note=HAT1-interacting factor 1	
+Q12373	UniProtKB	Repeat	186	220	.	.	.	Note=TPR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12373	UniProtKB	Repeat	229	262	.	.	.	Note=TPR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12373	UniProtKB	Repeat	289	322	.	.	.	Note=TPR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12373	UniProtKB	Region	80	199	.	.	.	Note=Important for interaction with heterotetrameric histone H3 and H4 and for interaction with dimeric histone H2A and H2B;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24946827,ECO:0000269|PubMed:27618665;Dbxref=PMID:24946827,PMID:27618665	
+Q12373	UniProtKB	Region	248	332	.	.	.	Note=Interaction with dimeric histone H2A and H2B;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665	
+Q12373	UniProtKB	Compositional bias	97	184	.	.	.	Note=Glu-rich	
+Q12373	UniProtKB	Modified residue	174	174	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12373	UniProtKB	Mutagenesis	80	158	.	.	.	Note=Abolishes interaction with heterotetrameric histone H3 and H4 and with dimeric histone H2A and H2B. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665	
+Q12373	UniProtKB	Mutagenesis	85	198	.	.	.	Note=Abolishes interaction with histones H2A%2C H2B%2C H3 and H4. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24946827,ECO:0000269|PubMed:27618665;Dbxref=PMID:24946827,PMID:27618665	
+Q12373	UniProtKB	Mutagenesis	95	158	.	.	.	Note=Mildly decreases interaction with heterotetrameric histone H3 and H4 and abolishes interaction with dimeric histone H2A and H2B. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665	
+Q12373	UniProtKB	Mutagenesis	135	158	.	.	.	Note=Minimal decrease of interaction with heterotetrameric histone H3 and H4 and with dimeric histone H2A and H2B. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24946827,ECO:0000269|PubMed:27618665;Dbxref=PMID:24946827,PMID:27618665	
+Q12373	UniProtKB	Mutagenesis	248	248	.	.	.	Note=Strongly reduces affinity for dimeric histone H2A and H2B%3B when associated with A-250%3B A-288%3B A-291 and 332-A--A-342. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665	
+Q12373	UniProtKB	Mutagenesis	250	250	.	.	.	Note=Strongly reduces affinity for dimeric histone H2A and H2B%3B when associated with A-248%3B A-288%3B A-291 and 332-A--A-342. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665	
+Q12373	UniProtKB	Mutagenesis	288	288	.	.	.	Note=Strongly reduces affinity for dimeric histone H2A and H2B%3B when associated with A-248%3B A-250%3B A-291 and 332-A--A-342. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665	
+Q12373	UniProtKB	Mutagenesis	291	291	.	.	.	Note=Strongly reduces affinity for dimeric histone H2A and H2B%3B when associated with A-248%3B A-250%3B A-288 and 332-A--A-342. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665	
+Q12373	UniProtKB	Mutagenesis	332	342	.	.	.	Note=Strongly reduces affinity for dimeric histone H2A and H2B%3B when associated with A-248%3B A-250%3B A-288 and A-291. QIQDDIDEVQE->AIQAAIDAVQA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665	
+Q12373	UniProtKB	Helix	14	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Helix	38	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Beta strand	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Helix	61	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Helix	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Helix	167	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Turn	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BT1	
+Q12373	UniProtKB	Helix	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Helix	194	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Helix	202	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Beta strand	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BT1	
+Q12373	UniProtKB	Helix	229	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Helix	252	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Helix	273	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Helix	298	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+Q12373	UniProtKB	Helix	323	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0	
+##sequence-region P53834 1 153
+P53834	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000215823;Note=Hsp90 co-chaperone HCH1	
+##sequence-region Q03281 1 663
+Q03281	UniProtKB	Chain	1	663	.	.	.	ID=PRO_0000202596;Note=Inner nuclear membrane protein HEH2	
+Q03281	UniProtKB	Transmembrane	317	337	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03281	UniProtKB	Motif	124	137	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03281	UniProtKB	Compositional bias	85	90	.	.	.	Note=Poly-Ser	
+Q03281	UniProtKB	Modified residue	123	123	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03281	UniProtKB	Mutagenesis	1	133	.	.	.	Note=No interaction with SRP1%3B when associated with missing 309-I--E-663. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16929305;Dbxref=PMID:16929305	
+Q03281	UniProtKB	Mutagenesis	1	52	.	.	.	Note=Interaction with SRP1%3B when associated with missing 309-I--E-663. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16929305;Dbxref=PMID:16929305	
+Q03281	UniProtKB	Mutagenesis	124	137	.	.	.	Note=No interaction with SRP1%3B when associated with missing 309-I--E-663. Mislocalized to the endoplasmic reticulum. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16929305;Dbxref=PMID:16929305	
+Q03281	UniProtKB	Mutagenesis	126	126	.	.	.	Note=Mislocalized to the endoplasmic reticulum. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16929305;Dbxref=PMID:16929305	
+Q03281	UniProtKB	Mutagenesis	309	663	.	.	.	Note=Interaction with SRP1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16929305;Dbxref=PMID:16929305	
+Q03281	UniProtKB	Turn	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVZ	
+Q03281	UniProtKB	Helix	113	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVZ	
+##sequence-region P36113 1 551
+P36113	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000056339;Note=E3 ubiquitin-protein ligase HEL1	
+P36113	UniProtKB	Zinc finger	179	223	.	.	.	Note=RING-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P36113	UniProtKB	Zinc finger	242	314	.	.	.	Note=IBR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36113	UniProtKB	Zinc finger	341	370	.	.	.	Note=RING-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P36113	UniProtKB	Active site	354	354	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y4X5	
+##sequence-region P06174 1 275
+P06174	UniProtKB	Chain	1	275	.	.	.	ID=PRO_0000135254;Note=Uroporphyrinogen-III synthase	
+P06174	UniProtKB	Sequence conflict	231	275	.	.	.	Note=HLRVASIGPTTKKYLDDNDVTSDVVSPKPDPKSLLDAIELYQRHK->IYGLRHRTYH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P46973 1 164
+P46973	UniProtKB	Chain	1	164	.	.	.	ID=PRO_0000173556;Note=Protein HIT1	
+P46973	UniProtKB	Zinc finger	8	49	.	.	.	Note=HIT-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00453	
+P46973	UniProtKB	Sequence conflict	36	37	.	.	.	Note=AA->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46973	UniProtKB	Turn	9	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95	
+P46973	UniProtKB	Beta strand	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95	
+P46973	UniProtKB	Turn	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95	
+P46973	UniProtKB	Beta strand	26	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95	
+P46973	UniProtKB	Helix	30	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95	
+P46973	UniProtKB	Beta strand	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95	
+P46973	UniProtKB	Helix	77	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF	
+P46973	UniProtKB	Helix	87	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF	
+P46973	UniProtKB	Helix	96	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF	
+P46973	UniProtKB	Beta strand	119	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF	
+P46973	UniProtKB	Helix	123	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF	
+P46973	UniProtKB	Turn	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF	
+P46973	UniProtKB	Helix	146	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF	
+##sequence-region P0CY11 1 126
+P0CY11	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000410465;Note=Silenced mating-type protein A1	
+P0CY11	UniProtKB	DNA binding	70	126	.	.	.	Note=Homeobox;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108	
+##sequence-region Q06629 1 674
+Q06629	UniProtKB	Chain	1	674	.	.	.	ID=PRO_0000083930;Note=HDA1 complex subunit 2	
+Q06629	UniProtKB	Coiled coil	468	637	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P05373 1 342
+P05373	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000140534;Note=Delta-aminolevulinic acid dehydratase	
+P05373	UniProtKB	Active site	210	210	.	.	.	Note=Schiff-base intermediate with substrate	
+P05373	UniProtKB	Active site	263	263	.	.	.	Note=Schiff-base intermediate with substrate	
+P05373	UniProtKB	Metal binding	133	133	.	.	.	Note=Zinc%3B catalytic	
+P05373	UniProtKB	Metal binding	135	135	.	.	.	Note=Zinc%3B catalytic	
+P05373	UniProtKB	Metal binding	143	143	.	.	.	Note=Zinc%3B catalytic	
+P05373	UniProtKB	Binding site	220	220	.	.	.	Note=Substrate 1	
+P05373	UniProtKB	Binding site	232	232	.	.	.	Note=Substrate 1	
+P05373	UniProtKB	Binding site	290	290	.	.	.	Note=Substrate 2	
+P05373	UniProtKB	Binding site	329	329	.	.	.	Note=Substrate 2	
+P05373	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P05373	UniProtKB	Sequence conflict	291	291	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05373	UniProtKB	Helix	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	19	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	25	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EB3	
+P05373	UniProtKB	Helix	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	41	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W31	
+P05373	UniProtKB	Beta strand	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	68	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	85	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	111	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	126	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Turn	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OHL	
+P05373	UniProtKB	Beta strand	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W31	
+P05373	UniProtKB	Beta strand	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	154	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	174	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	185	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Turn	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	203	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7P	
+P05373	UniProtKB	Helix	217	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Turn	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	242	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	258	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	266	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	269	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Turn	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	284	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	290	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	307	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Beta strand	324	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+P05373	UniProtKB	Helix	331	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N	
+##sequence-region P11353 1 328
+P11353	UniProtKB	Chain	1	328	.	.	.	ID=PRO_0000109878;Note=Oxygen-dependent coproporphyrinogen-III oxidase	
+P11353	UniProtKB	Region	57	66	.	.	.	Note=Important for dimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11353	UniProtKB	Region	133	135	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11353	UniProtKB	Region	266	302	.	.	.	Note=Important for dimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11353	UniProtKB	Region	285	290	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11353	UniProtKB	Active site	131	131	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11353	UniProtKB	Binding site	117	117	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11353	UniProtKB	Site	201	201	.	.	.	Note=Important for dimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11353	UniProtKB	Disulfide bond	193	193	.	.	.	Note=Interchain;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15194705;Dbxref=PMID:15194705	
+P11353	UniProtKB	Sequence conflict	226	226	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11353	UniProtKB	Helix	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL	
+P11353	UniProtKB	Helix	12	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Beta strand	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Beta strand	40	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL	
+P11353	UniProtKB	Helix	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL	
+P11353	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Beta strand	55	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Beta strand	62	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Helix	80	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Helix	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Beta strand	99	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL	
+P11353	UniProtKB	Beta strand	109	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Beta strand	129	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Beta strand	144	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Helix	164	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Helix	185	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Helix	193	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Beta strand	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL	
+P11353	UniProtKB	Beta strand	209	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Helix	221	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Helix	235	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Turn	245	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Helix	253	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Helix	265	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN	
+P11353	UniProtKB	Helix	275	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL	
+P11353	UniProtKB	Helix	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL	
+P11353	UniProtKB	Helix	292	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL	
+P11353	UniProtKB	Beta strand	297	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL	
+P11353	UniProtKB	Helix	312	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL	
+##sequence-region P04912 1 132
+P04912	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12915400;Dbxref=PMID:12915400	
+P04912	UniProtKB	Chain	2	132	.	.	.	ID=PRO_0000055327;Note=Histone H2A.2	
+P04912	UniProtKB	Motif	129	130	.	.	.	Note=[ST]-Q motif	
+P04912	UniProtKB	Site	120	120	.	.	.	Note=Not ubiquitinated;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04912	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12915400;Dbxref=PMID:12915400	
+P04912	UniProtKB	Modified residue	5	5	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10082517;Dbxref=PMID:10082517	
+P04912	UniProtKB	Modified residue	8	8	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10082517,ECO:0000269|PubMed:11545749;Dbxref=PMID:10082517,PMID:11545749	
+P04912	UniProtKB	Modified residue	106	106	.	.	.	Note=N5-methylglutamine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239	
+P04912	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:11140636;Dbxref=PMID:18407956,PMID:11140636	
+P04912	UniProtKB	Cross-link	127	127	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
+P04912	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Causes hypersensitivity to DNA-damage-inducing agents. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636	
+P04912	UniProtKB	Mutagenesis	129	129	.	.	.	Note=No effect. S->E%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636	
+P04912	UniProtKB	Helix	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P04912	UniProtKB	Helix	29	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P04912	UniProtKB	Turn	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P04912	UniProtKB	Beta strand	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P04912	UniProtKB	Helix	49	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P04912	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P04912	UniProtKB	Helix	82	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P04912	UniProtKB	Helix	93	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P04912	UniProtKB	Turn	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P04912	UniProtKB	Beta strand	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P04912	UniProtKB	Helix	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+##sequence-region Q12692 1 134
+Q12692	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16543223;Dbxref=PMID:22814378,PMID:16543223	
+Q12692	UniProtKB	Chain	2	134	.	.	.	ID=PRO_0000055340;Note=Histone H2A.Z	
+Q12692	UniProtKB	Region	98	108	.	.	.	Note=Interaction with VPS72;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16299513;Dbxref=PMID:16299513	
+Q12692	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16543223;Dbxref=PMID:22814378,PMID:16543223	
+Q12692	UniProtKB	Modified residue	4	4	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16543222,ECO:0000269|PubMed:16543223;Dbxref=PMID:16543222,PMID:16543223	
+Q12692	UniProtKB	Modified residue	9	9	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16543222,ECO:0000269|PubMed:16543223;Dbxref=PMID:16543222,PMID:16543223	
+Q12692	UniProtKB	Modified residue	11	11	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16543222,ECO:0000269|PubMed:16543223;Dbxref=PMID:16543222,PMID:16543223	
+Q12692	UniProtKB	Modified residue	15	15	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16543222,ECO:0000269|PubMed:16543223;Dbxref=PMID:16543222,PMID:16543223	
+Q12692	UniProtKB	Helix	25	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+Q12692	UniProtKB	Helix	35	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+Q12692	UniProtKB	Helix	54	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+Q12692	UniProtKB	Beta strand	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+Q12692	UniProtKB	Helix	89	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+Q12692	UniProtKB	Helix	100	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+##sequence-region P61830 1 136
+P61830	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7035169,ECO:0000269|PubMed:782914;Dbxref=PMID:7035169,PMID:782914	
+P61830	UniProtKB	Chain	2	136	.	.	.	ID=PRO_0000221370;Note=Histone H3	
+P61830	UniProtKB	Modified residue	5	5	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11742990,ECO:0000269|PubMed:11751634,ECO:0000269|PubMed:11752412,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12353038,ECO:0000269|PubMed:12845608,ECO:0000269|PubMed:15949446,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:16168379,ECO:0000269|PubMed:16185711,ECO:0000269|PubMed:17194708;Dbxref=PMID:11742990,PMID:11751634,PMID:11752412,PMID:12152067,PMID:12353038,PMID:12845608,PMID:15949446,PMID:16122352,PMID:16168379,PMID:16185711,PMID:17194708	
+P61830	UniProtKB	Modified residue	5	5	.	.	.	Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11742990,ECO:0000269|PubMed:11751634,ECO:0000269|PubMed:11752412,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12353038,ECO:0000269|PubMed:12845608,ECO:0000269|PubMed:15949446,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:16168379,ECO:0000269|PubMed:16185711,ECO:0000269|PubMed:17194708;Dbxref=PMID:11742990,PMID:11751634,PMID:11752412,PMID:12152067,PMID:12353038,PMID:12845608,PMID:15949446,PMID:16122352,PMID:16168379,PMID:16185711,PMID:17194708	
+P61830	UniProtKB	Modified residue	5	5	.	.	.	Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11742990,ECO:0000269|PubMed:11751634,ECO:0000269|PubMed:11752412,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12353038,ECO:0000269|PubMed:12845608,ECO:0000269|PubMed:15949446,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:16168379,ECO:0000269|PubMed:16185711,ECO:0000269|PubMed:17194708;Dbxref=PMID:11742990,PMID:11751634,PMID:11752412,PMID:12152067,PMID:12353038,PMID:12845608,PMID:15949446,PMID:16122352,PMID:16168379,PMID:16185711,PMID:17194708	
+P61830	UniProtKB	Modified residue	10	10	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:17194708,ECO:0000269|PubMed:9606197;Dbxref=PMID:11545749,PMID:16122352,PMID:17194708,PMID:9606197	
+P61830	UniProtKB	Modified residue	10	10	.	.	.	Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708	
+P61830	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10911986,ECO:0000269|PubMed:10975519,ECO:0000269|PubMed:15719021;Dbxref=PMID:10911986,PMID:10975519,PMID:15719021	
+P61830	UniProtKB	Modified residue	15	15	.	.	.	Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708	
+P61830	UniProtKB	Modified residue	15	15	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10082517,ECO:0000269|PubMed:10911986,ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:15719021,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:17194708,ECO:0000269|PubMed:9606197;Dbxref=PMID:10082517,PMID:10911986,PMID:11545749,PMID:15719021,PMID:16122352,PMID:17194708,PMID:9606197	
+P61830	UniProtKB	Modified residue	19	19	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:17194708,ECO:0000269|PubMed:9606197;Dbxref=PMID:11545749,PMID:16122352,PMID:17194708,PMID:9606197	
+P61830	UniProtKB	Modified residue	19	19	.	.	.	Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708	
+P61830	UniProtKB	Modified residue	24	24	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:17194708;Dbxref=PMID:11545749,PMID:17194708	
+P61830	UniProtKB	Modified residue	24	24	.	.	.	Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708	
+P61830	UniProtKB	Modified residue	28	28	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708	
+P61830	UniProtKB	Modified residue	28	28	.	.	.	Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708	
+P61830	UniProtKB	Modified residue	28	28	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:17194708;Dbxref=PMID:11545749,PMID:17194708	
+P61830	UniProtKB	Modified residue	28	28	.	.	.	Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708	
+P61830	UniProtKB	Modified residue	37	37	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11839797,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12629047,ECO:0000269|PubMed:12773564,ECO:0000269|PubMed:12917322,ECO:0000269|PubMed:15798214,ECO:0000269|PubMed:17194708;Dbxref=PMID:11839797,PMID:12152067,PMID:12629047,PMID:12773564,PMID:12917322,PMID:15798214,PMID:17194708	
+P61830	UniProtKB	Modified residue	37	37	.	.	.	Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11839797,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12629047,ECO:0000269|PubMed:12773564,ECO:0000269|PubMed:12917322,ECO:0000269|PubMed:15798214,ECO:0000269|PubMed:17194708;Dbxref=PMID:11839797,PMID:12152067,PMID:12629047,PMID:12773564,PMID:12917322,PMID:15798214,PMID:17194708	
+P61830	UniProtKB	Modified residue	37	37	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17189264,ECO:0000269|PubMed:17194708;Dbxref=PMID:17189264,PMID:17194708	
+P61830	UniProtKB	Modified residue	37	37	.	.	.	Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11839797,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12629047,ECO:0000269|PubMed:12773564,ECO:0000269|PubMed:12917322,ECO:0000269|PubMed:15798214,ECO:0000269|PubMed:17194708;Dbxref=PMID:11839797,PMID:12152067,PMID:12629047,PMID:12773564,PMID:12917322,PMID:15798214,PMID:17194708	
+P61830	UniProtKB	Modified residue	57	57	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15888442,ECO:0000269|PubMed:16015338,ECO:0000269|PubMed:16260619,ECO:0000269|PubMed:17194708,ECO:0000269|PubMed:17320445;Dbxref=PMID:15888442,PMID:16015338,PMID:16260619,PMID:17194708,PMID:17320445	
+P61830	UniProtKB	Modified residue	65	65	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708	
+P61830	UniProtKB	Modified residue	80	80	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12080090,ECO:0000269|PubMed:12097318,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12574507,ECO:0000269|PubMed:15632126,ECO:0000269|PubMed:17194708;Dbxref=PMID:12080090,PMID:12097318,PMID:12152067,PMID:12574507,PMID:15632126,PMID:17194708	
+P61830	UniProtKB	Modified residue	80	80	.	.	.	Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12080090,ECO:0000269|PubMed:12097318,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12574507,ECO:0000269|PubMed:15632126,ECO:0000269|PubMed:17194708;Dbxref=PMID:12080090,PMID:12097318,PMID:12152067,PMID:12574507,PMID:15632126,PMID:17194708	
+P61830	UniProtKB	Modified residue	80	80	.	.	.	Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12080090,ECO:0000269|PubMed:12097318,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12574507,ECO:0000269|PubMed:15632126,ECO:0000269|PubMed:17194708;Dbxref=PMID:12080090,PMID:12097318,PMID:12152067,PMID:12574507,PMID:15632126,PMID:17194708	
+P61830	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Impairs histone H3 phosphorylation and reduces transcription of some GCN5 regulated genes. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10911986,ECO:0000269|PubMed:10975519;Dbxref=PMID:10911986,PMID:10975519	
+P61830	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Lethal. R->A%2CK%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16260619;Dbxref=PMID:16260619	
+P61830	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Increases sensitivity to genotoxic agents inducing DNA breaks during replication. K->A%2CQ%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15888442,ECO:0000269|PubMed:16015338,ECO:0000269|PubMed:16260619;Dbxref=PMID:15888442,PMID:16015338,PMID:16260619	
+P61830	UniProtKB	Mutagenesis	80	80	.	.	.	Note=Compromises telomeric silencing. K->A%2CP%2CQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12080090,ECO:0000269|PubMed:16260619;Dbxref=PMID:12080090,PMID:16260619	
+P61830	UniProtKB	Mutagenesis	119	119	.	.	.	Note=Lethal. T->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16260619;Dbxref=PMID:16260619	
+P61830	UniProtKB	Sequence conflict	124	124	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P61830	UniProtKB	Beta strand	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RSN	
+P61830	UniProtKB	Beta strand	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNW	
+P61830	UniProtKB	Helix	46	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P61830	UniProtKB	Helix	66	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P61830	UniProtKB	Helix	87	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P61830	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P61830	UniProtKB	Helix	124	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IDC	
+##sequence-region P02309 1 103
+P02309	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02309	UniProtKB	Chain	2	103	.	.	.	ID=PRO_0000158377;Note=Histone H4	
+P02309	UniProtKB	DNA binding	17	21	.	.	.	.	
+P02309	UniProtKB	Modified residue	6	6	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.19	
+P02309	UniProtKB	Modified residue	13	13	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.19	
+P02309	UniProtKB	Modified residue	17	17	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11080160,ECO:0000269|PubMed:15150415,ECO:0000269|PubMed:17289592;Dbxref=PMID:11080160,PMID:15150415,PMID:17289592	
+P02309	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P02309	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P02309	UniProtKB	Modified residue	80	80	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16768447;Dbxref=PMID:16768447	
+P02309	UniProtKB	Sequence conflict	46	46	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02309	UniProtKB	Beta strand	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E3K	
+P02309	UniProtKB	Beta strand	16	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZD	
+P02309	UniProtKB	Helix	26	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P02309	UniProtKB	Helix	32	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSX	
+P02309	UniProtKB	Turn	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSX	
+P02309	UniProtKB	Turn	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L5A	
+P02309	UniProtKB	Helix	51	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P02309	UniProtKB	Beta strand	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P02309	UniProtKB	Helix	84	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P02309	UniProtKB	Beta strand	97	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+##sequence-region Q01766 1 294
+Q01766	UniProtKB	Chain	1	294	.	.	.	ID=PRO_0000083893;Note=Halotolerance protein HAL1	
+Q01766	UniProtKB	Modified residue	266	266	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P0CE41 1 1502
+P0CE41	UniProtKB	Chain	1	1502	.	.	.	ID=PRO_0000114945;Note=Heme-responsive zinc finger transcription factor HAP1	
+P0CE41	UniProtKB	Repeat	280	285	.	.	.	Note=HRM 1	
+P0CE41	UniProtKB	Repeat	299	304	.	.	.	Note=HRM 2	
+P0CE41	UniProtKB	Repeat	323	328	.	.	.	Note=HRM 3	
+P0CE41	UniProtKB	Repeat	347	352	.	.	.	Note=HRM 4	
+P0CE41	UniProtKB	Repeat	389	394	.	.	.	Note=HRM 5	
+P0CE41	UniProtKB	Repeat	415	420	.	.	.	Note=HRM 6	
+P0CE41	UniProtKB	Repeat	1192	1197	.	.	.	Note=HRM 7	
+P0CE41	UniProtKB	DNA binding	64	93	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P0CE41	UniProtKB	Region	244	444	.	.	.	Note=Heme-responsive%3B required for HMC formation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CE41	UniProtKB	Coiled coil	105	134	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE41	UniProtKB	Compositional bias	177	189	.	.	.	Note=Poly-Gln	
+P0CE41	UniProtKB	Metal binding	64	64	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CE41	UniProtKB	Metal binding	64	64	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CE41	UniProtKB	Metal binding	67	67	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CE41	UniProtKB	Metal binding	74	74	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CE41	UniProtKB	Metal binding	81	81	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CE41	UniProtKB	Metal binding	81	81	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CE41	UniProtKB	Metal binding	84	84	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CE41	UniProtKB	Metal binding	93	93	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P06774 1 265
+P06774	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P06774	UniProtKB	Chain	2	265	.	.	.	ID=PRO_0000198781;Note=Transcriptional activator HAP2	
+P06774	UniProtKB	DNA binding	192	217	.	.	.	Note=NFYA/HAP2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00966	
+P06774	UniProtKB	Region	23	180	.	.	.	Note=Interaction with the HAP2-HAP3-HAP5 heteromer	
+P06774	UniProtKB	Motif	162	185	.	.	.	Note=Subunit association domain (SAD)	
+P06774	UniProtKB	Compositional bias	120	133	.	.	.	Note=Poly-Gln	
+P06774	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P06774	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06774	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06774	UniProtKB	Mutagenesis	199	199	.	.	.	Note=Favors CCACC binding over CCAAT. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8223474;Dbxref=PMID:8223474	
+##sequence-region Q02516 1 242
+Q02516	UniProtKB	Chain	1	242	.	.	.	ID=PRO_0000218260;Note=Transcriptional activator HAP5	
+Q02516	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q03532 1 505
+Q03532	UniProtKB	Chain	1	505	.	.	.	ID=PRO_0000055046;Note=ATP-dependent RNA helicase HAS1	
+Q03532	UniProtKB	Domain	73	249	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q03532	UniProtKB	Domain	263	433	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q03532	UniProtKB	Nucleotide binding	86	93	.	.	.	Note=ATP	
+Q03532	UniProtKB	Motif	42	70	.	.	.	Note=Q motif	
+Q03532	UniProtKB	Motif	196	199	.	.	.	Note=DEAD box	
+Q03532	UniProtKB	Motif	275	291	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03532	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+Q03532	UniProtKB	Mutagenesis	92	92	.	.	.	Note=Lethal in vivo and impairs ATPase with 2-5%25 of wild-type ATPase activity%2C a 20-fold higher KM for ATP and unables RNA/DNA heteroduplexes unwinding activity in vitro. Leads to 13%25 of wild-type ATPase activity and higher RNA/DNA heteroduplexes unwinding activity in vitro%3B when associated with A-389. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15049817,ECO:0000269|PubMed:15718299;Dbxref=PMID:15049817,PMID:15718299	
+Q03532	UniProtKB	Mutagenesis	105	105	.	.	.	Note=Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius%3B when associated with S-315 and S-393. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15049817;Dbxref=PMID:15049817	
+Q03532	UniProtKB	Mutagenesis	228	228	.	.	.	Note=Slow growth at 18 and 16 degrees Celsius%2C no growth at 14 degrees Celsius and drastic decrease of the amount of 40S ribosomal subunits at 30 degrees Celsius in vivo. Leads to 70-80%25 of wild-type ATPase activity%2C a 2-fold lower KM for ATP and a slightly reduced RNA/DNA heteroduplexes unwinding activity in vitro. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718299;Dbxref=PMID:15718299	
+Q03532	UniProtKB	Mutagenesis	230	230	.	.	.	Note=Lethal in vivo and leads to 70-80%25 of wild-type ATPase activity%2C a 2-fold lower KM for ATP and a reduced RNA/DNA heteroduplexes unwinding activity in vitro. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718299;Dbxref=PMID:15718299	
+Q03532	UniProtKB	Mutagenesis	315	315	.	.	.	Note=Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius%3B when associated with Y-105 and S-393. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15049817;Dbxref=PMID:15049817	
+Q03532	UniProtKB	Mutagenesis	375	375	.	.	.	Note=Lethal in vivo and leads to 70-80%25 of wild-type ATPase activity%2C a 2-fold lower KM for ATP and a reduced RNA/DNA heteroduplexes unwinding activity in vitro. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718299;Dbxref=PMID:15718299	
+Q03532	UniProtKB	Mutagenesis	376	376	.	.	.	Note=Lethal in vivo and leads to less than 30%25 of wild-type ATPase activity and a 2-fold lower KM for ATP in vitro. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718299;Dbxref=PMID:15718299	
+Q03532	UniProtKB	Mutagenesis	389	389	.	.	.	Note=Increases 3-fold the ATPase activity and a higher RNA/DNA heteroduplexes unwinding activity in vitro. Leads to 13%25 of wild-type ATPase activity and lower RNA/DNA heteroduplexes unwinding activity in vitro%3B when associated with A-92. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718299;Dbxref=PMID:15718299	
+Q03532	UniProtKB	Mutagenesis	393	393	.	.	.	Note=Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius%3B when associated with Y-105 and S-315. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15049817;Dbxref=PMID:15049817	
+##sequence-region P39984 1 401
+P39984	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000051014;Note=Histone acetyltransferase type B subunit 2	
+P39984	UniProtKB	Repeat	116	147	.	.	.	Note=WD 1	
+P39984	UniProtKB	Repeat	158	189	.	.	.	Note=WD 2	
+P39984	UniProtKB	Repeat	206	237	.	.	.	Note=WD 3	
+P39984	UniProtKB	Repeat	249	280	.	.	.	Note=WD 4	
+P39984	UniProtKB	Repeat	293	324	.	.	.	Note=WD 5	
+P39984	UniProtKB	Repeat	350	381	.	.	.	Note=WD 6	
+P39984	UniProtKB	Region	335	339	.	.	.	Note=Interaction with the histone H4 N-terminus;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250	
+P39984	UniProtKB	Site	266	266	.	.	.	Note=Important for interaction with HAT1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250	
+P39984	UniProtKB	Mutagenesis	266	266	.	.	.	Note=Abolishes interaction with HAT1. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250	
+P39984	UniProtKB	Helix	10	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	25	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSX	
+P39984	UniProtKB	Beta strand	53	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	71	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Helix	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	108	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	121	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	130	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	143	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Turn	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	151	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	175	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	185	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	191	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	200	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	211	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	223	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	231	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	244	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	254	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	264	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	276	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	298	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	310	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	320	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Helix	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Helix	334	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	344	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	355	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	367	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Beta strand	375	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+P39984	UniProtKB	Turn	387	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW	
+##sequence-region P34243 1 683
+P34243	UniProtKB	Chain	1	683	.	.	.	ID=PRO_0000080726;Note=DNA polymerase alpha-associated DNA helicase A	
+P34243	UniProtKB	Nucleotide binding	229	236	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P16622 1 393
+P16622	UniProtKB	Transit peptide	1	31	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042776;Dbxref=PMID:3042776	
+P16622	UniProtKB	Chain	32	393	.	.	.	ID=PRO_0000008879;Note=Ferrochelatase%2C mitochondrial	
+P16622	UniProtKB	Active site	351	351	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16622	UniProtKB	Sequence conflict	34	34	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16622	UniProtKB	Beta strand	39	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	55	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Beta strand	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Beta strand	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	76	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	104	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Beta strand	129	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	142	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Turn	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Beta strand	156	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Turn	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	171	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Beta strand	191	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	203	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	225	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Beta strand	229	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	239	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Turn	243	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	248	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Turn	263	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Beta strand	269	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Beta strand	278	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Beta strand	284	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1L8X	
+P16622	UniProtKB	Helix	287	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	295	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Beta strand	301	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	313	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	317	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	330	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Beta strand	333	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	343	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	367	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+P16622	UniProtKB	Helix	383	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ	
+##sequence-region P35843 1 434
+P35843	UniProtKB	Chain	1	434	.	.	.	ID=PRO_0000100385;Note=Protein HES1	
+##sequence-region Q04458 1 532
+Q04458	UniProtKB	Chain	1	532	.	.	.	ID=PRO_0000056597;Note=Fatty aldehyde dehydrogenase HFD1	
+Q04458	UniProtKB	Transmembrane	134	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04458	UniProtKB	Nucleotide binding	214	219	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04458	UniProtKB	Active site	236	236	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007	
+Q04458	UniProtKB	Active site	273	273	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007	
+Q04458	UniProtKB	Modified residue	111	111	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P39982 1 102
+P39982	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000202603;Note=Hypersensitivity to hygromycin-B protein 1	
+P39982	UniProtKB	Topological domain	1	17	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39982	UniProtKB	Transmembrane	18	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39982	UniProtKB	Topological domain	39	69	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39982	UniProtKB	Transmembrane	70	90	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39982	UniProtKB	Topological domain	91	102	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32480 1 875
+P32480	UniProtKB	Chain	1	875	.	.	.	ID=PRO_0000051017;Note=Protein HIR2	
+P32480	UniProtKB	Repeat	10	47	.	.	.	Note=WD 1	
+P32480	UniProtKB	Repeat	118	158	.	.	.	Note=WD 2	
+P32480	UniProtKB	Repeat	163	201	.	.	.	Note=WD 3	
+P32480	UniProtKB	Repeat	237	277	.	.	.	Note=WD 4	
+P32480	UniProtKB	Repeat	278	316	.	.	.	Note=WD 5	
+P32480	UniProtKB	Repeat	320	359	.	.	.	Note=WD 6	
+P32480	UniProtKB	Repeat	546	587	.	.	.	Note=WD 7	
+P32480	UniProtKB	Repeat	589	626	.	.	.	Note=WD 8	
+P32480	UniProtKB	Modified residue	713	713	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32480	UniProtKB	Sequence conflict	284	285	.	.	.	Note=KG->NF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32480	UniProtKB	Sequence conflict	373	374	.	.	.	Note=KK->FL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P00498 1 297
+P00498	UniProtKB	Chain	1	297	.	.	.	ID=PRO_0000151958;Note=ATP phosphoribosyltransferase	
+P00498	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q04344 1 158
+Q04344	UniProtKB	Chain	1	158	.	.	.	ID=PRO_0000109800;Note=Hit family protein 1	
+Q04344	UniProtKB	Domain	26	129	.	.	.	Note=HIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00464	
+Q04344	UniProtKB	Motif	114	118	.	.	.	Note=Histidine triad motif	
+Q04344	UniProtKB	Active site	116	116	.	.	.	Note=Tele-AMP-histidine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11805111;Dbxref=PMID:11805111	
+Q04344	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Loss of enzymatic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11805111;Dbxref=PMID:11805111	
+##sequence-region P49775 1 206
+P49775	UniProtKB	Chain	1	206	.	.	.	ID=PRO_0000109801;Note=Bis(5'-adenosyl)-triphosphatase	
+P49775	UniProtKB	Domain	3	115	.	.	.	Note=HIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00464	
+P49775	UniProtKB	Motif	96	100	.	.	.	Note=Histidine triad motif	
+P49775	UniProtKB	Active site	98	98	.	.	.	Note=Tele-AMP-histidine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12028594;Dbxref=PMID:12028594	
+P49775	UniProtKB	Mutagenesis	98	98	.	.	.	Note=Fails to reduce intracellular dinucleoside polyphosphate levels. H->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12028594;Dbxref=PMID:12028594	
+##sequence-region P40481 1 377
+P40481	UniProtKB	Chain	1	377	.	.	.	ID=PRO_0000202964;Note=Histidine protein methyltransferase 1	
+##sequence-region Q05787 1 833
+Q05787	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05787	UniProtKB	Chain	21	833	.	.	.	ID=PRO_0000240369;Note=ERAD-associated E3 ubiquitin-protein ligase component HRD3	
+Q05787	UniProtKB	Transmembrane	768	788	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05787	UniProtKB	Repeat	103	139	.	.	.	Note=Sel1-like 1	
+Q05787	UniProtKB	Repeat	143	186	.	.	.	Note=Sel1-like 2	
+Q05787	UniProtKB	Repeat	187	222	.	.	.	Note=Sel1-like 3	
+Q05787	UniProtKB	Repeat	413	445	.	.	.	Note=Sel1-like 4	
+Q05787	UniProtKB	Repeat	552	595	.	.	.	Note=Sel1-like 5	
+Q05787	UniProtKB	Repeat	596	627	.	.	.	Note=Sel1-like 6	
+Q05787	UniProtKB	Repeat	628	663	.	.	.	Note=Sel1-like 7	
+Q05787	UniProtKB	Compositional bias	809	819	.	.	.	Note=Poly-Gln	
+Q05787	UniProtKB	Glycosylation	101	101	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05787	UniProtKB	Glycosylation	123	123	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05787	UniProtKB	Glycosylation	142	142	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05787	UniProtKB	Glycosylation	429	429	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05787	UniProtKB	Glycosylation	611	611	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q99383 1 534
+Q99383	UniProtKB	Chain	1	534	.	.	.	ID=PRO_0000081658;Note=Nuclear polyadenylated RNA-binding protein 4	
+Q99383	UniProtKB	Domain	159	241	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q99383	UniProtKB	Domain	243	320	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q99383	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q99383	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q99383	UniProtKB	Modified residue	206	206	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q99383	UniProtKB	Modified residue	458	458	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q99383	UniProtKB	Modified residue	462	462	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q99383	UniProtKB	Helix	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Beta strand	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Helix	172	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Turn	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Beta strand	185	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Turn	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Beta strand	203	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Helix	211	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Beta strand	223	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM8	
+Q99383	UniProtKB	Helix	236	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Beta strand	243	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Helix	256	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Beta strand	265	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM8	
+Q99383	UniProtKB	Beta strand	270	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Beta strand	277	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Beta strand	284	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Helix	294	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Beta strand	304	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Beta strand	308	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+Q99383	UniProtKB	Beta strand	313	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK	
+##sequence-region P29295 1 494
+P29295	UniProtKB	Chain	1	494	.	.	.	ID=PRO_0000192859;Note=Casein kinase I homolog HRR25	
+P29295	UniProtKB	Domain	9	278	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P29295	UniProtKB	Nucleotide binding	15	23	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P29295	UniProtKB	Compositional bias	395	494	.	.	.	Note=Gln/Pro-rich	
+P29295	UniProtKB	Active site	128	128	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P29295	UniProtKB	Binding site	38	38	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P29295	UniProtKB	Modified residue	143	143	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P29295	UniProtKB	Beta strand	9	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Beta strand	22	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Turn	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Beta strand	34	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Turn	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XHL	
+P29295	UniProtKB	Helix	49	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Turn	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Beta strand	68	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Beta strand	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Beta strand	85	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	89	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Turn	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	102	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CZO	
+P29295	UniProtKB	Beta strand	134	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Beta strand	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	182	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	192	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Turn	212	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	224	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	237	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Turn	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	246	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	266	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Turn	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	289	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	330	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	339	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Turn	345	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	361	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	367	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P29295	UniProtKB	Helix	379	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+##sequence-region Q06674 1 414
+Q06674	UniProtKB	Chain	1	414	.	.	.	ID=PRO_0000233013;Note=Protein HIM1	
+##sequence-region P32479 1 840
+P32479	UniProtKB	Chain	1	840	.	.	.	ID=PRO_0000051016;Note=Protein HIR1	
+P32479	UniProtKB	Repeat	15	54	.	.	.	Note=WD 1	
+P32479	UniProtKB	Repeat	77	116	.	.	.	Note=WD 2	
+P32479	UniProtKB	Repeat	135	174	.	.	.	Note=WD 3	
+P32479	UniProtKB	Repeat	177	216	.	.	.	Note=WD 4	
+P32479	UniProtKB	Repeat	230	273	.	.	.	Note=WD 5	
+P32479	UniProtKB	Repeat	312	350	.	.	.	Note=WD 6	
+P32479	UniProtKB	Repeat	354	393	.	.	.	Note=WD 7	
+P32479	UniProtKB	Region	1	389	.	.	.	Note=Mediates transcriptional repression	
+P32479	UniProtKB	Region	304	840	.	.	.	Note=Interaction with ASF1	
+P32479	UniProtKB	Region	392	840	.	.	.	Note=Mediates transcriptional repression%2C self-association and interaction with HIR2	
+P32479	UniProtKB	Modified residue	610	610	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P32479	UniProtKB	Sequence conflict	32	32	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32479	UniProtKB	Sequence conflict	260	260	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32479	UniProtKB	Sequence conflict	260	260	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32479	UniProtKB	Sequence conflict	340	340	.	.	.	Note=W->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07172 1 385
+P07172	UniProtKB	Chain	1	385	.	.	.	ID=PRO_0000153509;Note=Histidinol-phosphate aminotransferase	
+P07172	UniProtKB	Modified residue	230	230	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07172	UniProtKB	Sequence conflict	110	112	.	.	.	Note=PGK->RE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07172	UniProtKB	Sequence conflict	125	125	.	.	.	Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07172	UniProtKB	Sequence conflict	142	142	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07172	UniProtKB	Sequence conflict	294	294	.	.	.	Note=R->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40037 1 129
+P40037	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000170312;Note=Protein HMF1	
+P40037	UniProtKB	Cross-link	52	52	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40037	UniProtKB	Beta strand	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Beta strand	22	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Beta strand	29	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Helix	49	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Helix	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Beta strand	74	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Helix	87	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Beta strand	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Beta strand	104	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+P40037	UniProtKB	Beta strand	118	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1	
+##sequence-region Q03973 1 246
+Q03973	UniProtKB	Chain	1	246	.	.	.	ID=PRO_0000048564;Note=High mobility group protein 1	
+Q03973	UniProtKB	DNA binding	106	179	.	.	.	Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267	
+Q03973	UniProtKB	Compositional bias	228	241	.	.	.	Note=Poly-Lys	
+##sequence-region P19807 1 563
+P19807	UniProtKB	Chain	1	563	.	.	.	ID=PRO_0000054155;Note=Choline transport protein	
+P19807	UniProtKB	Topological domain	1	57	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Transmembrane	58	78	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Topological domain	79	87	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Topological domain	109	182	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Topological domain	204	205	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Transmembrane	206	226	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Topological domain	227	255	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Transmembrane	256	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Topological domain	277	293	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Transmembrane	294	314	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Topological domain	315	342	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Transmembrane	343	363	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Topological domain	364	398	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Transmembrane	399	417	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Topological domain	418	426	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Transmembrane	427	445	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Topological domain	446	465	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Transmembrane	466	486	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Topological domain	487	491	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Transmembrane	492	512	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Topological domain	513	563	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19807	UniProtKB	Modified residue	42	42	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19807	UniProtKB	Glycosylation	7	7	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Glycosylation	20	20	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Glycosylation	248	248	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19807	UniProtKB	Glycosylation	341	341	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47124 1 396
+P47124	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9434768;Dbxref=PMID:9434768	
+P47124	UniProtKB	Chain	2	396	.	.	.	ID=PRO_0000080564;Note=Putative glycosyltransferase HOC1	
+P47124	UniProtKB	Topological domain	2	13	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47124	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47124	UniProtKB	Topological domain	35	396	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47124	UniProtKB	Glycosylation	37	37	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47124	UniProtKB	Sequence conflict	393	393	.	.	.	Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q9URQ5 1 78
+Q9URQ5	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q9URQ5	UniProtKB	Chain	2	78	.	.	.	ID=PRO_0000084085;Note=High temperature lethal protein 1	
+Q9URQ5	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P45820 1 110
+P45820	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000202728;Note=Putative uncharacterized protein HUR1	
+P45820	UniProtKB	Transmembrane	18	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32874 1 2273
+P32874	UniProtKB	Transit peptide	1	104	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32874	UniProtKB	Chain	105	2273	.	.	.	ID=PRO_0000146771;Note=Acetyl-CoA carboxylase%2C mitochondrial	
+P32874	UniProtKB	Domain	134	635	.	.	.	Note=Biotin carboxylation	
+P32874	UniProtKB	Domain	292	484	.	.	.	Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P32874	UniProtKB	Domain	763	837	.	.	.	Note=Biotinyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066	
+P32874	UniProtKB	Domain	1532	1867	.	.	.	Note=CoA carboxyltransferase N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01136	
+P32874	UniProtKB	Domain	1871	2187	.	.	.	Note=CoA carboxyltransferase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01137	
+P32874	UniProtKB	Nucleotide binding	332	337	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P32874	UniProtKB	Region	1532	2187	.	.	.	Note=Carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01138	
+P32874	UniProtKB	Active site	459	459	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32874	UniProtKB	Binding site	1776	1776	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32874	UniProtKB	Binding site	2080	2080	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32874	UniProtKB	Binding site	2082	2082	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32874	UniProtKB	Modified residue	804	804	.	.	.	Note=N6-biotinyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066	
+P32874	UniProtKB	Sequence conflict	661	661	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32874	UniProtKB	Sequence conflict	1027	1027	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38074 1 348
+P38074	UniProtKB	Chain	1	348	.	.	.	ID=PRO_0000212341;Note=Protein arginine N-methyltransferase 1	
+P38074	UniProtKB	Domain	20	322	.	.	.	Note=SAM-dependent MTase PRMT-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01015	
+P38074	UniProtKB	Active site	132	132	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009	
+P38074	UniProtKB	Active site	141	141	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009	
+P38074	UniProtKB	Binding site	33	33	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009	
+P38074	UniProtKB	Binding site	42	42	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009	
+P38074	UniProtKB	Binding site	66	66	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009	
+P38074	UniProtKB	Binding site	88	88	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009	
+P38074	UniProtKB	Binding site	117	117	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009	
+P38074	UniProtKB	Mutagenesis	18	18	.	.	.	Note=Cold-sensitive%3B reduces catalytic activity more than 20-fold at 14 degrees Celsius. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10652296;Dbxref=PMID:10652296	
+P38074	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Reduces catalytic activity between 5- to 25-fold. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10652296;Dbxref=PMID:10652296	
+P38074	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Abolishes catalytic activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10652296;Dbxref=PMID:10652296	
+P38074	UniProtKB	Helix	30	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Helix	40	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	61	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Helix	71	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	82	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Helix	92	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Turn	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	109	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Turn	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	126	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Helix	144	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	155	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	165	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Helix	176	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Helix	197	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Helix	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	220	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Turn	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Helix	232	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	236	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	250	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	272	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	286	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	302	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	315	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Helix	334	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+P38074	UniProtKB	Beta strand	339	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q	
+##sequence-region P32339 1 317
+P32339	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000209704;Note=Heme-binding protein HMX1	
+P32339	UniProtKB	Topological domain	1	289	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32339	UniProtKB	Transmembrane	290	310	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32339	UniProtKB	Sequence conflict	128	128	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32339	UniProtKB	Sequence conflict	285	285	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32339	UniProtKB	Sequence conflict	310	310	.	.	.	Note=V->VK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53096 1 452
+P53096	UniProtKB	Chain	1	452	.	.	.	ID=PRO_0000114723;Note=Probable histone deacetylase HOS2	
+P53096	UniProtKB	Region	26	340	.	.	.	Note=Histone deacetylase	
+P53096	UniProtKB	Active site	197	197	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53096	UniProtKB	Mutagenesis	196	197	.	.	.	Note=Leads to hyperacetylation. HH->AA	
+P53096	UniProtKB	Sequence conflict	352	364	.	.	.	Note=PFRDSFGPDYSLY->HSGTHSGRIIHFI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02959 1 697
+Q02959	UniProtKB	Chain	1	697	.	.	.	ID=PRO_0000114727;Note=Histone deacetylase HOS3	
+Q02959	UniProtKB	Region	40	440	.	.	.	Note=Histone deacetylase	
+Q02959	UniProtKB	Active site	196	196	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02959	UniProtKB	Modified residue	582	582	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02959	UniProtKB	Modified residue	583	583	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02959	UniProtKB	Modified residue	613	613	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02959	UniProtKB	Modified residue	629	629	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+##sequence-region P32478 1 413
+P32478	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1570286,ECO:0000269|PubMed:9301021;Dbxref=PMID:1570286,PMID:9301021	
+P32478	UniProtKB	Propeptide	19	72	.	.	.	ID=PRO_0000033260;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10234784,ECO:0000269|PubMed:1570286,ECO:0000269|PubMed:18657192,ECO:0000269|PubMed:9301021;Dbxref=PMID:10234784,PMID:1570286,PMID:18657192,PMID:9301021	
+P32478	UniProtKB	Chain	73	413	.	.	.	ID=PRO_0000033261;Note=Cell wall mannoprotein HSP150	
+P32478	UniProtKB	Repeat	73	89	.	.	.	Note=PIR1/2/3 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32478	UniProtKB	Repeat	97	115	.	.	.	Note=PIR1/2/3 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32478	UniProtKB	Repeat	116	134	.	.	.	Note=PIR1/2/3 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32478	UniProtKB	Repeat	140	158	.	.	.	Note=PIR1/2/3 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32478	UniProtKB	Repeat	164	182	.	.	.	Note=PIR1/2/3 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32478	UniProtKB	Repeat	188	206	.	.	.	Note=PIR1/2/3 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32478	UniProtKB	Repeat	207	225	.	.	.	Note=PIR1/2/3 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32478	UniProtKB	Repeat	226	244	.	.	.	Note=PIR1/2/3 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32478	UniProtKB	Repeat	245	263	.	.	.	Note=PIR1/2/3 9;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32478	UniProtKB	Repeat	264	282	.	.	.	Note=PIR1/2/3 10;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32478	UniProtKB	Repeat	283	300	.	.	.	Note=PIR1/2/3 11;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+P32478	UniProtKB	Site	72	73	.	.	.	Note=Cleavage%3B by KEX2	
+P32478	UniProtKB	Site	81	81	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32478	UniProtKB	Site	107	107	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32478	UniProtKB	Site	126	126	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32478	UniProtKB	Site	150	150	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32478	UniProtKB	Site	174	174	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32478	UniProtKB	Site	198	198	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32478	UniProtKB	Site	217	217	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32478	UniProtKB	Site	236	236	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32478	UniProtKB	Site	255	255	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32478	UniProtKB	Site	274	274	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32478	UniProtKB	Site	292	292	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32478	UniProtKB	Natural variant	96	96	.	.	.	Note=In strain: B1%2C TD04/1a and TD04/1b. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657192;Dbxref=PMID:18657192	
+P32478	UniProtKB	Natural variant	116	163	.	.	.	Note=In strain: B1%2C TD04/1a and TD04/1b. Missing	
+P32478	UniProtKB	Natural variant	175	175	.	.	.	Note=In strain: TD04/1a and TD04/1b. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657192;Dbxref=PMID:18657192	
+P32478	UniProtKB	Natural variant	176	176	.	.	.	Note=In strain: TD04/1b. Q->QAATTTASVSTKSSAAAVSQIGDGQIQATTKTTAAAVSQIGDGQIQ	
+P32478	UniProtKB	Natural variant	199	199	.	.	.	Note=In strain: B1%2C TD04/1a and TD04/1b. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657192;Dbxref=PMID:18657192	
+P32478	UniProtKB	Natural variant	226	244	.	.	.	Note=In strain: B1%2C TD04/1a and TD04/1b. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657192;Dbxref=PMID:18657192	
+P32478	UniProtKB	Natural variant	297	297	.	.	.	Note=In strain: B1%2C TD04/1a and TD04/1b. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657192;Dbxref=PMID:18657192	
+P32478	UniProtKB	Sequence conflict	47	47	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32478	UniProtKB	Sequence conflict	121	123	.	.	.	Note=QIG->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32478	UniProtKB	Sequence conflict	152	175	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32478	UniProtKB	Sequence conflict	211	211	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32478	UniProtKB	Sequence conflict	211	211	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32478	UniProtKB	Sequence conflict	219	219	.	.	.	Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32478	UniProtKB	Sequence conflict	219	219	.	.	.	Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32478	UniProtKB	Sequence conflict	226	226	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32478	UniProtKB	Sequence conflict	226	226	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P34244 1 1518
+P34244	UniProtKB	Chain	1	1518	.	.	.	ID=PRO_0000086148;Note=Probable serine/threonine-protein kinase HSL1	
+P34244	UniProtKB	Domain	81	369	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P34244	UniProtKB	Nucleotide binding	87	95	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P34244	UniProtKB	Active site	239	239	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P34244	UniProtKB	Binding site	110	110	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P34244	UniProtKB	Modified residue	511	511	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34244	UniProtKB	Modified residue	629	629	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P34244	UniProtKB	Modified residue	685	685	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34244	UniProtKB	Modified residue	837	837	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34244	UniProtKB	Modified residue	866	866	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34244	UniProtKB	Modified residue	1220	1220	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P34244	UniProtKB	Modified residue	1250	1250	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34244	UniProtKB	Modified residue	1284	1284	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P34244	UniProtKB	Modified residue	1287	1287	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P34244	UniProtKB	Modified residue	1325	1325	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34244	UniProtKB	Sequence conflict	1482	1482	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P34244	UniProtKB	Sequence conflict	1482	1482	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P34244	UniProtKB	Sequence conflict	1482	1482	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32590 1 693
+P32590	UniProtKB	Chain	1	693	.	.	.	ID=PRO_0000078397;Note=Heat shock protein homolog SSE2	
+P32590	UniProtKB	Sequence conflict	160	167	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40985 1 892
+P40985	UniProtKB	Chain	1	892	.	.	.	ID=PRO_0000084094;Note=Probable E3 ubiquitin-protein ligase HUL4	
+P40985	UniProtKB	Domain	792	892	.	.	.	Note=HECT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104	
+P40985	UniProtKB	Active site	860	860	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104	
+P40985	UniProtKB	Sequence conflict	362	362	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40985	UniProtKB	Sequence conflict	410	410	.	.	.	Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40985	UniProtKB	Sequence conflict	418	418	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40985	UniProtKB	Sequence conflict	514	519	.	.	.	Note=GKSVDV->RQIRRR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40985	UniProtKB	Sequence conflict	589	607	.	.	.	Note=ESSRSWFAIDPPNFDKSKG->KKAHVHGLPLTLQILTNQR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40985	UniProtKB	Sequence conflict	705	705	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40985	UniProtKB	Sequence conflict	723	724	.	.	.	Note=KH->ND;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53982 1 420
+P53982	UniProtKB	Chain	1	420	.	.	.	ID=PRO_0000083588;Note=Isocitrate dehydrogenase [NADP]	
+P53982	UniProtKB	Nucleotide binding	75	77	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Nucleotide binding	310	315	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Region	94	100	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Metal binding	252	252	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Metal binding	275	275	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Binding site	77	77	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Binding site	82	82	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Binding site	109	109	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Binding site	132	132	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Binding site	260	260	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Binding site	328	328	.	.	.	Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Site	139	139	.	.	.	Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53982	UniProtKB	Site	212	212	.	.	.	Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P48362 1 394
+P48362	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P48362	UniProtKB	Chain	2	394	.	.	.	ID=PRO_0000083966;Note=Protein HGH1	
+P48362	UniProtKB	Compositional bias	371	389	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P48362	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P06775 1 603
+P06775	UniProtKB	Chain	1	603	.	.	.	ID=PRO_0000054154;Note=Histidine permease	
+P06775	UniProtKB	Topological domain	1	95	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	96	116	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	117	121	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	143	165	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	166	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	186	203	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	204	223	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	224	236	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	237	255	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	256	279	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	280	297	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	298	321	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	322	342	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	343	376	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	377	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	397	423	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	424	442	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	443	451	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	452	472	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	473	491	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	492	510	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	511	530	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Transmembrane	531	549	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Topological domain	550	603	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06775	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P12684 1 1045
+P12684	UniProtKB	Chain	1	1045	.	.	.	ID=PRO_0000114457;Note=3-hydroxy-3-methylglutaryl-coenzyme A reductase 2	
+P12684	UniProtKB	Topological domain	1	24	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Topological domain	46	186	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Topological domain	208	216	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Topological domain	238	243	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Transmembrane	244	264	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Topological domain	265	301	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Transmembrane	302	322	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Topological domain	323	324	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Transmembrane	325	345	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Topological domain	346	402	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Transmembrane	403	423	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Topological domain	424	497	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Transmembrane	498	518	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Topological domain	519	1045	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Domain	188	356	.	.	.	Note=SSD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00199	
+P12684	UniProtKB	Region	524	613	.	.	.	Note=Linker	
+P12684	UniProtKB	Region	614	1045	.	.	.	Note=Catalytic	
+P12684	UniProtKB	Active site	710	710	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12684	UniProtKB	Active site	844	844	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12684	UniProtKB	Active site	920	920	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12684	UniProtKB	Active site	1016	1016	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10003	
+P12684	UniProtKB	Modified residue	565	565	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P12684	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Glycosylation	150	150	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Glycosylation	158	158	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Glycosylation	179	179	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Glycosylation	428	428	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Glycosylation	455	455	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12684	UniProtKB	Sequence conflict	29	29	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53389 1 586
+P53389	UniProtKB	Chain	1	586	.	.	.	ID=PRO_0000084026;Note=Protein HOL1	
+P53389	UniProtKB	Topological domain	1	66	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Transmembrane	67	87	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Topological domain	88	103	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Topological domain	125	130	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Topological domain	152	189	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Transmembrane	190	210	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Topological domain	211	219	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Transmembrane	220	240	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Topological domain	241	362	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Transmembrane	363	383	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Topological domain	384	413	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Transmembrane	414	434	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Topological domain	435	448	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Transmembrane	449	469	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Topological domain	470	477	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Transmembrane	478	498	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Topological domain	499	508	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Transmembrane	509	529	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Topological domain	530	544	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Transmembrane	545	565	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Topological domain	566	586	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53389	UniProtKB	Sequence conflict	510	510	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05164 1 967
+Q05164	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05164	UniProtKB	Chain	24	946	.	.	.	ID=PRO_0000268177;Note=Haze protective factor 1	
+Q05164	UniProtKB	Propeptide	947	967	.	.	.	ID=PRO_0000268178;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05164	UniProtKB	Repeat	93	105	.	.	.	Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	106	118	.	.	.	Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	119	131	.	.	.	Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	132	144	.	.	.	Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	153	165	.	.	.	Note=1-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	166	178	.	.	.	Note=1-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	179	191	.	.	.	Note=1-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	192	204	.	.	.	Note=1-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	205	217	.	.	.	Note=1-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	218	230	.	.	.	Note=1-10%3B approximate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	234	247	.	.	.	Note=1-11%3B approximate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	248	259	.	.	.	Note=1-12%3B approximate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	266	278	.	.	.	Note=1-13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	745	780	.	.	.	Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	781	815	.	.	.	Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	816	854	.	.	.	Note=2-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	855	893	.	.	.	Note=2-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Repeat	894	902	.	.	.	Note=2-5%3B truncated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q05164	UniProtKB	Region	93	278	.	.	.	Note=13 X approximate repeats%2C Ser-rich	
+Q05164	UniProtKB	Region	745	902	.	.	.	Note=4.5 X approximate tandem repeats%2C Thr-rich	
+Q05164	UniProtKB	Lipidation	946	946	.	.	.	Note=GPI-anchor amidated alanine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05164	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05164	UniProtKB	Glycosylation	35	35	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05164	UniProtKB	Glycosylation	493	493	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05164	UniProtKB	Glycosylation	601	601	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05164	UniProtKB	Glycosylation	638	638	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38753 1 452
+P38753	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38753	UniProtKB	Chain	2	452	.	.	.	ID=PRO_0000202885;Note=Class E vacuolar protein-sorting machinery protein HSE1	
+P38753	UniProtKB	Domain	15	145	.	.	.	Note=VHS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00218	
+P38753	UniProtKB	Domain	162	181	.	.	.	Note=UIM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+P38753	UniProtKB	Domain	217	276	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P38753	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38753	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38753	UniProtKB	Helix	289	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW	
+P38753	UniProtKB	Helix	296	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW	
+P38753	UniProtKB	Helix	316	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW	
+P38753	UniProtKB	Helix	322	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW	
+P38753	UniProtKB	Helix	332	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW	
+P38753	UniProtKB	Helix	335	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW	
+P38753	UniProtKB	Turn	372	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW	
+##sequence-region P10961 1 833
+P10961	UniProtKB	Chain	1	833	.	.	.	ID=PRO_0000124581;Note=Heat shock factor protein	
+P10961	UniProtKB	DNA binding	172	277	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3044612;Dbxref=PMID:3044612	
+P10961	UniProtKB	Region	350	402	.	.	.	Note=Involved in trimerization	
+P10961	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P10961	UniProtKB	Modified residue	97	97	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P10961	UniProtKB	Modified residue	450	450	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P10961	UniProtKB	Modified residue	458	458	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P10961	UniProtKB	Modified residue	471	471	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P10961	UniProtKB	Modified residue	478	478	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P10961	UniProtKB	Modified residue	528	528	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P10961	UniProtKB	Sequence conflict	522	522	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10961	UniProtKB	Sequence conflict	557	580	.	.	.	Note=FDIESNNDRKISEIPFDDEEEEET->LISNLIMTAKFQKFLLMTKKKKKP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10961	UniProtKB	Sequence conflict	831	831	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99181 1 213
+Q99181	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000081613;Note=Protein HSH49	
+Q99181	UniProtKB	Domain	9	88	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q99181	UniProtKB	Domain	108	185	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q99181	UniProtKB	Beta strand	10	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL	
+Q99181	UniProtKB	Helix	22	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL	
+Q99181	UniProtKB	Turn	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL	
+Q99181	UniProtKB	Beta strand	35	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL	
+Q99181	UniProtKB	Turn	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL	
+Q99181	UniProtKB	Beta strand	51	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL	
+Q99181	UniProtKB	Helix	60	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL	
+Q99181	UniProtKB	Turn	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL	
+Q99181	UniProtKB	Beta strand	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL	
+Q99181	UniProtKB	Beta strand	108	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB	
+Q99181	UniProtKB	Helix	121	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB	
+Q99181	UniProtKB	Beta strand	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB	
+Q99181	UniProtKB	Beta strand	139	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB	
+Q99181	UniProtKB	Beta strand	148	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB	
+Q99181	UniProtKB	Helix	158	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB	
+Q99181	UniProtKB	Beta strand	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB	
+Q99181	UniProtKB	Beta strand	176	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB	
+Q99181	UniProtKB	Turn	192	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB	
+Q99181	UniProtKB	Helix	196	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB	
+##sequence-region P22943 1 109
+P22943	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000084081;Note=12 kDa heat shock protein	
+P22943	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P22943	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22943	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P22943	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P22943	UniProtKB	Modified residue	97	97	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P22943	UniProtKB	Natural variant	46	46	.	.	.	Note=In strain: Ar5-H12. P->T	
+P22943	UniProtKB	Helix	8	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9Q	
+P22943	UniProtKB	Helix	25	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9Q	
+P22943	UniProtKB	Helix	53	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9Q	
+P22943	UniProtKB	Helix	58	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9Q	
+P22943	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LJL	
+P22943	UniProtKB	Beta strand	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LJL	
+P22943	UniProtKB	Helix	74	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9Q	
+##sequence-region P53687 1 447
+P53687	UniProtKB	Chain	1	447	.	.	.	ID=PRO_0000110283;Note=NAD-dependent histone deacetylase HST3	
+P53687	UniProtKB	Domain	43	349	.	.	.	Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53687	UniProtKB	Nucleotide binding	60	79	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53687	UniProtKB	Nucleotide binding	151	154	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53687	UniProtKB	Nucleotide binding	282	284	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53687	UniProtKB	Nucleotide binding	312	314	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53687	UniProtKB	Active site	187	187	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53687	UniProtKB	Metal binding	195	195	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53687	UniProtKB	Metal binding	198	198	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53687	UniProtKB	Metal binding	220	220	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53687	UniProtKB	Metal binding	223	223	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53687	UniProtKB	Binding site	333	333	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53687	UniProtKB	Sequence conflict	418	418	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32485 1 435
+P32485	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32485	UniProtKB	Chain	2	435	.	.	.	ID=PRO_0000186331;Note=Mitogen-activated protein kinase HOG1	
+P32485	UniProtKB	Domain	23	302	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32485	UniProtKB	Nucleotide binding	29	37	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32485	UniProtKB	Motif	174	176	.	.	.	Note=TXY	
+P32485	UniProtKB	Compositional bias	364	379	.	.	.	Note=Ala-rich	
+P32485	UniProtKB	Active site	144	144	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P32485	UniProtKB	Binding site	52	52	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32485	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32485	UniProtKB	Modified residue	174	174	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12637550;Dbxref=PMID:12637550	
+P32485	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12637550;Dbxref=PMID:19779198,PMID:12637550	
+P32485	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Impairs catalytic activity%2C nuclear translocation%2C expression of CTT1 and increases sensitivity to osmotic shock. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16896207,ECO:0000269|PubMed:17363249,ECO:0000269|PubMed:7523111,ECO:0000269|PubMed:8943326;Dbxref=PMID:16896207,PMID:17363249,PMID:7523111,PMID:8943326	
+P32485	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396	
+P32485	UniProtKB	Mutagenesis	144	144	.	.	.	Note=Impairs catalytic activity and nuclear translocation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16896207;Dbxref=PMID:16896207	
+P32485	UniProtKB	Mutagenesis	170	170	.	.	.	Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396	
+P32485	UniProtKB	Mutagenesis	174	174	.	.	.	Note=Impairs catalytic activity%2C expression of CTT1 and increases sensitivity to osmotic shock. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12637550,ECO:0000269|PubMed:7523111;Dbxref=PMID:12637550,PMID:7523111	
+P32485	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Impairs expression of CTT1 and increases sensitivity to osmotic shock. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12637550,ECO:0000269|PubMed:7523111;Dbxref=PMID:12637550,PMID:7523111	
+P32485	UniProtKB	Mutagenesis	314	314	.	.	.	Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396	
+P32485	UniProtKB	Mutagenesis	318	318	.	.	.	Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. F->L%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396	
+P32485	UniProtKB	Mutagenesis	320	320	.	.	.	Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396	
+P32485	UniProtKB	Mutagenesis	322	322	.	.	.	Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396	
+P32485	UniProtKB	Mutagenesis	332	332	.	.	.	Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396	
+P32485	UniProtKB	Mutagenesis	391	391	.	.	.	Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396	
+P32485	UniProtKB	Sequence conflict	9	9	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32485	UniProtKB	Sequence conflict	409	435	.	.	.	Note=VSDHVAANDTITDYGNQAIQYANEFQQ->GQRSCSCK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12122 1 440
+Q12122	UniProtKB	Domain	37	290	.	.	.	Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151	
+Q12122	UniProtKB	Modified residue	399	399	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48570	
+Q12122	UniProtKB	Modified residue	410	410	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12122	UniProtKB	Sequence conflict	199	199	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03213 1 719
+Q03213	UniProtKB	Chain	1	719	.	.	.	ID=PRO_0000203317;Note=High-osmolarity-induced transcription protein 1	
+Q03213	UniProtKB	Modified residue	146	146	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03213	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03213	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Impairs HOT1 phosphorylation%3B when associated with A-70%3B A-153%3B A-360 and A-410. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12743037;Dbxref=PMID:12743037	
+Q03213	UniProtKB	Mutagenesis	70	70	.	.	.	Note=Impairs HOT1 phosphorylation%3B when associated with A-30%3B A-153%3B A-360 and A-410. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12743037;Dbxref=PMID:12743037	
+Q03213	UniProtKB	Mutagenesis	153	153	.	.	.	Note=Impairs HOT1 phosphorylation%3B when associated with A-30%3B A-70%3B A-360 and A-410. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12743037;Dbxref=PMID:12743037	
+Q03213	UniProtKB	Mutagenesis	360	360	.	.	.	Note=Impairs HOT1 phosphorylation%3B when associated with A-30%3B A-70%3B A-153 and A-410. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12743037;Dbxref=PMID:12743037	
+Q03213	UniProtKB	Mutagenesis	410	410	.	.	.	Note=Impairs HOT1 phosphorylation%3B when associated with A-30%3B A-70%3B A-153 and A-360. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12743037;Dbxref=PMID:12743037	
+##sequence-region P39734 1 528
+P39734	UniProtKB	Chain	1	528	.	.	.	ID=PRO_0000202415;Note=Protein HPH2	
+P39734	UniProtKB	Transmembrane	505	521	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39734	UniProtKB	Compositional bias	308	328	.	.	.	Note=Poly-Ser	
+P39734	UniProtKB	Compositional bias	512	517	.	.	.	Note=Poly-Ile	
+##sequence-region Q12347 1 344
+Q12347	UniProtKB	Chain	1	344	.	.	.	ID=PRO_0000245842;Note=F-box protein HRT3	
+Q12347	UniProtKB	Repeat	14	47	.	.	.	Note=TPR	
+Q12347	UniProtKB	Domain	98	148	.	.	.	Note=F-box	
+##sequence-region P15992 1 214
+P15992	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:2673926;Dbxref=PMID:22814378,PMID:2673926	
+P15992	UniProtKB	Chain	2	214	.	.	.	ID=PRO_0000126004;Note=Heat shock protein 26	
+P15992	UniProtKB	Domain	86	207	.	.	.	Note=sHSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00285	
+P15992	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P15992	UniProtKB	Modified residue	42	42	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P15992	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P15992	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P15992	UniProtKB	Modified residue	208	208	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P15992	UniProtKB	Modified residue	211	211	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P15992	UniProtKB	Sequence conflict	32	32	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15992	UniProtKB	Sequence conflict	207	207	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15992	UniProtKB	Sequence conflict	212	212	.	.	.	Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25619 1 332
+P25619	UniProtKB	Chain	1	332	.	.	.	ID=PRO_0000196284;Note=30 kDa heat shock protein	
+P25619	UniProtKB	Topological domain	1	34	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Topological domain	56	65	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Topological domain	87	121	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Topological domain	143	157	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Transmembrane	158	178	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Topological domain	179	181	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Topological domain	203	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Topological domain	237	248	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Transmembrane	249	269	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Topological domain	270	332	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25619	UniProtKB	Compositional bias	290	332	.	.	.	Note=Glu-rich (acidic)	
+P25619	UniProtKB	Modified residue	308	308	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25619	UniProtKB	Modified residue	331	331	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q08992 1 237
+Q08992	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000270555;Note=Probable glutathione-independent glyoxalase HSP32	
+Q08992	UniProtKB	Active site	138	138	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432	
+Q08992	UniProtKB	Active site	139	139	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432	
+Q08992	UniProtKB	Active site	170	170	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432	
+##sequence-region P40325 1 198
+P40325	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40325	UniProtKB	Chain	2	198	.	.	.	ID=PRO_0000202865;Note=Proline-rich protein HUA1	
+P40325	UniProtKB	Compositional bias	27	92	.	.	.	Note=Pro-rich	
+P40325	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40325	UniProtKB	Cross-link	3	3	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P40325	UniProtKB	Cross-link	18	18	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region Q6Q546 1 73
+Q6Q546	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000114879;Note=Ubiquitin-like modifier HUB1	
+Q6Q546	UniProtKB	Domain	1	73	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+Q6Q546	UniProtKB	Sequence conflict	12	12	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q6Q546	UniProtKB	Beta strand	1	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU	
+Q6Q546	UniProtKB	Turn	9	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M94	
+Q6Q546	UniProtKB	Beta strand	13	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU	
+Q6Q546	UniProtKB	Helix	24	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU	
+Q6Q546	UniProtKB	Helix	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU	
+Q6Q546	UniProtKB	Beta strand	42	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU	
+Q6Q546	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU	
+Q6Q546	UniProtKB	Beta strand	67	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU	
+##sequence-region Q12345 1 250
+Q12345	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000084155;Note=Ino eighty subunit 3	
+Q12345	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12345	UniProtKB	Modified residue	211	211	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P39730 1 1002
+P39730	UniProtKB	Chain	1	1002	.	.	.	ID=PRO_0000137296;Note=Eukaryotic translation initiation factor 5B	
+P39730	UniProtKB	Domain	403	621	.	.	.	Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P39730	UniProtKB	Nucleotide binding	415	420	.	.	.	Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24686316;Dbxref=PMID:24686316	
+P39730	UniProtKB	Nucleotide binding	437	439	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9	
+P39730	UniProtKB	Nucleotide binding	530	533	.	.	.	Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24686316;Dbxref=PMID:24686316	
+P39730	UniProtKB	Nucleotide binding	599	600	.	.	.	Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24686316;Dbxref=PMID:24686316	
+P39730	UniProtKB	Region	412	419	.	.	.	Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P39730	UniProtKB	Region	437	441	.	.	.	Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P39730	UniProtKB	Region	476	479	.	.	.	Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P39730	UniProtKB	Region	530	533	.	.	.	Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P39730	UniProtKB	Region	598	600	.	.	.	Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P39730	UniProtKB	Compositional bias	361	371	.	.	.	Note=Poly-Glu	
+P39730	UniProtKB	Metal binding	415	415	.	.	.	Note=Monovalent cation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9	
+P39730	UniProtKB	Metal binding	419	419	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9	
+P39730	UniProtKB	Metal binding	437	437	.	.	.	Note=Monovalent cation%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9	
+P39730	UniProtKB	Metal binding	439	439	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9	
+P39730	UniProtKB	Binding site	431	431	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9	
+P39730	UniProtKB	Modified residue	405	405	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39730	UniProtKB	Mutagenesis	439	439	.	.	.	Note=Impairs the GTPase activity%2C but not the ribosome joining function. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12507428;Dbxref=PMID:12507428	
+P39730	UniProtKB	Mutagenesis	479	479	.	.	.	Note=Reduces GTP binding and impairs subunit joining and ribosome-dependent GTP hydrolysis. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17913624;Dbxref=PMID:17913624	
+P39730	UniProtKB	Mutagenesis	480	480	.	.	.	Note=Impairs the GTPase activity%2C but not the ribosome joining function. H->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12471154,ECO:0000269|PubMed:12507428;Dbxref=PMID:12471154,PMID:12507428	
+P39730	UniProtKB	Sequence conflict	266	266	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39730	UniProtKB	Sequence conflict	293	293	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39730	UniProtKB	Sequence conflict	460	460	.	.	.	Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39730	UniProtKB	Sequence conflict	471	471	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39730	UniProtKB	Sequence conflict	641	641	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39730	UniProtKB	Sequence conflict	722	722	.	.	.	Note=L->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39730	UniProtKB	Sequence conflict	970	970	.	.	.	Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39730	UniProtKB	Beta strand	407	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Helix	421	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	428	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Beta strand	439	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Beta strand	442	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	449	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	457	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	469	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	478	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	481	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	487	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	490	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	495	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Turn	503	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	509	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	525	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	532	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	546	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	555	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Turn	574	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	578	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	582	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Turn	588	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	591	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Turn	599	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	605	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Turn	621	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	631	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Turn	641	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	644	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	661	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	669	681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	685	688	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	692	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	720	723	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Beta strand	726	728	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	730	746	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	750	752	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Beta strand	755	761	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	762	774	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	779	781	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	784	787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	789	796	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	798	801	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	803	805	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Beta strand	807	812	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	817	826	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	829	835	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Helix	836	851	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S	
+P39730	UniProtKB	Beta strand	866	879	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Beta strand	881	892	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Beta strand	896	903	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Turn	904	907	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Beta strand	908	922	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Beta strand	925	931	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Beta strand	939	944	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Turn	954	956	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Beta strand	963	965	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Helix	969	974	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Helix	978	981	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+P39730	UniProtKB	Helix	986	999	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI	
+##sequence-region Q04432 1 237
+Q04432	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000157852;Note=Glutathione-independent glyoxalase HSP31	
+Q04432	UniProtKB	Active site	138	138	.	.	.	Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:14745011,ECO:0000305|PubMed:15130476;Dbxref=PMID:14745011,PMID:15130476	
+Q04432	UniProtKB	Active site	139	139	.	.	.	Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:14745011,ECO:0000305|PubMed:15130476;Dbxref=PMID:14745011,PMID:15130476	
+Q04432	UniProtKB	Active site	170	170	.	.	.	Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:14745011,ECO:0000305|PubMed:15130476;Dbxref=PMID:14745011,PMID:15130476	
+Q04432	UniProtKB	Modified residue	138	138	.	.	.	Note=Cysteine sulfinic acid (-SO2H);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14745011;Dbxref=PMID:14745011	
+Q04432	UniProtKB	Sequence conflict	31	31	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q04432	UniProtKB	Beta strand	5	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	28	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Beta strand	44	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Beta strand	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QVZ	
+Q04432	UniProtKB	Helix	58	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Turn	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	68	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	80	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Beta strand	100	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	118	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Beta strand	133	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	140	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Turn	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Beta strand	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Turn	156	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	167	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	176	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	187	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Beta strand	209	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Beta strand	215	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+Q04432	UniProtKB	Helix	224	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX	
+##sequence-region Q12329 1 375
+Q12329	UniProtKB	Chain	1	375	.	.	.	ID=PRO_0000126005;Note=Heat shock protein 42	
+Q12329	UniProtKB	Domain	237	356	.	.	.	Note=sHSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00285	
+Q12329	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12329	UniProtKB	Modified residue	213	213	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12329	UniProtKB	Modified residue	214	214	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12329	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12329	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q05931 1 657
+Q05931	UniProtKB	Mutagenesis	462	462	.	.	.	Note=Decreased interaction with ISU1. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15958384;Dbxref=PMID:15958384	
+Q05931	UniProtKB	Mutagenesis	472	472	.	.	.	Note=10-fold decrease in interaction with ISU1. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15958384;Dbxref=PMID:15958384	
+##sequence-region P38790 1 280
+P38790	UniProtKB	Chain	1	280	.	.	.	ID=PRO_0000202898;Note=Hydroxyacyl-thioester dehydratase type 2%2C mitochondrial	
+##sequence-region P53119 1 910
+P53119	UniProtKB	Chain	1	910	.	.	.	ID=PRO_0000084095;Note=Probable E3 ubiquitin-protein ligase HUL5	
+P53119	UniProtKB	Domain	810	910	.	.	.	Note=HECT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104	
+P53119	UniProtKB	Active site	878	878	.	.	.	Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104	
+P53119	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P39924 1 564
+P39924	UniProtKB	Chain	1	564	.	.	.	ID=PRO_0000050402;Note=Hexose transporter HXT13	
+P39924	UniProtKB	Topological domain	1	52	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	74	109	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	131	136	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	137	157	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	158	167	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	189	194	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	195	215	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	216	229	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	230	250	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	251	333	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	334	350	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	351	356	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	357	374	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	375	381	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	382	402	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	403	424	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	425	445	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	446	462	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	463	483	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	484	484	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Transmembrane	485	505	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39924	UniProtKB	Topological domain	506	564	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P54854 1 567
+P54854	UniProtKB	Chain	1	567	.	.	.	ID=PRO_0000050404;Note=Hexose transporter HXT15	
+P54854	UniProtKB	Topological domain	1	55	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	77	112	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	134	139	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	161	170	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	192	197	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	219	232	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	254	336	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	337	353	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	354	359	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	360	377	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	378	384	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	385	405	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	406	427	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	428	448	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	449	465	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	466	486	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	487	487	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Transmembrane	488	508	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54854	UniProtKB	Topological domain	509	567	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32465 1 570
+P32465	UniProtKB	Chain	1	570	.	.	.	ID=PRO_0000050391;Note=Low-affinity glucose transporter HXT1	
+P32465	UniProtKB	Topological domain	1	60	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	61	81	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	82	116	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	138	143	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	144	164	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	165	174	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	196	201	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	223	236	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	237	257	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	258	340	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	341	357	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	358	363	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	364	381	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	382	388	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	389	409	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	410	431	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	432	452	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	453	469	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	470	490	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	491	491	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Transmembrane	492	512	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Topological domain	513	570	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32465	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32465	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32465	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32465	UniProtKB	Sequence conflict	70	70	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32465	UniProtKB	Sequence conflict	469	469	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32466 1 567
+P32466	UniProtKB	Chain	1	567	.	.	.	ID=PRO_0000050393;Note=Low-affinity glucose transporter HXT3	
+P32466	UniProtKB	Topological domain	1	57	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	58	78	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	79	113	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	135	140	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	162	171	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	172	192	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	193	198	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	220	233	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	234	254	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	255	337	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	338	354	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	355	360	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	361	378	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	379	385	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	386	406	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	407	428	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	429	449	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	450	466	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	467	487	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	488	488	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Transmembrane	489	509	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Topological domain	510	567	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32466	UniProtKB	Glycosylation	225	225	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32466	UniProtKB	Glycosylation	416	416	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38695 1 592
+P38695	UniProtKB	Chain	1	592	.	.	.	ID=PRO_0000050395;Note=Probable glucose transporter HXT5	
+P38695	UniProtKB	Topological domain	1	81	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	103	137	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	138	158	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	159	164	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	165	185	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	186	195	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	196	216	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	217	222	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	223	243	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	244	257	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	258	278	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	279	361	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	362	378	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	379	384	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	385	402	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	403	409	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	410	430	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	431	452	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	453	473	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	474	490	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	491	511	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	512	512	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Transmembrane	513	533	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Topological domain	534	592	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Glycosylation	126	126	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Glycosylation	249	249	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38695	UniProtKB	Cross-link	61	61	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region P39004 1 570
+P39004	UniProtKB	Chain	1	570	.	.	.	ID=PRO_0000050397;Note=High-affinity hexose transporter HXT7	
+P39004	UniProtKB	Topological domain	1	60	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	61	81	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	82	116	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	138	143	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	144	164	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	165	174	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	196	201	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	223	236	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	237	257	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	258	340	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	341	357	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	358	363	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	364	381	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	382	388	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	389	409	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	410	431	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	432	452	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	453	469	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	470	490	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	491	491	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Transmembrane	492	512	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Topological domain	513	570	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Modified residue	556	556	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39004	UniProtKB	Glycosylation	91	91	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39004	UniProtKB	Cross-link	560	560	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region P32464 1 399
+P32464	UniProtKB	Chain	1	399	.	.	.	ID=PRO_0000209836;Note=Protein HYM1	
+##sequence-region P41734 1 238
+P41734	UniProtKB	Chain	1	238	.	.	.	ID=PRO_0000084126;Note=Isoamyl acetate-hydrolyzing esterase	
+P41734	UniProtKB	Active site	12	12	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41734	UniProtKB	Active site	187	187	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41734	UniProtKB	Active site	190	190	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41734	UniProtKB	Binding site	53	53	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41734	UniProtKB	Binding site	83	83	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41734	UniProtKB	Beta strand	4	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	12	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Turn	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	32	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Turn	40	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Beta strand	44	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	56	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Beta strand	73	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Turn	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Beta strand	86	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	95	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Beta strand	115	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	126	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	134	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	145	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	169	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	178	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Beta strand	185	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	193	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	216	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Helix	226	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+P41734	UniProtKB	Turn	234	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL	
+##sequence-region P46958 1 469
+P46958	UniProtKB	Chain	1	469	.	.	.	ID=PRO_0000084152;Note=IME2-dependent-signaling protein	
+P46958	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P46958	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46958	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46958	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46958	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46958	UniProtKB	Modified residue	122	122	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46958	UniProtKB	Modified residue	130	130	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46958	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46958	UniProtKB	Modified residue	147	147	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46958	UniProtKB	Modified residue	148	148	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46958	UniProtKB	Sequence conflict	268	268	.	.	.	Note=G->GF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46958	UniProtKB	Sequence conflict	282	282	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46958	UniProtKB	Sequence conflict	361	361	.	.	.	Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40060 1 125
+P40060	UniProtKB	Chain	1	125	.	.	.	ID=PRO_0000084157;Note=Ino eighty subunit 5	
+P40060	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P20459 1 304
+P20459	UniProtKB	Chain	1	304	.	.	.	ID=PRO_0000137389;Note=Eukaryotic translation initiation factor 2 subunit alpha	
+P20459	UniProtKB	Domain	17	88	.	.	.	Note=S1 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+P20459	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine%3B by GCN2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1739968;Dbxref=PMID:1739968	
+P20459	UniProtKB	Modified residue	292	292	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P20459	UniProtKB	Modified residue	294	294	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P20459	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Strongly impairs derepression of GCN4 expression in amino acid-starved cells. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1739968;Dbxref=PMID:1739968	
+P20459	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Weakly impairs derepression of GCN4 expression in amino acid-starved cells. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1739968;Dbxref=PMID:1739968	
+P20459	UniProtKB	Sequence conflict	258	258	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20459	UniProtKB	Beta strand	8	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Beta strand	19	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Beta strand	31	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Turn	37	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Beta strand	43	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Helix	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q46	
+P20459	UniProtKB	Helix	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q46	
+P20459	UniProtKB	Beta strand	67	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Turn	78	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Beta strand	82	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Helix	92	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Helix	123	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Helix	131	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Helix	141	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Helix	152	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+P20459	UniProtKB	Helix	163	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19	
+##sequence-region P28817 1 500
+P28817	UniProtKB	Chain	1	500	.	.	.	ID=PRO_0000109357;Note=3-hydroxyisobutyryl-CoA hydrolase%2C mitochondrial	
+P28817	UniProtKB	Binding site	124	124	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28817	UniProtKB	Binding site	149	149	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28817	UniProtKB	Binding site	172	172	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28817	UniProtKB	Binding site	180	180	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28817	UniProtKB	Modified residue	326	326	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P28817	UniProtKB	Sequence conflict	139	139	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CY09 1 210
+P0CY09	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000410464;Note=Silenced mating-type protein ALPHA2	
+P0CY09	UniProtKB	DNA binding	129	191	.	.	.	Note=Homeobox%3B TALE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108	
+P0CY09	UniProtKB	Region	1	102	.	.	.	Note=N-terminal domain	
+P0CY09	UniProtKB	Region	103	128	.	.	.	Note=Flexible linker	
+P0CY09	UniProtKB	Region	190	210	.	.	.	Note=C-terminal tail	
+P0CY09	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0CY08	
+P0CY09	UniProtKB	Sequence conflict	56	56	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CY09	UniProtKB	Sequence conflict	56	56	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CY09	UniProtKB	Sequence conflict	56	56	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12039 1 706
+Q12039	UniProtKB	Chain	1	692	.	.	.	ID=PRO_0000013297;Note=ATP-dependent DNA helicase HMI1%2C mitochondrial	
+Q12039	UniProtKB	Propeptide	693	706	.	.	.	ID=PRO_0000013298;Note=Cleaved upon import into mitochondrion	
+Q12039	UniProtKB	Domain	5	277	.	.	.	Note=UvrD-like helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00560	
+Q12039	UniProtKB	Domain	278	593	.	.	.	Note=UvrD-like helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00617	
+Q12039	UniProtKB	Nucleotide binding	29	34	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00560	
+Q12039	UniProtKB	Binding site	275	275	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12039	UniProtKB	Mutagenesis	704	704	.	.	.	Note=Impaired import into mitochondrion. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669756;Dbxref=PMID:10669756	
+Q12039	UniProtKB	Mutagenesis	705	705	.	.	.	Note=Impaired import into mitochondrion. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669756;Dbxref=PMID:10669756	
+##sequence-region P20050 1 605
+P20050	UniProtKB	Chain	1	605	.	.	.	ID=PRO_0000126123;Note=Meiosis-specific protein HOP1	
+P20050	UniProtKB	Domain	20	250	.	.	.	Note=HORMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00109	
+P20050	UniProtKB	Zinc finger	348	364	.	.	.	.	
+P20050	UniProtKB	Natural variant	595	595	.	.	.	Note=In allele HOP1-628%3B TS. S->N	
+##sequence-region Q05827 1 59
+Q05827	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05827	UniProtKB	Chain	20	59	.	.	.	ID=PRO_0000021448;Note=Protein HOR7	
+Q05827	UniProtKB	Compositional bias	22	28	.	.	.	Note=Poly-Ser	
+##sequence-region Q06592 1 156
+Q06592	UniProtKB	Chain	1	156	.	.	.	ID=PRO_0000074633;Note=Histone acetyltransferase HPA2	
+Q06592	UniProtKB	Domain	9	156	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+Q06592	UniProtKB	Region	93	106	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10600387;Dbxref=PMID:10600387	
+Q06592	UniProtKB	Site	139	139	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10600387;Dbxref=PMID:10600387	
+Q06592	UniProtKB	Beta strand	9	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Helix	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Helix	19	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Helix	39	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Turn	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSO	
+Q06592	UniProtKB	Beta strand	56	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Beta strand	69	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Beta strand	87	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Helix	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Helix	104	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Beta strand	124	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Helix	133	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Beta strand	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+Q06592	UniProtKB	Beta strand	147	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM	
+##sequence-region Q04178 1 221
+Q04178	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04178	UniProtKB	Chain	2	221	.	.	.	ID=PRO_0000257807;Note=Hypoxanthine-guanine phosphoribosyltransferase	
+Q04178	UniProtKB	Nucleotide binding	110	118	.	.	.	Note=GMP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18245832;Dbxref=PMID:18245832	
+Q04178	UniProtKB	Nucleotide binding	188	194	.	.	.	Note=GMP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18245832;Dbxref=PMID:18245832	
+Q04178	UniProtKB	Active site	114	114	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04178	UniProtKB	Binding site	85	85	.	.	.	Note=GMP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18245832;Dbxref=PMID:18245832	
+Q04178	UniProtKB	Binding site	159	159	.	.	.	Note=GMP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18245832;Dbxref=PMID:18245832	
+Q04178	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04178	UniProtKB	Beta strand	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JKY	
+Q04178	UniProtKB	Helix	11	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Turn	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Beta strand	31	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Helix	37	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Beta strand	60	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Beta strand	85	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Helix	94	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Beta strand	105	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Helix	117	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Turn	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Helix	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Beta strand	150	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Helix	169	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Turn	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Beta strand	178	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JKY	
+Q04178	UniProtKB	Helix	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+Q04178	UniProtKB	Helix	198	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU	
+##sequence-region P38922 1 454
+P38922	UniProtKB	Chain	1	454	.	.	.	ID=PRO_0000081612;Note=Protein HRB1	
+P38922	UniProtKB	Domain	161	237	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P38922	UniProtKB	Domain	261	338	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P38922	UniProtKB	Domain	376	453	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P38922	UniProtKB	Compositional bias	13	127	.	.	.	Note=Arg-rich	
+P38922	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38922	UniProtKB	Modified residue	355	355	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38922	UniProtKB	Beta strand	161	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR	
+P38922	UniProtKB	Helix	174	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR	
+P38922	UniProtKB	Helix	182	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR	
+P38922	UniProtKB	Beta strand	187	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR	
+P38922	UniProtKB	Beta strand	203	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR	
+P38922	UniProtKB	Helix	212	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR	
+P38922	UniProtKB	Turn	218	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR	
+P38922	UniProtKB	Beta strand	232	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR	
+P38922	UniProtKB	Beta strand	263	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS	
+P38922	UniProtKB	Helix	274	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS	
+P38922	UniProtKB	Beta strand	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS	
+P38922	UniProtKB	Beta strand	304	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS	
+P38922	UniProtKB	Helix	311	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS	
+P38922	UniProtKB	Beta strand	325	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS	
+P38922	UniProtKB	Beta strand	333	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS	
+P38922	UniProtKB	Helix	359	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT	
+P38922	UniProtKB	Turn	364	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT	
+P38922	UniProtKB	Beta strand	368	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT	
+P38922	UniProtKB	Beta strand	376	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT	
+P38922	UniProtKB	Helix	389	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT	
+P38922	UniProtKB	Turn	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT	
+P38922	UniProtKB	Beta strand	402	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT	
+P38922	UniProtKB	Beta strand	415	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT	
+P38922	UniProtKB	Helix	426	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT	
+P38922	UniProtKB	Turn	436	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT	
+P38922	UniProtKB	Beta strand	447	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT	
+##sequence-region Q08109 1 551
+Q08109	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000240367;Note=ERAD-associated E3 ubiquitin-protein ligase HRD1	
+Q08109	UniProtKB	Topological domain	1	8	.	.	.	Note=Cytoplasmic	
+Q08109	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical%3B Name%3D1	
+Q08109	UniProtKB	Topological domain	30	45	.	.	.	Note=Lumenal	
+Q08109	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical%3B Name%3D2	
+Q08109	UniProtKB	Topological domain	67	82	.	.	.	Note=Cytoplasmic	
+Q08109	UniProtKB	Transmembrane	83	103	.	.	.	Note=Helical%3B Name%3D3	
+Q08109	UniProtKB	Topological domain	104	104	.	.	.	Note=Lumenal	
+Q08109	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical%3B Name%3D4	
+Q08109	UniProtKB	Topological domain	126	144	.	.	.	Note=Cytoplasmic	
+Q08109	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical%3B Name%3D5	
+Q08109	UniProtKB	Topological domain	166	184	.	.	.	Note=Lumenal	
+Q08109	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical%3B Name%3D6	
+Q08109	UniProtKB	Topological domain	206	551	.	.	.	Note=Cytoplasmic	
+Q08109	UniProtKB	Zinc finger	349	400	.	.	.	Note=RING-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q08109	UniProtKB	Region	517	551	.	.	.	Note=Interaction with USA1	
+Q08109	UniProtKB	Compositional bias	413	483	.	.	.	Note=Thr-rich	
+Q08109	UniProtKB	Mutagenesis	399	399	.	.	.	Note=Stabilizes HRD1. Reduced interaction with substrate. Formation of oligomer with or without USA1. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11018054,ECO:0000269|PubMed:11139575,ECO:0000269|PubMed:11146622,ECO:0000269|PubMed:20005842,ECO:0000269|PubMed:21074049;Dbxref=PMID:11018054,PMID:11139575,PMID:11146622,PMID:20005842,PMID:21074049	
+##sequence-region Q08732 1 759
+Q08732	UniProtKB	Chain	1	759	.	.	.	ID=PRO_0000086002;Note=Serine/threonine-protein kinase HRK1	
+Q08732	UniProtKB	Domain	215	722	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q08732	UniProtKB	Nucleotide binding	221	229	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q08732	UniProtKB	Compositional bias	628	647	.	.	.	Note=Poly-Gln	
+Q08732	UniProtKB	Compositional bias	648	653	.	.	.	Note=Poly-His	
+Q08732	UniProtKB	Active site	340	340	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q08732	UniProtKB	Binding site	244	244	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q08732	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q08732	UniProtKB	Modified residue	382	382	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08732	UniProtKB	Modified residue	472	472	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08732	UniProtKB	Modified residue	495	495	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q08732	UniProtKB	Modified residue	498	498	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P69852 1 69
+P69852	UniProtKB	Chain	1	69	.	.	.	ID=PRO_0000084079;Note=DASH complex subunit HSK3	
+P69852	UniProtKB	Coiled coil	1	39	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08914 1 237
+Q08914	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000270556;Note=Probable glutathione-independent glyoxalase HSP33	
+Q08914	UniProtKB	Active site	138	138	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21139195;Dbxref=PMID:21139195	
+Q08914	UniProtKB	Active site	139	139	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21139195;Dbxref=PMID:21139195	
+Q08914	UniProtKB	Active site	170	170	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21139195;Dbxref=PMID:21139195	
+Q08914	UniProtKB	Beta strand	5	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	28	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Turn	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Beta strand	44	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MII	
+Q08914	UniProtKB	Helix	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MII	
+Q08914	UniProtKB	Helix	69	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MII	
+Q08914	UniProtKB	Helix	82	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Beta strand	100	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	118	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Beta strand	133	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	140	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Turn	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Beta strand	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Turn	156	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	167	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Turn	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	176	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	187	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Turn	193	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Beta strand	209	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Beta strand	215	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+Q08914	UniProtKB	Helix	224	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL	
+##sequence-region P50079 1 448
+P50079	UniProtKB	Chain	1	448	.	.	.	ID=PRO_0000051034;Note=SVP1-like protein 2	
+P50079	UniProtKB	Repeat	222	262	.	.	.	Note=WD 1	
+P50079	UniProtKB	Repeat	267	306	.	.	.	Note=WD 2	
+P50079	UniProtKB	Glycosylation	61	61	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50079	UniProtKB	Glycosylation	155	155	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50079	UniProtKB	Glycosylation	256	256	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50079	UniProtKB	Glycosylation	280	280	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50079	UniProtKB	Glycosylation	315	315	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50079	UniProtKB	Glycosylation	421	421	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q6Q5K6 1 68
+Q6Q5K6	UniProtKB	Chain	1	68	.	.	.	ID=PRO_0000240383;Note=MEC1-mediated checkpoint protein HUG1	
+##sequence-region P04806 1 485
+P04806	UniProtKB	Chain	1	485	.	.	.	ID=PRO_0000197601;Note=Hexokinase-1	
+P04806	UniProtKB	Domain	21	468	.	.	.	Note=Hexokinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+P04806	UniProtKB	Nucleotide binding	86	91	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04806	UniProtKB	Nucleotide binding	307	308	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04806	UniProtKB	Nucleotide binding	344	348	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04806	UniProtKB	Nucleotide binding	419	423	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04806	UniProtKB	Region	75	209	.	.	.	Note=Hexokinase small subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+P04806	UniProtKB	Region	175	176	.	.	.	Note=Substrate binding	
+P04806	UniProtKB	Region	210	457	.	.	.	Note=Hexokinase large subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+P04806	UniProtKB	Region	210	211	.	.	.	Note=Substrate binding	
+P04806	UniProtKB	Binding site	111	111	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04806	UniProtKB	Binding site	158	158	.	.	.	Note=Substrate%3B via carbonyl oxygen	
+P04806	UniProtKB	Binding site	237	237	.	.	.	Note=Substrate	
+P04806	UniProtKB	Binding site	269	269	.	.	.	Note=Substrate	
+P04806	UniProtKB	Binding site	302	302	.	.	.	Note=Substrate	
+P04806	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04806	UniProtKB	Modified residue	272	272	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04806	UniProtKB	Sequence conflict	61	61	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04806	UniProtKB	Sequence conflict	103	103	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04806	UniProtKB	Sequence conflict	194	194	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04806	UniProtKB	Sequence conflict	244	244	.	.	.	Note=V->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04806	UniProtKB	Sequence conflict	356	357	.	.	.	Note=EN->VF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04806	UniProtKB	Sequence conflict	364	364	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04806	UniProtKB	Sequence conflict	388	388	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04806	UniProtKB	Sequence conflict	444	444	.	.	.	Note=D->EN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04806	UniProtKB	Sequence conflict	479	480	.	.	.	Note=SL->VS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04806	UniProtKB	Helix	21	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	38	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	80	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	89	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	101	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	116	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	125	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	151	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	188	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	197	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	202	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	211	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	226	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	244	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	248	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	263	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Turn	273	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	278	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	284	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	293	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	300	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	307	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Turn	323	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	326	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Turn	334	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	345	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	359	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	375	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	398	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	410	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	419	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	427	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Turn	444	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	449	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Turn	458	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Helix	461	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+P04806	UniProtKB	Beta strand	480	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A	
+##sequence-region P04807 1 486
+P04807	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9718324;Dbxref=PMID:9718324	
+P04807	UniProtKB	Chain	2	486	.	.	.	ID=PRO_0000197602;Note=Hexokinase-2	
+P04807	UniProtKB	Domain	21	469	.	.	.	Note=Hexokinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+P04807	UniProtKB	Nucleotide binding	86	91	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04807	UniProtKB	Nucleotide binding	307	308	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04807	UniProtKB	Nucleotide binding	344	348	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04807	UniProtKB	Nucleotide binding	419	423	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04807	UniProtKB	Region	75	209	.	.	.	Note=Hexokinase small subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+P04807	UniProtKB	Region	175	176	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04807	UniProtKB	Region	210	458	.	.	.	Note=Hexokinase large subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+P04807	UniProtKB	Region	210	211	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04807	UniProtKB	Binding site	111	111	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04807	UniProtKB	Binding site	158	158	.	.	.	Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04807	UniProtKB	Binding site	237	237	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04807	UniProtKB	Binding site	269	269	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04807	UniProtKB	Binding site	302	302	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04807	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:8286332,ECO:0000269|PubMed:9718324;Dbxref=PMID:19779198,PMID:8286332,PMID:9718324	
+P04807	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04807	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:9047292;Dbxref=PMID:18407956,PMID:9047292	
+P04807	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04807	UniProtKB	Modified residue	272	272	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04806	
+P04807	UniProtKB	Sequence conflict	29	29	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	33	33	.	.	.	Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	33	33	.	.	.	Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	61	61	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	197	197	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	202	202	.	.	.	Note=P->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	421	422	.	.	.	Note=YN->ST;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	421	422	.	.	.	Note=YN->ST;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	444	445	.	.	.	Note=TS->PH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	444	445	.	.	.	Note=TS->PH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	453	453	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	453	453	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	462	462	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Sequence conflict	462	462	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04807	UniProtKB	Helix	21	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Helix	38	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Beta strand	79	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Beta strand	89	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Beta strand	105	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Helix	126	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Beta strand	152	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Beta strand	159	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Helix	189	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Beta strand	203	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	211	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Beta strand	226	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	244	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	248	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Beta strand	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Beta strand	264	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Turn	271	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Beta strand	278	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	284	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Beta strand	293	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Helix	300	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	310	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Beta strand	326	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Turn	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Helix	345	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Beta strand	355	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	359	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	375	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	398	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Beta strand	410	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	419	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8	
+P04807	UniProtKB	Helix	427	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	446	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Beta strand	449	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Turn	459	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+P04807	UniProtKB	Helix	462	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX	
+##sequence-region Q12134 1 243
+Q12134	UniProtKB	Chain	1	243	.	.	.	ID=PRO_0000270558;Note=Protein HUA2	
+##sequence-region Q12520 1 339
+Q12520	UniProtKB	Chain	1	339	.	.	.	ID=PRO_0000213414;Note=UDP-galactose transporter homolog 1	
+Q12520	UniProtKB	Topological domain	1	4	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Transmembrane	5	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Topological domain	26	42	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Topological domain	64	106	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Transmembrane	107	127	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Topological domain	128	136	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Transmembrane	137	157	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Topological domain	158	174	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Transmembrane	175	192	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Topological domain	193	214	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Transmembrane	215	235	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Topological domain	236	245	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Transmembrane	246	266	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Topological domain	267	280	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Transmembrane	281	303	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Topological domain	304	307	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Transmembrane	308	327	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Topological domain	328	339	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12520	UniProtKB	Glycosylation	165	165	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12385 1 394
+Q12385	UniProtKB	Chain	1	394	.	.	.	ID=PRO_0000080854;Note=1-acylglycerol-3-phosphate O-acyltransferase ICT1	
+Q12385	UniProtKB	Domain	74	381	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12385	UniProtKB	Motif	374	379	.	.	.	Note=HXXXXD motif	
+##sequence-region P15496 1 288
+P15496	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2681212;Dbxref=PMID:2681212	
+P15496	UniProtKB	Chain	2	288	.	.	.	ID=PRO_0000205231;Note=Isopentenyl-diphosphate Delta-isomerase	
+P15496	UniProtKB	Domain	102	259	.	.	.	Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794	
+P15496	UniProtKB	Active site	139	139	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15496	UniProtKB	Active site	207	207	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15496	UniProtKB	Metal binding	93	93	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15496	UniProtKB	Metal binding	104	104	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15496	UniProtKB	Metal binding	205	205	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15496	UniProtKB	Metal binding	207	207	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15496	UniProtKB	Binding site	89	89	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15496	UniProtKB	Binding site	123	123	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15496	UniProtKB	Binding site	127	127	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15496	UniProtKB	Binding site	140	140	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15496	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P15496	UniProtKB	Mutagenesis	138	138	.	.	.	Note=10-fold reduction in activity. C->S%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7908830;Dbxref=PMID:7908830	
+P15496	UniProtKB	Mutagenesis	139	139	.	.	.	Note=Inactive. C->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7908830;Dbxref=PMID:7908830	
+P15496	UniProtKB	Mutagenesis	139	139	.	.	.	Note=Reduces activity over 100000-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7908830;Dbxref=PMID:7908830	
+P15496	UniProtKB	Mutagenesis	207	207	.	.	.	Note=Inactive. E->Q%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7908830;Dbxref=PMID:7908830	
+##sequence-region P09064 1 285
+P09064	UniProtKB	Chain	1	285	.	.	.	ID=PRO_0000137415;Note=Eukaryotic translation initiation factor 2 subunit beta	
+P09064	UniProtKB	Zinc finger	236	262	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P09064	UniProtKB	Compositional bias	16	23	.	.	.	Note=Lys-rich (basic)	
+P09064	UniProtKB	Compositional bias	49	56	.	.	.	Note=Lys-rich (basic)	
+P09064	UniProtKB	Compositional bias	82	89	.	.	.	Note=Lys-rich (basic)	
+P09064	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P09064	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P09064	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P09064	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P09064	UniProtKB	Modified residue	112	112	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P09064	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P09064	UniProtKB	Modified residue	118	118	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P09064	UniProtKB	Mutagenesis	16	23	.	.	.	Note=Abolishes interaction with TIF5%3B when associated with 49-K--K-56 and 82-K--K-89. KKKKKTKK->AAAAATAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937	
+P09064	UniProtKB	Mutagenesis	49	56	.	.	.	Note=Abolishes interaction with TIF5%3B when associated with 16-K--K-23 and 82-K--K-89. KKKKKKSK->AAAAAASA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937	
+P09064	UniProtKB	Mutagenesis	82	89	.	.	.	Note=Abolishes interaction with TIF5%3B when associated with 16-K--K-23 and 49-K--K-56. KKKKKKTK->AAAAAATA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937	
+P09064	UniProtKB	Sequence conflict	141	141	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P10081 1 395
+P10081	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649	
+P10081	UniProtKB	Chain	2	395	.	.	.	ID=PRO_0000054968;Note=ATP-dependent RNA helicase eIF4A	
+P10081	UniProtKB	Domain	53	222	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P10081	UniProtKB	Domain	233	394	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P10081	UniProtKB	Nucleotide binding	66	73	.	.	.	Note=ATP	
+P10081	UniProtKB	Motif	22	50	.	.	.	Note=Q motif	
+P10081	UniProtKB	Motif	170	173	.	.	.	Note=DEAD box	
+P10081	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649	
+P10081	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P10081	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P10081	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P10081	UniProtKB	Modified residue	146	146	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P10081	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Lethal in vivo and reduces ATP binding and ATPase activity in vitro. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527	
+P10081	UniProtKB	Mutagenesis	42	42	.	.	.	Note=Slow growth in vivo and reduces ATP binding and ATPase activity in vitro. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527	
+P10081	UniProtKB	Mutagenesis	46	46	.	.	.	Note=Reduces ATP binding and ATPase activity in vitro. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527	
+P10081	UniProtKB	Mutagenesis	49	49	.	.	.	Note=Reduces ATP binding and ATPase activity in vitro. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527	
+P10081	UniProtKB	Mutagenesis	49	49	.	.	.	Note=Increases about 3-fold ATP binding but reduces about 2-fold ATPase activity in vitro. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527	
+P10081	UniProtKB	Mutagenesis	66	66	.	.	.	Note=Slow growth. A->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1502180,ECO:0000269|PubMed:2046664;Dbxref=PMID:1502180,PMID:2046664	
+P10081	UniProtKB	Mutagenesis	66	66	.	.	.	Note=Lethal and dominant negative if overexpressed in vivo. Impairs ATP hydrolysis%2C RNA-helicase and translation activity in vitro. A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1502180,ECO:0000269|PubMed:2046664;Dbxref=PMID:1502180,PMID:2046664	
+P10081	UniProtKB	Mutagenesis	72	72	.	.	.	Note=Lethal in vivo and reduces ATP binding and ATPase activity in vitro. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527	
+P10081	UniProtKB	Mutagenesis	79	79	.	.	.	Note=In TIF1-1%3B no growth at 36 degrees Celsius. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664	
+P10081	UniProtKB	Mutagenesis	126	126	.	.	.	Note=Lethal. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664	
+P10081	UniProtKB	Mutagenesis	127	127	.	.	.	Note=Slow growth. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664	
+P10081	UniProtKB	Mutagenesis	145	145	.	.	.	Note=Lethal. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664	
+P10081	UniProtKB	Mutagenesis	145	145	.	.	.	Note=Slow growth. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664	
+P10081	UniProtKB	Mutagenesis	170	170	.	.	.	Note=Lethal. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664	
+P10081	UniProtKB	Mutagenesis	173	173	.	.	.	Note=Lethal. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664	
+P10081	UniProtKB	Mutagenesis	311	311	.	.	.	Note=Slow growth. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664	
+P10081	UniProtKB	Mutagenesis	347	347	.	.	.	Note=Lethal and dominant negative if overexpressed. R->E%2CG%2CI%2CS%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664	
+P10081	UniProtKB	Beta strand	13	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUU	
+P10081	UniProtKB	Helix	24	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Helix	31	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Helix	47	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Beta strand	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Helix	72	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Helix	100	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Turn	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Beta strand	121	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Helix	130	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUU	
+P10081	UniProtKB	Beta strand	141	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Helix	147	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Beta strand	166	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Helix	172	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Helix	181	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Beta strand	196	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Helix	206	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Beta strand	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE	
+P10081	UniProtKB	Beta strand	235	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Helix	244	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Helix	247	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Beta strand	263	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Helix	270	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Beta strand	287	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Helix	296	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Beta strand	312	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Helix	318	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Turn	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Beta strand	330	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Helix	341	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Beta strand	359	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Turn	366	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Helix	369	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+P10081	UniProtKB	Beta strand	383	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUU	
+P10081	UniProtKB	Turn	391	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK	
+##sequence-region P39936 1 914
+P39936	UniProtKB	Chain	1	914	.	.	.	ID=PRO_0000213332;Note=Eukaryotic initiation factor 4F subunit p130	
+P39936	UniProtKB	Domain	567	810	.	.	.	Note=MIF4G	
+P39936	UniProtKB	Region	201	315	.	.	.	Note=Interaction with PAB1	
+P39936	UniProtKB	Compositional bias	32	97	.	.	.	Note=Asn-rich	
+P39936	UniProtKB	Compositional bias	459	510	.	.	.	Note=Arg/Ser-rich	
+P39936	UniProtKB	Compositional bias	840	863	.	.	.	Note=Arg/Ser-rich	
+P39936	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39936	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39936	UniProtKB	Modified residue	301	301	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P39936	UniProtKB	Modified residue	503	503	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39936	UniProtKB	Modified residue	913	913	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P39936	UniProtKB	Mutagenesis	233	236	.	.	.	Note=In TIF4632-233%3B abolishes interaction with PAB1 and inhibits poly(A)-dependent translation. RLRK->AVAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9256432;Dbxref=PMID:9256432	
+##sequence-region P47175 1 358
+P47175	UniProtKB	Chain	1	358	.	.	.	ID=PRO_0000124596;Note=Probable transcription factor HMS2	
+P47175	UniProtKB	DNA binding	12	116	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P09932 1 586
+P09932	UniProtKB	Chain	1	586	.	.	.	ID=PRO_0000084030;Note=Homothallic switching endonuclease	
+P09932	UniProtKB	Domain	215	370	.	.	.	Note=DOD-type homing endonuclease;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00273	
+P09932	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09932	UniProtKB	Sequence conflict	223	223	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09932	UniProtKB	Sequence conflict	405	405	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09932	UniProtKB	Sequence conflict	475	475	.	.	.	Note=L->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39979 1 161
+P39979	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39979	UniProtKB	Chain	2	161	.	.	.	ID=PRO_0000074634;Note=D-amino-acid N-acetyltransferase HPA3	
+P39979	UniProtKB	Domain	14	161	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+P39979	UniProtKB	Region	98	111	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06592	
+P39979	UniProtKB	Site	144	144	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06592	
+P39979	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P38348 1 480
+P38348	UniProtKB	Chain	1	480	.	.	.	ID=PRO_0000202532;Note=DNA mismatch repair protein HSM3	
+P38348	UniProtKB	Helix	10	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Beta strand	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A3T	
+P38348	UniProtKB	Helix	29	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	52	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	73	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	89	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	98	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	110	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	126	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	134	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	150	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	167	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Turn	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	178	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	190	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Turn	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	214	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	221	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	231	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	257	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	264	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Turn	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	278	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	285	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Beta strand	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FP7	
+P38348	UniProtKB	Helix	304	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Turn	316	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLE	
+P38348	UniProtKB	Helix	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	323	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	332	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	340	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	351	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	354	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	364	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	371	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	376	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	384	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	398	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	409	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	421	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	427	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	445	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	449	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+P38348	UniProtKB	Helix	452	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD	
+##sequence-region P19882 1 572
+P19882	UniProtKB	Transit peptide	1	25	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19882	UniProtKB	Chain	26	572	.	.	.	ID=PRO_0000005044;Note=Heat shock protein 60%2C mitochondrial	
+P19882	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P19882	UniProtKB	Modified residue	485	485	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P22202 1 642
+P22202	UniProtKB	Chain	1	642	.	.	.	ID=PRO_0000078388;Note=Heat shock protein SSA4	
+P22202	UniProtKB	Modified residue	552	552	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22202	UniProtKB	Helix	637	639	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV	
+##sequence-region P33416 1 811
+P33416	UniProtKB	Transit peptide	1	44	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33416	UniProtKB	Chain	45	811	.	.	.	ID=PRO_0000005500;Note=Heat shock protein 78%2C mitochondrial	
+P33416	UniProtKB	Nucleotide binding	143	150	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33416	UniProtKB	Nucleotide binding	541	548	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33416	UniProtKB	Region	98	344	.	.	.	Note=NBD1	
+P33416	UniProtKB	Region	467	658	.	.	.	Note=NBD2	
+P33416	UniProtKB	Coiled coil	345	430	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33416	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Abolishes ATPase activity. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11734006;Dbxref=PMID:11734006	
+P33416	UniProtKB	Mutagenesis	547	547	.	.	.	Note=Impairs oligomerization. Reduces ATPase activity by 92%25. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11734006;Dbxref=PMID:11734006	
+P33416	UniProtKB	Sequence conflict	106	106	.	.	.	Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33416	UniProtKB	Sequence conflict	245	245	.	.	.	Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33416	UniProtKB	Sequence conflict	429	429	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33416	UniProtKB	Sequence conflict	549	549	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33416	UniProtKB	Sequence conflict	608	608	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53685 1 503
+P53685	UniProtKB	Chain	1	503	.	.	.	ID=PRO_0000110281;Note=NAD-dependent protein deacetylase HST1	
+P53685	UniProtKB	Domain	191	470	.	.	.	Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53685	UniProtKB	Nucleotide binding	208	227	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53685	UniProtKB	Nucleotide binding	290	293	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53685	UniProtKB	Nucleotide binding	412	414	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53685	UniProtKB	Nucleotide binding	437	439	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53685	UniProtKB	Active site	310	310	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53685	UniProtKB	Metal binding	318	318	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53685	UniProtKB	Metal binding	321	321	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53685	UniProtKB	Metal binding	342	342	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53685	UniProtKB	Metal binding	345	345	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53685	UniProtKB	Binding site	454	454	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53686 1 357
+P53686	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53686	UniProtKB	Chain	2	357	.	.	.	ID=PRO_0000110282;Note=NAD-dependent protein deacetylase HST2	
+P53686	UniProtKB	Domain	13	286	.	.	.	Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53686	UniProtKB	Nucleotide binding	32	52	.	.	.	Note=NAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:15150415;Dbxref=PMID:14502267,PMID:15150415	
+P53686	UniProtKB	Nucleotide binding	115	118	.	.	.	Note=NAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:15150415;Dbxref=PMID:14502267,PMID:15150415	
+P53686	UniProtKB	Nucleotide binding	223	225	.	.	.	Note=NAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:15150415;Dbxref=PMID:14502267,PMID:15150415	
+P53686	UniProtKB	Nucleotide binding	248	250	.	.	.	Note=NAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:15150415;Dbxref=PMID:14502267,PMID:15150415	
+P53686	UniProtKB	Active site	135	135	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:20726530;Dbxref=PMID:20726530	
+P53686	UniProtKB	Metal binding	143	143	.	.	.	Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:14604530,ECO:0000269|PubMed:15150415,ECO:0000269|PubMed:17289592;Dbxref=PMID:14502267,PMID:14604530,PMID:15150415,PMID:17289592	
+P53686	UniProtKB	Metal binding	146	146	.	.	.	Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:14604530,ECO:0000269|PubMed:15150415,ECO:0000269|PubMed:17289592;Dbxref=PMID:14502267,PMID:14604530,PMID:15150415,PMID:17289592	
+P53686	UniProtKB	Metal binding	170	170	.	.	.	Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:14604530,ECO:0000269|PubMed:15150415,ECO:0000269|PubMed:17289592;Dbxref=PMID:14502267,PMID:14604530,PMID:15150415,PMID:17289592	
+P53686	UniProtKB	Metal binding	173	173	.	.	.	Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:14604530,ECO:0000269|PubMed:15150415,ECO:0000269|PubMed:17289592;Dbxref=PMID:14502267,PMID:14604530,PMID:15150415,PMID:17289592	
+P53686	UniProtKB	Binding site	270	270	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:15150415;Dbxref=PMID:14502267,PMID:15150415	
+P53686	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53686	UniProtKB	Modified residue	340	340	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53686	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Nearly or completely catalytically inactive. I->A%2CD%2CH%2CW%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17289592;Dbxref=PMID:17289592	
+P53686	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Near wild-type activity for deacetylation. Increases slightly the KM for NAD(+) to 25 uM. I->F%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17289592;Dbxref=PMID:17289592	
+P53686	UniProtKB	Beta strand	3	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZD	
+P53686	UniProtKB	Helix	9	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Beta strand	27	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	33	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	63	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	69	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	77	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Beta strand	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	95	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Beta strand	109	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	120	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Beta strand	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Beta strand	136	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Turn	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	153	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Beta strand	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZD	
+P53686	UniProtKB	Turn	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Beta strand	176	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	191	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Beta strand	218	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Turn	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	233	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Beta strand	242	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	254	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Beta strand	264	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	270	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	284	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A	
+P53686	UniProtKB	Helix	304	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q14	
+##sequence-region P54862 1 567
+P54862	UniProtKB	Chain	1	567	.	.	.	ID=PRO_0000050401;Note=Hexose transporter HXT11	
+P54862	UniProtKB	Topological domain	1	56	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	78	112	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	134	139	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	161	170	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	192	197	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	219	232	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	254	336	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	337	353	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	354	359	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	360	377	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	378	384	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	385	405	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	406	429	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	430	450	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	451	467	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	468	488	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	489	489	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Transmembrane	490	510	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Topological domain	511	567	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Glycosylation	87	87	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54862	UniProtKB	Glycosylation	227	227	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P42833 1 540
+P42833	UniProtKB	Chain	1	540	.	.	.	ID=PRO_0000050403;Note=Hexose transporter HXT14	
+P42833	UniProtKB	Topological domain	1	56	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	57	76	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	77	119	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	141	146	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	168	177	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	178	198	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	199	204	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	205	225	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	226	243	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	244	264	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	265	357	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	358	374	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	375	380	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	381	398	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	399	405	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	406	426	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	427	440	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	441	461	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	462	478	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	479	499	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	500	500	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Transmembrane	501	521	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42833	UniProtKB	Topological domain	522	540	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47185 1 567
+P47185	UniProtKB	Chain	1	567	.	.	.	ID=PRO_0000050405;Note=Hexose transporter HXT16	
+P47185	UniProtKB	Topological domain	1	55	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	77	112	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	134	139	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	161	170	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	192	197	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	219	232	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	254	336	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	337	353	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	354	359	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	360	377	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	378	384	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	385	405	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	406	427	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	428	448	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	449	465	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	466	486	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	487	487	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Transmembrane	488	508	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47185	UniProtKB	Topological domain	509	567	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40886 1 569
+P40886	UniProtKB	Chain	1	569	.	.	.	ID=PRO_0000050398;Note=Hexose transporter HXT8	
+P40886	UniProtKB	Topological domain	1	61	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	83	118	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	140	145	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	167	176	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	198	203	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	225	238	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	239	259	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	260	342	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	343	359	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	360	365	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	366	383	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	384	390	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	391	411	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	412	433	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	434	454	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	455	471	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	472	492	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	493	493	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Transmembrane	494	514	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Topological domain	515	569	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Glycosylation	92	92	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Glycosylation	102	102	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40886	UniProtKB	Glycosylation	429	429	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53688 1 370
+P53688	UniProtKB	Chain	1	370	.	.	.	ID=PRO_0000110284;Note=NAD-dependent histone deacetylase HST4	
+P53688	UniProtKB	Domain	83	370	.	.	.	Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53688	UniProtKB	Nucleotide binding	100	119	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53688	UniProtKB	Nucleotide binding	184	187	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53688	UniProtKB	Nucleotide binding	310	312	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53688	UniProtKB	Nucleotide binding	340	342	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53688	UniProtKB	Active site	213	213	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53688	UniProtKB	Metal binding	221	221	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53688	UniProtKB	Metal binding	224	224	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53688	UniProtKB	Metal binding	251	251	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53688	UniProtKB	Metal binding	254	254	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P53688	UniProtKB	Binding site	363	363	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53892 1 351
+P53892	UniProtKB	Chain	1	351	.	.	.	ID=PRO_0000203413;Note=Protein IBD2	
+P53892	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53892	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53892	UniProtKB	Modified residue	211	211	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40499 1 491
+P40499	UniProtKB	Chain	1	491	.	.	.	ID=PRO_0000202975;Note=Protein ICE2	
+P40499	UniProtKB	Topological domain	1	13	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Topological domain	35	40	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Transmembrane	41	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Topological domain	62	74	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Topological domain	96	149	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Topological domain	171	184	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Topological domain	206	218	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Transmembrane	219	239	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Topological domain	240	294	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Transmembrane	295	315	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Topological domain	316	373	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Transmembrane	374	394	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Topological domain	395	413	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Transmembrane	414	434	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Topological domain	435	461	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Transmembrane	462	482	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Topological domain	483	491	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40499	UniProtKB	Sequence conflict	93	93	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40051 1 511
+P40051	UniProtKB	Chain	1	511	.	.	.	ID=PRO_0000185098;Note=Intermediate cleaving peptidase 55	
+P40051	UniProtKB	Metal binding	327	327	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40051	UniProtKB	Metal binding	338	338	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40051	UniProtKB	Metal binding	338	338	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40051	UniProtKB	Metal binding	417	417	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40051	UniProtKB	Metal binding	444	444	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40051	UniProtKB	Metal binding	467	467	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40051	UniProtKB	Metal binding	467	467	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38284 1 255
+P38284	UniProtKB	Chain	1	255	.	.	.	ID=PRO_0000202499;Note=Increased copper sensitivity protein 2	
+P38284	UniProtKB	Compositional bias	13	189	.	.	.	Note=Ser-rich	
+P38284	UniProtKB	Modified residue	217	217	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P38284	UniProtKB	Sequence conflict	90	90	.	.	.	Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38284	UniProtKB	Sequence conflict	90	90	.	.	.	Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04329 1 127
+Q04329	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000203325;Note=Interacting with cytoskeleton protein 1	
+##sequence-region P38274 1 827
+P38274	UniProtKB	Chain	1	827	.	.	.	ID=PRO_0000212347;Note=Protein arginine N-methyltransferase HSL7	
+P38274	UniProtKB	Domain	329	675	.	.	.	Note=SAM-dependent MTase PRMT-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01015	
+P38274	UniProtKB	Region	354	355	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744	
+P38274	UniProtKB	Region	441	442	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744	
+P38274	UniProtKB	Active site	463	463	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744	
+P38274	UniProtKB	Active site	472	472	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744	
+P38274	UniProtKB	Binding site	345	345	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744	
+P38274	UniProtKB	Binding site	414	414	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744	
+P38274	UniProtKB	Site	348	348	.	.	.	Note=Critical for specifying symmetric addition of methyl groups;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P46580	
+P38274	UniProtKB	Modified residue	317	317	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38274	UniProtKB	Modified residue	614	614	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38274	UniProtKB	Mutagenesis	387	387	.	.	.	Note=Almost completely abolishes catalytic activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18515076;Dbxref=PMID:18515076	
+P38274	UniProtKB	Mutagenesis	387	387	.	.	.	Note=Completely abolishes catalytic activity%3B when associated with V-389. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18515076;Dbxref=PMID:18515076	
+P38274	UniProtKB	Mutagenesis	389	389	.	.	.	Note=Completely abolishes catalytic activity%3B when associated with V-387. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18515076;Dbxref=PMID:18515076	
+##sequence-region P09435 1 649
+P09435	UniProtKB	Chain	1	649	.	.	.	ID=PRO_0000078387;Note=Heat shock protein SSA3	
+P09435	UniProtKB	Sequence conflict	620	620	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CS90 1 654
+P0CS90	UniProtKB	Transit peptide	1	23	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2265609;Dbxref=PMID:2265609	
+P0CS90	UniProtKB	Chain	24	654	.	.	.	ID=PRO_0000013553;Note=Heat shock protein SSC1%2C mitochondrial	
+P0CS90	UniProtKB	Compositional bias	634	646	.	.	.	Note=Asn-rich	
+P0CS90	UniProtKB	Modified residue	330	330	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P0CS90	UniProtKB	Mutagenesis	442	442	.	.	.	Note=No interaction with TIM44. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12032075;Dbxref=PMID:12032075	
+##sequence-region P39987 1 644
+##sequence-region P28834 1 360
+P28834	UniProtKB	Transit peptide	1	11	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2198251;Dbxref=PMID:2198251	
+P28834	UniProtKB	Chain	12	360	.	.	.	ID=PRO_0000014431;Note=Isocitrate dehydrogenase [NAD] subunit 1%2C mitochondrial	
+P28834	UniProtKB	Metal binding	228	228	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28834	UniProtKB	Binding site	109	109	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28834	UniProtKB	Binding site	140	140	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28834	UniProtKB	Binding site	228	228	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28834	UniProtKB	Site	194	194	.	.	.	Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28834	UniProtKB	Beta strand	29	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	38	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	57	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	71	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	85	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	95	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	102	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	114	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	135	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	158	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	167	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	188	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Turn	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	201	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	220	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	227	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	242	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	248	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	265	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	269	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	278	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Turn	283	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLV	
+P28834	UniProtKB	Helix	300	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	317	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Beta strand	332	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	338	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28834	UniProtKB	Helix	346	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+##sequence-region P41939 1 412
+P41939	UniProtKB	Chain	1	412	.	.	.	ID=PRO_0000083587;Note=Isocitrate dehydrogenase [NADP] cytoplasmic	
+P41939	UniProtKB	Nucleotide binding	75	77	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Nucleotide binding	310	315	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Region	94	100	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Metal binding	252	252	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Metal binding	275	275	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Binding site	77	77	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Binding site	82	82	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Binding site	109	109	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Binding site	132	132	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Binding site	260	260	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Binding site	328	328	.	.	.	Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Site	139	139	.	.	.	Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Site	212	212	.	.	.	Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41939	UniProtKB	Sequence conflict	24	27	.	.	.	Note=HLIR->SFNQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41939	UniProtKB	Sequence conflict	68	68	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41939	UniProtKB	Sequence conflict	185	185	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41939	UniProtKB	Sequence conflict	232	239	.	.	.	Note=ARSYKEKF->LEVIKRSL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41939	UniProtKB	Sequence conflict	267	267	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41939	UniProtKB	Sequence conflict	306	307	.	.	.	Note=EA->DR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41939	UniProtKB	Sequence conflict	316	323	.	.	.	Note=FRQHQQGK->LTDYDKGR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25038 1 676
+P25038	UniProtKB	Domain	143	326	.	.	.	Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P25038	UniProtKB	Nucleotide binding	152	159	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25038	UniProtKB	Nucleotide binding	200	203	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25038	UniProtKB	Nucleotide binding	254	257	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25038	UniProtKB	Region	152	159	.	.	.	Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P25038	UniProtKB	Region	177	181	.	.	.	Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P25038	UniProtKB	Region	200	203	.	.	.	Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P25038	UniProtKB	Region	254	257	.	.	.	Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P25038	UniProtKB	Region	296	298	.	.	.	Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P25038	UniProtKB	Sequence conflict	462	462	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P19211 1 157
+P19211	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000142487;Note=Eukaryotic translation initiation factor 5A-2	
+P19211	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19211	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19211	UniProtKB	Modified residue	51	51	.	.	.	Note=Hypusine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1903841;Dbxref=PMID:1903841	
+##sequence-region Q12522 1 245
+Q12522	UniProtKB	Chain	1	245	.	.	.	ID=PRO_0000153742;Note=Eukaryotic translation initiation factor 6	
+Q12522	UniProtKB	Modified residue	174	174	.	.	.	Note=Phosphoserine%3B by CK1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03132	
+Q12522	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphoserine%3B by CK1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03132	
+Q12522	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12522	UniProtKB	Beta strand	2	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Helix	13	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	24	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Helix	32	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Turn	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Helix	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	67	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Helix	78	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	92	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Helix	104	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	112	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Helix	123	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	135	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Helix	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	151	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Helix	167	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Turn	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Helix	193	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	197	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Beta strand	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+Q12522	UniProtKB	Helix	212	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62	
+##sequence-region P06168 1 395
+P06168	UniProtKB	Transit peptide	1	47	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06168	UniProtKB	Chain	48	395	.	.	.	ID=PRO_0000015634;Note=Ketol-acid reductoisomerase%2C mitochondrial	
+P06168	UniProtKB	Nucleotide binding	84	93	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06168	UniProtKB	Nucleotide binding	108	113	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06168	UniProtKB	Nucleotide binding	146	150	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06168	UniProtKB	Region	363	395	.	.	.	Note=Hydrophilic	
+P06168	UniProtKB	Active site	171	171	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06168	UniProtKB	Metal binding	255	255	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06168	UniProtKB	Metal binding	255	255	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06168	UniProtKB	Metal binding	259	259	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06168	UniProtKB	Modified residue	355	355	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P39567 1 403
+P39567	UniProtKB	Chain	1	403	.	.	.	ID=PRO_0000093681;Note=Putative inosine-5'-monophosphate dehydrogenase 1	
+P39567	UniProtKB	Domain	121	183	.	.	.	Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P39567	UniProtKB	Domain	184	240	.	.	.	Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P39567	UniProtKB	Nucleotide binding	278	280	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097	
+P39567	UniProtKB	Nucleotide binding	328	330	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097	
+P39567	UniProtKB	Region	368	370	.	.	.	Note=IMP binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097	
+P39567	UniProtKB	Active site	335	335	.	.	.	Note=Thioimidate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097	
+P39567	UniProtKB	Metal binding	330	330	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097	
+P39567	UniProtKB	Metal binding	332	332	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097	
+P39567	UniProtKB	Metal binding	335	335	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097	
+P39567	UniProtKB	Binding site	333	333	.	.	.	Note=IMP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097	
+##sequence-region P50095 1 523
+P50095	UniProtKB	Chain	1	523	.	.	.	ID=PRO_0000093683;Note=Inosine-5'-monophosphate dehydrogenase 3	
+P50095	UniProtKB	Domain	121	183	.	.	.	Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Domain	184	240	.	.	.	Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Nucleotide binding	278	280	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Nucleotide binding	328	330	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Region	368	370	.	.	.	Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Region	391	392	.	.	.	Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Region	415	419	.	.	.	Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Active site	335	335	.	.	.	Note=Thioimidate intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Active site	437	437	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Metal binding	330	330	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Metal binding	332	332	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Metal binding	335	335	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Metal binding	508	508	.	.	.	Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Metal binding	509	509	.	.	.	Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Metal binding	510	510	.	.	.	Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Binding site	333	333	.	.	.	Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Binding site	449	449	.	.	.	Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50095	UniProtKB	Mutagenesis	253	253	.	.	.	Note=Increases drug-resistance to MPA. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16278936;Dbxref=PMID:16278936	
+##sequence-region Q02888 1 182
+Q02888	UniProtKB	Transit peptide	1	45	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02888	UniProtKB	Chain	46	182	.	.	.	ID=PRO_0000238621;Note=Inner membrane assembly complex subunit 17;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02888	UniProtKB	Topological domain	46	107	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24942160;Dbxref=PMID:24942160	
+Q02888	UniProtKB	Transmembrane	108	127	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02888	UniProtKB	Topological domain	128	182	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24942160;Dbxref=PMID:24942160	
+Q02888	UniProtKB	Coiled coil	128	158	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03824 1 705
+Q03824	UniProtKB	Chain	1	705	.	.	.	ID=PRO_0000203314;Note=Inheritance of peroxisomes protein 2	
+Q03824	UniProtKB	Transmembrane	215	231	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03824	UniProtKB	Glycosylation	275	275	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03824	UniProtKB	Glycosylation	343	343	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03824	UniProtKB	Glycosylation	344	344	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03824	UniProtKB	Glycosylation	379	379	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03824	UniProtKB	Glycosylation	517	517	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03824	UniProtKB	Glycosylation	569	569	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03824	UniProtKB	Glycosylation	574	574	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12271 1 1107
+Q12271	UniProtKB	Chain	1	1107	.	.	.	ID=PRO_0000268681;Note=Polyphosphatidylinositol phosphatase INP53	
+Q12271	UniProtKB	Domain	142	482	.	.	.	Note=SAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00183	
+Q12271	UniProtKB	Compositional bias	957	989	.	.	.	Note=Pro-rich	
+Q12271	UniProtKB	Modified residue	497	497	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50942	
+Q12271	UniProtKB	Modified residue	986	986	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12271	UniProtKB	Modified residue	1035	1035	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12271	UniProtKB	Modified residue	1105	1105	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12271	UniProtKB	Mutagenesis	421	421	.	.	.	Note=Reduces hydrolysis of PtdIns(4)P%3B when associated with A-424 and A-427. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12686590;Dbxref=PMID:12686590	
+Q12271	UniProtKB	Mutagenesis	424	424	.	.	.	Note=Reduces hydrolysis of PtdIns(4)P%3B when associated with A-421 and A-427. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12686590;Dbxref=PMID:12686590	
+Q12271	UniProtKB	Mutagenesis	427	427	.	.	.	Note=Reduces hydrolysis of PtdIns(4)P%3B when associated with A-421 and A-424. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12686590;Dbxref=PMID:12686590	
+Q12271	UniProtKB	Mutagenesis	746	746	.	.	.	Note=Abolishes hydrolysis of PtdIns(4%2C5)P2%3B when associated with A-748. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12686590;Dbxref=PMID:12686590	
+Q12271	UniProtKB	Mutagenesis	748	748	.	.	.	Note=Abolishes hydrolysis of PtdIns(4%2C5)P2%3B when associated with A-746. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12686590;Dbxref=PMID:12686590	
+##sequence-region P00724 1 532
+P00724	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2113524;Dbxref=PMID:2113524	
+P00724	UniProtKB	Chain	20	532	.	.	.	ID=PRO_0000033399;Note=Invertase 2	
+P00724	UniProtKB	Region	39	42	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00724	UniProtKB	Region	102	103	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00724	UniProtKB	Region	170	171	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00724	UniProtKB	Active site	42	42	.	.	.	Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10067,ECO:0000269|PubMed:2113524;Dbxref=PMID:2113524	
+P00724	UniProtKB	Binding site	60	60	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00724	UniProtKB	Binding site	223	223	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00724	UniProtKB	Binding site	311	311	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00724	UniProtKB	Glycosylation	23	23	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	64	64	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	97	97	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	111	111	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	118	118	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	165	165	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	266	266	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	275	275	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	356	356	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	369	369	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	384	384	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	398	398	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Glycosylation	512	512	.	.	.	Note=N-linked (GlcNAc...) asparagine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881	
+P00724	UniProtKB	Alternative sequence	1	20	.	.	.	ID=VSP_019611;Note=In isoform Intracellular. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00724	UniProtKB	Mutagenesis	42	42	.	.	.	Note=Loss of activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2113524;Dbxref=PMID:2113524	
+P00724	UniProtKB	Sequence conflict	51	51	.	.	.	Note=K->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00724	UniProtKB	Sequence conflict	409	409	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00724	UniProtKB	Beta strand	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	36	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Turn	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	54	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	73	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	86	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	100	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Helix	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	127	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	139	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	147	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	170	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Turn	178	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	182	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Helix	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	194	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	207	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	223	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	239	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	257	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	270	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	278	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	287	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Turn	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	303	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Turn	311	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	316	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	320	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	329	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	345	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	374	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	387	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	410	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	418	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	425	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Turn	431	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	435	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Helix	446	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	465	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	471	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Turn	490	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	494	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	503	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	510	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+P00724	UniProtKB	Beta strand	521	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV	
+##sequence-region P28239 1 310
+P28239	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28239	UniProtKB	Chain	31	310	.	.	.	ID=PRO_0000025413;Note=Inorganic pyrophosphatase%2C mitochondrial	
+P28239	UniProtKB	Metal binding	152	152	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28239	UniProtKB	Metal binding	157	157	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28239	UniProtKB	Metal binding	157	157	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28239	UniProtKB	Metal binding	189	189	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P32589 1 693
+P32589	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P32589	UniProtKB	Chain	2	693	.	.	.	ID=PRO_0000078396;Note=Heat shock protein homolog SSE1	
+P32589	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P32589	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32589	UniProtKB	Modified residue	660	660	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32589	UniProtKB	Cross-link	195	195	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32589	UniProtKB	Sequence conflict	269	270	.	.	.	Note=TA->NT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32589	UniProtKB	Sequence conflict	269	270	.	.	.	Note=TA->NT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32589	UniProtKB	Beta strand	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	11	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	23	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	34	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	44	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	81	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	90	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	98	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	109	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	115	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	140	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	151	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	167	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	174	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	197	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	209	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	220	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	234	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	257	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	261	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	282	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	291	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	297	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	303	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	311	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Turn	315	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	319	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	332	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	337	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	343	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	348	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Turn	368	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	371	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	385	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QXL	
+P32589	UniProtKB	Beta strand	393	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	402	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	414	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	423	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	439	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	448	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	457	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	476	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	490	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	505	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C7N	
+P32589	UniProtKB	Beta strand	520	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C7N	
+P32589	UniProtKB	Beta strand	529	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Beta strand	534	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	544	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Turn	586	589	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	590	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	595	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Turn	612	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	615	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+P32589	UniProtKB	Helix	621	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F	
+##sequence-region P17709 1 500
+P17709	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P17709	UniProtKB	Chain	2	500	.	.	.	ID=PRO_0000197603;Note=Glucokinase-1	
+P17709	UniProtKB	Domain	12	498	.	.	.	Note=Hexokinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+P17709	UniProtKB	Nucleotide binding	487	492	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17709	UniProtKB	Region	74	216	.	.	.	Note=Hexokinase small subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+P17709	UniProtKB	Region	158	184	.	.	.	Note=Glucose-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17709	UniProtKB	Region	217	487	.	.	.	Note=Hexokinase large subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084	
+P17709	UniProtKB	Binding site	110	110	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17709	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P17709	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P17709	UniProtKB	Modified residue	470	470	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P43581 1 546
+P43581	UniProtKB	Chain	1	546	.	.	.	ID=PRO_0000050400;Note=Hexose transporter HXT10	
+P43581	UniProtKB	Topological domain	1	44	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	66	100	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	122	127	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	149	158	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	159	179	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	180	185	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	186	206	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	207	220	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	221	241	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	242	324	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	325	341	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	342	347	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	348	365	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	366	372	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	394	415	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	416	436	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	437	453	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	454	474	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	475	475	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Transmembrane	476	496	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Topological domain	497	546	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43581	UniProtKB	Glycosylation	75	75	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40441 1 457
+P40441	UniProtKB	Chain	1	457	.	.	.	ID=PRO_0000050408;Note=Putative hexose transporter 12	
+P40441	UniProtKB	Topological domain	1	2	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Topological domain	24	29	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Transmembrane	30	50	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Topological domain	51	60	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Transmembrane	61	81	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Topological domain	82	87	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Topological domain	109	122	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Topological domain	144	247	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Transmembrane	248	268	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Topological domain	269	274	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Transmembrane	275	295	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Topological domain	296	319	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Transmembrane	320	340	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Topological domain	341	353	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Transmembrane	354	374	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Topological domain	375	379	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Transmembrane	380	400	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Topological domain	401	457	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40441	UniProtKB	Glycosylation	194	194	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53631 1 564
+P53631	UniProtKB	Chain	1	564	.	.	.	ID=PRO_0000050406;Note=Hexose transporter HXT17	
+P53631	UniProtKB	Topological domain	1	52	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	74	109	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	131	136	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	137	157	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	158	167	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	189	194	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	195	215	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	216	229	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	230	250	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	251	333	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	334	350	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	351	356	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	357	374	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	375	381	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	382	402	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	403	424	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	425	445	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	446	462	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	463	483	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	484	484	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Transmembrane	485	505	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53631	UniProtKB	Topological domain	506	564	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P23585 1 541
+P23585	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P23585	UniProtKB	Chain	2	541	.	.	.	ID=PRO_0000050392;Note=High-affinity glucose transporter HXT2	
+P23585	UniProtKB	Topological domain	2	49	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	71	107	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	108	128	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	129	134	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	135	155	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	156	162	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	163	183	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	184	192	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	193	213	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	214	227	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	228	248	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	249	327	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	328	347	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	348	350	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	351	371	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	372	379	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	380	400	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	401	418	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	419	439	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	440	456	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	457	477	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	478	484	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Transmembrane	485	505	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Topological domain	506	541	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P23585	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P23585	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P23585	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P23585	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P23585	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23585	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P23585	UniProtKB	Modified residue	266	266	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Modified residue	539	539	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23585	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32467 1 576
+P32467	UniProtKB	Chain	1	576	.	.	.	ID=PRO_0000050394;Note=Low-affinity glucose transporter HXT4	
+P32467	UniProtKB	Topological domain	1	66	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	67	87	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	88	122	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	144	149	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	171	180	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	181	201	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	202	207	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	229	242	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	264	346	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	347	363	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	364	369	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	370	387	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	388	394	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	395	415	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	416	437	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	438	458	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	459	475	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	476	496	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	497	497	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Transmembrane	498	518	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Topological domain	519	576	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Glycosylation	425	425	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32467	UniProtKB	Cross-link	45	45	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538	
+##sequence-region P39003 1 570
+P39003	UniProtKB	Chain	1	570	.	.	.	ID=PRO_0000050396;Note=High-affinity hexose transporter HXT6	
+P39003	UniProtKB	Topological domain	1	60	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	61	81	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	82	116	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	138	143	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	144	164	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	165	174	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	196	201	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	223	236	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	237	257	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	258	340	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	341	357	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	358	363	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	364	381	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	382	388	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	389	409	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	410	431	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	432	452	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	453	469	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	470	490	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	491	491	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Transmembrane	492	512	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Topological domain	513	570	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Glycosylation	91	91	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39003	UniProtKB	Cross-link	560	560	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P39003	UniProtKB	Sequence conflict	293	293	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40885 1 567
+P40885	UniProtKB	Chain	1	567	.	.	.	ID=PRO_0000050399;Note=Hexose transporter HXT9	
+P40885	UniProtKB	Topological domain	1	56	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	78	112	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	134	139	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	161	170	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	192	197	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	219	232	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	254	336	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	337	353	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	354	359	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	360	377	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	378	384	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	385	405	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	406	429	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	430	450	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	451	467	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	468	488	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	489	489	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Transmembrane	490	510	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Topological domain	511	567	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Glycosylation	87	87	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40885	UniProtKB	Glycosylation	227	227	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47125 1 453
+P47125	UniProtKB	Chain	1	453	.	.	.	ID=PRO_0000215208;Note=Indoleamine 2%2C3-dioxygenase	
+P47125	UniProtKB	Metal binding	331	331	.	.	.	Note=Iron (heme proximal ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P43598 1 195
+P43598	UniProtKB	Chain	1	195	.	.	.	ID=PRO_0000202687;Note=Inhibitor of glycogen debranching 1	
+P43598	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43598	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43598	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43598	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43598	UniProtKB	Modified residue	132	132	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43598	UniProtKB	Modified residue	164	164	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P39522 1 585
+P39522	UniProtKB	Metal binding	143	143	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39522	UniProtKB	Metal binding	221	221	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39522	UniProtKB	Sequence conflict	82	89	.	.	.	Note=SQSIEKAG->MFSIIEKR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39522	UniProtKB	Sequence conflict	238	238	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39522	UniProtKB	Sequence conflict	242	242	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39522	UniProtKB	Sequence conflict	492	492	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39522	UniProtKB	Sequence conflict	520	520	.	.	.	Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39522	UniProtKB	Sequence conflict	551	551	.	.	.	Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02821 1 542
+Q02821	UniProtKB	Chain	1	542	.	.	.	ID=PRO_0000120744;Note=Importin subunit alpha	
+Q02821	UniProtKB	Domain	1	65	.	.	.	Note=IBB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00561	
+Q02821	UniProtKB	Repeat	89	122	.	.	.	Note=ARM 1%3B truncated;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485	
+Q02821	UniProtKB	Repeat	123	162	.	.	.	Note=ARM 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485	
+Q02821	UniProtKB	Repeat	163	204	.	.	.	Note=ARM 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485	
+Q02821	UniProtKB	Repeat	205	251	.	.	.	Note=ARM 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485	
+Q02821	UniProtKB	Repeat	252	288	.	.	.	Note=ARM 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485	
+Q02821	UniProtKB	Repeat	289	330	.	.	.	Note=ARM 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485	
+Q02821	UniProtKB	Repeat	331	372	.	.	.	Note=ARM 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485	
+Q02821	UniProtKB	Repeat	373	417	.	.	.	Note=ARM 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485	
+Q02821	UniProtKB	Repeat	418	471	.	.	.	Note=ARM 9;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485	
+Q02821	UniProtKB	Repeat	472	508	.	.	.	Note=ARM 10%3B atypical;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485	
+Q02821	UniProtKB	Region	209	335	.	.	.	Note=NLS binding site 1	
+Q02821	UniProtKB	Region	419	505	.	.	.	Note=NLS binding site 2	
+Q02821	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q02821	UniProtKB	Mutagenesis	116	116	.	.	.	Note=In SRP1-31%3B temperature-sensitive mutant%3B reduced growth rate and chromosome loss. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713	
+Q02821	UniProtKB	Mutagenesis	145	145	.	.	.	Note=In SRP1-49%3B temperature-sensitive mutant%3B alteration in nucleolar and microtubule morphology. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713	
+Q02821	UniProtKB	Mutagenesis	219	219	.	.	.	Note=In SRP1-1%3B temperature-sensitive mutant. P->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713	
+Q02821	UniProtKB	Mutagenesis	286	286	.	.	.	Note=In SRP1-3%3B temperature-sensitive mutant. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713	
+Q02821	UniProtKB	Mutagenesis	360	360	.	.	.	Note=In SRP1-2%3B temperature-sensitive mutant. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713	
+Q02821	UniProtKB	Mutagenesis	459	459	.	.	.	Note=In SRP1-54%3B temperature-sensitive mutant%3B reduced growth rate. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713	
+Q02821	UniProtKB	Helix	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	89	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Beta strand	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XZR	
+Q02821	UniProtKB	Helix	101	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	123	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	132	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	145	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	163	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	175	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	187	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	205	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	217	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	229	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Beta strand	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	252	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	259	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	271	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Beta strand	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XZR	
+Q02821	UniProtKB	Helix	289	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	301	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	313	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	331	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	342	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	355	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	373	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	385	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	397	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Turn	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	419	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	430	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Turn	437	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	442	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	472	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	482	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Helix	488	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Beta strand	492	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C1T	
+Q02821	UniProtKB	Helix	495	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+Q02821	UniProtKB	Beta strand	509	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5	
+##sequence-region P40069 1 1113
+P40069	UniProtKB	Chain	1	1113	.	.	.	ID=PRO_0000120776;Note=Importin subunit beta-4	
+P40069	UniProtKB	Repeat	3	35	.	.	.	Note=HEAT 1;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Domain	25	92	.	.	.	Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115	
+P40069	UniProtKB	Repeat	40	74	.	.	.	Note=HEAT 2;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	92	115	.	.	.	Note=HEAT 3;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	120	147	.	.	.	Note=HEAT 4;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	157	191	.	.	.	Note=HEAT 5;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	208	244	.	.	.	Note=HEAT 6;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	252	287	.	.	.	Note=HEAT 7;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	296	348	.	.	.	Note=HEAT 8;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	350	384	.	.	.	Note=HEAT 9;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	388	428	.	.	.	Note=HEAT 10;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	430	469	.	.	.	Note=HEAT 11;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	472	513	.	.	.	Note=HEAT 12;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	515	558	.	.	.	Note=HEAT 13;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	560	605	.	.	.	Note=HEAT 14;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	607	680	.	.	.	Note=HEAT 15;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	683	737	.	.	.	Note=HEAT 16;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	744	783	.	.	.	Note=HEAT 17;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	790	856	.	.	.	Note=HEAT 18;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	859	894	.	.	.	Note=HEAT 19;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	902	934	.	.	.	Note=HEAT 20;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	942	991	.	.	.	Note=HEAT 21;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	999	1030	.	.	.	Note=HEAT 22;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	1049	1084	.	.	.	Note=HEAT 23;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Repeat	1085	1110	.	.	.	Note=HEAT 24;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588	
+P40069	UniProtKB	Modified residue	646	646	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32581 1 645
+P32581	UniProtKB	Chain	1	645	.	.	.	ID=PRO_0000086023;Note=Meiosis induction protein kinase IME2/SME1	
+P32581	UniProtKB	Domain	38	386	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32581	UniProtKB	Nucleotide binding	44	52	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32581	UniProtKB	Active site	193	193	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P32581	UniProtKB	Binding site	67	67	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region P25626 1 169
+P25626	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25626	UniProtKB	Chain	17	169	.	.	.	ID=PRO_0000030477;Note=54S ribosomal protein IMG1%2C mitochondrial	
+##sequence-region P46972 1 177
+P46972	UniProtKB	Chain	1	177	.	.	.	ID=PRO_0000109538;Note=Mitochondrial inner membrane protease subunit 2	
+P46972	UniProtKB	Transmembrane	134	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46972	UniProtKB	Active site	41	41	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46972	UniProtKB	Active site	91	91	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46972	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Abolishes enzymatic activity. S->A%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835	
+P46972	UniProtKB	Mutagenesis	91	91	.	.	.	Note=Abolishes enzymatic activity. K->H%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835	
+P46972	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Reduces processing of CYB2 and presence of IMP1 and SOM1 in the IMP complex. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15118906;Dbxref=PMID:15118906	
+P46972	UniProtKB	Mutagenesis	123	123	.	.	.	Note=Reduces processing of cytochrome c1%3B no effect on presence of IMP1 and SOM1 in the IMP complex. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15118906;Dbxref=PMID:15118906	
+P46972	UniProtKB	Mutagenesis	124	124	.	.	.	Note=Abolishes enzymatic activity. D->N%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835	
+P46972	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Abolishes enzymatic activity. D->N%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835	
+##sequence-region P53941 1 290
+P53941	UniProtKB	Chain	1	290	.	.	.	ID=PRO_0000120245;Note=U3 small nucleolar ribonucleoprotein protein IMP4	
+P53941	UniProtKB	Domain	86	267	.	.	.	Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034	
+P53941	UniProtKB	Mutagenesis	119	119	.	.	.	Note=No effect on RNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489263;Dbxref=PMID:15489263	
+P53941	UniProtKB	Mutagenesis	201	201	.	.	.	Note=No effect on RNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489263;Dbxref=PMID:15489263	
+P53941	UniProtKB	Mutagenesis	220	220	.	.	.	Note=Loss of RNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489263;Dbxref=PMID:15489263	
+P53941	UniProtKB	Mutagenesis	253	253	.	.	.	Note=Loss of RNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489263;Dbxref=PMID:15489263	
+##sequence-region Q03694 1 420
+Q03694	UniProtKB	Chain	1	420	.	.	.	ID=PRO_0000203328;Note=Inheritance of peroxisomes protein 1	
+Q03694	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q08630 1 104
+Q08630	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000299728;Note=Increased recombination centers protein 13	
+Q08630	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04772 1 201
+Q04772	UniProtKB	Chain	1	201	.	.	.	ID=PRO_0000166039;Note=Increased recombination centers protein 21	
+Q04772	UniProtKB	Domain	122	200	.	.	.	Note=Cytochrome b5 heme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+Q04772	UniProtKB	Metal binding	158	158	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+Q04772	UniProtKB	Metal binding	182	182	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+##sequence-region P47046 1 822
+P47046	UniProtKB	Chain	1	822	.	.	.	ID=PRO_0000203064;Note=Uncharacterized protein IRC8	
+P47046	UniProtKB	Topological domain	1	13	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47046	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47046	UniProtKB	Topological domain	35	44	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47046	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47046	UniProtKB	Topological domain	66	76	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47046	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47046	UniProtKB	Topological domain	98	120	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47046	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47046	UniProtKB	Topological domain	142	822	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47046	UniProtKB	Modified residue	690	690	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P28241 1 369
+P28241	UniProtKB	Transit peptide	1	15	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2198251,ECO:0000269|PubMed:7505425;Dbxref=PMID:2198251,PMID:7505425	
+P28241	UniProtKB	Chain	16	369	.	.	.	ID=PRO_0000014434;Note=Isocitrate dehydrogenase [NAD] subunit 2%2C mitochondrial	
+P28241	UniProtKB	Metal binding	237	237	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28241	UniProtKB	Metal binding	263	263	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28241	UniProtKB	Metal binding	267	267	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28241	UniProtKB	Binding site	119	119	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28241	UniProtKB	Binding site	129	129	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28241	UniProtKB	Binding site	150	150	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28241	UniProtKB	Binding site	237	237	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28241	UniProtKB	Site	157	157	.	.	.	Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28241	UniProtKB	Site	204	204	.	.	.	Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28241	UniProtKB	Modified residue	105	105	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P28241	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P28241	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P28241	UniProtKB	Modified residue	349	349	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P28241	UniProtKB	Sequence conflict	25	25	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28241	UniProtKB	Helix	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLV	
+P28241	UniProtKB	Turn	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	48	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Turn	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	86	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	96	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	114	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	124	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	145	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	153	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	168	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	177	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	197	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Turn	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	210	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	229	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	236	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	247	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	253	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	259	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	277	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	281	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Beta strand	290	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Turn	303	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	311	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	327	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	337	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	350	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+P28241	UniProtKB	Helix	358	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX	
+##sequence-region P40154 1 320
+P40154	UniProtKB	Chain	1	320	.	.	.	ID=PRO_0000084154;Note=Ino eighty subunit 2	
+P40154	UniProtKB	Modified residue	67	67	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40154	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32617 1 166
+P32617	UniProtKB	Chain	1	166	.	.	.	ID=PRO_0000084158;Note=Chromatin-remodeling complex subunit IES6	
+P32617	UniProtKB	Sequence conflict	32	32	.	.	.	Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47170 1 1584
+P47170	UniProtKB	Chain	1	1584	.	.	.	ID=PRO_0000203123;Note=Vacuolar membrane-associated protein IML1	
+P47170	UniProtKB	Domain	1198	1273	.	.	.	Note=DEP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00066	
+P47170	UniProtKB	Modified residue	680	680	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47170	UniProtKB	Modified residue	737	737	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q05533 1 292
+Q05533	UniProtKB	Chain	1	292	.	.	.	ID=PRO_0000245568;Note=Inositol monophosphatase 2	
+Q05533	UniProtKB	Region	96	99	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05533	UniProtKB	Metal binding	75	75	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05533	UniProtKB	Metal binding	94	94	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05533	UniProtKB	Metal binding	94	94	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05533	UniProtKB	Metal binding	96	96	.	.	.	Note=Magnesium 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05533	UniProtKB	Metal binding	97	97	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05533	UniProtKB	Metal binding	231	231	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05533	UniProtKB	Binding site	75	75	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05533	UniProtKB	Binding site	231	231	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53901 1 409
+P53901	UniProtKB	Chain	1	409	.	.	.	ID=PRO_0000203419;Note=Ingression protein 1	
+P53901	UniProtKB	Domain	1	134	.	.	.	Note=C2	
+P53901	UniProtKB	Compositional bias	303	310	.	.	.	Note=Poly-Asp	
+P53901	UniProtKB	Modified residue	392	392	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53901	UniProtKB	Mutagenesis	28	28	.	.	.	Note=Impairs plasma membrane ingression%3B when associated with A-31. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18344988;Dbxref=PMID:18344988	
+P53901	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Impairs plasma membrane ingression%3B when associated with A-28. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18344988;Dbxref=PMID:18344988	
+P53901	UniProtKB	Sequence conflict	221	221	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P50942 1 1183
+P50942	UniProtKB	Chain	1	1183	.	.	.	ID=PRO_0000209745;Note=Polyphosphatidylinositol phosphatase INP52	
+P50942	UniProtKB	Domain	167	507	.	.	.	Note=SAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00183	
+P50942	UniProtKB	Modified residue	152	152	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P50942	UniProtKB	Modified residue	522	522	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50942	UniProtKB	Modified residue	1005	1005	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P50942	UniProtKB	Modified residue	1016	1016	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50942	UniProtKB	Modified residue	1032	1032	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P50942	UniProtKB	Modified residue	1095	1095	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12271	
+P50942	UniProtKB	Mutagenesis	631	631	.	.	.	Note=Impairs completely enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10962003;Dbxref=PMID:10962003	
+P50942	UniProtKB	Mutagenesis	730	730	.	.	.	Note=Impairs completely enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10962003;Dbxref=PMID:10962003	
+P50942	UniProtKB	Mutagenesis	771	771	.	.	.	Note=Impairs completely enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10962003;Dbxref=PMID:10962003	
+##sequence-region Q12072 1 812
+Q12072	UniProtKB	Chain	1	812	.	.	.	ID=PRO_0000240452;Note=ISWI one complex protein 2	
+Q12072	UniProtKB	Coiled coil	673	714	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12072	UniProtKB	Compositional bias	761	807	.	.	.	Note=Gln-rich	
+##sequence-region Q04213 1 475
+Q04213	UniProtKB	Chain	1	475	.	.	.	ID=PRO_0000203276;Note=ISWI one complex protein 4	
+Q04213	UniProtKB	Compositional bias	74	77	.	.	.	Note=Poly-Glu	
+Q04213	UniProtKB	Compositional bias	186	195	.	.	.	Note=Poly-Glu	
+Q04213	UniProtKB	Compositional bias	243	251	.	.	.	Note=Poly-Glu	
+Q04213	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04213	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04213	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04213	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04213	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P07250 1 355
+P07250	UniProtKB	Chain	1	355	.	.	.	ID=PRO_0000066873;Note=Inositol polyphosphate multikinase	
+P07250	UniProtKB	Region	127	135	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07250	UniProtKB	Compositional bias	282	301	.	.	.	Note=Asp-rich (acidic)	
+P07250	UniProtKB	Metal binding	133	133	.	.	.	Note=Manganese;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17050532;Dbxref=PMID:17050532	
+P07250	UniProtKB	Metal binding	271	271	.	.	.	Note=Calcium%3B via carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17050532;Dbxref=PMID:17050532	
+P07250	UniProtKB	Metal binding	274	274	.	.	.	Note=Calcium;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17050532;Dbxref=PMID:17050532	
+P07250	UniProtKB	Metal binding	325	325	.	.	.	Note=Manganese;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17050532;Dbxref=PMID:17050532	
+P07250	UniProtKB	Metal binding	334	334	.	.	.	Note=Calcium%3B via carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17050532;Dbxref=PMID:17050532	
+P07250	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07250	UniProtKB	Modified residue	97	97	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07250	UniProtKB	Sequence conflict	109	109	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07250	UniProtKB	Beta strand	28	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Helix	35	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Helix	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Beta strand	69	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Beta strand	113	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Turn	120	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Beta strand	125	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Helix	145	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Helix	159	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Beta strand	164	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Helix	176	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Helix	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Beta strand	194	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Helix	200	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Turn	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Helix	211	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Helix	226	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Beta strand	252	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Helix	267	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Turn	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Beta strand	319	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Beta strand	329	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+P07250	UniProtKB	Helix	339	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW	
+##sequence-region P38954 1 527
+P38954	UniProtKB	Chain	1	527	.	.	.	ID=PRO_0000084224;Note=Inositolphosphotransferase 1	
+P38954	UniProtKB	Topological domain	1	24	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Topological domain	46	99	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Topological domain	121	152	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Topological domain	174	190	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Transmembrane	191	211	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Topological domain	212	219	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Transmembrane	220	240	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Topological domain	241	288	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Transmembrane	289	309	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Topological domain	310	435	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Transmembrane	436	456	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Topological domain	457	461	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Transmembrane	462	482	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Topological domain	483	527	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38954	UniProtKB	Compositional bias	378	384	.	.	.	Note=Poly-Ser	
+##sequence-region P47034 1 131
+P47034	UniProtKB	Chain	1	131	.	.	.	ID=PRO_0000203052;Note=Increased copper sensitivity protein 3	
+P47034	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47034	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P07260 1 213
+P07260	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000193653;Note=Eukaryotic translation initiation factor 4E	
+P07260	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592868;Dbxref=PMID:7592868	
+P07260	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:7592868;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198,PMID:7592868	
+P07260	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P07260	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07260	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P07260	UniProtKB	Cross-link	114	114	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P07260	UniProtKB	Beta strand	9	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8	
+P07260	UniProtKB	Beta strand	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Helix	26	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8	
+P07260	UniProtKB	Beta strand	36	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Helix	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Helix	58	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Beta strand	63	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Helix	72	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Turn	83	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Beta strand	92	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Turn	104	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Beta strand	112	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Beta strand	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Helix	127	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Turn	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Turn	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Beta strand	149	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Beta strand	161	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Helix	172	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Beta strand	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8	
+P07260	UniProtKB	Beta strand	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Helix	199	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+P07260	UniProtKB	Beta strand	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8	
+##sequence-region P39520 1 1085
+P39520	UniProtKB	Chain	1	1085	.	.	.	ID=PRO_0000084164;Note=Protein IFH1	
+P39520	UniProtKB	Compositional bias	122	163	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P39520	UniProtKB	Modified residue	208	208	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39520	UniProtKB	Modified residue	1041	1041	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P25605 1 309
+P25605	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7483834;Dbxref=PMID:7483834	
+P25605	UniProtKB	Chain	25	309	.	.	.	ID=PRO_0000015637;Note=Acetolactate synthase small subunit%2C mitochondrial	
+P25605	UniProtKB	Domain	79	159	.	.	.	Note=ACT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007	
+P25605	UniProtKB	Compositional bias	25	30	.	.	.	Note=Poly-Ser	
+##sequence-region P07342 1 687
+P07342	UniProtKB	Transit peptide	1	90	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07342	UniProtKB	Chain	91	687	.	.	.	ID=PRO_0000035664;Note=Acetolactate synthase catalytic subunit%2C mitochondrial	
+P07342	UniProtKB	Nucleotide binding	355	376	.	.	.	Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496246;Dbxref=PMID:12496246	
+P07342	UniProtKB	Nucleotide binding	407	426	.	.	.	Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496246;Dbxref=PMID:12496246	
+P07342	UniProtKB	Region	499	579	.	.	.	Note=Thiamine pyrophosphate binding	
+P07342	UniProtKB	Metal binding	550	550	.	.	.	Note=Magnesium	
+P07342	UniProtKB	Metal binding	577	577	.	.	.	Note=Magnesium	
+P07342	UniProtKB	Metal binding	579	579	.	.	.	Note=Magnesium%3B via carbonyl oxygen	
+P07342	UniProtKB	Binding site	139	139	.	.	.	Note=Thiamine pyrophosphate	
+P07342	UniProtKB	Binding site	241	241	.	.	.	Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496246;Dbxref=PMID:12496246	
+P07342	UniProtKB	Turn	88	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	94	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	109	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	119	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	139	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	157	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	171	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	184	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	193	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Turn	196	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IMS	
+P07342	UniProtKB	Helix	206	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	214	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	226	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	244	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	251	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	264	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	272	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	279	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	300	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	308	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	316	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	331	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	335	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	348	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	358	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	368	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	379	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	385	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	390	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	402	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	410	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	415	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	420	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	427	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	445	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	467	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JSC	
+P07342	UniProtKB	Helix	473	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	491	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	499	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	512	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IMS	
+P07342	UniProtKB	Helix	528	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	542	549	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	550	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	557	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	560	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	571	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	582	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	589	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IMS	
+P07342	UniProtKB	Beta strand	594	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IMS	
+P07342	UniProtKB	Helix	605	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	614	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	622	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Helix	625	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	639	645	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU	
+P07342	UniProtKB	Beta strand	652	654	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FEM	
+P07342	UniProtKB	Helix	669	682	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FEM	
+P07342	UniProtKB	Turn	683	685	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FEM	
+##sequence-region P21954 1 428
+P21954	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1989987;Dbxref=PMID:1989987	
+P21954	UniProtKB	Chain	17	428	.	.	.	ID=PRO_0000014426;Note=Isocitrate dehydrogenase [NADP]%2C mitochondrial	
+P21954	UniProtKB	Nucleotide binding	91	93	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Nucleotide binding	327	332	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Region	110	116	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Metal binding	269	269	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Metal binding	292	292	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Binding site	93	93	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Binding site	98	98	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Binding site	125	125	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Binding site	148	148	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Binding site	277	277	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Binding site	345	345	.	.	.	Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Site	155	155	.	.	.	Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Site	229	229	.	.	.	Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21954	UniProtKB	Beta strand	26	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	33	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Turn	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	55	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	62	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Turn	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	71	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	84	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	96	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	111	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	121	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	142	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	153	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	158	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	164	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Turn	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	183	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	194	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	203	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	224	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Turn	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	236	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	253	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	263	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	268	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	280	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	288	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	307	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Beta strand	315	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFX	
+P21954	UniProtKB	Beta strand	320	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	330	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	347	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	367	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	392	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	403	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+P21954	UniProtKB	Helix	409	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY	
+##sequence-region P43579 1 692
+P43579	UniProtKB	Chain	1	692	.	.	.	ID=PRO_0000084153;Note=Ino eighty subunit 1	
+P43579	UniProtKB	Coiled coil	340	385	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43579	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43579	UniProtKB	Modified residue	487	487	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43579	UniProtKB	Modified residue	493	493	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43579	UniProtKB	Modified residue	504	504	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43579	UniProtKB	Modified residue	507	507	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43579	UniProtKB	Sequence conflict	219	219	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08561 1 116
+Q08561	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000084156;Note=Ino eighty subunit 4	
+##sequence-region P38912 1 153
+P38912	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000145113;Note=Eukaryotic translation initiation factor 1A	
+P38912	UniProtKB	Domain	22	96	.	.	.	Note=S1-like	
+P38912	UniProtKB	Beta strand	33	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P38912	UniProtKB	Beta strand	46	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P38912	UniProtKB	Beta strand	56	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P38912	UniProtKB	Helix	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P38912	UniProtKB	Beta strand	76	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P38912	UniProtKB	Beta strand	86	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P38912	UniProtKB	Helix	98	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+##sequence-region P32481 1 527
+P32481	UniProtKB	Chain	1	527	.	.	.	ID=PRO_0000137448;Note=Eukaryotic translation initiation factor 2 subunit gamma	
+P32481	UniProtKB	Domain	98	307	.	.	.	Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32481	UniProtKB	Nucleotide binding	107	114	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32481	UniProtKB	Nucleotide binding	193	197	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32481	UniProtKB	Nucleotide binding	249	252	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32481	UniProtKB	Region	107	114	.	.	.	Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32481	UniProtKB	Region	135	139	.	.	.	Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32481	UniProtKB	Region	193	196	.	.	.	Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32481	UniProtKB	Region	249	252	.	.	.	Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32481	UniProtKB	Region	284	286	.	.	.	Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P32481	UniProtKB	Compositional bias	155	179	.	.	.	Note=Cys-rich	
+P32481	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32481	UniProtKB	Modified residue	258	258	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P32481	UniProtKB	Beta strand	425	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN	
+P32481	UniProtKB	Beta strand	460	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN	
+P32481	UniProtKB	Beta strand	469	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN	
+P32481	UniProtKB	Beta strand	480	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN	
+P32481	UniProtKB	Beta strand	498	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN	
+P32481	UniProtKB	Beta strand	506	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN	
+##sequence-region P39935 1 952
+P39935	UniProtKB	Chain	1	952	.	.	.	ID=PRO_0000213331;Note=Eukaryotic initiation factor 4F subunit p150	
+P39935	UniProtKB	Domain	607	850	.	.	.	Note=MIF4G	
+P39935	UniProtKB	Region	188	299	.	.	.	Note=Interaction with PAB1	
+P39935	UniProtKB	Compositional bias	173	200	.	.	.	Note=Pro/Ser/Thr-rich	
+P39935	UniProtKB	Compositional bias	375	384	.	.	.	Note=Ala/Glu-rich	
+P39935	UniProtKB	Compositional bias	488	553	.	.	.	Note=Arg/Ser-rich	
+P39935	UniProtKB	Compositional bias	869	872	.	.	.	Note=Poly-Glu	
+P39935	UniProtKB	Compositional bias	873	899	.	.	.	Note=Arg/Ser-rich	
+P39935	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P39935	UniProtKB	Modified residue	883	883	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39935	UniProtKB	Modified residue	888	888	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39935	UniProtKB	Modified residue	908	908	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39935	UniProtKB	Modified residue	948	948	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39935	UniProtKB	Mutagenesis	214	217	.	.	.	Note=In TIF4631-213%3B abolishes interaction with PAB1 and inhibits poly(A)-dependent translation. KLRK->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9256432;Dbxref=PMID:9256432	
+P39935	UniProtKB	Sequence conflict	7	7	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39935	UniProtKB	Sequence conflict	37	37	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39935	UniProtKB	Sequence conflict	110	110	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39935	UniProtKB	Sequence conflict	207	207	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39935	UniProtKB	Sequence conflict	361	361	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39935	UniProtKB	Helix	411	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8	
+P39935	UniProtKB	Helix	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8	
+P39935	UniProtKB	Helix	443	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8	
+P39935	UniProtKB	Helix	454	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8	
+P39935	UniProtKB	Helix	471	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8	
+P39935	UniProtKB	Helix	603	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+P39935	UniProtKB	Beta strand	619	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSX	
+P39935	UniProtKB	Helix	622	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+P39935	UniProtKB	Helix	635	638	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+P39935	UniProtKB	Helix	643	658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+P39935	UniProtKB	Helix	660	662	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+P39935	UniProtKB	Helix	663	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+P39935	UniProtKB	Helix	692	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+P39935	UniProtKB	Helix	733	755	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+P39935	UniProtKB	Helix	761	776	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+P39935	UniProtKB	Helix	781	798	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+P39935	UniProtKB	Helix	812	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+P39935	UniProtKB	Helix	834	848	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO	
+##sequence-region P23301 1 157
+P23301	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:8243648;Dbxref=PMID:22814378,PMID:8243648	
+P23301	UniProtKB	Chain	2	157	.	.	.	ID=PRO_0000142488;Note=Eukaryotic translation initiation factor 5A-1	
+P23301	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:8243648;Dbxref=PMID:22814378,PMID:8243648	
+P23301	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:8243648,ECO:0000269|PubMed:8325852;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198,PMID:8243648,PMID:8325852	
+P23301	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23301	UniProtKB	Modified residue	51	51	.	.	.	Note=Hypusine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19120453;Dbxref=PMID:19120453	
+P23301	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P23301	UniProtKB	Cross-link	86	86	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P23301	UniProtKB	Mutagenesis	22	22	.	.	.	Note=Temperature-sensitive growth phenotype%3B when associated with F-93. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Temperature-sensitive growth phenotype. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	39	39	.	.	.	Note=Temperature-sensitive growth phenotype. Lethal%3B when associated with L-83 and D-118 or with I-66 and D-118 or with D-118 and I-142 or with L-116 and D-118. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10229683,ECO:0000269|PubMed:18341589;Dbxref=PMID:10229683,PMID:18341589	
+P23301	UniProtKB	Mutagenesis	50	50	.	.	.	Note=Lethal. G->A%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	51	51	.	.	.	Note=Impairs association to the ribosome and cell growth. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16215987,ECO:0000269|PubMed:16914118,ECO:0000269|PubMed:18341589,ECO:0000269|PubMed:19120453,ECO:0000269|PubMed:19424157;Dbxref=PMID:16215987,PMID:16914118,PMID:18341589,PMID:19120453,PMID:19424157	
+P23301	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Lethal. H->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Lethal. G->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Lethal. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	56	56	.	.	.	Note=Temperature-sensitive growth phenotype. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	56	56	.	.	.	Note=Lethal. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Temperature-sensitive growth phenotype. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Impairs programmed ribosomal frameshifting. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19424157;Dbxref=PMID:19424157	
+P23301	UniProtKB	Mutagenesis	66	66	.	.	.	Note=Temperature-sensitive growth phenotype. Lethal%3B when associated with Y-39 and D-118. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Temperature-sensitive growth phenotype. Lethal%3B when associated with Y-39 and D-118. P->S%2CL;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10229683,ECO:0000269|PubMed:18341589;Dbxref=PMID:10229683,PMID:18341589	
+P23301	UniProtKB	Mutagenesis	93	93	.	.	.	Note=Lethal. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Temperature-sensitive growth phenotype. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16408210;Dbxref=PMID:16408210	
+P23301	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Temperature-sensitive growth phenotype%3B when associated with D-118. Lethal%3B when associated with Y-39 and D-118. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	118	118	.	.	.	Note=Temperature-sensitive growth phenotype%3B when associated with L-116 or W-122 or F-140 or I-142. Lethal%3B when associated with Y-39 and I-66 or with Y-39 and L-83 or with Y-39 and L-116 or with Y-39 and F-140 or with Y-39 and I-142 or with N-120 and D-124. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	118	118	.	.	.	Note=Temperature-sensitive growth phenotype%3B when associated with W-122. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Lethal%3B when associated with D-118 and D-124. L->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Temperature-sensitive growth phenotype%3B when associated with V-118. D->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	124	124	.	.	.	Note=Lethal%3B when associated with D-118 and N-120. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	140	140	.	.	.	Note=Temperature-sensitive growth phenotype%3B when associated with D-118. Lethal%3B when associated with Y-39 and D-118. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	142	142	.	.	.	Note=Temperature-sensitive growth phenotype%3B when associated with D-118. Lethal%3B when associated with Y-39 and D-118. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589	
+P23301	UniProtKB	Mutagenesis	149	149	.	.	.	Note=In ts1159%3B temperature-sensitive growth phenotype and impairs programmed ribosomal frameshifting. S->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18341589,ECO:0000269|PubMed:19424157,ECO:0000269|PubMed:9582285;Dbxref=PMID:18341589,PMID:19424157,PMID:9582285	
+P23301	UniProtKB	Beta strand	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Turn	23	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Beta strand	31	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Beta strand	37	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Beta strand	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Beta strand	56	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Beta strand	70	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Beta strand	87	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Turn	96	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Beta strand	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Helix	120	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Beta strand	135	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+P23301	UniProtKB	Beta strand	144	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0	
+##sequence-region Q9P305 1 131
+Q9P305	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q9P305	UniProtKB	Chain	2	131	.	.	.	ID=PRO_0000245365;Note=mRNA stability protein IGO2	
+Q9P305	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q9P305	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q9P305	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+Q9P305	UniProtKB	Modified residue	108	108	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q9P305	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P47042 1 667
+P47042	UniProtKB	Chain	1	667	.	.	.	ID=PRO_0000086138;Note=Probable serine/threonine-protein kinase IKS1	
+P47042	UniProtKB	Domain	173	530	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P47042	UniProtKB	Nucleotide binding	179	187	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P47042	UniProtKB	Active site	350	350	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P47042	UniProtKB	Binding site	205	205	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P47042	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P47155 1 203
+P47155	UniProtKB	Chain	1	203	.	.	.	ID=PRO_0000203115;Note=Protein ILM1	
+P47155	UniProtKB	Topological domain	1	3	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47155	UniProtKB	Transmembrane	4	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47155	UniProtKB	Topological domain	25	58	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47155	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47155	UniProtKB	Topological domain	80	92	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47155	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47155	UniProtKB	Topological domain	114	114	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47155	UniProtKB	Transmembrane	115	135	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47155	UniProtKB	Topological domain	136	203	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38217 1 918
+P38217	UniProtKB	Chain	1	918	.	.	.	ID=PRO_0000120770;Note=Importin subunit beta-2	
+P38217	UniProtKB	Repeat	11	38	.	.	.	Note=HEAT 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	43	92	.	.	.	Note=HEAT 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	103	137	.	.	.	Note=HEAT 3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	145	181	.	.	.	Note=HEAT 4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	190	222	.	.	.	Note=HEAT 5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	235	263	.	.	.	Note=HEAT 6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	275	303	.	.	.	Note=HEAT 7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	320	413	.	.	.	Note=HEAT 8;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	421	449	.	.	.	Note=HEAT 9;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	461	488	.	.	.	Note=HEAT 10;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	501	534	.	.	.	Note=HEAT 11;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	542	577	.	.	.	Note=HEAT 12;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	583	620	.	.	.	Note=HEAT 13;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	628	678	.	.	.	Note=HEAT 14;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	694	725	.	.	.	Note=HEAT 15;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	777	814	.	.	.	Note=HEAT 17;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	825	858	.	.	.	Note=HEAT 18;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Repeat	867	900	.	.	.	Note=HEAT 19;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973	
+P38217	UniProtKB	Compositional bias	373	392	.	.	.	Note=Asp/Glu-rich (acidic)	
+##sequence-region P21190 1 360
+P21190	UniProtKB	Chain	1	360	.	.	.	ID=PRO_0000084181;Note=Meiosis-inducing protein 1	
+##sequence-region P41833 1 600
+P41833	UniProtKB	Chain	1	600	.	.	.	ID=PRO_0000207634;Note=N6-adenosine-methyltransferase IME4	
+P41833	UniProtKB	Mutagenesis	348	348	.	.	.	Note=Impairs ability to sporulate. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384598;Dbxref=PMID:12384598	
+P41833	UniProtKB	Mutagenesis	351	351	.	.	.	Note=Impairs ability to sporulate. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384598;Dbxref=PMID:12384598	
+##sequence-region P53219 1 342
+P53219	UniProtKB	Transit peptide	1	38	.	.	.	Note=Mitochondrion	
+P53219	UniProtKB	Propeptide	39	46	.	.	.	ID=PRO_0000410798;Note=Removed in mature form	
+P53219	UniProtKB	Chain	47	342	.	.	.	ID=PRO_0000202791;Note=Abhydrolase domain-containing protein IMO32	
+P53219	UniProtKB	Domain	75	326	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53219	UniProtKB	Active site	152	152	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53219	UniProtKB	Active site	319	319	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P32899 1 183
+P32899	UniProtKB	Chain	1	183	.	.	.	ID=PRO_0000132712;Note=U3 small nucleolar ribonucleoprotein protein IMP3	
+P32899	UniProtKB	Domain	109	175	.	.	.	Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182	
+##sequence-region P40573 1 187
+P40573	UniProtKB	Chain	1	187	.	.	.	ID=PRO_0000076520;Note=Transcriptional activator of sulfur metabolism MET28	
+P40573	UniProtKB	Domain	105	168	.	.	.	Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P40573	UniProtKB	Region	106	136	.	.	.	Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P40573	UniProtKB	Region	137	151	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+##sequence-region Q03081 1 177
+Q03081	UniProtKB	Chain	1	177	.	.	.	ID=PRO_0000046808;Note=Transcriptional regulator MET31	
+Q03081	UniProtKB	Zinc finger	95	117	.	.	.	Note=C2H2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+##sequence-region P47169 1 1442
+P47169	UniProtKB	Chain	1	1442	.	.	.	ID=PRO_0000199968;Note=Sulfite reductase [NADPH] subunit beta	
+P47169	UniProtKB	Domain	682	831	.	.	.	Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088	
+P47169	UniProtKB	Metal binding	1300	1300	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47169	UniProtKB	Metal binding	1306	1306	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47169	UniProtKB	Metal binding	1345	1345	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47169	UniProtKB	Metal binding	1349	1349	.	.	.	Note=Iron (siroheme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47169	UniProtKB	Metal binding	1349	1349	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47169	UniProtKB	Modified residue	903	903	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P05694 1 767
+P05694	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7483834;Dbxref=PMID:7483834	
+P05694	UniProtKB	Chain	2	767	.	.	.	ID=PRO_0000098704;Note=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase	
+P05694	UniProtKB	Metal binding	655	655	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05694	UniProtKB	Metal binding	657	657	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05694	UniProtKB	Metal binding	737	737	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05694	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P05694	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P05694	UniProtKB	Modified residue	566	566	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P05694	UniProtKB	Modified residue	629	629	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P05694	UniProtKB	Modified residue	706	706	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P05694	UniProtKB	Sequence conflict	72	80	.	.	.	Note=LSLLFNVIP->FVFVVQCHS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05694	UniProtKB	Sequence conflict	407	407	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P10659 1 382
+P10659	UniProtKB	Chain	1	382	.	.	.	ID=PRO_0000174451;Note=S-adenosylmethionine synthase 1	
+P10659	UniProtKB	Nucleotide binding	166	168	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266	
+P10659	UniProtKB	Nucleotide binding	234	237	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266	
+P10659	UniProtKB	Nucleotide binding	251	252	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P10659	UniProtKB	Metal binding	10	10	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13444	
+P10659	UniProtKB	Metal binding	44	44	.	.	.	Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P10659	UniProtKB	Binding site	16	16	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266	
+P10659	UniProtKB	Binding site	57	57	.	.	.	Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P10659	UniProtKB	Binding site	100	100	.	.	.	Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P10659	UniProtKB	Binding site	245	245	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266	
+P10659	UniProtKB	Binding site	245	245	.	.	.	Note=Methionine%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P10659	UniProtKB	Binding site	268	268	.	.	.	Note=ATP%3B via amide nitrogen%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P10659	UniProtKB	Binding site	272	272	.	.	.	Note=ATP%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P10659	UniProtKB	Binding site	276	276	.	.	.	Note=ATP%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13444	
+P10659	UniProtKB	Binding site	276	276	.	.	.	Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P10659	UniProtKB	Sequence conflict	246	246	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10659	UniProtKB	Sequence conflict	357	357	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04922 1 465
+Q04922	UniProtKB	Chain	1	465	.	.	.	ID=PRO_0000253803;Note=Mitochondrial F-box protein MFB1	
+Q04922	UniProtKB	Domain	14	60	.	.	.	Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080	
+##sequence-region P32787 1 269
+P32787	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32787	UniProtKB	Chain	31	269	.	.	.	ID=PRO_0000021719;Note=Mitochondrial genome maintenance protein MGM101	
+##sequence-region P28321 1 313
+P28321	UniProtKB	Chain	1	313	.	.	.	ID=PRO_0000203164;Note=Monoglyceride lipase	
+P28321	UniProtKB	Active site	123	123	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35678	
+P28321	UniProtKB	Active site	251	251	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35678	
+P28321	UniProtKB	Active site	281	281	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35678	
+P28321	UniProtKB	Sequence conflict	244	244	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28321	UniProtKB	Sequence conflict	290	290	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P28321	UniProtKB	Beta strand	16	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Beta strand	23	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Beta strand	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Beta strand	40	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	53	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	57	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Turn	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	92	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Beta strand	117	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	124	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Turn	137	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Beta strand	143	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Beta strand	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	156	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	164	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Turn	171	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	186	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	193	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Turn	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	212	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	232	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Beta strand	243	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Beta strand	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	256	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Beta strand	269	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Turn	283	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+P28321	UniProtKB	Helix	289	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN	
+##sequence-region P32266 1 881
+P32266	UniProtKB	Transit peptide	1	59	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12707284;Dbxref=PMID:12707284	
+P32266	UniProtKB	Chain	60	881	.	.	.	ID=PRO_0000007400;Note=Dynamin-like GTPase MGM1 large isoform	
+P32266	UniProtKB	Chain	140	881	.	.	.	ID=PRO_0000007401;Note=Dynamin-like GTPase MGM1 small isoform	
+P32266	UniProtKB	Topological domain	60	72	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32266	UniProtKB	Transmembrane	73	92	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32266	UniProtKB	Topological domain	93	881	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32266	UniProtKB	Domain	207	505	.	.	.	Note=Dynamin-type G	
+P32266	UniProtKB	Domain	780	872	.	.	.	Note=GED;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00720	
+P32266	UniProtKB	Nucleotide binding	217	224	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32266	UniProtKB	Nucleotide binding	317	321	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32266	UniProtKB	Nucleotide binding	385	388	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32266	UniProtKB	Compositional bias	149	178	.	.	.	Note=Asp-rich (acidic)	
+P32266	UniProtKB	Mutagenesis	1	1	.	.	.	Note=Abolishes translation. M->A	
+P32266	UniProtKB	Mutagenesis	39	39	.	.	.	Note=No effect on translation. M->A	
+P32266	UniProtKB	Mutagenesis	79	79	.	.	.	Note=Loss of function%3B most MGM1 processed to s-MGM1. G->D%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15096522;Dbxref=PMID:15096522	
+P32266	UniProtKB	Mutagenesis	81	81	.	.	.	Note=No effect on translation. M->A	
+P32266	UniProtKB	Mutagenesis	92	92	.	.	.	Note=No effect on translation. M->A	
+P32266	UniProtKB	Mutagenesis	223	223	.	.	.	Note=Loss of stability. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12566426;Dbxref=PMID:12566426	
+P32266	UniProtKB	Mutagenesis	224	224	.	.	.	Note=Loss of GTPase activity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10037792,ECO:0000269|PubMed:12566426;Dbxref=PMID:10037792,PMID:12566426	
+P32266	UniProtKB	Mutagenesis	224	224	.	.	.	Note=Loss of GTPase activity. S->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10037792,ECO:0000269|PubMed:12566426;Dbxref=PMID:10037792,PMID:12566426	
+P32266	UniProtKB	Mutagenesis	244	244	.	.	.	Note=Loss of GTPase activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12566426;Dbxref=PMID:12566426	
+P32266	UniProtKB	Mutagenesis	294	294	.	.	.	Note=In mdm17%3B loss of function at 37 degrees Celsius. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10037792;Dbxref=PMID:10037792	
+P32266	UniProtKB	Mutagenesis	824	824	.	.	.	Note=Loss of GED function. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12566426;Dbxref=PMID:12566426	
+P32266	UniProtKB	Mutagenesis	854	854	.	.	.	Note=Loss of GED function. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12566426;Dbxref=PMID:12566426	
+P32266	UniProtKB	Sequence conflict	4	4	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32266	UniProtKB	Sequence conflict	129	129	.	.	.	Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32266	UniProtKB	Sequence conflict	170	170	.	.	.	Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P26188 1 188
+P26188	UniProtKB	Chain	1	188	.	.	.	ID=PRO_0000139362;Note=Methylated-DNA--protein-cysteine methyltransferase	
+P26188	UniProtKB	Active site	151	151	.	.	.	Note=Nucleophile%3B methyl group acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10017	
+P26188	UniProtKB	Binding site	120	120	.	.	.	Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26188	UniProtKB	Binding site	121	121	.	.	.	Note=DNA%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26188	UniProtKB	Binding site	134	134	.	.	.	Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26188	UniProtKB	Binding site	157	157	.	.	.	Note=DNA%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04472 1 501
+Q04472	UniProtKB	Chain	1	501	.	.	.	ID=PRO_0000203293;Note=Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR3	
+Q04472	UniProtKB	Topological domain	1	77	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18843051;Dbxref=PMID:18843051	
+Q04472	UniProtKB	Transmembrane	78	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04472	UniProtKB	Topological domain	96	501	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18843051;Dbxref=PMID:18843051	
+Q04472	UniProtKB	Repeat	109	144	.	.	.	Note=TPR 1	
+Q04472	UniProtKB	Repeat	154	187	.	.	.	Note=TPR 2	
+Q04472	UniProtKB	Repeat	386	420	.	.	.	Note=TPR 3	
+Q04472	UniProtKB	Repeat	440	473	.	.	.	Note=TPR 4	
+##sequence-region P36046 1 403
+P36046	UniProtKB	Transit peptide	1	31	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15620710;Dbxref=PMID:15620710	
+P36046	UniProtKB	Chain	32	403	.	.	.	ID=PRO_0000203135;Note=Mitochondrial intermembrane space import and assembly protein 40	
+P36046	UniProtKB	Topological domain	33	46	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36046	UniProtKB	Transmembrane	47	66	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36046	UniProtKB	Topological domain	67	403	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36046	UniProtKB	Domain	304	348	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+P36046	UniProtKB	Motif	307	317	.	.	.	Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+P36046	UniProtKB	Motif	330	340	.	.	.	Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+P36046	UniProtKB	Disulfide bond	296	298	.	.	.	Note=Redox-active;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19667201;Dbxref=PMID:19667201	
+P36046	UniProtKB	Disulfide bond	307	340	.	.	.	Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000269|PubMed:19667201;Dbxref=PMID:19667201	
+P36046	UniProtKB	Disulfide bond	317	330	.	.	.	Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000269|PubMed:19667201;Dbxref=PMID:19667201	
+P36046	UniProtKB	Mutagenesis	296	296	.	.	.	Note=Loss of function%3B when associated with S-298. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15364952,ECO:0000269|PubMed:15620710;Dbxref=PMID:15364952,PMID:15620710	
+P36046	UniProtKB	Mutagenesis	298	298	.	.	.	Note=Loss of function%3B when associated with S-296. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15364952,ECO:0000269|PubMed:15620710;Dbxref=PMID:15364952,PMID:15620710	
+P36046	UniProtKB	Mutagenesis	307	307	.	.	.	Note=Loss of function%3B when associated with S-317. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15364952,ECO:0000269|PubMed:15620710;Dbxref=PMID:15364952,PMID:15620710	
+P36046	UniProtKB	Mutagenesis	317	317	.	.	.	Note=Loss of function%3B when associated with S-307. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15364952;Dbxref=PMID:15364952	
+P36046	UniProtKB	Mutagenesis	330	330	.	.	.	Note=Loss of function%3B when associated with S-340. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15364952;Dbxref=PMID:15364952	
+P36046	UniProtKB	Mutagenesis	340	340	.	.	.	Note=Loss of function%3B when associated with S-330. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15364952;Dbxref=PMID:15364952	
+P36046	UniProtKB	Helix	282	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C	
+P36046	UniProtKB	Turn	287	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C	
+P36046	UniProtKB	Helix	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C	
+P36046	UniProtKB	Turn	300	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C	
+P36046	UniProtKB	Helix	308	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C	
+P36046	UniProtKB	Beta strand	323	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C	
+P36046	UniProtKB	Turn	326	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C	
+P36046	UniProtKB	Helix	331	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C	
+P36046	UniProtKB	Turn	345	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C	
+##sequence-region P50945 1 234
+P50945	UniProtKB	Chain	1	234	.	.	.	ID=PRO_0000203438;Note=MICOS complex subunit MIC27	
+P50945	UniProtKB	Topological domain	1	100	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50945	UniProtKB	Transmembrane	101	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50945	UniProtKB	Topological domain	121	141	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50945	UniProtKB	Transmembrane	142	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50945	UniProtKB	Topological domain	162	234	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39943 1 394
+P39943	UniProtKB	Chain	1	394	.	.	.	ID=PRO_0000046886;Note=Transcription corepressor MIG3	
+P39943	UniProtKB	Zinc finger	17	39	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39943	UniProtKB	Zinc finger	45	69	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39943	UniProtKB	Compositional bias	163	296	.	.	.	Note=Ser-rich	
+##sequence-region Q08176 1 113
+Q08176	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000218767;Note=Mitochondrial import protein 1	
+Q08176	UniProtKB	Transmembrane	39	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04341 1 121
+Q04341	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000242621;Note=Mitochondrial intermembrane space cysteine motif-containing protein MIX14	
+Q04341	UniProtKB	Domain	14	56	.	.	.	Note=CHCH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q04341	UniProtKB	Domain	60	105	.	.	.	Note=CHCH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q04341	UniProtKB	Motif	17	27	.	.	.	Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q04341	UniProtKB	Motif	38	48	.	.	.	Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q04341	UniProtKB	Motif	63	73	.	.	.	Note=Cx9C motif 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q04341	UniProtKB	Motif	87	97	.	.	.	Note=Cx9C motif 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q04341	UniProtKB	Disulfide bond	17	48	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q04341	UniProtKB	Disulfide bond	27	38	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q04341	UniProtKB	Disulfide bond	63	97	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q04341	UniProtKB	Disulfide bond	73	87	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+##sequence-region P38920 1 769
+P38920	UniProtKB	Chain	1	769	.	.	.	ID=PRO_0000178008;Note=DNA mismatch repair protein MLH1	
+P38920	UniProtKB	Region	1	335	.	.	.	Note=DNA- and ATP-binding	
+P38920	UniProtKB	Region	501	756	.	.	.	Note=Interaction with PMS1	
+P38920	UniProtKB	Modified residue	441	441	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38920	UniProtKB	Natural variant	240	240	.	.	.	Note=In strain: SK1. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	242	242	.	.	.	Note=In strain: YJM326 and YJM339. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	271	271	.	.	.	Note=In strain: EAY1066%2C EAY1068%2C M2-8%2C M7-8%2C M5-7%2C SK1%2C YJM269%2C YJM280%2C YJM320%2C YJM326%2C YJM339 and YJM627. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	309	309	.	.	.	Note=In strain: M2-8. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	321	321	.	.	.	Note=In strain: EAY1066. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	333	333	.	.	.	Note=In strain: SK1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	375	375	.	.	.	Note=In strain: YJM339. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	452	452	.	.	.	Note=In strain: EAY1068%2C M2-8%2C M7-8%2C M5-7%2C YJM269 and YJM627. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	465	465	.	.	.	Note=In strain: EAY1066 and YJM280. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	470	470	.	.	.	Note=In strain: YJM339. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	607	607	.	.	.	Note=In strain: EAY1068%2C M2-8%2C M7-8%2C M5-7 and YJM627. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	678	678	.	.	.	Note=In strain: SK1%2C YJM320 and YJM339. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	703	703	.	.	.	Note=In strain: SK1%2C YJM320 and YJM339. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Natural variant	761	761	.	.	.	Note=In strain: EAY1066%2C EAY1068%2C M2-8%2C M7-8%2C M5-7%2C SK1%2C YJM145%2C YJM269%2C YJM320%2C YJM339 and YJM627%3B forms a non-functional heterodimer with PMS1 from strain S288c%2C resulting in an accumulation of mutations in spore progeny of crosses between these strains. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P38920	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Reduces ATPase activity by 98%25. Displays 3300-fold increase in spontaneous mutation accumulation. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10938116,ECO:0000269|PubMed:11717305;Dbxref=PMID:10938116,PMID:11717305	
+P38920	UniProtKB	Mutagenesis	35	35	.	.	.	Note=Abolishes ATP binding%2C reducing ATPase activity by 95%25. Displays 9800-fold increase in spontaneous mutation accumulation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11717305;Dbxref=PMID:11717305	
+P38920	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Defective in a mismatch repair assay. Abolishes heterodimer formation. Displays an increases spontaneous mutation accumulation. A->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11555625,ECO:0000269|PubMed:9234704;Dbxref=PMID:11555625,PMID:9234704	
+P38920	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Reduces heterodimer formation. Displays an weak increase in spontaneous mutation accumulation. A->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11555625,ECO:0000269|PubMed:9234704;Dbxref=PMID:11555625,PMID:9234704	
+P38920	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Fully functional in a mismatch repair assay. A->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11555625,ECO:0000269|PubMed:9234704;Dbxref=PMID:11555625,PMID:9234704	
+P38920	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Defective in a mismatch repair assay. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Defective in a mismatch repair assay. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	96	96	.	.	.	Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704	
+P38920	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704	
+P38920	UniProtKB	Mutagenesis	98	98	.	.	.	Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10938116,ECO:0000269|PubMed:9234704;Dbxref=PMID:10938116,PMID:9234704	
+P38920	UniProtKB	Mutagenesis	98	98	.	.	.	Note=Abolishes heterodimer formation. Displays an increase in spontaneous mutation accumulation. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10938116,ECO:0000269|PubMed:9234704;Dbxref=PMID:10938116,PMID:9234704	
+P38920	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Defective in a mismatch repair assay. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Defective in a mismatch repair assay. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Defective in a mismatch repair assay. T->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	214	214	.	.	.	Note=Partially defective in a mismatch repair assay. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Fully functional in a mismatch repair assay. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	265	265	.	.	.	Note=Partially defective in a mismatch repair assay. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	265	265	.	.	.	Note=Partially defective in a mismatch repair assay. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	273	273	.	.	.	Note=Strongly reduces DNA-binding and displays 12000-fold increase in spontaneous mutation accumulation%3B when associated with E-274. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12682353;Dbxref=PMID:12682353	
+P38920	UniProtKB	Mutagenesis	274	274	.	.	.	Note=Reduces DNA-binding and displays a 1700-fold increase in spontaneous mutation accumulation. Strongly reduces DNA-binding and displays 12000-fold increase in spontaneous mutation accumulation%3B when associated with E-273. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12682353;Dbxref=PMID:12682353	
+P38920	UniProtKB	Mutagenesis	326	326	.	.	.	Note=Partially defective in a mismatch repair assay. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	326	326	.	.	.	Note=Fully functional in a mismatch repair assay. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	552	552	.	.	.	Note=Defective in a mismatch repair assay. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	672	672	.	.	.	Note=Defective in a mismatch repair assay. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	694	694	.	.	.	Note=Fully functional in a mismatch repair assay. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P38920	UniProtKB	Mutagenesis	764	764	.	.	.	Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704	
+P38920	UniProtKB	Mutagenesis	764	764	.	.	.	Note=No effect. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704	
+P38920	UniProtKB	Mutagenesis	766	766	.	.	.	Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704	
+P38920	UniProtKB	Mutagenesis	767	767	.	.	.	Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704	
+P38920	UniProtKB	Mutagenesis	769	769	.	.	.	Note=No effect. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704	
+P38920	UniProtKB	Mutagenesis	769	769	.	.	.	Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704	
+P38920	UniProtKB	Sequence conflict	258	258	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38920	UniProtKB	Sequence conflict	288	288	.	.	.	Note=N->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38920	UniProtKB	Sequence conflict	708	708	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38920	UniProtKB	Helix	512	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	527	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Beta strand	537	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Turn	544	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Beta strand	548	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Beta strand	556	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	562	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Beta strand	582	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	591	593	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	597	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	610	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	624	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Beta strand	634	639	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	644	646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Beta strand	647	654	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	666	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	682	697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	714	733	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	735	742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	747	752	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Beta strand	753	758	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P38920	UniProtKB	Helix	759	765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+##sequence-region P40457 1 1679
+P40457	UniProtKB	Chain	1	1679	.	.	.	ID=PRO_0000096502;Note=Protein MLP2	
+P40457	UniProtKB	Coiled coil	32	176	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40457	UniProtKB	Coiled coil	233	466	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40457	UniProtKB	Coiled coil	516	1064	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40457	UniProtKB	Coiled coil	1099	1491	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40457	UniProtKB	Motif	417	433	.	.	.	Note=Bipartite nuclear localization signal 1	
+P40457	UniProtKB	Motif	639	655	.	.	.	Note=Bipartite nuclear localization signal 2	
+P40457	UniProtKB	Motif	1433	1449	.	.	.	Note=Bipartite nuclear localization signal 3	
+P40457	UniProtKB	Compositional bias	467	470	.	.	.	Note=Poly-Leu	
+P40457	UniProtKB	Compositional bias	1393	1508	.	.	.	Note=Glu-rich	
+P40457	UniProtKB	Modified residue	1512	1512	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40457	UniProtKB	Modified residue	1670	1670	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53102 1 219
+P53102	UniProtKB	Chain	1	219	.	.	.	ID=PRO_0000096522;Note=Meiotic nuclear division protein 1	
+P53102	UniProtKB	Coiled coil	88	181	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P24720 1 663
+P24720	UniProtKB	Chain	1	663	.	.	.	ID=PRO_0000096524;Note=Protein MNE1	
+##sequence-region P18408 1 261
+P18408	UniProtKB	Chain	1	261	.	.	.	ID=PRO_0000100662;Note=Phosphoadenosine phosphosulfate reductase	
+P18408	UniProtKB	Sequence conflict	242	261	.	.	.	Note=KTECGIHEASRFAQFLKQDA->RPSVEFMKPADSRNF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18408	UniProtKB	Beta strand	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Beta strand	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	14	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	30	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Beta strand	42	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	52	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Turn	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Beta strand	72	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	83	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Beta strand	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	115	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	126	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	131	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	140	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Beta strand	153	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	165	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Beta strand	172	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Turn	177	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Beta strand	181	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Turn	186	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	192	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	208	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Turn	232	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Turn	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+P18408	UniProtKB	Helix	251	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2	
+##sequence-region Q07684 1 458
+Q07684	UniProtKB	Chain	1	458	.	.	.	ID=PRO_0000242483;Note=Morphogenetic regulator of filamentous growth protein 1	
+Q07684	UniProtKB	Compositional bias	5	64	.	.	.	Note=Pro-rich	
+##sequence-region P53152 1 137
+P53152	UniProtKB	Chain	1	137	.	.	.	ID=PRO_0000082598;Note=Ubiquitin-conjugating enzyme variant MMS2	
+P53152	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53152	UniProtKB	Mutagenesis	8	8	.	.	.	Note=Strongly reduces UBC13 binding and interferes with error-free DNA repair. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11440714;Dbxref=PMID:11440714	
+P53152	UniProtKB	Helix	6	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P53152	UniProtKB	Beta strand	26	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P53152	UniProtKB	Beta strand	40	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P53152	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P53152	UniProtKB	Turn	52	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P53152	UniProtKB	Beta strand	57	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P53152	UniProtKB	Turn	66	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P53152	UniProtKB	Beta strand	74	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P53152	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GMI	
+P53152	UniProtKB	Turn	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P53152	UniProtKB	Helix	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P53152	UniProtKB	Helix	109	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+P53152	UniProtKB	Helix	123	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT	
+##sequence-region P38888 1 796
+P38888	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38888	UniProtKB	Chain	21	796	.	.	.	ID=PRO_0000210324;Note=ER degradation-enhancing alpha-mannosidase-like protein 1	
+P38888	UniProtKB	Active site	372	372	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31723	
+P38888	UniProtKB	Metal binding	495	495	.	.	.	Note=Calcium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32906	
+P38888	UniProtKB	Glycosylation	86	86	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38888	UniProtKB	Glycosylation	517	517	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38888	UniProtKB	Glycosylation	672	672	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38888	UniProtKB	Glycosylation	762	762	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P41821 1 548
+P41821	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Chain	21	548	.	.	.	ID=PRO_0000096483;Note=Stretch-activated cation channel MID1	
+P41821	UniProtKB	Topological domain	21	341	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Transmembrane	342	358	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Topological domain	359	548	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Compositional bias	431	450	.	.	.	Note=Cys-rich	
+P41821	UniProtKB	Compositional bias	487	506	.	.	.	Note=Cys-rich	
+P41821	UniProtKB	Glycosylation	32	32	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	70	70	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	112	112	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	125	125	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	159	159	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	175	175	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	238	238	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	265	265	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	282	282	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	285	285	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	291	291	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Glycosylation	324	324	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41821	UniProtKB	Mutagenesis	356	356	.	.	.	Note=Significantly low viability and relatively normal Ca(2+) accumulation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14697255;Dbxref=PMID:14697255	
+P41821	UniProtKB	Mutagenesis	356	356	.	.	.	Note=Substitution by hydrophilic amino acids causes lethality and low Ca(2+) accumulation. F->H%2CQ%2CD%2CE%2CK%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14697255;Dbxref=PMID:14697255	
+P41821	UniProtKB	Mutagenesis	356	356	.	.	.	Note=Substitution by hydrophobic%2C large amino acids does not cause lethality nor low Ca(2+) accumulation. F->L%2CW%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14697255;Dbxref=PMID:14697255	
+P41821	UniProtKB	Mutagenesis	417	417	.	.	.	Note=Non-functional. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727	
+P41821	UniProtKB	Mutagenesis	431	431	.	.	.	Note=Non-functional. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727	
+P41821	UniProtKB	Mutagenesis	434	434	.	.	.	Note=Non-functional. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727	
+P41821	UniProtKB	Mutagenesis	491	491	.	.	.	Note=Functionally impaired. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727	
+P41821	UniProtKB	Mutagenesis	498	498	.	.	.	Note=Non-functional. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727	
+P41821	UniProtKB	Mutagenesis	506	506	.	.	.	Note=Functionally impaired. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727	
+P41821	UniProtKB	Mutagenesis	531	531	.	.	.	Note=Functionally impaired. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727	
+##sequence-region P53035 1 382
+P53035	UniProtKB	Chain	1	382	.	.	.	ID=PRO_0000046882;Note=Regulatory protein MIG2	
+P53035	UniProtKB	Zinc finger	17	39	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P53035	UniProtKB	Zinc finger	45	69	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+##sequence-region P32491 1 506
+P32491	UniProtKB	Chain	1	506	.	.	.	ID=PRO_0000086333;Note=MAP kinase kinase MKK2/SSP33	
+P32491	UniProtKB	Domain	214	481	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32491	UniProtKB	Nucleotide binding	220	228	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32491	UniProtKB	Active site	342	342	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P32491	UniProtKB	Binding site	243	243	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32491	UniProtKB	Sequence conflict	252	252	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P34072 1 584
+P34072	UniProtKB	Chain	1	584	.	.	.	ID=PRO_0000096494;Note=Negative regulator of RAS-cAMP pathway	
+P34072	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34072	UniProtKB	Modified residue	247	247	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P34072	UniProtKB	Modified residue	276	276	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34072	UniProtKB	Modified residue	442	442	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P34072	UniProtKB	Modified residue	518	518	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06580 1 163
+Q06580	UniProtKB	Chain	1	163	.	.	.	ID=PRO_0000198766;Note=Myosin light chain 2	
+Q06580	UniProtKB	Domain	15	50	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+Q06580	UniProtKB	Domain	92	127	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+Q06580	UniProtKB	Calcium binding	28	39	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+##sequence-region P32047 1 452
+P32047	UniProtKB	Chain	1	452	.	.	.	ID=PRO_0000096499;Note=Protein MLF3	
+P32047	UniProtKB	Compositional bias	211	214	.	.	.	Note=Poly-Thr	
+P32047	UniProtKB	Compositional bias	271	274	.	.	.	Note=Poly-Ser	
+P32047	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P32047	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32047	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32047	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32047	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32047	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	145	145	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	156	156	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	169	169	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	171	171	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P32047	UniProtKB	Modified residue	173	173	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32047	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32047	UniProtKB	Modified residue	228	228	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	295	295	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32047	UniProtKB	Modified residue	297	297	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32047	UniProtKB	Modified residue	320	320	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	353	353	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32047	UniProtKB	Modified residue	439	439	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q12372 1 583
+Q12372	UniProtKB	Chain	1	583	.	.	.	ID=PRO_0000054157;Note=S-methylmethionine permease 1	
+Q12372	UniProtKB	Topological domain	1	77	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	78	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	97	101	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	102	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	124	143	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	144	164	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	165	182	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	204	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	237	254	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	255	274	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	275	298	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	299	319	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	320	356	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	357	377	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	378	402	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	403	423	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	424	428	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	429	449	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	450	473	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	474	494	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	495	505	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Transmembrane	506	526	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Topological domain	527	583	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12372	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08986	
+Q12372	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12372	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q06324 1 491
+Q06324	UniProtKB	Chain	1	491	.	.	.	ID=PRO_0000245841;Note=Mitochondrial MYO2 receptor-related protein 1	
+Q06324	UniProtKB	Region	300	439	.	.	.	Note=Interaction with MYO2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201867;Dbxref=PMID:15201867	
+Q06324	UniProtKB	Coiled coil	295	384	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06324	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06324	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06324	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P46982 1 586
+P46982	UniProtKB	Signal peptide	1	29	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46982	UniProtKB	Chain	30	586	.	.	.	ID=PRO_0000203019;Note=Alpha-1%2C2-mannosyltransferase MNN5	
+P46982	UniProtKB	Glycosylation	113	113	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46982	UniProtKB	Glycosylation	136	136	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46982	UniProtKB	Glycosylation	259	259	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46982	UniProtKB	Glycosylation	264	264	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46982	UniProtKB	Sequence conflict	395	395	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39107 1 395
+P39107	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9434768;Dbxref=PMID:9434768	
+P39107	UniProtKB	Chain	2	395	.	.	.	ID=PRO_0000193670;Note=Mannan polymerase complexes subunit MNN9	
+P39107	UniProtKB	Topological domain	2	17	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39107	UniProtKB	Transmembrane	18	33	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39107	UniProtKB	Topological domain	34	395	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39107	UniProtKB	Mutagenesis	236	236	.	.	.	Note=Reduced activity of the M-Pol I complex. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12235155;Dbxref=PMID:12235155	
+P39107	UniProtKB	Helix	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Turn	108	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Beta strand	116	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Helix	128	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Helix	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Beta strand	144	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Helix	154	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Helix	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Beta strand	180	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Helix	204	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Beta strand	229	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Helix	246	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Beta strand	256	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Turn	269	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Beta strand	273	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Helix	288	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Turn	308	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Helix	317	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Beta strand	331	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Beta strand	338	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Helix	345	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Helix	364	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+P39107	UniProtKB	Beta strand	379	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8	
+##sequence-region P40549 1 630
+P40549	UniProtKB	Chain	1	630	.	.	.	ID=PRO_0000080560;Note=Alpha-1%2C3-mannosyltransferase MNT3	
+P40549	UniProtKB	Topological domain	1	14	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40549	UniProtKB	Transmembrane	15	31	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40549	UniProtKB	Topological domain	32	630	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40549	UniProtKB	Glycosylation	34	34	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40549	UniProtKB	Glycosylation	168	168	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53745 1 580
+P53745	UniProtKB	Chain	1	580	.	.	.	ID=PRO_0000080561;Note=Probable alpha-1%2C3-mannosyltransferase MNT4	
+P53745	UniProtKB	Topological domain	1	10	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53745	UniProtKB	Transmembrane	11	29	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53745	UniProtKB	Topological domain	30	580	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53745	UniProtKB	Glycosylation	132	132	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53745	UniProtKB	Glycosylation	167	167	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53745	UniProtKB	Glycosylation	223	223	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53745	UniProtKB	Glycosylation	349	349	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53745	UniProtKB	Sequence conflict	50	50	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53745	UniProtKB	Sequence conflict	87	87	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53745	UniProtKB	Sequence conflict	134	134	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53745	UniProtKB	Sequence conflict	206	206	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53745	UniProtKB	Sequence conflict	254	267	.	.	.	Note=LNYPPQELWFLDVK->PGTELELRPQFTG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43563 1 287
+P43563	UniProtKB	Chain	1	287	.	.	.	ID=PRO_0000193583;Note=CBK1 kinase activator protein MOB2	
+P43563	UniProtKB	Modified residue	33	33	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43563	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43563	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43563	UniProtKB	Turn	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P43563	UniProtKB	Helix	122	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P43563	UniProtKB	Helix	183	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P43563	UniProtKB	Turn	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P43563	UniProtKB	Helix	211	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P43563	UniProtKB	Helix	234	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P43563	UniProtKB	Helix	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P43563	UniProtKB	Helix	243	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P43563	UniProtKB	Turn	265	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+P43563	UniProtKB	Helix	272	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS	
+##sequence-region P23641 1 311
+P23641	UniProtKB	Chain	1	311	.	.	.	ID=PRO_0000090635;Note=Mitochondrial phosphate carrier protein	
+P23641	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed%3B alternate;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P23641	UniProtKB	Chain	2	311	.	.	.	ID=PRO_0000423225;Note=Mitochondrial phosphate carrier protein%2C N-terminally processed	
+P23641	UniProtKB	Topological domain	1	19	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Topological domain	41	62	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Topological domain	84	115	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Topological domain	137	165	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Transmembrane	166	186	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Topological domain	187	214	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Transmembrane	215	235	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Topological domain	236	253	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Transmembrane	254	274	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Topological domain	275	311	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23641	UniProtKB	Repeat	15	100	.	.	.	Note=Solcar 1	
+P23641	UniProtKB	Repeat	114	197	.	.	.	Note=Solcar 2	
+P23641	UniProtKB	Repeat	212	297	.	.	.	Note=Solcar 3	
+P23641	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine%3B in Mitochondrial phosphate carrier protein%2C N-terminally processed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P23641	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P23641	UniProtKB	Modified residue	145	145	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P23641	UniProtKB	Sequence conflict	2	2	.	.	.	Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47083 1 593
+P47083	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P47083	UniProtKB	Chain	2	593	.	.	.	ID=PRO_0000121534;Note=U3 small nucleolar RNA-associated protein MPP10	
+P47083	UniProtKB	Compositional bias	226	229	.	.	.	Note=Poly-Glu	
+P47083	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P47083	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47083	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47083	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q03667 1 156
+Q03667	UniProtKB	Transit peptide	1	21	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03667	UniProtKB	Chain	22	156	.	.	.	ID=PRO_0000203267;Note=Mitochondrial intermembrane space cysteine motif-containing protein MIX17	
+Q03667	UniProtKB	Domain	115	156	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q03667	UniProtKB	Motif	118	128	.	.	.	Note=Cx9C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q03667	UniProtKB	Compositional bias	32	36	.	.	.	Note=Poly-Gln	
+Q03667	UniProtKB	Compositional bias	96	99	.	.	.	Note=Poly-Gln	
+Q03667	UniProtKB	Disulfide bond	118	149	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03667	UniProtKB	Disulfide bond	128	139	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38162 1 196
+P38162	UniProtKB	Chain	1	196	.	.	.	ID=PRO_0000202439;Note=Mitochondrial intermembrane space cysteine motif-containing protein MIX23	
+P38162	UniProtKB	Motif	99	114	.	.	.	Note=Cx14C motif	
+P38162	UniProtKB	Motif	178	192	.	.	.	Note=Cx13C motif	
+##sequence-region Q06211 1 1407
+Q06211	UniProtKB	Chain	1	1407	.	.	.	ID=PRO_0000257820;Note=E3 ubiquitin-protein ligase linker protein MMS1	
+Q06211	UniProtKB	Region	1	600	.	.	.	Note=Required for interaction with MMS22	
+Q06211	UniProtKB	Modified residue	1294	1294	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region Q12205 1 849
+Q12205	UniProtKB	Chain	1	849	.	.	.	ID=PRO_0000247229;Note=Putative endoplasmic reticulum mannosidase MNL2	
+Q12205	UniProtKB	Topological domain	1	12	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12205	UniProtKB	Transmembrane	13	32	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12205	UniProtKB	Topological domain	33	849	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12205	UniProtKB	Glycosylation	45	45	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12205	UniProtKB	Disulfide bond	559	598	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32906	
+##sequence-region P46985 1 422
+P46985	UniProtKB	Chain	1	422	.	.	.	ID=PRO_0000215165;Note=Probable alpha-1%2C6-mannosyltransferase MNN11	
+P46985	UniProtKB	Topological domain	1	31	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46985	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46985	UniProtKB	Topological domain	53	422	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46985	UniProtKB	Sequence conflict	298	298	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38069 1 597
+P38069	UniProtKB	Chain	1	597	.	.	.	ID=PRO_0000065676;Note=Alpha-1%2C2-mannosyltransferase MNN2	
+P38069	UniProtKB	Topological domain	1	12	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38069	UniProtKB	Transmembrane	13	28	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38069	UniProtKB	Topological domain	29	597	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38069	UniProtKB	Glycosylation	34	34	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38069	UniProtKB	Glycosylation	363	363	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38069	UniProtKB	Glycosylation	473	473	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38069	UniProtKB	Sequence conflict	287	287	.	.	.	Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53129 1 644
+P53129	UniProtKB	Chain	1	644	.	.	.	ID=PRO_0000202744;Note=Vacuolar fusion protein MON1	
+P53129	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53129	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53129	UniProtKB	Sequence conflict	113	113	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53129	UniProtKB	Sequence conflict	113	113	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53311 1 146
+P53311	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53311	UniProtKB	Chain	21	146	.	.	.	ID=PRO_0000212800;Note=Mitochondrial pyruvate carrier 3	
+P53311	UniProtKB	Transmembrane	23	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53311	UniProtKB	Transmembrane	55	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53311	UniProtKB	Transmembrane	78	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CD99 1 609
+P0CD99	UniProtKB	Chain	1	609	.	.	.	ID=PRO_0000050424;Note=Alpha-glucosides permease MPH2	
+P0CD99	UniProtKB	Topological domain	1	106	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	107	127	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	128	142	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	143	163	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	164	178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	200	200	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	201	221	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	222	234	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	235	255	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	256	270	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	271	291	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	292	363	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	364	384	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	385	397	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	398	418	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	419	426	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	427	447	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	448	459	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	460	480	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	481	492	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	493	513	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	514	525	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CD99	UniProtKB	Transmembrane	526	546	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CD99	UniProtKB	Topological domain	547	609	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P23748 1 554
+P23748	UniProtKB	Chain	1	554	.	.	.	ID=PRO_0000198662;Note=M-phase inducer phosphatase	
+P23748	UniProtKB	Domain	261	373	.	.	.	Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+P23748	UniProtKB	Active site	320	320	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23748	UniProtKB	Sequence conflict	238	239	.	.	.	Note=ND->MT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23748	UniProtKB	Sequence conflict	241	248	.	.	.	Note=FPRISPET->SLEFLQKR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23748	UniProtKB	Sequence conflict	365	367	.	.	.	Note=FDN->LT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23748	UniProtKB	Sequence conflict	475	554	.	.	.	Note=ILSKSSMSSNSNLSTSHMLLMDGLDTPSYFSFEDERGNHQQVSGDEEQDGDFTFVGSDREDLPRPARRSLFPSLETEDKK->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53379 1 596
+P53379	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Propeptide	23	65	.	.	.	ID=PRO_0000025835;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Chain	66	575	.	.	.	ID=PRO_0000025836;Note=Aspartic proteinase MKC7	
+P53379	UniProtKB	Propeptide	576	596	.	.	.	ID=PRO_0000025837;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Domain	81	468	.	.	.	Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
+P53379	UniProtKB	Compositional bias	532	536	.	.	.	Note=Poly-Ser	
+P53379	UniProtKB	Compositional bias	567	570	.	.	.	Note=Poly-Ser	
+P53379	UniProtKB	Active site	99	99	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P53379	UniProtKB	Active site	360	360	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+P53379	UniProtKB	Lipidation	575	575	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Glycosylation	180	180	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Glycosylation	190	190	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Glycosylation	219	219	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Glycosylation	229	229	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Glycosylation	232	232	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Glycosylation	286	286	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Glycosylation	346	346	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Glycosylation	471	471	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Glycosylation	517	517	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53379	UniProtKB	Sequence conflict	546	546	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53379	UniProtKB	Sequence conflict	571	571	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06164 1 1454
+Q06164	UniProtKB	Chain	1	1454	.	.	.	ID=PRO_0000257821;Note=E3 ubiquitin-protein ligase substrate receptor MMS22	
+Q06164	UniProtKB	Region	1201	1454	.	.	.	Note=Required for interaction with MMS1	
+##sequence-region P40577 1 368
+P40577	UniProtKB	Chain	1	368	.	.	.	ID=PRO_0000096523;Note=Anaphase-promoting complex subunit MND2	
+P40577	UniProtKB	Modified residue	293	293	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P39106 1 762
+P39106	UniProtKB	Chain	1	762	.	.	.	ID=PRO_0000080558;Note=Alpha-1%2C3-mannosyltransferase MNN1	
+P39106	UniProtKB	Topological domain	1	16	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39106	UniProtKB	Transmembrane	17	33	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39106	UniProtKB	Topological domain	34	762	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39106	UniProtKB	Glycosylation	50	50	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39106	UniProtKB	Glycosylation	225	225	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39106	UniProtKB	Glycosylation	254	254	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39106	UniProtKB	Glycosylation	383	383	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39106	UniProtKB	Sequence conflict	338	338	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36044 1 1178
+P36044	UniProtKB	Chain	1	1178	.	.	.	ID=PRO_0000096525;Note=Protein MNN4	
+P36044	UniProtKB	Topological domain	1	27	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36044	UniProtKB	Transmembrane	28	48	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36044	UniProtKB	Topological domain	49	1178	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36044	UniProtKB	Repeat	1042	1049	.	.	.	Note=1	
+P36044	UniProtKB	Repeat	1050	1057	.	.	.	Note=2	
+P36044	UniProtKB	Repeat	1058	1065	.	.	.	Note=3	
+P36044	UniProtKB	Repeat	1066	1073	.	.	.	Note=4	
+P36044	UniProtKB	Repeat	1074	1081	.	.	.	Note=5	
+P36044	UniProtKB	Repeat	1082	1089	.	.	.	Note=6	
+P36044	UniProtKB	Repeat	1090	1097	.	.	.	Note=7%3B approximate	
+P36044	UniProtKB	Repeat	1098	1105	.	.	.	Note=8	
+P36044	UniProtKB	Repeat	1106	1113	.	.	.	Note=9%3B approximate	
+P36044	UniProtKB	Repeat	1114	1121	.	.	.	Note=10%3B approximate	
+P36044	UniProtKB	Repeat	1122	1129	.	.	.	Note=11%3B approximate	
+P36044	UniProtKB	Repeat	1130	1137	.	.	.	Note=12	
+P36044	UniProtKB	Repeat	1138	1144	.	.	.	Note=13%3B approximate	
+P36044	UniProtKB	Repeat	1145	1152	.	.	.	Note=14%3B approximate	
+P36044	UniProtKB	Repeat	1153	1160	.	.	.	Note=15%3B approximate	
+P36044	UniProtKB	Repeat	1161	1168	.	.	.	Note=16%3B approximate	
+P36044	UniProtKB	Repeat	1169	1174	.	.	.	Note=17%3B truncated	
+P36044	UniProtKB	Region	1042	1174	.	.	.	Note=17 X 8 AA tandem repeats of K-K-K-K-E-E-E-E	
+P36044	UniProtKB	Compositional bias	37	40	.	.	.	Note=Poly-Ile	
+P36044	UniProtKB	Compositional bias	1032	1174	.	.	.	Note=Arg/Glu/Lys-rich (highly charged)	
+P36044	UniProtKB	Compositional bias	1042	1045	.	.	.	Note=Poly-Lys	
+P36044	UniProtKB	Compositional bias	1046	1049	.	.	.	Note=Poly-Glu	
+P36044	UniProtKB	Compositional bias	1050	1053	.	.	.	Note=Poly-Lys	
+P36044	UniProtKB	Compositional bias	1054	1057	.	.	.	Note=Poly-Glu	
+P36044	UniProtKB	Compositional bias	1058	1061	.	.	.	Note=Poly-Lys	
+P36044	UniProtKB	Compositional bias	1062	1065	.	.	.	Note=Poly-Glu	
+P36044	UniProtKB	Compositional bias	1066	1069	.	.	.	Note=Poly-Lys	
+P36044	UniProtKB	Compositional bias	1070	1073	.	.	.	Note=Poly-Glu	
+P36044	UniProtKB	Compositional bias	1074	1077	.	.	.	Note=Poly-Lys	
+P36044	UniProtKB	Compositional bias	1078	1081	.	.	.	Note=Poly-Glu	
+P36044	UniProtKB	Compositional bias	1082	1085	.	.	.	Note=Poly-Lys	
+P36044	UniProtKB	Compositional bias	1086	1089	.	.	.	Note=Poly-Glu	
+P36044	UniProtKB	Compositional bias	1094	1097	.	.	.	Note=Poly-Glu	
+P36044	UniProtKB	Compositional bias	1098	1101	.	.	.	Note=Poly-Lys	
+P36044	UniProtKB	Compositional bias	1102	1105	.	.	.	Note=Poly-Glu	
+P36044	UniProtKB	Compositional bias	1134	1137	.	.	.	Note=Poly-Glu	
+P36044	UniProtKB	Compositional bias	1157	1160	.	.	.	Note=Poly-Glu	
+P36044	UniProtKB	Compositional bias	1165	1168	.	.	.	Note=Poly-Glu	
+##sequence-region P35724 1 969
+P35724	UniProtKB	Chain	1	969	.	.	.	ID=PRO_0000201537;Note=Manganese resistance protein MNR2	
+P35724	UniProtKB	Topological domain	1	912	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35724	UniProtKB	Transmembrane	913	933	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35724	UniProtKB	Topological domain	934	941	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35724	UniProtKB	Transmembrane	942	962	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35724	UniProtKB	Topological domain	963	969	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35724	UniProtKB	Modified residue	114	114	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P35724	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P35724	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35724	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35724	UniProtKB	Modified residue	383	383	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35724	UniProtKB	Modified residue	571	571	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P35724	UniProtKB	Modified residue	576	576	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P35724	UniProtKB	Modified residue	582	582	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53059 1 558
+P53059	UniProtKB	Chain	1	558	.	.	.	ID=PRO_0000080559;Note=Alpha-1%2C3-mannosyltransferase MNT2	
+P53059	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53059	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53059	UniProtKB	Topological domain	28	558	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53059	UniProtKB	Glycosylation	187	187	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53157 1 130
+P53157	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000212805;Note=Mitochondrial pyruvate carrier 1	
+P53157	UniProtKB	Transmembrane	23	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53157	UniProtKB	Transmembrane	55	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12411 1 609
+Q12411	UniProtKB	Chain	1	609	.	.	.	ID=PRO_0000096556;Note=Sporulation-specific protein 21	
+Q12411	UniProtKB	Coiled coil	283	342	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12411	UniProtKB	Coiled coil	357	393	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12411	UniProtKB	Coiled coil	424	483	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12411	UniProtKB	Compositional bias	65	162	.	.	.	Note=Ser-rich	
+##sequence-region Q01926 1 470
+Q01926	UniProtKB	Transit peptide	1	32	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01926	UniProtKB	Chain	33	470	.	.	.	ID=PRO_0000021753;Note=Magnesium transporter MRS2%2C mitochondrial	
+Q01926	UniProtKB	Topological domain	33	314	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01926	UniProtKB	Transmembrane	315	333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01926	UniProtKB	Topological domain	334	344	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01926	UniProtKB	Transmembrane	345	361	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01926	UniProtKB	Topological domain	362	470	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01926	UniProtKB	Motif	332	335	.	.	.	Note=YGMN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01926	UniProtKB	Mutagenesis	97	97	.	.	.	Note=No effect on Mg(2+) import. D->A%2CF%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23999289;Dbxref=PMID:23999289	
+Q01926	UniProtKB	Mutagenesis	309	309	.	.	.	Note=Increases Mg(2+) import into mitochondria. M->E%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23999289;Dbxref=PMID:23999289	
+Q01926	UniProtKB	Mutagenesis	309	309	.	.	.	Note=Decreases Mg(2+) import into mitochondria. M->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23999289;Dbxref=PMID:23999289	
+Q01926	UniProtKB	Mutagenesis	315	315	.	.	.	Note=No effect on Mg(2+) import. V->E%2CF%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23999289;Dbxref=PMID:23999289	
+Q01926	UniProtKB	Sequence conflict	371	371	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01926	UniProtKB	Sequence conflict	371	371	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01926	UniProtKB	Sequence conflict	448	448	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01926	UniProtKB	Sequence conflict	448	448	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01926	UniProtKB	Helix	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Beta strand	63	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Beta strand	75	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Helix	84	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Helix	95	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Beta strand	111	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Beta strand	119	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Beta strand	126	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Beta strand	135	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Helix	143	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Helix	170	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Helix	210	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Helix	244	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+Q01926	UniProtKB	Helix	263	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG	
+##sequence-region P47084 1 519
+P47084	UniProtKB	Transit peptide	1	35	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47084	UniProtKB	Chain	36	519	.	.	.	ID=PRO_0000203081;Note=MIOREX complex component 12	
+##sequence-region P53869 1 86
+P53869	UniProtKB	Chain	1	86	.	.	.	ID=PRO_0000203390;Note=MIOREX complex component 7	
+##sequence-region Q07980 1 695
+Q07980	UniProtKB	Chain	1	695	.	.	.	ID=PRO_0000245569;Note=DNA mismatch repair protein MLH2	
+##sequence-region P38257 1 691
+P38257	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38257	UniProtKB	Chain	2	691	.	.	.	ID=PRO_0000096516;Note=Crossover junction endonuclease MMS4	
+P38257	UniProtKB	Region	598	691	.	.	.	Note=Interaction with MUS81	
+P38257	UniProtKB	Coiled coil	364	391	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38257	UniProtKB	Coiled coil	507	529	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38257	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38257	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38257	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38257	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38257	UniProtKB	Mutagenesis	173	173	.	.	.	Note=In allele MMS4-1%3B loss of activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9604884;Dbxref=PMID:9604884	
+##sequence-region P40484 1 314
+P40484	UniProtKB	Chain	1	314	.	.	.	ID=PRO_0000193582;Note=DBF2 kinase activator protein MOB1	
+P40484	UniProtKB	Compositional bias	48	55	.	.	.	Note=Poly-Asn	
+P40484	UniProtKB	Metal binding	179	179	.	.	.	Note=Zinc	
+P40484	UniProtKB	Metal binding	184	184	.	.	.	Note=Zinc	
+P40484	UniProtKB	Metal binding	261	261	.	.	.	Note=Zinc	
+P40484	UniProtKB	Metal binding	266	266	.	.	.	Note=Zinc	
+P40484	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40484	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40484	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40484	UniProtKB	Modified residue	229	229	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40484	UniProtKB	Mutagenesis	105	105	.	.	.	Note=No effect. T->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16934835;Dbxref=PMID:16934835	
+P40484	UniProtKB	Mutagenesis	107	107	.	.	.	Note=No effect. S->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16934835;Dbxref=PMID:16934835	
+P40484	UniProtKB	Beta strand	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Helix	127	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Helix	153	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Helix	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Beta strand	193	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Helix	210	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Turn	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Helix	243	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Helix	248	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Helix	267	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Helix	276	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Helix	298	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+P40484	UniProtKB	Helix	305	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN	
+##sequence-region P54785 1 490
+P54785	UniProtKB	Chain	1	490	.	.	.	ID=PRO_0000046807;Note=Transcriptional activator/repressor MOT3	
+P54785	UniProtKB	Zinc finger	346	368	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P54785	UniProtKB	Zinc finger	374	397	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P54785	UniProtKB	Region	98	295	.	.	.	Note=Prion domain (PrD)	
+P54785	UniProtKB	Compositional bias	8	35	.	.	.	Note=Poly-Gln	
+P54785	UniProtKB	Compositional bias	98	104	.	.	.	Note=Poly-Asn	
+P54785	UniProtKB	Compositional bias	143	157	.	.	.	Note=Poly-Asn	
+P54785	UniProtKB	Compositional bias	173	177	.	.	.	Note=Poly-Ala	
+P54785	UniProtKB	Compositional bias	240	245	.	.	.	Note=Poly-His	
+P54785	UniProtKB	Compositional bias	417	420	.	.	.	Note=Poly-Ser	
+P54785	UniProtKB	Compositional bias	421	433	.	.	.	Note=Poly-Asn	
+P54785	UniProtKB	Compositional bias	441	450	.	.	.	Note=Poly-Ala	
+P54785	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P41940 1 361
+P41940	UniProtKB	Chain	1	361	.	.	.	ID=PRO_0000068741;Note=Mannose-1-phosphate guanyltransferase	
+P41940	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P41940	UniProtKB	Cross-link	244	244	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P41940	UniProtKB	Sequence conflict	50	50	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40562 1 993
+P40562	UniProtKB	Chain	1	993	.	.	.	ID=PRO_0000055193;Note=ATP-dependent DNA helicase MPH1	
+P40562	UniProtKB	Domain	94	261	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P40562	UniProtKB	Domain	507	655	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P40562	UniProtKB	Nucleotide binding	107	114	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P40562	UniProtKB	Motif	209	212	.	.	.	Note=DEAH box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+##sequence-region P0CE00 1 602
+P0CE00	UniProtKB	Chain	1	602	.	.	.	ID=PRO_0000391710;Note=Alpha-glucosides permease MPH3	
+P0CE00	UniProtKB	Topological domain	1	106	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	107	127	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	128	142	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	143	163	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	164	178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	200	200	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	201	221	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	222	234	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	235	255	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	256	270	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	271	291	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	292	363	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	364	384	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	385	397	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	398	418	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	419	426	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	427	447	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	448	459	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	460	480	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	481	492	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	493	513	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	514	525	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Transmembrane	526	546	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE00	UniProtKB	Topological domain	547	602	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53725 1 186
+P53725	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53725	UniProtKB	Chain	2	186	.	.	.	ID=PRO_0000203474;Note=M-phase phosphoprotein 6 homolog	
+P53725	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53725	UniProtKB	Modified residue	42	42	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53725	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53159 1 387
+P53159	UniProtKB	Chain	1	387	.	.	.	ID=PRO_0000202760;Note=Monopolar spindle protein 2	
+P53159	UniProtKB	Transmembrane	311	327	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53159	UniProtKB	Coiled coil	117	232	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08471 1 629
+Q08471	UniProtKB	Chain	1	629	.	.	.	ID=PRO_0000237651;Note=G1-specific transcription factors activator MSA1	
+Q08471	UniProtKB	Compositional bias	317	333	.	.	.	Note=Asn-rich	
+Q08471	UniProtKB	Compositional bias	446	475	.	.	.	Note=Gln-rich	
+Q08471	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P08593 1 268
+P08593	UniProtKB	Chain	1	268	.	.	.	ID=PRO_0000096602;Note=Protein MSS18	
+##sequence-region P40990 1 351
+P40990	UniProtKB	Repeat	155	188	.	.	.	Note=TPR 1	
+P40990	UniProtKB	Repeat	260	294	.	.	.	Note=TPR 2	
+P40990	UniProtKB	Sequence conflict	286	351	.	.	.	Note=TGMEIMDLECFFGFFDCCVKEENFKGARDCLESVKKLGNDKDKKTMINVFLESRKDSIKLLDKARL->RVWNMT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07938 1 337
+Q07938	UniProtKB	Chain	1	337	.	.	.	ID=PRO_0000184556;Note=S-methyl-5'-thioadenosine phosphorylase	
+Q07938	UniProtKB	Region	88	89	.	.	.	Note=Phosphate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155	
+Q07938	UniProtKB	Region	121	122	.	.	.	Note=Phosphate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155	
+Q07938	UniProtKB	Region	254	256	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155	
+Q07938	UniProtKB	Binding site	41	41	.	.	.	Note=Phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155	
+Q07938	UniProtKB	Binding site	230	230	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155	
+Q07938	UniProtKB	Binding site	231	231	.	.	.	Note=Phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155	
+Q07938	UniProtKB	Site	212	212	.	.	.	Note=Important for substrate specificity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155	
+Q07938	UniProtKB	Site	267	267	.	.	.	Note=Important for substrate specificity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155	
+Q07938	UniProtKB	Sequence conflict	55	55	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q07938	UniProtKB	Sequence conflict	157	157	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03218 1 510
+Q03218	UniProtKB	Transmembrane	165	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03218	UniProtKB	Transmembrane	194	214	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03218	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03218	UniProtKB	Transmembrane	286	306	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03218	UniProtKB	Transmembrane	333	353	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03218	UniProtKB	Transmembrane	356	376	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03218	UniProtKB	Sequence conflict	408	408	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08970 1 484
+Q08970	UniProtKB	Transit peptide	1	56	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08970	UniProtKB	Chain	57	484	.	.	.	ID=PRO_0000255968;Note=Mitochondrial metal transporter 2	
+Q08970	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08970	UniProtKB	Transmembrane	158	178	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08970	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08970	UniProtKB	Transmembrane	256	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08970	UniProtKB	Transmembrane	316	336	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08970	UniProtKB	Sequence conflict	17	17	.	.	.	Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07884 1 428
+P07884	UniProtKB	Chain	1	428	.	.	.	ID=PRO_0000019025;Note=tRNA dimethylallyltransferase%2C mitochondrial	
+P07884	UniProtKB	Nucleotide binding	21	28	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07884	UniProtKB	Zinc finger	373	409	.	.	.	Note=Matrin-type	
+P07884	UniProtKB	Region	23	28	.	.	.	Note=Substrate binding	
+P07884	UniProtKB	Region	46	49	.	.	.	Note=Interaction with substrate tRNA	
+P07884	UniProtKB	Region	170	174	.	.	.	Note=Interaction with substrate tRNA	
+P07884	UniProtKB	Region	199	207	.	.	.	Note=Core aggregation region	
+P07884	UniProtKB	Region	210	232	.	.	.	Note=Interaction with isopentenylpyrophosphate transferase	
+P07884	UniProtKB	Region	256	258	.	.	.	Note=Interaction with substrate tRNA	
+P07884	UniProtKB	Region	284	302	.	.	.	Note=Interaction with substrate tRNA	
+P07884	UniProtKB	Region	294	301	.	.	.	Note=Interaction with substrate tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07884	UniProtKB	Site	112	112	.	.	.	Note=Interaction with substrate tRNA	
+P07884	UniProtKB	Site	193	193	.	.	.	Note=Interaction with substrate tRNA	
+P07884	UniProtKB	Alternative sequence	1	11	.	.	.	ID=VSP_018811;Note=In isoform II. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07884	UniProtKB	Sequence conflict	313	313	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07884	UniProtKB	Sequence conflict	375	375	.	.	.	Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07884	UniProtKB	Beta strand	15	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Beta strand	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	27	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Beta strand	40	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Turn	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Turn	55	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Turn	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Beta strand	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	85	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Turn	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Beta strand	105	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	113	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Beta strand	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	135	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Beta strand	144	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	149	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	158	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	169	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	186	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Beta strand	198	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	210	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	229	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Turn	241	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	247	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	253	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	261	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	278	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	304	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Turn	308	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Beta strand	312	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Turn	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Turn	324	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	328	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	351	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	359	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	363	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Beta strand	372	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Beta strand	385	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	391	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+P07884	UniProtKB	Helix	401	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH	
+##sequence-region P38191 1 138
+P38191	UniProtKB	Chain	1	138	.	.	.	ID=PRO_0000212410;Note=Protein yippee-like MOH1	
+P38191	UniProtKB	Domain	41	138	.	.	.	Note=Yippee;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01128	
+P38191	UniProtKB	Metal binding	45	45	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01128	
+P38191	UniProtKB	Metal binding	48	48	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01128	
+P38191	UniProtKB	Metal binding	101	101	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01128	
+P38191	UniProtKB	Metal binding	104	104	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01128	
+##sequence-region P32333 1 1867
+P32333	UniProtKB	Chain	1	1867	.	.	.	ID=PRO_0000074335;Note=TATA-binding protein-associated factor MOT1	
+P32333	UniProtKB	Repeat	289	326	.	.	.	Note=HEAT 1	
+P32333	UniProtKB	Repeat	445	482	.	.	.	Note=HEAT 2	
+P32333	UniProtKB	Repeat	541	578	.	.	.	Note=HEAT 3	
+P32333	UniProtKB	Repeat	1108	1145	.	.	.	Note=HEAT 4	
+P32333	UniProtKB	Repeat	1188	1225	.	.	.	Note=HEAT 5	
+P32333	UniProtKB	Domain	1284	1457	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32333	UniProtKB	Repeat	1495	1537	.	.	.	Note=HEAT 6	
+P32333	UniProtKB	Domain	1639	1787	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P32333	UniProtKB	Nucleotide binding	1297	1304	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32333	UniProtKB	Motif	195	211	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32333	UniProtKB	Motif	1408	1411	.	.	.	Note=DEGH box	
+P32333	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32333	UniProtKB	Modified residue	677	677	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P32333	UniProtKB	Mutagenesis	1226	1226	.	.	.	Note=Temperature sensitive in mot1-301. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16387868;Dbxref=PMID:16387868	
+P32333	UniProtKB	Mutagenesis	1303	1303	.	.	.	Note=No ATPase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11880621;Dbxref=PMID:11880621	
+##sequence-region P32829 1 692
+P32829	UniProtKB	Chain	1	692	.	.	.	ID=PRO_0000138680;Note=Double-strand break repair protein MRE11	
+P32829	UniProtKB	Active site	125	125	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32829	UniProtKB	Natural variant	380	380	.	.	.	Note=In strain: SK1. P->S	
+P32829	UniProtKB	Natural variant	659	659	.	.	.	Note=In strain: SK1. P->S	
+##sequence-region P53166 1 561
+P53166	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53166	UniProtKB	Chain	27	561	.	.	.	ID=PRO_0000041929;Note=ATP-dependent RNA helicase MRH4%2C mitochondrial	
+P53166	UniProtKB	Domain	151	339	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53166	UniProtKB	Domain	370	561	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P53166	UniProtKB	Nucleotide binding	164	171	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53166	UniProtKB	Motif	117	141	.	.	.	Note=Q motif	
+P53166	UniProtKB	Motif	287	290	.	.	.	Note=DEAD box	
+P53166	UniProtKB	Natural variant	67	67	.	.	.	Note=In strain: DBY947. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12702275;Dbxref=PMID:12702275	
+P53166	UniProtKB	Natural variant	438	438	.	.	.	Note=In strain: DBY947. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12702275;Dbxref=PMID:12702275	
+##sequence-region P40185 1 145
+P40185	UniProtKB	Transit peptide	1	17	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11003673,ECO:0000269|Ref.5;Dbxref=PMID:11003673	
+P40185	UniProtKB	Chain	18	145	.	.	.	ID=PRO_0000036209;Note=Protein MMF1%2C mitochondrial	
+P40185	UniProtKB	Beta strand	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+P40185	UniProtKB	Beta strand	38	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+P40185	UniProtKB	Beta strand	45	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+P40185	UniProtKB	Helix	65	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+P40185	UniProtKB	Helix	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+P40185	UniProtKB	Beta strand	90	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+P40185	UniProtKB	Helix	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+P40185	UniProtKB	Helix	103	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+P40185	UniProtKB	Beta strand	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+P40185	UniProtKB	Beta strand	120	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+P40185	UniProtKB	Helix	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+P40185	UniProtKB	Beta strand	134	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW	
+##sequence-region P50108 1 393
+P50108	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000215164;Note=Probable alpha-1%2C6-mannosyltransferase MNN10	
+P50108	UniProtKB	Topological domain	1	52	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50108	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50108	UniProtKB	Topological domain	74	393	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50108	UniProtKB	Sequence conflict	238	238	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53163 1 194
+P53163	UniProtKB	Transit peptide	1	33	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15221522;Dbxref=PMID:15221522	
+P53163	UniProtKB	Chain	34	194	.	.	.	ID=PRO_0000030460;Note=54S ribosomal protein L12%2C mitochondrial	
+P53163	UniProtKB	Glycosylation	34	34	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53163	UniProtKB	Sequence conflict	34	34	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32906 1 549
+P32906	UniProtKB	Chain	1	549	.	.	.	ID=PRO_0000210319;Note=Endoplasmic reticulum mannosyl-oligosaccharide 1%2C2-alpha-mannosidase	
+P32906	UniProtKB	Topological domain	1	4	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32906	UniProtKB	Transmembrane	5	24	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32906	UniProtKB	Topological domain	25	354	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32906	UniProtKB	Active site	399	399	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31723	
+P32906	UniProtKB	Metal binding	525	525	.	.	.	Note=Calcium;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10675327;Dbxref=PMID:10675327	
+P32906	UniProtKB	Glycosylation	96	96	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6I	
+P32906	UniProtKB	Glycosylation	155	155	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6I	
+P32906	UniProtKB	Glycosylation	224	224	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6I	
+P32906	UniProtKB	Disulfide bond	340	385	.	.	.	Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1DL2,ECO:0000244|PDB:1G6I,ECO:0000269|PubMed:10675327;Dbxref=PMID:10675327	
+P32906	UniProtKB	Disulfide bond	468	471	.	.	.	Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1DL2,ECO:0000244|PDB:1G6I,ECO:0000269|PubMed:10675327;Dbxref=PMID:10675327	
+P32906	UniProtKB	Natural variant	40	40	.	.	.	Note=D->Y	
+P32906	UniProtKB	Natural variant	376	376	.	.	.	Note=D->L	
+P32906	UniProtKB	Helix	35	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Turn	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	84	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	102	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	125	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	130	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	156	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	172	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	176	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	184	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Turn	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	212	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	225	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	235	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	244	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	253	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Turn	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Turn	272	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	275	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	291	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	309	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Turn	313	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	318	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Turn	324	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6I	
+P32906	UniProtKB	Beta strand	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	337	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	342	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	356	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	372	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	399	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	417	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	425	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	435	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	451	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	468	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Turn	474	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	482	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	498	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	504	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	520	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Beta strand	529	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+P32906	UniProtKB	Helix	535	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2	
+##sequence-region P47123 1 218
+P47123	UniProtKB	Chain	1	218	.	.	.	ID=PRO_0000215203;Note=Nuclear import protein MOG1	
+P47123	UniProtKB	Beta strand	34	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Helix	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Beta strand	43	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Helix	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Beta strand	64	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Beta strand	86	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Helix	100	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Helix	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Beta strand	117	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Turn	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Beta strand	133	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Beta strand	154	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Helix	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Beta strand	168	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Helix	180	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Turn	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Helix	193	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Beta strand	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+P47123	UniProtKB	Helix	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6	
+##sequence-region P53583 1 542
+P53583	UniProtKB	Chain	1	542	.	.	.	ID=PRO_0000096549;Note=Protein MPA43	
+P53583	UniProtKB	Sequence conflict	46	53	.	.	.	Note=KKSWKFWQ->RSHGNLA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38857 1 129
+P38857	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000212801;Note=Mitochondrial pyruvate carrier 2	
+P38857	UniProtKB	Transmembrane	23	39	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38857	UniProtKB	Transmembrane	55	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38857	UniProtKB	Transmembrane	75	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12404 1 318
+Q12404	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12404	UniProtKB	Chain	22	318	.	.	.	ID=PRO_0000034220;Note=Protein disulfide-isomerase MPD1	
+Q12404	UniProtKB	Domain	22	158	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+Q12404	UniProtKB	Motif	315	318	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138	
+Q12404	UniProtKB	Glycosylation	47	47	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12404	UniProtKB	Glycosylation	307	307	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12404	UniProtKB	Disulfide bond	59	62	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+Q12404	UniProtKB	Helix	36	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Beta strand	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Beta strand	50	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Helix	60	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Helix	66	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Turn	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Beta strand	80	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Turn	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Helix	93	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Beta strand	103	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Beta strand	132	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Helix	142	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Helix	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Helix	166	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Beta strand	174	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Helix	189	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Beta strand	202	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Helix	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Helix	226	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Beta strand	246	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Turn	252	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Beta strand	256	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Helix	267	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Beta strand	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+Q12404	UniProtKB	Helix	289	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3	
+##sequence-region P35728 1 441
+P35728	UniProtKB	Chain	1	441	.	.	.	ID=PRO_0000076265;Note=Protein MPE1	
+P35728	UniProtKB	Domain	5	78	.	.	.	Note=DWNN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00612	
+P35728	UniProtKB	Zinc finger	180	197	.	.	.	Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+P35728	UniProtKB	Modified residue	221	221	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P40364 1 252
+P40364	UniProtKB	Chain	1	252	.	.	.	ID=PRO_0000203056;Note=Mitochondrial peculiar membrane protein 1	
+##sequence-region P54199 1 764
+P54199	UniProtKB	Chain	1	764	.	.	.	ID=PRO_0000086391;Note=Serine/threonine-protein kinase MPS1	
+P54199	UniProtKB	Domain	440	720	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P54199	UniProtKB	Nucleotide binding	446	454	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P54199	UniProtKB	Compositional bias	273	282	.	.	.	Note=Poly-Ser	
+P54199	UniProtKB	Compositional bias	309	315	.	.	.	Note=Poly-Ser	
+P54199	UniProtKB	Active site	563	563	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P54199	UniProtKB	Binding site	468	468	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P54199	UniProtKB	Mutagenesis	580	580	.	.	.	Note=Loss of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7737118;Dbxref=PMID:7737118	
+P54199	UniProtKB	Sequence conflict	146	146	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54199	UniProtKB	Sequence conflict	211	213	.	.	.	Note=TKR->RRE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54199	UniProtKB	Sequence conflict	211	213	.	.	.	Note=TKR->RRE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47069 1 682
+P47069	UniProtKB	Chain	1	682	.	.	.	ID=PRO_0000076266;Note=Spindle pole body assembly component MPS3	
+P47069	UniProtKB	Topological domain	1	154	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47069	UniProtKB	Transmembrane	155	175	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47069	UniProtKB	Topological domain	176	682	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47069	UniProtKB	Domain	427	616	.	.	.	Note=SUN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00802	
+P47069	UniProtKB	Nucleotide binding	187	194	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47069	UniProtKB	Region	171	682	.	.	.	Note=Interaction with CDC31;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12486115;Dbxref=PMID:12486115	
+P47069	UniProtKB	Region	431	650	.	.	.	Note=Interaction with JEM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12493774;Dbxref=PMID:12493774	
+P47069	UniProtKB	Coiled coil	241	273	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47069	UniProtKB	Compositional bias	55	129	.	.	.	Note=Asp-rich	
+P47069	UniProtKB	Compositional bias	391	429	.	.	.	Note=Gln-rich	
+P47069	UniProtKB	Mutagenesis	465	465	.	.	.	Note=Lethal%3B when associated with E-466. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	466	466	.	.	.	Note=Lethal%3B when associated with E-465. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	472	472	.	.	.	Note=In mps3-1%3B defective in spindle pole body assembly and duplication. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12486115;Dbxref=PMID:12486115	
+P47069	UniProtKB	Mutagenesis	476	476	.	.	.	Note=Lethal. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	477	477	.	.	.	Note=Defective in spindle pole body duplication at 37 degrees Celsius. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	487	487	.	.	.	Note=Defective in spindle pole body duplication at 37 degrees Celsius. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	489	489	.	.	.	Note=Lethal. I->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	494	494	.	.	.	Note=Lethal%3B when associated with A-495%3B A-496%3B A-497 and A-498. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	495	495	.	.	.	Note=Lethal%3B when associated with A-494%3B A-496%3B A-497 and A-498. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	496	496	.	.	.	Note=Lethal%3B when associated with A-494%3B A-495%3B A-497 and A-498. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	497	497	.	.	.	Note=Lethal%3B when associated with A-494%3B A-495%3B A-496 and A-498. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	498	498	.	.	.	Note=Lethal%3B when associated with A-494%3B A-495%3B A-496 and A-497. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	500	500	.	.	.	Note=Lethal. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	502	502	.	.	.	Note=Defective in spindle pole body duplication at 37 degrees Celsius. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	504	504	.	.	.	Note=Lethal. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	512	512	.	.	.	Note=Lethal. H->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	517	517	.	.	.	Note=Lethal. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	523	523	.	.	.	Note=Lethal. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	540	540	.	.	.	Note=Defective in spindle pole body duplication at 37 degrees Celsius. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	572	572	.	.	.	Note=Defective in spindle pole body duplication at 37 degrees Celsius%3B when associated with L-573. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	573	573	.	.	.	Note=Defective in spindle pole body duplication at 37 degrees Celsius%3B when associated with L-572. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	590	590	.	.	.	Note=Lethal. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	592	592	.	.	.	Note=Defective in spindle pole body duplication at 37 degrees Celsius. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	593	593	.	.	.	Note=Lethal%3B when associated with D-594. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	594	594	.	.	.	Note=Lethal%3B when associated with A-593. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	597	597	.	.	.	Note=In nep98-7%3B defective in spindle organization during nuclear division and in G2/M progression. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12493774;Dbxref=PMID:12493774	
+P47069	UniProtKB	Mutagenesis	599	599	.	.	.	Note=Lethal. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	604	604	.	.	.	Note=Lethal. I->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	605	605	.	.	.	Note=Lethal%3B when associated with Q-606. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	606	606	.	.	.	Note=Lethal%3B when associated with C-605. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	611	611	.	.	.	Note=Lethal. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+P47069	UniProtKB	Mutagenesis	613	613	.	.	.	Note=Lethal. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827	
+##sequence-region P39016 1 859
+P39016	UniProtKB	Chain	1	859	.	.	.	ID=PRO_0000075923;Note=Suppressor protein MPT5	
+P39016	UniProtKB	Domain	188	596	.	.	.	Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318	
+P39016	UniProtKB	Repeat	209	247	.	.	.	Note=Pumilio 1	
+P39016	UniProtKB	Repeat	248	283	.	.	.	Note=Pumilio 2	
+P39016	UniProtKB	Repeat	284	320	.	.	.	Note=Pumilio 3	
+P39016	UniProtKB	Repeat	325	362	.	.	.	Note=Pumilio 4	
+P39016	UniProtKB	Repeat	363	400	.	.	.	Note=Pumilio 5	
+P39016	UniProtKB	Repeat	401	438	.	.	.	Note=Pumilio 6	
+P39016	UniProtKB	Repeat	439	474	.	.	.	Note=Pumilio 7	
+P39016	UniProtKB	Repeat	503	539	.	.	.	Note=Pumilio 8	
+P39016	UniProtKB	Compositional bias	647	653	.	.	.	Note=Poly-Asn	
+P39016	UniProtKB	Modified residue	662	662	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39016	UniProtKB	Modified residue	834	834	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39016	UniProtKB	Modified residue	838	838	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39016	UniProtKB	Helix	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	215	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	222	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Turn	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	238	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	253	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	262	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Turn	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	275	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	289	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	298	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	312	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Turn	324	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	329	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	341	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	354	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	358	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	369	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	379	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	392	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	406	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Turn	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	415	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	426	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	429	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	441	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	444	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	453	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	488	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	509	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	518	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	528	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	532	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	554	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Helix	576	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+P39016	UniProtKB	Beta strand	580	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZV	
+P39016	UniProtKB	Helix	585	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1	
+##sequence-region P25336 1 1018
+P25336	UniProtKB	Chain	1	1018	.	.	.	ID=PRO_0000115195;Note=DNA mismatch repair protein MSH3	
+P25336	UniProtKB	Nucleotide binding	791	798	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25336	UniProtKB	Region	126	256	.	.	.	Note=Mispair-binding domain	
+P25336	UniProtKB	Motif	4	11	.	.	.	Note=PIP box	
+P25336	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Partially functional in a mismatch repair assay%3B when associated with 10-AA-11. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11005803;Dbxref=PMID:11005803	
+P25336	UniProtKB	Mutagenesis	10	11	.	.	.	Note=Partially functional in a mismatch repair assay%3B when associated with A-4. FF->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11005803;Dbxref=PMID:11005803	
+P25336	UniProtKB	Mutagenesis	158	158	.	.	.	Note=Alters DNA-binding activity and impairs MSH2-MSH3-mediated DNA mismatch repair%3B when associated with ALA-160. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157869;Dbxref=PMID:17157869	
+P25336	UniProtKB	Mutagenesis	160	160	.	.	.	Note=Alters DNA-binding activity and impairs MSH2-MSH3-mediated DNA mismatch repair%3B when associated with ALA-158. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157869;Dbxref=PMID:17157869	
+P25336	UniProtKB	Mutagenesis	203	203	.	.	.	Note=No effect. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157869;Dbxref=PMID:17157869	
+P25336	UniProtKB	Mutagenesis	226	226	.	.	.	Note=No effect. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157869;Dbxref=PMID:17157869	
+P25336	UniProtKB	Mutagenesis	247	247	.	.	.	Note=Impairs MSH2-MSH3-mediated DNA mismatch repair. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157869;Dbxref=PMID:17157869	
+P25336	UniProtKB	Mutagenesis	796	796	.	.	.	Note=Defective in MMR and in NHTR. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644	
+##sequence-region P53045 1 309
+P53045	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000117039;Note=Methylsterol monooxygenase	
+P53045	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53045	UniProtKB	Motif	160	164	.	.	.	Note=Histidine box-1	
+P53045	UniProtKB	Motif	173	177	.	.	.	Note=Histidine box-2	
+P53045	UniProtKB	Motif	257	263	.	.	.	Note=Histidine box-3	
+P53045	UniProtKB	Cross-link	96	96	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P53045	UniProtKB	Sequence conflict	302	302	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P22148 1 382
+P22148	UniProtKB	Chain	1	382	.	.	.	ID=PRO_0000096598;Note=Protein MSN1	
+P22148	UniProtKB	Region	12	26	.	.	.	Note=Leucine-zipper	
+P22148	UniProtKB	Motif	266	271	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22148	UniProtKB	Sequence conflict	360	360	.	.	.	Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P52918 1 1224
+P52918	UniProtKB	Chain	1	1224	.	.	.	ID=PRO_0000096599;Note=Protein MSN5	
+P52918	UniProtKB	Sequence conflict	886	886	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P52918	UniProtKB	Sequence conflict	1011	1011	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33748 1 704
+P33748	UniProtKB	Chain	1	704	.	.	.	ID=PRO_0000046810;Note=Zinc finger protein MSN2	
+P33748	UniProtKB	Zinc finger	647	665	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P33748	UniProtKB	Zinc finger	676	698	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P33748	UniProtKB	Motif	261	269	.	.	.	Note=9aaTAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618436;Dbxref=PMID:27618436	
+P33748	UniProtKB	Compositional bias	1	109	.	.	.	Note=Asp-rich (acidic)	
+P33748	UniProtKB	Compositional bias	260	279	.	.	.	Note=Asp-rich (acidic)	
+P33748	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P33748	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P33748	UniProtKB	Modified residue	451	451	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P33748	UniProtKB	Modified residue	582	582	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33748	UniProtKB	Modified residue	633	633	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P40029 1 184
+P40029	UniProtKB	Chain	1	184	.	.	.	ID=PRO_0000138630;Note=Peptide methionine sulfoxide reductase	
+P40029	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40029	UniProtKB	Helix	2	4	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Beta strand	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIL	
+P40029	UniProtKB	Turn	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Beta strand	17	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Helix	26	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Helix	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Beta strand	41	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Helix	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIL	
+P40029	UniProtKB	Helix	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIL	
+P40029	UniProtKB	Beta strand	75	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Turn	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Helix	89	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Beta strand	104	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIL	
+P40029	UniProtKB	Beta strand	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIL	
+P40029	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Beta strand	119	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Helix	125	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Helix	139	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Beta strand	149	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+P40029	UniProtKB	Helix	159	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM	
+##sequence-region Q03825 1 758
+Q03825	UniProtKB	Chain	1	758	.	.	.	ID=PRO_0000203315;Note=Transcription activator MSS11	
+Q03825	UniProtKB	Domain	51	83	.	.	.	Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126	
+Q03825	UniProtKB	Compositional bias	290	329	.	.	.	Note=Poly-Gln	
+Q03825	UniProtKB	Compositional bias	605	637	.	.	.	Note=Poly-Asn	
+Q03825	UniProtKB	Compositional bias	653	656	.	.	.	Note=Poly-Ser	
+Q03825	UniProtKB	Mutagenesis	133	134	.	.	.	Note=Reduces ability to activate transcription and to induce invasive growth. FL->GA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12492858;Dbxref=PMID:12492858	
+Q03825	UniProtKB	Mutagenesis	137	138	.	.	.	Note=Reduces ability to activate transcription and to induce invasive growth. WW->GA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12492858;Dbxref=PMID:12492858	
+Q03825	UniProtKB	Mutagenesis	140	141	.	.	.	Note=Reduces ability to activate transcription and to induce invasive growth. IF->GA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12492858;Dbxref=PMID:12492858	
+Q03825	UniProtKB	Mutagenesis	144	145	.	.	.	Note=Reduces ability to activate transcription and to induce invasive growth. LF->GA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12492858;Dbxref=PMID:12492858	
+##sequence-region P36066 1 463
+P36066	UniProtKB	Chain	1	463	.	.	.	ID=PRO_0000203149;Note=Protein MRG3-like	
+P36066	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36066	UniProtKB	Repeat	84	118	.	.	.	Note=TPR 1	
+P36066	UniProtKB	Repeat	128	161	.	.	.	Note=TPR 2	
+P36066	UniProtKB	Repeat	358	389	.	.	.	Note=TPR 3	
+P36066	UniProtKB	Repeat	409	442	.	.	.	Note=TPR 4	
+P36066	UniProtKB	Sequence conflict	252	252	.	.	.	Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q3E829 1 80
+Q3E829	UniProtKB	Chain	1	80	.	.	.	ID=PRO_0000240877;Note=MHF histone-fold complex subunit 2	
+Q3E829	UniProtKB	Helix	5	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R	
+Q3E829	UniProtKB	Turn	12	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R	
+Q3E829	UniProtKB	Turn	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R	
+Q3E829	UniProtKB	Helix	27	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R	
+Q3E829	UniProtKB	Helix	66	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R	
+##sequence-region P38341 1 106
+P38341	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000202527;Note=MICOS complex subunit MIC12	
+P38341	UniProtKB	Topological domain	1	10	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38341	UniProtKB	Transmembrane	11	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38341	UniProtKB	Topological domain	28	106	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36112 1 540
+P36112	UniProtKB	Transit peptide	1	17	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36112	UniProtKB	Chain	18	540	.	.	.	ID=PRO_0000203197;Note=MICOS complex subunit MIC60	
+P36112	UniProtKB	Topological domain	18	37	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36112	UniProtKB	Transmembrane	38	57	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36112	UniProtKB	Topological domain	58	540	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36112	UniProtKB	Coiled coil	173	268	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40850 1 830
+P40850	UniProtKB	Chain	1	830	.	.	.	ID=PRO_0000096495;Note=Protein MKT1	
+P40850	UniProtKB	Modified residue	358	358	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40850	UniProtKB	Modified residue	362	362	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40850	UniProtKB	Modified residue	371	371	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40850	UniProtKB	Cross-link	4	4	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40850	UniProtKB	Natural variant	30	30	.	.	.	Note=In strain: 2574%2C ATCC 24657 / D273-10B%2C ATCC 200060 / W303%2C Sigma 1278B%2C YJM 1129%2C YJM 270%2C YJM 627 and YJM 789. D->G	
+P40850	UniProtKB	Natural variant	453	453	.	.	.	Note=In strain: ATCC 24657 / D273-10B%2C ATCC 200060 / W303%2C Sigma 1278B%2C YJM 1129%2C YJM 270%2C YJM 627 and YJM 789. K->R	
+P40850	UniProtKB	Sequence conflict	809	830	.	.	.	Note=IDENVFKLFTKAVEFTTTALSS->TMKTCLNYH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08925 1 612
+Q08925	UniProtKB	Chain	1	612	.	.	.	ID=PRO_0000082038;Note=RNA-binding protein MRN1	
+Q08925	UniProtKB	Domain	201	274	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q08925	UniProtKB	Domain	292	379	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q08925	UniProtKB	Domain	431	504	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q08925	UniProtKB	Domain	522	602	.	.	.	Note=RRM 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q08925	UniProtKB	Compositional bias	6	19	.	.	.	Note=Poly-Asn	
+Q08925	UniProtKB	Compositional bias	22	28	.	.	.	Note=Poly-Asn	
+Q08925	UniProtKB	Compositional bias	45	48	.	.	.	Note=Poly-Ser	
+Q08925	UniProtKB	Compositional bias	413	419	.	.	.	Note=Poly-Ala	
+##sequence-region P33201 1 236
+P33201	UniProtKB	Chain	1	236	.	.	.	ID=PRO_0000154815;Note=Ribosome assembly factor MRT4	
+P33201	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Bypasses the requirement for phosphatase YVH1 for the release of MRT4. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19797078;Dbxref=PMID:19797078	
+##sequence-region Q05648 1 414
+Q05648	UniProtKB	Transit peptide	1	29	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05648	UniProtKB	Chain	30	414	.	.	.	ID=PRO_0000229731;Note=MIOREX complex component 10	
+Q05648	UniProtKB	Topological domain	30	373	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23022099;Dbxref=PMID:23022099	
+Q05648	UniProtKB	Transmembrane	374	394	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05648	UniProtKB	Topological domain	395	414	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23022099;Dbxref=PMID:23022099	
+##sequence-region P40050 1 688
+P40050	UniProtKB	Transit peptide	1	46	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40050	UniProtKB	Chain	47	688	.	.	.	ID=PRO_0000202635;Note=MIOREX complex component 1	
+##sequence-region P48564 1 524
+P48564	UniProtKB	Transit peptide	1	34	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48564	UniProtKB	Chain	35	524	.	.	.	ID=PRO_0000203374;Note=MIOREX complex component 6	
+##sequence-region P15424 1 664
+P15424	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15424	UniProtKB	Chain	27	664	.	.	.	ID=PRO_0000030812;Note=ATP-dependent RNA helicase MSS116%2C mitochondrial	
+P15424	UniProtKB	Domain	139	326	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P15424	UniProtKB	Domain	355	512	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P15424	UniProtKB	Nucleotide binding	152	159	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P15424	UniProtKB	Motif	106	134	.	.	.	Note=Q motif	
+P15424	UniProtKB	Motif	267	270	.	.	.	Note=DEAD box	
+P15424	UniProtKB	Beta strand	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	104	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	115	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Turn	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TYW	
+P15424	UniProtKB	Helix	131	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	142	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	158	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Turn	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	190	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	215	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	224	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	237	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	243	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TYY	
+P15424	UniProtKB	Beta strand	263	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	269	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Turn	275	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	278	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	300	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	311	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Turn	316	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	322	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	333	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	342	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	354	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Turn	370	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	375	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	383	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Turn	398	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	403	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	412	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	426	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	434	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	437	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TZ0	
+P15424	UniProtKB	Beta strand	447	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	455	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TYY	
+P15424	UniProtKB	Helix	459	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	469	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TYN	
+P15424	UniProtKB	Beta strand	474	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	482	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	485	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	501	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	509	518	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	523	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	541	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	548	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	558	562	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	570	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Helix	574	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	583	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TYW	
+P15424	UniProtKB	Helix	586	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+P15424	UniProtKB	Beta strand	592	594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X	
+##sequence-region Q08818 1 692
+Q08818	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08818	UniProtKB	Chain	31	692	.	.	.	ID=PRO_0000042820;Note=Meiotic sister-chromatid recombination protein 6%2C mitochondrial	
+##sequence-region P25846 1 959
+P25846	UniProtKB	Transit peptide	1	21	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7961998;Dbxref=PMID:7961998	
+P25846	UniProtKB	Chain	22	959	.	.	.	ID=PRO_0000115179;Note=DNA mismatch repair protein MSH1%2C mitochondrial	
+P25846	UniProtKB	Nucleotide binding	771	778	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25846	UniProtKB	Mutagenesis	105	105	.	.	.	Note=Increases the rate of point mutations 35-fold and displays a significant decrease in respiration-competent cells during a time course. F->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15611870,ECO:0000269|PubMed:16337661;Dbxref=PMID:15611870,PMID:16337661	
+P25846	UniProtKB	Mutagenesis	776	776	.	.	.	Note=Increases the rate of point mutations 19-fold and displays a moderate decrease in respiration-competent cells during a time course. G->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11862493,ECO:0000269|PubMed:15611870,ECO:0000269|PubMed:16337661;Dbxref=PMID:11862493,PMID:15611870,PMID:16337661	
+P25846	UniProtKB	Mutagenesis	813	813	.	.	.	Note=Slightly increases the frequency of point mutations and repeat-mediated deletion rates in mtDNA. R->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11862493,ECO:0000269|PubMed:16337661;Dbxref=PMID:11862493,PMID:16337661	
+P25846	UniProtKB	Sequence conflict	437	437	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25846	UniProtKB	Sequence conflict	695	695	.	.	.	Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40965 1 878
+P40965	UniProtKB	Chain	1	878	.	.	.	ID=PRO_0000115201;Note=MutS protein homolog 4	
+P40965	UniProtKB	Nucleotide binding	634	641	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40965	UniProtKB	Sequence conflict	811	812	.	.	.	Note=IH->MD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12175 1 901
+Q12175	UniProtKB	Chain	1	901	.	.	.	ID=PRO_0000115206;Note=MutS protein homolog 5	
+Q12175	UniProtKB	Nucleotide binding	643	650	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12175	UniProtKB	Mutagenesis	643	644	.	.	.	Note=Abolishes function%3B no effect on interaction with MSH4. GA->DV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9374523;Dbxref=PMID:9374523	
+Q12175	UniProtKB	Mutagenesis	648	648	.	.	.	Note=Abolishes function%3B no effect on interaction with MSH4. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9374523;Dbxref=PMID:9374523	
+##sequence-region P40567 1 111
+P40567	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000081895;Note=U2 small nuclear ribonucleoprotein B''	
+P40567	UniProtKB	Domain	28	106	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P40567	UniProtKB	Beta strand	30	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40567	UniProtKB	Helix	41	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40567	UniProtKB	Turn	66	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40567	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40567	UniProtKB	Helix	79	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40567	UniProtKB	Beta strand	100	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P53604 1 210
+P53604	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000096600;Note=Protein MSO1	
+P53604	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53604	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53604	UniProtKB	Alternative sequence	1	1	.	.	.	ID=VSP_058125;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P20676 1 1076
+P20676	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P20676	UniProtKB	Chain	2	1076	.	.	.	ID=PRO_0000204902;Note=Nucleoporin NUP1	
+P20676	UniProtKB	Repeat	336	338	.	.	.	Note=FXF 1	
+P20676	UniProtKB	Repeat	384	386	.	.	.	Note=FXF 2	
+P20676	UniProtKB	Repeat	406	409	.	.	.	Note=FXFG 1	
+P20676	UniProtKB	Repeat	422	425	.	.	.	Note=FXFG 2	
+P20676	UniProtKB	Repeat	448	451	.	.	.	Note=FXFG 3	
+P20676	UniProtKB	Repeat	484	487	.	.	.	Note=FXFG 4	
+P20676	UniProtKB	Repeat	510	513	.	.	.	Note=FXFG 5	
+P20676	UniProtKB	Repeat	525	528	.	.	.	Note=FXFG 6	
+P20676	UniProtKB	Repeat	543	546	.	.	.	Note=FXFG 7	
+P20676	UniProtKB	Repeat	571	574	.	.	.	Note=FXFG 8	
+P20676	UniProtKB	Repeat	591	593	.	.	.	Note=FXF 3	
+P20676	UniProtKB	Repeat	614	616	.	.	.	Note=FXF 4	
+P20676	UniProtKB	Repeat	636	638	.	.	.	Note=FXF 5	
+P20676	UniProtKB	Repeat	657	659	.	.	.	Note=FXF 6	
+P20676	UniProtKB	Repeat	671	674	.	.	.	Note=FXFG 9	
+P20676	UniProtKB	Repeat	689	691	.	.	.	Note=FXF 7	
+P20676	UniProtKB	Repeat	708	711	.	.	.	Note=FXFG 10	
+P20676	UniProtKB	Repeat	727	730	.	.	.	Note=FXFG 11	
+P20676	UniProtKB	Repeat	753	755	.	.	.	Note=FXF 8	
+P20676	UniProtKB	Repeat	800	803	.	.	.	Note=FXFG 12	
+P20676	UniProtKB	Repeat	819	821	.	.	.	Note=FXF 9	
+P20676	UniProtKB	Repeat	866	868	.	.	.	Note=FXF 10	
+P20676	UniProtKB	Repeat	885	888	.	.	.	Note=FXFG 13	
+P20676	UniProtKB	Repeat	929	931	.	.	.	Note=FXF 11	
+P20676	UniProtKB	Repeat	1008	1009	.	.	.	Note=FG 1	
+P20676	UniProtKB	Repeat	1027	1028	.	.	.	Note=FG 2	
+P20676	UniProtKB	Repeat	1038	1039	.	.	.	Note=FG 3	
+P20676	UniProtKB	Region	1040	1076	.	.	.	Note=Interaction with KAP95	
+P20676	UniProtKB	Compositional bias	81	84	.	.	.	Note=Poly-Asn	
+P20676	UniProtKB	Compositional bias	718	723	.	.	.	Note=Poly-Thr	
+P20676	UniProtKB	Compositional bias	830	833	.	.	.	Note=Poly-Thr	
+P20676	UniProtKB	Compositional bias	881	1022	.	.	.	Note=Asn-rich	
+P20676	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P20676	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P20676	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P20676	UniProtKB	Modified residue	381	381	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P20676	UniProtKB	Modified residue	383	383	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P20676	UniProtKB	Modified residue	637	637	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P20676	UniProtKB	Helix	1004	1006	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+P20676	UniProtKB	Turn	1007	1009	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+##sequence-region Q02199 1 472
+Q02199	UniProtKB	Chain	1	472	.	.	.	ID=PRO_0000204867;Note=Nucleoporin NUP49/NSP49	
+Q02199	UniProtKB	Repeat	2	3	.	.	.	Note=FG 1	
+Q02199	UniProtKB	Repeat	14	17	.	.	.	Note=GLFG 1	
+Q02199	UniProtKB	Repeat	33	34	.	.	.	Note=FG 2	
+Q02199	UniProtKB	Repeat	48	51	.	.	.	Note=GLFG 2	
+Q02199	UniProtKB	Repeat	65	66	.	.	.	Note=FG 3	
+Q02199	UniProtKB	Repeat	77	78	.	.	.	Note=FG 4	
+Q02199	UniProtKB	Repeat	86	89	.	.	.	Note=GLFG 3	
+Q02199	UniProtKB	Repeat	101	104	.	.	.	Note=GLFG 4	
+Q02199	UniProtKB	Repeat	113	116	.	.	.	Note=SLFG 1	
+Q02199	UniProtKB	Repeat	125	128	.	.	.	Note=GLFG 5	
+Q02199	UniProtKB	Repeat	148	151	.	.	.	Note=GLFG 6	
+Q02199	UniProtKB	Repeat	159	162	.	.	.	Note=SLFG 2	
+Q02199	UniProtKB	Repeat	175	178	.	.	.	Note=GLFG 7%3B approximate	
+Q02199	UniProtKB	Repeat	185	188	.	.	.	Note=SLFG 3	
+Q02199	UniProtKB	Repeat	199	202	.	.	.	Note=GLFG 8	
+Q02199	UniProtKB	Repeat	210	213	.	.	.	Note=SLFG 4	
+Q02199	UniProtKB	Repeat	233	236	.	.	.	Note=GLFG 9	
+Q02199	UniProtKB	Compositional bias	13	207	.	.	.	Note=Gly-rich	
+Q02199	UniProtKB	Compositional bias	67	73	.	.	.	Note=Poly-Gln	
+Q02199	UniProtKB	Compositional bias	90	226	.	.	.	Note=Asn-rich	
+Q02199	UniProtKB	Compositional bias	216	226	.	.	.	Note=Poly-Asn	
+Q02199	UniProtKB	Compositional bias	238	289	.	.	.	Note=Gln-rich	
+Q02199	UniProtKB	Compositional bias	238	249	.	.	.	Note=Poly-Gln	
+##sequence-region Q12454 1 224
+Q12454	UniProtKB	Chain	1	224	.	.	.	ID=PRO_0000244442;Note=Putative tyrosine-protein phosphatase OCA6	
+Q12454	UniProtKB	Active site	114	114	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12454	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12454	UniProtKB	Sequence conflict	208	208	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P31755 1 480
+P31755	UniProtKB	Chain	1	480	.	.	.	ID=PRO_0000080563;Note=Initiation-specific alpha-1%2C6-mannosyltransferase	
+P31755	UniProtKB	Topological domain	1	15	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1628616;Dbxref=PMID:1628616	
+P31755	UniProtKB	Transmembrane	16	30	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255,ECO:0000303;evidence=ECO:0000255,ECO:0000303|PubMed:1628616;Dbxref=PMID:1628616	
+P31755	UniProtKB	Topological domain	31	480	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269,ECO:0000303;evidence=ECO:0000269|PubMed:8601597,ECO:0000303|PubMed:1628616;Dbxref=PMID:8601597,PMID:1628616	
+P31755	UniProtKB	Motif	187	189	.	.	.	Note=DXD motif;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17042779;Dbxref=PMID:17042779	
+P31755	UniProtKB	Glycosylation	203	203	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31755	UniProtKB	Glycosylation	281	281	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31755	UniProtKB	Glycosylation	341	341	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31755	UniProtKB	Glycosylation	393	393	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31755	UniProtKB	Mutagenesis	187	187	.	.	.	Note=Loss of mannosyltransferase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17042779;Dbxref=PMID:17042779	
+##sequence-region Q99297 1 307
+Q99297	UniProtKB	Chain	1	307	.	.	.	ID=PRO_0000090649;Note=Mitochondrial 2-oxodicarboxylate carrier 2	
+Q99297	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99297	UniProtKB	Transmembrane	76	95	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99297	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99297	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99297	UniProtKB	Transmembrane	215	235	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99297	UniProtKB	Transmembrane	280	300	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99297	UniProtKB	Repeat	10	106	.	.	.	Note=Solcar 1	
+Q99297	UniProtKB	Repeat	116	200	.	.	.	Note=Solcar 2	
+Q99297	UniProtKB	Repeat	209	299	.	.	.	Note=Solcar 3	
+##sequence-region P38325 1 134
+P38325	UniProtKB	Chain	1	134	.	.	.	ID=PRO_0000202518;Note=Mitochondrial outer membrane protein OM14	
+P38325	UniProtKB	Transmembrane	71	87	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38325	UniProtKB	Transmembrane	105	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38325	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38325	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q07521 1 108
+Q07521	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000299776;Note=Putative uncharacterized protein OPI6	
+##sequence-region Q06593 1 877
+Q06593	UniProtKB	Chain	1	877	.	.	.	ID=PRO_0000262733;Note=Oligopeptide transporter 2	
+Q06593	UniProtKB	Topological domain	1	167	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	189	189	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	190	210	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	211	240	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	262	272	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	273	293	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	294	334	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	335	355	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	356	374	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	375	395	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	396	404	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	405	425	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	426	480	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	481	501	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	502	553	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	554	574	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	575	582	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	583	603	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	604	614	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	615	635	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	636	671	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	672	692	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	693	730	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	731	751	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	752	766	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	767	789	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	790	811	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Transmembrane	812	832	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Topological domain	833	877	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Glycosylation	374	374	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06593	UniProtKB	Glycosylation	860	860	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P50874 1 479
+P50874	UniProtKB	Chain	1	479	.	.	.	ID=PRO_0000127096;Note=Origin recognition complex subunit 5	
+P50874	UniProtKB	Nucleotide binding	37	44	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06144 1 216
+Q06144	UniProtKB	Chain	1	216	.	.	.	ID=PRO_0000215646;Note=Protein ORM2	
+Q06144	UniProtKB	Topological domain	1	78	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06144	UniProtKB	Transmembrane	79	99	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06144	UniProtKB	Topological domain	100	103	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06144	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06144	UniProtKB	Topological domain	125	148	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06144	UniProtKB	Transmembrane	149	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06144	UniProtKB	Topological domain	170	177	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06144	UniProtKB	Transmembrane	178	198	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06144	UniProtKB	Topological domain	199	216	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06144	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06144	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06144	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06144	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06144	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53224	
+Q06144	UniProtKB	Modified residue	51	51	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53224	
+Q06144	UniProtKB	Mutagenesis	9	9	.	.	.	Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-15%2C A-18%2C A-36 and 46-A--A-48. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505	
+Q06144	UniProtKB	Mutagenesis	15	15	.	.	.	Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-9%2C A-18%2C A-36 and 46-A--A-48. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505	
+Q06144	UniProtKB	Mutagenesis	18	18	.	.	.	Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-9%2C A-15%2C A-36 and 46-A--A-48. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505	
+Q06144	UniProtKB	Mutagenesis	36	36	.	.	.	Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-9%2C A-15%2C A-18 and 46-A--A-48. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505	
+Q06144	UniProtKB	Mutagenesis	46	48	.	.	.	Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-9%2C A-15%2C A-18%2C and A-36. SSS->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505	
+##sequence-region P21375 1 501
+P21375	UniProtKB	Transit peptide	1	32	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9587404;Dbxref=PMID:9587404	
+P21375	UniProtKB	Chain	33	501	.	.	.	ID=PRO_0000158668;Note=Fumarate reductase 2	
+P21375	UniProtKB	Nucleotide binding	37	51	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21375	UniProtKB	Active site	281	281	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21375	UniProtKB	Active site	304	304	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21375	UniProtKB	Sequence conflict	106	107	.	.	.	Note=LH->FD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21375	UniProtKB	Sequence conflict	170	170	.	.	.	Note=A->AR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21375	UniProtKB	Sequence conflict	191	192	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21375	UniProtKB	Sequence conflict	439	439	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21375	UniProtKB	Sequence conflict	456	457	.	.	.	Note=SV->TL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03723 1 332
+Q03723	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03723	UniProtKB	Chain	25	332	.	.	.	ID=PRO_0000058098;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6	
+Q03723	UniProtKB	Topological domain	25	188	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03723	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03723	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03723	UniProtKB	Transmembrane	268	288	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03723	UniProtKB	Transmembrane	303	323	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03723	UniProtKB	Topological domain	324	332	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03723	UniProtKB	Domain	35	162	.	.	.	Note=Thioredoxin	
+Q03723	UniProtKB	Disulfide bond	78	81	.	.	.	Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03723	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Alters glycosyltransferase efficiency towards a subset of target proteins%3B when associated with S-81. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19549845;Dbxref=PMID:19549845	
+Q03723	UniProtKB	Mutagenesis	81	81	.	.	.	Note=Alters glycosyltransferase efficiency towards a subset of target proteins%3B when associated with S-78. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19549845;Dbxref=PMID:19549845	
+Q03723	UniProtKB	Sequence conflict	33	33	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03723	UniProtKB	Helix	31	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Beta strand	41	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Helix	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Beta strand	61	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Helix	79	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Beta strand	104	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Turn	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Helix	115	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Beta strand	128	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Helix	137	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Turn	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Helix	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+Q03723	UniProtKB	Helix	163	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4	
+##sequence-region Q02795 1 286
+Q02795	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8175708;Dbxref=PMID:8175708	
+Q02795	UniProtKB	Chain	20	286	.	.	.	ID=PRO_0000021962;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit SWP1	
+Q02795	UniProtKB	Topological domain	20	194	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02795	UniProtKB	Transmembrane	195	215	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02795	UniProtKB	Topological domain	216	228	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02795	UniProtKB	Transmembrane	229	249	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02795	UniProtKB	Topological domain	250	252	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02795	UniProtKB	Transmembrane	253	273	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02795	UniProtKB	Topological domain	274	286	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08692 1 278
+Q08692	UniProtKB	Chain	1	278	.	.	.	ID=PRO_0000268695;Note=Outer spore wall protein 1	
+##sequence-region P43558 1 301
+P43558	UniProtKB	Chain	1	301	.	.	.	ID=PRO_0000202672;Note=Ubiquitin thioesterase OTU1	
+P43558	UniProtKB	Domain	109	229	.	.	.	Note=OTU;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00139	
+P43558	UniProtKB	Zinc finger	270	294	.	.	.	Note=C2H2-type	
+P43558	UniProtKB	Region	4	80	.	.	.	Note=UBX-like;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6	
+P43558	UniProtKB	Region	114	120	.	.	.	Note=Cys-loop;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6	
+P43558	UniProtKB	Region	169	179	.	.	.	Note=Variable-loop;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6	
+P43558	UniProtKB	Region	218	222	.	.	.	Note=His-loop;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6	
+P43558	UniProtKB	Region	243	248	.	.	.	Note=S2 site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6	
+P43558	UniProtKB	Active site	117	117	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96FW1	
+P43558	UniProtKB	Active site	120	120	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43558	UniProtKB	Active site	222	222	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6	
+P43558	UniProtKB	Active site	294	294	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96FW1	
+P43558	UniProtKB	Binding site	221	221	.	.	.	Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6	
+P43558	UniProtKB	Cross-link	160	160	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P43558	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16427015;Dbxref=PMID:16427015	
+P43558	UniProtKB	Beta strand	1	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL	
+P43558	UniProtKB	Beta strand	10	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL	
+P43558	UniProtKB	Helix	22	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL	
+P43558	UniProtKB	Beta strand	34	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL	
+P43558	UniProtKB	Turn	39	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL	
+P43558	UniProtKB	Beta strand	43	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL	
+P43558	UniProtKB	Helix	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL	
+P43558	UniProtKB	Helix	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL	
+P43558	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL	
+P43558	UniProtKB	Beta strand	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Turn	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Beta strand	107	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Helix	120	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Helix	136	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Turn	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Helix	155	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Helix	162	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Helix	178	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Beta strand	191	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Turn	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Beta strand	201	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Turn	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Beta strand	211	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Beta strand	223	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Turn	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+P43558	UniProtKB	Helix	242	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4	
+##sequence-region P32336 1 851
+P32336	UniProtKB	Chain	1	851	.	.	.	ID=PRO_0000057981;Note=Protein NUD1	
+P32336	UniProtKB	Repeat	544	566	.	.	.	Note=LRR 1	
+P32336	UniProtKB	Repeat	567	588	.	.	.	Note=LRR 2	
+P32336	UniProtKB	Repeat	589	609	.	.	.	Note=LRR 3	
+P32336	UniProtKB	Repeat	621	642	.	.	.	Note=LRR 4	
+P32336	UniProtKB	Repeat	643	664	.	.	.	Note=LRR 5	
+P32336	UniProtKB	Compositional bias	223	248	.	.	.	Note=Asn-rich	
+P32336	UniProtKB	Compositional bias	223	239	.	.	.	Note=Poly-Asn	
+P32336	UniProtKB	Compositional bias	266	274	.	.	.	Note=Poly-Ser	
+P32336	UniProtKB	Modified residue	388	388	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32336	UniProtKB	Modified residue	392	392	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32336	UniProtKB	Modified residue	417	417	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32336	UniProtKB	Modified residue	419	419	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32336	UniProtKB	Cross-link	357	357	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32336	UniProtKB	Sequence conflict	5	6	.	.	.	Note=TQ->SE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38738 1 679
+P38738	UniProtKB	Chain	1	679	.	.	.	ID=PRO_0000202881;Note=Oxidant-induced cell-cycle arrest protein 5	
+P38738	UniProtKB	Domain	50	441	.	.	.	Note=Rab-GAP TBC	
+P38738	UniProtKB	Compositional bias	263	271	.	.	.	Note=Poly-Asn	
+P38738	UniProtKB	Compositional bias	609	637	.	.	.	Note=Ser-rich	
+##sequence-region P16387 1 420
+P16387	UniProtKB	Transit peptide	1	33	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2684159;Dbxref=PMID:2684159	
+P16387	UniProtKB	Chain	34	420	.	.	.	ID=PRO_0000020452;Note=Pyruvate dehydrogenase E1 component subunit alpha%2C mitochondrial	
+P16387	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphoserine%3B by PDK1 and PDK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18180296;Dbxref=PMID:15665377,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198,PMID:18180296	
+P16387	UniProtKB	Sequence conflict	76	76	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P16547 1 393
+P16547	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000058041;Note=Mitochondrial outer membrane protein OM45	
+P16547	UniProtKB	Topological domain	1	4	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16547	UniProtKB	Transmembrane	5	22	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16547	UniProtKB	Topological domain	23	393	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16547	UniProtKB	Sequence conflict	51	51	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06810 1 360
+Q06810	UniProtKB	Chain	1	360	.	.	.	ID=PRO_0000268694;Note=Protein OPY2	
+Q06810	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06810	UniProtKB	Region	266	345	.	.	.	Note=STE50-binding	
+Q06810	UniProtKB	Compositional bias	2	86	.	.	.	Note=Ser-rich	
+Q06810	UniProtKB	Compositional bias	147	159	.	.	.	Note=Asp-rich	
+Q06810	UniProtKB	Modified residue	285	285	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06810	UniProtKB	Modified residue	348	348	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06810	UniProtKB	Glycosylation	172	172	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06810	UniProtKB	Glycosylation	185	185	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06810	UniProtKB	Sequence conflict	234	234	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P54784 1 914
+P54784	UniProtKB	Chain	1	914	.	.	.	ID=PRO_0000127074;Note=Origin recognition complex subunit 1	
+P54784	UniProtKB	Domain	48	188	.	.	.	Note=BAH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370	
+P54784	UniProtKB	Nucleotide binding	479	486	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54784	UniProtKB	Nucleotide binding	726	733	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54784	UniProtKB	Compositional bias	281	292	.	.	.	Note=Poly-Glu	
+P54784	UniProtKB	Compositional bias	759	768	.	.	.	Note=Poly-Asp	
+P54784	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P54784	UniProtKB	Helix	6	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Beta strand	11	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Beta strand	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Beta strand	38	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Turn	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Beta strand	55	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Turn	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Beta strand	65	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Turn	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Beta strand	83	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Helix	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Helix	98	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Helix	107	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Helix	116	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Beta strand	131	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Beta strand	146	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Helix	155	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Helix	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Turn	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Beta strand	170	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Turn	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZBX	
+P54784	UniProtKB	Beta strand	182	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZBX	
+P54784	UniProtKB	Helix	189	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+P54784	UniProtKB	Helix	201	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z	
+##sequence-region Q99380 1 36
+Q99380	UniProtKB	Chain	1	36	.	.	.	ID=PRO_0000058093;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4	
+Q99380	UniProtKB	Topological domain	1	9	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12810948;Dbxref=PMID:12810948	
+Q99380	UniProtKB	Transmembrane	10	28	.	.	.	Note=Helical	
+Q99380	UniProtKB	Topological domain	29	36	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12810948;Dbxref=PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	18	18	.	.	.	Note=Severe growth defect%3B abolishes interaction with OST3 and STT3. M->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	18	18	.	.	.	Note=No effect on interaction between OST3 and STT3. M->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Severe growth defect%3B abolishes interaction with OST3. M->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Disrupts interaction between OST3 and STT3. M->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	20	20	.	.	.	Note=Severe growth defect. T->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	20	20	.	.	.	Note=Severe growth defect%3B abolishes interaction with OST3%3B disrupts interaction between OST3 and STT3. T->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	21	21	.	.	.	Note=Abolishes interaction with OST3 and STT3%3B disrupts interaction between OST3 and STT3. L->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	23	23	.	.	.	Note=Severe growth defect. V->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	23	23	.	.	.	Note=Severe growth defect%3B abolishes interaction with OST3%3B disrupts interaction between OST3 and STT3. V->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Severe growth defect. I->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Disrupts interaction between OST3 and STT3. I->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948	
+Q99380	UniProtKB	Mutagenesis	25	25	.	.	.	Note=Severe growth defect. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10677492;Dbxref=PMID:10677492	
+Q99380	UniProtKB	Helix	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RKL	
+Q99380	UniProtKB	Helix	9	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RKL	
+##sequence-region P53136 1 463
+P53136	UniProtKB	Chain	1	463	.	.	.	ID=PRO_0000202748;Note=Ribosome biogenesis protein NSA1	
+P53136	UniProtKB	Beta strand	1	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Helix	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	12	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	33	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Helix	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	47	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	57	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Turn	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	66	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	102	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Helix	120	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUM	
+P53136	UniProtKB	Beta strand	140	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	154	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	162	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	173	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	188	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	198	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	203	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	212	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	226	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	248	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	269	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	277	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Turn	284	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	291	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Helix	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	303	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Helix	328	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	332	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	342	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	351	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Turn	357	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	366	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Turn	371	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	374	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	383	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Turn	389	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	394	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+P53136	UniProtKB	Beta strand	404	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI	
+##sequence-region P52891 1 726
+P52891	UniProtKB	Chain	1	726	.	.	.	ID=PRO_0000204884;Note=Nucleoporin NUP84	
+P52891	UniProtKB	Coiled coil	563	583	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52891	UniProtKB	Helix	8	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	12	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	36	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	61	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	102	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	114	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	145	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	171	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	193	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	206	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Turn	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	225	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Turn	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Beta strand	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	240	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Beta strand	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	258	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	274	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	282	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	310	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	324	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	336	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	344	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	356	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	383	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	406	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	426	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	429	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P52891	UniProtKB	Helix	437	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+##sequence-region P07991 1 424
+P07991	UniProtKB	Chain	1	424	.	.	.	ID=PRO_0000120499;Note=Ornithine aminotransferase	
+P07991	UniProtKB	Modified residue	272	272	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07991	UniProtKB	Cross-link	390	390	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P07991	UniProtKB	Sequence conflict	8	8	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07991	UniProtKB	Sequence conflict	8	8	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07991	UniProtKB	Sequence conflict	38	38	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07991	UniProtKB	Sequence conflict	38	38	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07991	UniProtKB	Sequence conflict	99	99	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07991	UniProtKB	Sequence conflict	212	212	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07991	UniProtKB	Sequence conflict	385	385	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P20967 1 1014
+P20967	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20967	UniProtKB	Chain	31	1014	.	.	.	ID=PRO_0000020436;Note=2-oxoglutarate dehydrogenase%2C mitochondrial	
+P20967	UniProtKB	Sequence conflict	325	327	.	.	.	Note=SEF->LNL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20967	UniProtKB	Sequence conflict	513	513	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20967	UniProtKB	Sequence conflict	568	568	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P16451 1 410
+P16451	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2682658;Dbxref=PMID:2682658	
+P16451	UniProtKB	Chain	31	410	.	.	.	ID=PRO_0000020487;Note=Pyruvate dehydrogenase complex protein X component%2C mitochondrial	
+P16451	UniProtKB	Domain	32	108	.	.	.	Note=Lipoyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066	
+P16451	UniProtKB	Domain	169	210	.	.	.	Note=Peripheral subunit-binding (PSBD);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01170	
+P16451	UniProtKB	Modified residue	73	73	.	.	.	Note=N6-lipoyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066	
+P16451	UniProtKB	Sequence conflict	378	378	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06668 1 471
+Q06668	UniProtKB	Transit peptide	1	39	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06668	UniProtKB	Chain	40	471	.	.	.	ID=PRO_0000268693;Note=Methyltransferase OMS1%2C mitochondrial	
+Q06668	UniProtKB	Topological domain	40	103	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355998;Dbxref=PMID:15355998	
+Q06668	UniProtKB	Transmembrane	104	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06668	UniProtKB	Topological domain	124	471	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355998;Dbxref=PMID:15355998	
+##sequence-region A0A023PZI1 1 117
+A0A023PZI1	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000431061;Note=Putative uncharacterized protein OPI11	
+##sequence-region P87286 1 144
+P87286	UniProtKB	Chain	1	144	.	.	.	ID=PRO_0000299777;Note=Putative uncharacterized protein OPI7	
+P87286	UniProtKB	Compositional bias	9	82	.	.	.	Note=Ser-rich	
+##sequence-region P38271 1 328
+P38271	UniProtKB	Chain	1	328	.	.	.	ID=PRO_0000058074;Note=Protein OPY1	
+P38271	UniProtKB	Domain	215	318	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+##sequence-region Q02630 1 1113
+Q02630	UniProtKB	Chain	1	1113	.	.	.	ID=PRO_0000204835;Note=Nucleoporin NUP116/NSP116	
+Q02630	UniProtKB	Repeat	2	3	.	.	.	Note=FG 1	
+Q02630	UniProtKB	Repeat	17	18	.	.	.	Note=FG 2	
+Q02630	UniProtKB	Repeat	24	25	.	.	.	Note=FG 3	
+Q02630	UniProtKB	Repeat	40	41	.	.	.	Note=FG 4	
+Q02630	UniProtKB	Repeat	55	58	.	.	.	Note=GLFG 1%3B approximate	
+Q02630	UniProtKB	Repeat	66	67	.	.	.	Note=FG 5	
+Q02630	UniProtKB	Repeat	79	80	.	.	.	Note=FG 6	
+Q02630	UniProtKB	Repeat	94	95	.	.	.	Note=FG 7	
+Q02630	UniProtKB	Repeat	167	168	.	.	.	Note=FG 8	
+Q02630	UniProtKB	Repeat	189	190	.	.	.	Note=FG 9	
+Q02630	UniProtKB	Repeat	205	208	.	.	.	Note=GLFG 2	
+Q02630	UniProtKB	Repeat	214	217	.	.	.	Note=GLFG 3%3B approximate	
+Q02630	UniProtKB	Repeat	224	227	.	.	.	Note=GLFG 4%3B approximate	
+Q02630	UniProtKB	Repeat	235	238	.	.	.	Note=GLFG 5	
+Q02630	UniProtKB	Repeat	249	250	.	.	.	Note=FG 10	
+Q02630	UniProtKB	Repeat	259	262	.	.	.	Note=GLFG 6	
+Q02630	UniProtKB	Repeat	276	279	.	.	.	Note=GLFG 7	
+Q02630	UniProtKB	Repeat	288	291	.	.	.	Note=GLFG 8	
+Q02630	UniProtKB	Repeat	297	298	.	.	.	Note=FG 11	
+Q02630	UniProtKB	Repeat	306	309	.	.	.	Note=GLFG 9%3B approximate	
+Q02630	UniProtKB	Repeat	327	330	.	.	.	Note=GLFG 10%3B approximate	
+Q02630	UniProtKB	Repeat	339	342	.	.	.	Note=GLFG 11%3B approximate	
+Q02630	UniProtKB	Repeat	351	352	.	.	.	Note=FG 12	
+Q02630	UniProtKB	Repeat	359	362	.	.	.	Note=GLFG 12	
+Q02630	UniProtKB	Repeat	370	371	.	.	.	Note=FG 13	
+Q02630	UniProtKB	Repeat	382	385	.	.	.	Note=GLFG 13	
+Q02630	UniProtKB	Repeat	395	398	.	.	.	Note=GLFG 14	
+Q02630	UniProtKB	Repeat	407	410	.	.	.	Note=GLFG 15	
+Q02630	UniProtKB	Repeat	420	423	.	.	.	Note=GLFG 16	
+Q02630	UniProtKB	Repeat	431	432	.	.	.	Note=FG 14	
+Q02630	UniProtKB	Repeat	439	442	.	.	.	Note=GLFG 17	
+Q02630	UniProtKB	Repeat	448	451	.	.	.	Note=GLFG 18	
+Q02630	UniProtKB	Repeat	470	471	.	.	.	Note=FG 15	
+Q02630	UniProtKB	Repeat	482	485	.	.	.	Note=GLFG 19	
+Q02630	UniProtKB	Repeat	497	500	.	.	.	Note=GLFG 20	
+Q02630	UniProtKB	Repeat	510	511	.	.	.	Note=FG 16	
+Q02630	UniProtKB	Repeat	525	526	.	.	.	Note=FG 17	
+Q02630	UniProtKB	Repeat	532	533	.	.	.	Note=FG 18	
+Q02630	UniProtKB	Repeat	572	575	.	.	.	Note=GLFG 21	
+Q02630	UniProtKB	Repeat	585	588	.	.	.	Note=GLFG 22	
+Q02630	UniProtKB	Repeat	604	607	.	.	.	Note=GLFG 23	
+Q02630	UniProtKB	Repeat	616	617	.	.	.	Note=FG 19	
+Q02630	UniProtKB	Repeat	630	633	.	.	.	Note=GLFG 24%3B approximate	
+Q02630	UniProtKB	Repeat	648	651	.	.	.	Note=GLFG 25	
+Q02630	UniProtKB	Repeat	665	668	.	.	.	Note=GLFG 26	
+Q02630	UniProtKB	Repeat	683	686	.	.	.	Note=GLFG 27	
+Q02630	UniProtKB	Domain	967	1109	.	.	.	Note=Peptidase S59;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00765	
+Q02630	UniProtKB	Region	110	166	.	.	.	Note=GLE2 binding sequence (GLEBS)	
+Q02630	UniProtKB	Region	160	362	.	.	.	Note=Interaction with MEX67%2C not KAP95;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11104765;Dbxref=PMID:11104765	
+Q02630	UniProtKB	Region	362	535	.	.	.	Note=Sufficient for interaction with MEX67 and KAP95;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11104765;Dbxref=PMID:11104765	
+Q02630	UniProtKB	Region	536	732	.	.	.	Note=Interaction with KAP95%2C not MEX67	
+Q02630	UniProtKB	Region	967	1113	.	.	.	Note=Interaction with NUP82 NPC subcomplex	
+Q02630	UniProtKB	Region	969	1108	.	.	.	Note=Nucleoporin RNA-binding motif (NRM)	
+Q02630	UniProtKB	Compositional bias	27	50	.	.	.	Note=Gln-rich	
+Q02630	UniProtKB	Compositional bias	27	32	.	.	.	Note=Poly-Gln	
+Q02630	UniProtKB	Compositional bias	164	712	.	.	.	Note=Gly-rich	
+Q02630	UniProtKB	Compositional bias	263	304	.	.	.	Note=Asn-rich	
+Q02630	UniProtKB	Compositional bias	280	567	.	.	.	Note=Gln-rich	
+Q02630	UniProtKB	Compositional bias	475	478	.	.	.	Note=Poly-Gln	
+Q02630	UniProtKB	Compositional bias	669	707	.	.	.	Note=Asn-rich	
+Q02630	UniProtKB	Compositional bias	669	672	.	.	.	Note=Poly-Asn	
+Q02630	UniProtKB	Compositional bias	716	740	.	.	.	Note=Gln-rich	
+Q02630	UniProtKB	Compositional bias	729	735	.	.	.	Note=Poly-Gln	
+Q02630	UniProtKB	Modified residue	886	886	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02630	UniProtKB	Sequence conflict	26	26	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02630	UniProtKB	Sequence conflict	536	536	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02630	UniProtKB	Sequence conflict	720	720	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02630	UniProtKB	Sequence conflict	1018	1018	.	.	.	Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02630	UniProtKB	Sequence conflict	1023	1023	.	.	.	Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02630	UniProtKB	Beta strand	970	974	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Helix	976	981	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Beta strand	988	990	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Beta strand	994	997	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Turn	998	1000	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Beta strand	1001	1007	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Turn	1019	1022	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Beta strand	1023	1027	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Beta strand	1030	1034	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Beta strand	1042	1044	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AIV	
+Q02630	UniProtKB	Beta strand	1051	1056	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Turn	1063	1065	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Helix	1075	1084	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Beta strand	1088	1095	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Turn	1097	1099	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+Q02630	UniProtKB	Beta strand	1102	1107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+##sequence-region P33895 1 451
+P33895	UniProtKB	Chain	1	451	.	.	.	ID=PRO_0000057995;Note=Kinetochore protein NUF2	
+P33895	UniProtKB	Coiled coil	153	291	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33895	UniProtKB	Coiled coil	341	371	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33895	UniProtKB	Coiled coil	398	432	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33895	UniProtKB	Mutagenesis	338	338	.	.	.	Note=Temperature-sensitive. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751	
+P33895	UniProtKB	Mutagenesis	340	340	.	.	.	Note=Temperature-sensitive. I->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751	
+P33895	UniProtKB	Mutagenesis	383	383	.	.	.	Note=Temperature-sensitive. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751	
+P33895	UniProtKB	Mutagenesis	410	410	.	.	.	Note=Temperature-sensitive. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751	
+P33895	UniProtKB	Mutagenesis	441	441	.	.	.	Note=Temperature-sensitive. K->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751	
+P33895	UniProtKB	Mutagenesis	446	446	.	.	.	Note=Temperature-sensitive. M->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751	
+P33895	UniProtKB	Sequence conflict	240	240	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33895	UniProtKB	Beta strand	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P33895	UniProtKB	Helix	13	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P33895	UniProtKB	Turn	30	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P33895	UniProtKB	Helix	40	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P33895	UniProtKB	Helix	57	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P33895	UniProtKB	Beta strand	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P33895	UniProtKB	Helix	79	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P33895	UniProtKB	Helix	109	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P33895	UniProtKB	Helix	116	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P33895	UniProtKB	Helix	407	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+##sequence-region Q12255 1 253
+Q12255	UniProtKB	Chain	1	253	.	.	.	ID=PRO_0000206780;Note=Vacuolar v-SNARE NYV1	
+Q12255	UniProtKB	Topological domain	1	231	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12255	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12255	UniProtKB	Topological domain	253	253	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12255	UniProtKB	Domain	167	227	.	.	.	Note=v-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00290	
+Q12255	UniProtKB	Beta strand	7	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0	
+Q12255	UniProtKB	Beta strand	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0	
+Q12255	UniProtKB	Beta strand	26	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0	
+Q12255	UniProtKB	Helix	43	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0	
+Q12255	UniProtKB	Helix	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0	
+Q12255	UniProtKB	Beta strand	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0	
+Q12255	UniProtKB	Beta strand	74	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0	
+Q12255	UniProtKB	Beta strand	90	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0	
+Q12255	UniProtKB	Helix	104	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0	
+Q12255	UniProtKB	Helix	124	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0	
+Q12255	UniProtKB	Turn	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0	
+##sequence-region P25366 1 362
+P25366	UniProtKB	Chain	1	362	.	.	.	ID=PRO_0000202581;Note=Protein OCA4	
+##sequence-region P19262 1 463
+P19262	UniProtKB	Domain	73	148	.	.	.	Note=Lipoyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066	
+P19262	UniProtKB	Repeat	185	190	.	.	.	Note=1	
+P19262	UniProtKB	Repeat	191	196	.	.	.	Note=2	
+P19262	UniProtKB	Repeat	197	202	.	.	.	Note=3	
+P19262	UniProtKB	Repeat	204	209	.	.	.	Note=4%3B approximate	
+P19262	UniProtKB	Region	185	209	.	.	.	Note=4 X 6 AA approximate tandem repeats of A-[SP]-K-K-E-[AV]	
+P19262	UniProtKB	Active site	435	435	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19262	UniProtKB	Active site	439	439	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19262	UniProtKB	Modified residue	114	114	.	.	.	Note=N6-lipoyllysine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066	
+P19262	UniProtKB	Modified residue	340	340	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P19262	UniProtKB	Sequence conflict	170	208	.	.	.	Note=PSQGVAARENSSEETASKKEAAPKKEAAPKKEVTEPKKA->HRKVSPQGKTQVRKRLQRKKLLQRKKPLQRKKLQNQKRT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19262	UniProtKB	Sequence conflict	441	445	.	.	.	Note=REAVT->EKLLS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19262	UniProtKB	Sequence conflict	460	463	.	.	.	Note=MLLW->CCYGDLKFAAHTNLIS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P12695 1 482
+P12695	UniProtKB	Transit peptide	1	28	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3050999;Dbxref=PMID:3050999	
+P12695	UniProtKB	Chain	29	482	.	.	.	ID=PRO_0000020483;Note=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex%2C mitochondrial	
+P12695	UniProtKB	Domain	34	110	.	.	.	Note=Lipoyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066	
+P12695	UniProtKB	Domain	175	212	.	.	.	Note=Peripheral subunit-binding (PSBD);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01170	
+P12695	UniProtKB	Active site	455	455	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12695	UniProtKB	Active site	459	459	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12695	UniProtKB	Modified residue	75	75	.	.	.	Note=N6-lipoyllysine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01066,ECO:0000269|PubMed:3050999;Dbxref=PMID:3050999	
+##sequence-region P54790 1 616
+P54790	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P54790	UniProtKB	Chain	2	616	.	.	.	ID=PRO_0000127086;Note=Origin recognition complex subunit 3	
+P54790	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q12375 1 292
+Q12375	UniProtKB	Chain	1	292	.	.	.	ID=PRO_0000090684;Note=Mitochondrial ornithine transporter 1	
+Q12375	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12375	UniProtKB	Transmembrane	69	89	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12375	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12375	UniProtKB	Transmembrane	171	187	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12375	UniProtKB	Transmembrane	213	233	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12375	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12375	UniProtKB	Repeat	11	97	.	.	.	Note=Solcar 1	
+Q12375	UniProtKB	Repeat	105	196	.	.	.	Note=Solcar 2	
+Q12375	UniProtKB	Repeat	211	292	.	.	.	Note=Solcar 3	
+Q12375	UniProtKB	Sequence conflict	105	105	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12375	UniProtKB	Sequence conflict	105	105	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12375	UniProtKB	Sequence conflict	105	105	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P48439 1 350
+P48439	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7622558;Dbxref=PMID:7622558	
+P48439	UniProtKB	Chain	23	350	.	.	.	ID=PRO_0000020275;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3	
+P48439	UniProtKB	Transmembrane	186	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48439	UniProtKB	Transmembrane	218	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48439	UniProtKB	Transmembrane	272	288	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48439	UniProtKB	Transmembrane	310	329	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48439	UniProtKB	Domain	29	171	.	.	.	Note=Thioredoxin	
+P48439	UniProtKB	Disulfide bond	73	76	.	.	.	Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P05150 1 338
+P05150	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P05150	UniProtKB	Chain	2	338	.	.	.	ID=PRO_0000113082;Note=Ornithine carbamoyltransferase	
+P05150	UniProtKB	Region	67	71	.	.	.	Note=Ornithine and carbamoyl phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05150	UniProtKB	Region	145	148	.	.	.	Note=Ornithine and carbamoyl phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05150	UniProtKB	Region	249	253	.	.	.	Note=Ornithine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05150	UniProtKB	Region	288	291	.	.	.	Note=Ornithine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05150	UniProtKB	Active site	289	289	.	.	.	.	
+P05150	UniProtKB	Binding site	118	118	.	.	.	Note=Carbamoyl phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05150	UniProtKB	Binding site	118	118	.	.	.	Note=Ornithine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05150	UniProtKB	Binding site	145	145	.	.	.	Note=Carbamoyl phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05150	UniProtKB	Binding site	185	185	.	.	.	Note=Ornithine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05150	UniProtKB	Binding site	316	316	.	.	.	Note=Carbamoyl phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05150	UniProtKB	Binding site	316	316	.	.	.	Note=Ornithine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05150	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P05150	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Reduces activity by 95%25. Reduces affinity for ornithine 2-fold. T->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340	
+P05150	UniProtKB	Mutagenesis	181	181	.	.	.	Note=Loss of activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340	
+P05150	UniProtKB	Mutagenesis	182	182	.	.	.	Note=Reduces activity by 33%25. Reduces affinity for ornithine 30-fold. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340	
+P05150	UniProtKB	Mutagenesis	184	184	.	.	.	Note=Reduces activity by 50%25. Reduces affinity for ornithine 20-fold. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340	
+P05150	UniProtKB	Mutagenesis	185	185	.	.	.	Note=No effect on activity. Reduces affinity for ornithine 200-fold. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340	
+P05150	UniProtKB	Mutagenesis	256	256	.	.	.	Note=Reduces activity by 50%25. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340	
+P05150	UniProtKB	Mutagenesis	263	263	.	.	.	Note=Reduces activity by 70%25. Reduces affinity for ornithine 18-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340	
+P05150	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Reduces activity by 90%25. Reduces affinity for ornithine 6-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340	
+P05150	UniProtKB	Mutagenesis	290	290	.	.	.	Note=Reduces activity by 86%25. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340	
+##sequence-region P52593 1 1655
+P52593	UniProtKB	Chain	1	1655	.	.	.	ID=PRO_0000204856;Note=Nucleoporin NUP188	
+P52593	UniProtKB	Region	250	271	.	.	.	Note=Leucine-zipper	
+P52593	UniProtKB	Coiled coil	35	62	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52593	UniProtKB	Compositional bias	485	489	.	.	.	Note=Poly-Ser	
+P52593	UniProtKB	Compositional bias	533	545	.	.	.	Note=Gln-rich	
+P52593	UniProtKB	Compositional bias	533	541	.	.	.	Note=Poly-Gln	
+P52593	UniProtKB	Compositional bias	1385	1391	.	.	.	Note=Poly-Leu	
+P52593	UniProtKB	Compositional bias	1504	1507	.	.	.	Note=Poly-Leu	
+P52593	UniProtKB	Modified residue	340	340	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P52593	UniProtKB	Cross-link	406	406	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q02803 1 292
+Q02803	UniProtKB	Chain	1	292	.	.	.	ID=PRO_0000220871;Note=Ornithine decarboxylase antizyme	
+##sequence-region P21957 1 404
+P21957	UniProtKB	Chain	1	404	.	.	.	ID=PRO_0000058061;Note=Transcriptional repressor OPI1	
+P21957	UniProtKB	Region	109	138	.	.	.	Note=Basic motif	
+P21957	UniProtKB	Region	139	160	.	.	.	Note=Leucine-zipper	
+P21957	UniProtKB	Motif	200	206	.	.	.	Note=FFAT	
+P21957	UniProtKB	Compositional bias	89	93	.	.	.	Note=Poly-Asp	
+P21957	UniProtKB	Compositional bias	193	198	.	.	.	Note=Poly-Asp	
+P21957	UniProtKB	Compositional bias	286	298	.	.	.	Note=Poly-Gln	
+P21957	UniProtKB	Compositional bias	306	310	.	.	.	Note=Poly-Gln	
+P21957	UniProtKB	Compositional bias	377	381	.	.	.	Note=Poly-Gln	
+P21957	UniProtKB	Compositional bias	384	387	.	.	.	Note=Poly-Gln	
+P21957	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P54791 1 529
+P54791	UniProtKB	Chain	1	529	.	.	.	ID=PRO_0000127091;Note=Origin recognition complex subunit 4	
+P54791	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P33400 1 625
+P33400	UniProtKB	Chain	1	625	.	.	.	ID=PRO_0000046847;Note=pH-response transcription factor pacC/RIM101	
+P33400	UniProtKB	Zinc finger	146	171	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P33400	UniProtKB	Zinc finger	182	206	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P33400	UniProtKB	Zinc finger	212	234	.	.	.	Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P33400	UniProtKB	Motif	228	234	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33400	UniProtKB	Motif	450	453	.	.	.	Note=YPX[LI] motif 1	
+P33400	UniProtKB	Motif	620	623	.	.	.	Note=YPX[LI] motif 2	
+P33400	UniProtKB	Compositional bias	76	120	.	.	.	Note=Ser-rich	
+P33400	UniProtKB	Compositional bias	131	140	.	.	.	Note=Poly-Asp	
+P33400	UniProtKB	Compositional bias	579	601	.	.	.	Note=Asp/Glu-rich (acidic)	
+P33400	UniProtKB	Mutagenesis	153	153	.	.	.	Note=Abolishes transcriptional activation of target genes. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8367297;Dbxref=PMID:8367297	
+P33400	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Abolishes transcriptional activation of target genes. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8367297;Dbxref=PMID:8367297	
+P33400	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Abolishes transcriptional activation of target genes. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8367297;Dbxref=PMID:8367297	
+P33400	UniProtKB	Mutagenesis	255	255	.	.	.	Note=Reduces transcriptional activation of target genes. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8367297;Dbxref=PMID:8367297	
+P33400	UniProtKB	Sequence conflict	68	68	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33400	UniProtKB	Sequence conflict	90	90	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33400	UniProtKB	Sequence conflict	111	111	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33400	UniProtKB	Sequence conflict	249	249	.	.	.	Note=W->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33400	UniProtKB	Sequence conflict	261	261	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33400	UniProtKB	Sequence conflict	276	276	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33400	UniProtKB	Sequence conflict	308	308	.	.	.	Note=Q->QQQQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33400	UniProtKB	Sequence conflict	358	358	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33400	UniProtKB	Sequence conflict	486	486	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33400	UniProtKB	Sequence conflict	519	519	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38351 1 445
+P38351	UniProtKB	Chain	1	445	.	.	.	ID=PRO_0000058174;Note=RNA polymerase II-associated protein 1	
+P38351	UniProtKB	Compositional bias	363	445	.	.	.	Note=Asp/Glu-rich (acidic)	
+P38351	UniProtKB	Modified residue	147	147	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38351	UniProtKB	Modified residue	422	422	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q12033 1 661
+Q12033	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12033	UniProtKB	Chain	2	661	.	.	.	ID=PRO_0000218885;Note=pH-response regulator protein palA/RIM20	
+Q12033	UniProtKB	Domain	3	371	.	.	.	Note=BRO1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00526	
+Q12033	UniProtKB	Coiled coil	388	422	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12033	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12033	UniProtKB	Mutagenesis	292	293	.	.	.	Note=In RIM20-292%3B prevents cleavage of RIM101. DN->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11698381;Dbxref=PMID:11698381	
+##sequence-region P37304 1 830
+P37304	UniProtKB	Chain	1	830	.	.	.	ID=PRO_0000058220;Note=Protein PAM1	
+P37304	UniProtKB	Coiled coil	379	400	.	.	.	.	
+P37304	UniProtKB	Coiled coil	481	514	.	.	.	.	
+P37304	UniProtKB	Compositional bias	515	522	.	.	.	Note=Poly-Gln	
+P37304	UniProtKB	Compositional bias	810	830	.	.	.	Note=Arg/Lys-rich (highly basic)	
+P37304	UniProtKB	Modified residue	659	659	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P37304	UniProtKB	Modified residue	732	732	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P37304	UniProtKB	Modified residue	767	767	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P37304	UniProtKB	Sequence conflict	256	256	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53010 1 1115
+P53010	UniProtKB	Chain	1	1115	.	.	.	ID=PRO_0000058222;Note=PAN2-PAN3 deadenylation complex catalytic subunit PAN2	
+P53010	UniProtKB	Repeat	27	66	.	.	.	Note=WD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182	
+P53010	UniProtKB	Repeat	112	153	.	.	.	Note=WD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182	
+P53010	UniProtKB	Repeat	155	194	.	.	.	Note=WD 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182	
+P53010	UniProtKB	Repeat	197	236	.	.	.	Note=WD 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182	
+P53010	UniProtKB	Repeat	295	334	.	.	.	Note=WD 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182	
+P53010	UniProtKB	Domain	474	855	.	.	.	Note=USP;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03182,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344	
+P53010	UniProtKB	Domain	907	1079	.	.	.	Note=Exonuclease;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182	
+P53010	UniProtKB	Region	337	473	.	.	.	Note=Linker;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03182,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344	
+P53010	UniProtKB	Metal binding	660	660	.	.	.	Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4Q8G,ECO:0000269|PubMed:24880344;Dbxref=PMID:24880344	
+P53010	UniProtKB	Metal binding	662	662	.	.	.	Note=Zinc%3B via pros nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4Q8G,ECO:0000269|PubMed:24880344;Dbxref=PMID:24880344	
+P53010	UniProtKB	Metal binding	713	713	.	.	.	Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4Q8G,ECO:0000269|PubMed:24880344;Dbxref=PMID:24880344	
+P53010	UniProtKB	Metal binding	716	716	.	.	.	Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4Q8G,ECO:0000269|PubMed:24880344;Dbxref=PMID:24880344	
+P53010	UniProtKB	Metal binding	910	910	.	.	.	Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000305;evidence=ECO:0000250|UniProtKB:O95453,ECO:0000255|HAMAP-Rule:MF_03182,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344	
+P53010	UniProtKB	Metal binding	912	912	.	.	.	Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000305;evidence=ECO:0000250|UniProtKB:O95453,ECO:0000255|HAMAP-Rule:MF_03182,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344	
+P53010	UniProtKB	Metal binding	1020	1020	.	.	.	Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:O95453,ECO:0000255|HAMAP-Rule:MF_03182	
+P53010	UniProtKB	Metal binding	1071	1071	.	.	.	Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000305;evidence=ECO:0000250|UniProtKB:O95453,ECO:0000255|HAMAP-Rule:MF_03182,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344	
+P53010	UniProtKB	Mutagenesis	912	912	.	.	.	Note=Abolishes nuclease activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24872509;Dbxref=PMID:24872509	
+P53010	UniProtKB	Mutagenesis	1020	1020	.	.	.	Note=Abolishes nuclease activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24880344;Dbxref=PMID:24880344	
+P53010	UniProtKB	Turn	460	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	477	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	488	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	497	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	502	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Turn	512	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	516	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	527	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	546	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	560	562	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	568	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	595	600	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Turn	603	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Beta strand	610	613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	618	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	637	639	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	643	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	650	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	659	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	666	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	696	703	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	704	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Turn	714	716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	719	728	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	733	739	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	743	751	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	752	754	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Beta strand	758	765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	768	774	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	775	777	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	782	797	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	803	813	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Turn	814	817	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	818	825	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	828	832	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	834	838	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Beta strand	845	854	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	857	859	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G	
+P53010	UniProtKB	Helix	865	867	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	873	876	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	897	899	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Beta strand	906	915	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Beta strand	937	946	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Beta strand	948	950	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Turn	951	954	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Beta strand	956	962	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	973	976	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Beta strand	983	986	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Turn	988	990	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Turn	994	996	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	997	1008	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Beta strand	1011	1013	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	1017	1024	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	1030	1032	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	1036	1039	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	1049	1056	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	1068	1087	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+P53010	UniProtKB	Helix	1091	1105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H	
+##sequence-region P36102 1 679
+P36102	UniProtKB	Chain	1	679	.	.	.	ID=PRO_0000058223;Note=PAN2-PAN3 deadenylation complex subunit PAN3	
+P36102	UniProtKB	Zinc finger	8	37	.	.	.	Note=C3H1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03181	
+P36102	UniProtKB	Nucleotide binding	376	383	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03181	
+P36102	UniProtKB	Nucleotide binding	430	431	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03181	
+P36102	UniProtKB	Region	275	548	.	.	.	Note=Pseudokinase domain;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03181,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344	
+P36102	UniProtKB	Region	588	679	.	.	.	Note=Knob domain;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03181,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344	
+P36102	UniProtKB	Coiled coil	549	587	.	.	.	Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03181,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344	
+P36102	UniProtKB	Motif	143	163	.	.	.	Note=PABPC-interacting motif-2 (PAM-2);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17595167;Dbxref=PMID:17595167	
+P36102	UniProtKB	Binding site	325	325	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03181	
+P36102	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36102	UniProtKB	Modified residue	252	252	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36102	UniProtKB	Mutagenesis	156	156	.	.	.	Note=Significantly decreases interaction with PAN1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17595167;Dbxref=PMID:17595167	
+P36102	UniProtKB	Helix	6	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CYK	
+P36102	UniProtKB	Helix	15	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CYK	
+P36102	UniProtKB	Helix	24	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CYK	
+##sequence-region Q03050 1 120
+Q03050	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03050	UniProtKB	Chain	21	120	.	.	.	ID=PRO_0000253888;Note=Seripauperin-10	
+##sequence-region P0CE89 1 120
+P0CE89	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE89	UniProtKB	Chain	21	120	.	.	.	ID=PRO_0000392929;Note=Seripauperin-14	
+P0CE89	UniProtKB	Sequence conflict	84	84	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CE88 1 120
+P0CE88	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE88	UniProtKB	Chain	21	120	.	.	.	ID=PRO_0000203778;Note=Seripauperin-1	
+P0CE88	UniProtKB	Sequence conflict	25	25	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CE88	UniProtKB	Sequence conflict	84	84	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CE88	UniProtKB	Sequence conflict	100	100	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CE88	UniProtKB	Sequence conflict	108	108	.	.	.	Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07987 1 124
+Q07987	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07987	UniProtKB	Chain	21	124	.	.	.	ID=PRO_0000033241;Note=Seripauperin-23	
+##sequence-region P0CE90 1 120
+P0CE90	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE90	UniProtKB	Chain	21	120	.	.	.	ID=PRO_0000203783;Note=Seripauperin-6	
+##sequence-region P53298 1 406
+P53298	UniProtKB	Chain	1	406	.	.	.	ID=PRO_0000058039;Note=Central kinetochore subunit OKP1	
+P53298	UniProtKB	Coiled coil	239	285	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53298	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P28273 1 1286
+P28273	UniProtKB	Chain	1	1286	.	.	.	ID=PRO_0000208582;Note=5-oxoprolinase	
+P28273	UniProtKB	Modified residue	930	930	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P28273	UniProtKB	Modified residue	1077	1077	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P28273	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Impairs ATPase and 5-oxoprolinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20402795;Dbxref=PMID:20402795	
+P28273	UniProtKB	Mutagenesis	324	324	.	.	.	Note=Impairs ATPase and 5-oxoprolinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20402795;Dbxref=PMID:20402795	
+P28273	UniProtKB	Mutagenesis	497	497	.	.	.	Note=Impairs ATPase and 5-oxoprolinase activity%3B when associated with A-498. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20402795;Dbxref=PMID:20402795	
+P28273	UniProtKB	Mutagenesis	498	498	.	.	.	Note=Impairs ATPase and 5-oxoprolinase activity%3B when associated with A-497. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20402795;Dbxref=PMID:20402795	
+##sequence-region P40897 1 799
+P40897	UniProtKB	Chain	1	799	.	.	.	ID=PRO_0000213788;Note=Oligopeptide transporter 1	
+P40897	UniProtKB	Topological domain	1	108	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	130	135	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	157	177	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	178	198	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	199	210	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	211	231	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	232	276	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	277	297	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	298	313	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	314	334	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	335	359	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	360	380	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	381	428	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	429	449	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	450	482	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	483	503	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	504	508	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	509	529	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	530	540	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	541	561	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	562	590	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	591	611	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	612	659	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	660	680	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	681	736	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Transmembrane	737	757	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Topological domain	758	799	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40897	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40897	UniProtKB	Modified residue	51	51	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40897	UniProtKB	Glycosylation	46	46	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40897	UniProtKB	Glycosylation	640	640	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32833 1 620
+P32833	UniProtKB	Chain	1	620	.	.	.	ID=PRO_0000127082;Note=Origin recognition complex subunit 2	
+P32833	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32833	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32833	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P33751 1 242
+P33751	UniProtKB	Transit peptide	1	58	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197	
+P33751	UniProtKB	Chain	59	242	.	.	.	ID=PRO_0000134984;Note=Flavin prenyltransferase PAD1%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197	
+P33751	UniProtKB	Nucleotide binding	63	65	.	.	.	Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197	
+P33751	UniProtKB	Nucleotide binding	140	143	.	.	.	Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197	
+P33751	UniProtKB	Binding site	89	89	.	.	.	Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197	
+P33751	UniProtKB	Binding site	175	175	.	.	.	Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197	
+P33751	UniProtKB	Binding site	205	205	.	.	.	Note=DMAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197	
+P33751	UniProtKB	Binding site	221	221	.	.	.	Note=DMAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197	
+P33751	UniProtKB	Sequence conflict	76	76	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32567 1 862
+P32567	UniProtKB	Chain	1	862	.	.	.	ID=PRO_0000209887;Note=Phosphatidic acid phosphohydrolase 1	
+P32567	UniProtKB	Region	19	104	.	.	.	Note=N-LIP	
+P32567	UniProtKB	Motif	398	402	.	.	.	Note=DXDXT motif	
+P32567	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16968695;Dbxref=PMID:16968695	
+P32567	UniProtKB	Modified residue	114	114	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16968695;Dbxref=PMID:16968695	
+P32567	UniProtKB	Modified residue	168	168	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16968695;Dbxref=PMID:16968695	
+P32567	UniProtKB	Modified residue	511	511	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32567	UniProtKB	Modified residue	602	602	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:16968695,ECO:0000269|PubMed:21081492;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:16968695,PMID:21081492	
+P32567	UniProtKB	Modified residue	723	723	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16968695,ECO:0000269|PubMed:21081492;Dbxref=PMID:16968695,PMID:21081492	
+P32567	UniProtKB	Modified residue	744	744	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:16968695,ECO:0000269|PubMed:21081492;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:16968695,PMID:21081492	
+P32567	UniProtKB	Modified residue	748	748	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:16968695;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:16968695	
+P32567	UniProtKB	Modified residue	773	773	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32567	UniProtKB	Modified residue	774	774	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32567	UniProtKB	Modified residue	810	810	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32567	UniProtKB	Modified residue	814	814	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32567	UniProtKB	Modified residue	816	816	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32567	UniProtKB	Modified residue	844	844	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32567	UniProtKB	Modified residue	847	847	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32567	UniProtKB	Mutagenesis	8	8	.	.	.	Note=Impairs membrane recruitiment%3B when associated with A-11 and A-15. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20876142;Dbxref=PMID:20876142	
+P32567	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Impairs membrane recruitiment%3B when associated with A-8 and A-15. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20876142;Dbxref=PMID:20876142	
+P32567	UniProtKB	Mutagenesis	15	15	.	.	.	Note=Impairs membrane recruitiment%3B when associated with A-8 and A-11. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20876142;Dbxref=PMID:20876142	
+P32567	UniProtKB	Mutagenesis	80	80	.	.	.	Note=Impairs phosphatidate phosphatase activity. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17971454,ECO:0000269|PubMed:21422231;Dbxref=PMID:17971454,PMID:21422231	
+P32567	UniProtKB	Mutagenesis	398	398	.	.	.	Note=Impairs phosphatidate phosphatase activity. D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17971454,ECO:0000269|PubMed:21422231;Dbxref=PMID:17971454,PMID:21422231	
+P32567	UniProtKB	Mutagenesis	400	400	.	.	.	Note=Impairs phosphatidate phosphatase activity. D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17971454,ECO:0000269|PubMed:21422231;Dbxref=PMID:17971454,PMID:21422231	
+##sequence-region P36129 1 213
+P36129	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000203208;Note=Putative uncharacterized protein OPI8	
+##sequence-region P38826 1 435
+P38826	UniProtKB	Chain	1	435	.	.	.	ID=PRO_0000127102;Note=Origin recognition complex subunit 6	
+P38826	UniProtKB	Modified residue	146	146	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q12447 1 191
+Q12447	UniProtKB	Chain	1	191	.	.	.	ID=PRO_0000245843;Note=Polyamine N-acetyltransferase 1	
+Q12447	UniProtKB	Domain	12	179	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+##sequence-region Q05518 1 499
+Q05518	UniProtKB	Chain	1	499	.	.	.	ID=PRO_0000253820;Note=Protein PAL1	
+Q05518	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05518	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05518	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05518	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05518	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q05518	UniProtKB	Modified residue	114	114	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05518	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05518	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05518	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05518	UniProtKB	Modified residue	307	307	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05518	UniProtKB	Cross-link	135	135	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q05518	UniProtKB	Cross-link	138	138	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q05518	UniProtKB	Cross-link	292	292	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q05518	UniProtKB	Cross-link	328	328	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q05518	UniProtKB	Cross-link	445	445	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q05518	UniProtKB	Sequence conflict	227	227	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53179 1 542
+P53179	UniProtKB	Chain	1	542	.	.	.	ID=PRO_0000058194;Note=pH-response regulator protein palF/RIM8	
+P53179	UniProtKB	Compositional bias	244	250	.	.	.	Note=Poly-Ser	
+P53179	UniProtKB	Cross-link	521	521	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P48565 1 533
+P48565	UniProtKB	Chain	1	533	.	.	.	ID=PRO_0000058205;Note=pH-response regulator protein palH/RIM21	
+P48565	UniProtKB	Topological domain	1	94	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Transmembrane	95	115	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Topological domain	116	127	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Topological domain	149	178	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Topological domain	200	209	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Transmembrane	210	230	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Topological domain	231	247	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Transmembrane	248	268	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Topological domain	269	280	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Transmembrane	281	301	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Topological domain	302	307	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Transmembrane	308	328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Topological domain	329	533	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48565	UniProtKB	Modified residue	409	409	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q04734 1 239
+Q04734	UniProtKB	Chain	1	239	.	.	.	ID=PRO_0000058216;Note=pH-response regulator protein palI/RIM9	
+Q04734	UniProtKB	Topological domain	1	3	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04734	UniProtKB	Transmembrane	4	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04734	UniProtKB	Topological domain	25	90	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04734	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04734	UniProtKB	Topological domain	112	128	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04734	UniProtKB	Transmembrane	129	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04734	UniProtKB	Topological domain	150	155	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04734	UniProtKB	Transmembrane	156	176	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04734	UniProtKB	Topological domain	177	239	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36147 1 197
+P36147	UniProtKB	Transit peptide	1	14	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36147	UniProtKB	Chain	15	197	.	.	.	ID=PRO_0000043179;Note=Presequence translocated-associated motor subunit PAM17%2C mitochondrial	
+P36147	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36147	UniProtKB	Transmembrane	103	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32521 1 1480
+P32521	UniProtKB	Chain	1	1480	.	.	.	ID=PRO_0000058221;Note=Actin cytoskeleton-regulatory complex protein PAN1	
+P32521	UniProtKB	Repeat	142	153	.	.	.	Note=1-1	
+P32521	UniProtKB	Repeat	164	175	.	.	.	Note=1-2	
+P32521	UniProtKB	Repeat	188	199	.	.	.	Note=1-3	
+P32521	UniProtKB	Repeat	215	226	.	.	.	Note=1-4	
+P32521	UniProtKB	Repeat	235	246	.	.	.	Note=1-5	
+P32521	UniProtKB	Domain	270	359	.	.	.	Note=EH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077	
+P32521	UniProtKB	Repeat	328	350	.	.	.	Note=2-1	
+P32521	UniProtKB	Repeat	392	403	.	.	.	Note=1-6	
+P32521	UniProtKB	Repeat	409	420	.	.	.	Note=1-7	
+P32521	UniProtKB	Repeat	422	433	.	.	.	Note=1-8	
+P32521	UniProtKB	Repeat	446	457	.	.	.	Note=1-9	
+P32521	UniProtKB	Repeat	467	478	.	.	.	Note=1-10	
+P32521	UniProtKB	Repeat	498	509	.	.	.	Note=1-11	
+P32521	UniProtKB	Repeat	510	518	.	.	.	Note=1-12	
+P32521	UniProtKB	Repeat	538	548	.	.	.	Note=1-13	
+P32521	UniProtKB	Repeat	549	556	.	.	.	Note=1-14	
+P32521	UniProtKB	Repeat	564	575	.	.	.	Note=1-15	
+P32521	UniProtKB	Domain	600	689	.	.	.	Note=EH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077	
+P32521	UniProtKB	Repeat	658	680	.	.	.	Note=2-2	
+P32521	UniProtKB	Repeat	1084	1089	.	.	.	Note=3-1	
+P32521	UniProtKB	Repeat	1090	1095	.	.	.	Note=3-2	
+P32521	UniProtKB	Repeat	1096	1101	.	.	.	Note=3-3	
+P32521	UniProtKB	Repeat	1102	1107	.	.	.	Note=3-4	
+P32521	UniProtKB	Repeat	1108	1113	.	.	.	Note=3-5	
+P32521	UniProtKB	Repeat	1114	1119	.	.	.	Note=3-6	
+P32521	UniProtKB	Repeat	1120	1125	.	.	.	Note=3-7	
+P32521	UniProtKB	Repeat	1315	1320	.	.	.	Note=4-1	
+P32521	UniProtKB	Repeat	1321	1326	.	.	.	Note=4-2	
+P32521	UniProtKB	Repeat	1327	1332	.	.	.	Note=4-3	
+P32521	UniProtKB	Repeat	1340	1345	.	.	.	Note=4-4	
+P32521	UniProtKB	Repeat	1346	1350	.	.	.	Note=4-5	
+P32521	UniProtKB	Repeat	1355	1360	.	.	.	Note=4-6	
+P32521	UniProtKB	Repeat	1361	1366	.	.	.	Note=4-7	
+P32521	UniProtKB	Repeat	1372	1377	.	.	.	Note=4-8	
+P32521	UniProtKB	Region	142	575	.	.	.	Note=15 X 12 AA tandem repeats of [SPNAG]-[IL]-[QKNGT]-[PSA]-[QT]-[GQAPISTLYK]-T-G-[YFGML]-[YVMGAQL]-[QVLNPAG]-[ASQPN]	
+P32521	UniProtKB	Region	328	680	.	.	.	Note=2 X 23 AA repeats of F-A-L-[AG]-M-H-L-[IV]-[NY]-[DG]-[VK]-L-[QN]-G-[DK]-[TP]-I-P-[YN]-[EV]-L-[DP]-S	
+P32521	UniProtKB	Region	1084	1125	.	.	.	Note=7 X 6 AA tandem repeats of Q-[PS]-T-Q-P-V	
+P32521	UniProtKB	Region	1315	1377	.	.	.	Note=8 X 6 AA repeats of [ATVSP]-P-[LVI]-P-[SPQILA]-[VAS]	
+P32521	UniProtKB	Coiled coil	1131	1190	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32521	UniProtKB	Compositional bias	13	22	.	.	.	Note=Poly-Gln	
+P32521	UniProtKB	Compositional bias	29	34	.	.	.	Note=Poly-Gln	
+P32521	UniProtKB	Compositional bias	98	106	.	.	.	Note=Poly-Gln	
+P32521	UniProtKB	Compositional bias	1400	1406	.	.	.	Note=Poly-Pro	
+P32521	UniProtKB	Compositional bias	1452	1455	.	.	.	Note=Poly-Glu	
+P32521	UniProtKB	Compositional bias	1474	1480	.	.	.	Note=Poly-Pro	
+P32521	UniProtKB	Modified residue	241	241	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32521	UniProtKB	Modified residue	570	570	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32521	UniProtKB	Modified residue	747	747	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32521	UniProtKB	Modified residue	757	757	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32521	UniProtKB	Modified residue	993	993	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32521	UniProtKB	Modified residue	995	995	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32521	UniProtKB	Modified residue	1003	1003	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32521	UniProtKB	Modified residue	1180	1180	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32521	UniProtKB	Modified residue	1250	1250	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32521	UniProtKB	Modified residue	1253	1253	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32521	UniProtKB	Modified residue	1281	1281	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32521	UniProtKB	Modified residue	1321	1321	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32521	UniProtKB	Sequence conflict	235	235	.	.	.	Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32521	UniProtKB	Sequence conflict	266	273	.	.	.	Note=ITAQDQAK->YYCPRSGKN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32521	UniProtKB	Sequence conflict	474	487	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32521	UniProtKB	Sequence conflict	653	657	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32521	UniProtKB	Sequence conflict	1291	1291	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32521	UniProtKB	Sequence conflict	1396	1480	.	.	.	Note=GGVLPPPPPLPTQQASTSEPIIAHVDNYNGAEKGTGAYGSDSDDDVLSIPESVGTDEEEEGAQPVSTAGIPSIPPAGIPPPPPLP->EAFCLHPHLYQLNKLPLQNLLSLTLITTMVLKKARAHMDPILMMTFYRFLNQLVQMKRKKGHNQFLLQVSHQFHLQVFLHPHPFHEDLICFL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40459 1 309
+P40459	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000128298;Note=Pantoate--beta-alanine ligase	
+##sequence-region Q08202 1 246
+Q08202	UniProtKB	Chain	1	246	.	.	.	ID=PRO_0000245260;Note=Protein OPI10	
+##sequence-region O94084 1 285
+O94084	UniProtKB	Chain	1	285	.	.	.	ID=PRO_0000299778;Note=Putative uncharacterized protein OPI9	
+O94084	UniProtKB	Transmembrane	197	217	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O94084	UniProtKB	Compositional bias	10	141	.	.	.	Note=Gly-rich	
+O94084	UniProtKB	Compositional bias	232	250	.	.	.	Note=Gly-rich	
+##sequence-region P54964 1 269
+P54964	UniProtKB	Domain	55	227	.	.	.	Note=Exonuclease	
+P54964	UniProtKB	Active site	184	184	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54964	UniProtKB	Sequence conflict	100	100	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54964	UniProtKB	Sequence conflict	124	127	.	.	.	Note=GLTA->ESHP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54964	UniProtKB	Sequence conflict	181	181	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P54964	UniProtKB	Sequence conflict	223	269	.	.	.	Note=SIAQLQWYMDNYLKPPQETESVESIGSEQPESPSSSTSSLKRQRTDF->HSSIAMVHGQLLEATTGNRVGRVNRI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12451 1 1283
+Q12451	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q12451	UniProtKB	Chain	2	1283	.	.	.	ID=PRO_0000100388;Note=Oxysterol-binding protein homolog 2	
+Q12451	UniProtKB	Repeat	106	134	.	.	.	Note=ANK 1	
+Q12451	UniProtKB	Repeat	206	235	.	.	.	Note=ANK 2	
+Q12451	UniProtKB	Domain	289	386	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+Q12451	UniProtKB	Motif	745	751	.	.	.	Note=FFAT	
+Q12451	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q12451	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q12451	UniProtKB	Modified residue	422	422	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+Q12451	UniProtKB	Modified residue	445	445	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12451	UniProtKB	Modified residue	451	451	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12451	UniProtKB	Modified residue	455	455	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12451	UniProtKB	Modified residue	458	458	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12451	UniProtKB	Modified residue	459	459	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12451	UniProtKB	Modified residue	486	486	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12451	UniProtKB	Modified residue	488	488	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12451	UniProtKB	Modified residue	512	512	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12451	UniProtKB	Modified residue	515	515	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12451	UniProtKB	Modified residue	717	717	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12451	UniProtKB	Modified residue	783	783	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12451	UniProtKB	Modified residue	787	787	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12451	UniProtKB	Modified residue	825	825	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12451	UniProtKB	Modified residue	1151	1151	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q02201 1 448
+Q02201	UniProtKB	Chain	1	448	.	.	.	ID=PRO_0000100390;Note=Oxysterol-binding protein homolog 6	
+Q02201	UniProtKB	Region	64	69	.	.	.	Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936	
+Q02201	UniProtKB	Region	64	69	.	.	.	Note=Phosphatidylserine binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4B2Z,ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Region	126	129	.	.	.	Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936	
+Q02201	UniProtKB	Region	157	158	.	.	.	Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936	
+Q02201	UniProtKB	Binding site	129	129	.	.	.	Note=Phosphatidylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4B2Z,ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Binding site	183	183	.	.	.	Note=Phosphatidylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4B2Z,ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Binding site	351	351	.	.	.	Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936	
+Q02201	UniProtKB	Binding site	355	355	.	.	.	Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936	
+Q02201	UniProtKB	Binding site	359	359	.	.	.	Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936	
+Q02201	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q02201	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Strongly reduced binding to phosphatidylserine. L->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Strongly reduced binding to phosphatidylserine and phosphatidylinositol 4-phosphate (PI4P). L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936	
+Q02201	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Does not affect binding to phosphatidylserine. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Abolished binding to phosphatidylserine. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Strongly reduced binding to phosphatidylserine. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Mutagenesis	126	126	.	.	.	Note=Strongly reduced binding to phosphatidylserine. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Strongly reduced binding to phosphatidylserine. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Mutagenesis	157	158	.	.	.	Note=Strongly reduced binding to phosphatidylinositol 4-phosphate (PI4P). Does not affect binding to phosphatidylserine. HH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936	
+Q02201	UniProtKB	Mutagenesis	157	157	.	.	.	Note=Does not affect binding to phosphatidylserine. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Mutagenesis	158	158	.	.	.	Note=Does not affect binding to phosphatidylserine. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Mutagenesis	182	182	.	.	.	Note=Does not affect binding to phosphatidylserine. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Mutagenesis	351	351	.	.	.	Note=Does not affect binding to phosphatidylserine. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110	
+Q02201	UniProtKB	Mutagenesis	351	351	.	.	.	Note=Strongly reduced binding to phosphatidylinositol 4-phosphate (PI4P). Does not affect binding to phosphatidylserine. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936	
+Q02201	UniProtKB	Helix	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	45	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	74	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	79	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	90	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	102	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Turn	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	135	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	147	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Turn	157	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	161	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	173	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	181	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	187	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	197	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	210	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	222	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	227	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	233	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	238	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	248	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	263	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	277	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	287	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	302	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Turn	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	328	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	333	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	344	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	375	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Beta strand	387	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	400	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	421	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	427	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z	
+Q02201	UniProtKB	Helix	436	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PH7	
+##sequence-region P38122 1 312
+P38122	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000184927;Note=3-methyl-2-oxobutanoate hydroxymethyltransferase	
+##sequence-region P50946 1 238
+P50946	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P50946	UniProtKB	Chain	2	238	.	.	.	ID=PRO_0000203439;Note=Putative tyrosine-protein phosphatase OCA1	
+P50946	UniProtKB	Active site	168	168	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50946	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P50946	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50946	UniProtKB	Natural variant	66	66	.	.	.	Note=In strain: SK1. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+##sequence-region P36163 1 345
+P36163	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000203225;Note=Mitochondrial metalloendopeptidase OMA1	
+P36163	UniProtKB	Topological domain	1	67	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36163	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36163	UniProtKB	Topological domain	89	223	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36163	UniProtKB	Transmembrane	224	244	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36163	UniProtKB	Topological domain	245	345	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36163	UniProtKB	Active site	204	204	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P36163	UniProtKB	Metal binding	203	203	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P36163	UniProtKB	Metal binding	207	207	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P36163	UniProtKB	Metal binding	257	257	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P36163	UniProtKB	Mutagenesis	204	204	.	.	.	Note=Loss of protease activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963738;Dbxref=PMID:12963738	
+P36163	UniProtKB	Mutagenesis	207	207	.	.	.	Note=Loss of protease activity. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963738;Dbxref=PMID:12963738	
+P36163	UniProtKB	Mutagenesis	212	212	.	.	.	Note=Loss of protease activity. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963738;Dbxref=PMID:12963738	
+##sequence-region P33767 1 430
+P33767	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33767	UniProtKB	Chain	21	430	.	.	.	ID=PRO_0000021961;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1	
+P33767	UniProtKB	Topological domain	21	393	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33767	UniProtKB	Transmembrane	394	414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33767	UniProtKB	Topological domain	415	430	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33767	UniProtKB	Glycosylation	60	60	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33767	UniProtKB	Glycosylation	332	332	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12202 1 724
+Q12202	UniProtKB	Chain	1	724	.	.	.	ID=PRO_0000076276;Note=Outer spore wall protein 2	
+##sequence-region P43611 1 510
+P43611	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43611	UniProtKB	Chain	24	510	.	.	.	ID=PRO_0000202694;Note=Outer spore wall protein 7	
+P43611	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P32263 1 286
+P32263	UniProtKB	Chain	1	286	.	.	.	ID=PRO_0000187328;Note=Pyrroline-5-carboxylate reductase	
+P32263	UniProtKB	Modified residue	246	246	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32263	UniProtKB	Modified residue	279	279	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32263	UniProtKB	Cross-link	171	171	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P40960 1 533
+P40960	UniProtKB	Chain	1	533	.	.	.	ID=PRO_0000051114;Note=WD repeat-containing protein PAC11	
+P40960	UniProtKB	Repeat	380	422	.	.	.	Note=WD 1	
+P40960	UniProtKB	Repeat	432	475	.	.	.	Note=WD 2	
+P40960	UniProtKB	Sequence conflict	140	140	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40960	UniProtKB	Beta strand	76	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HT6	
+##sequence-region P39937 1 518
+P39937	UniProtKB	Chain	1	518	.	.	.	ID=PRO_0000083526;Note=Protein PAC2	
+P39937	UniProtKB	Domain	23	67	.	.	.	Note=CAP-Gly;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00045	
+P39937	UniProtKB	Repeat	153	174	.	.	.	Note=LRR 1	
+P39937	UniProtKB	Repeat	179	201	.	.	.	Note=LRR 2	
+P39937	UniProtKB	Repeat	204	227	.	.	.	Note=LRR 3	
+P39937	UniProtKB	Repeat	229	252	.	.	.	Note=LRR 4	
+P39937	UniProtKB	Repeat	255	276	.	.	.	Note=LRR 5	
+P39937	UniProtKB	Repeat	277	298	.	.	.	Note=LRR 6	
+P39937	UniProtKB	Repeat	299	319	.	.	.	Note=LRR 7	
+P39937	UniProtKB	Repeat	324	345	.	.	.	Note=LRR 8	
+##sequence-region P41543 1 476
+P41543	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7860628;Dbxref=PMID:7860628	
+P41543	UniProtKB	Chain	23	476	.	.	.	ID=PRO_0000021960;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1	
+P41543	UniProtKB	Topological domain	23	449	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41543	UniProtKB	Transmembrane	450	470	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41543	UniProtKB	Topological domain	471	476	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41543	UniProtKB	Glycosylation	18	18	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41543	UniProtKB	Glycosylation	99	99	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41543	UniProtKB	Glycosylation	217	217	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41543	UniProtKB	Glycosylation	336	336	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41543	UniProtKB	Glycosylation	400	400	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46964 1 130
+P46964	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593165;Dbxref=PMID:7593165	
+P46964	UniProtKB	Chain	2	130	.	.	.	ID=PRO_0000124032;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2	
+P46964	UniProtKB	Topological domain	2	46	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46964	UniProtKB	Transmembrane	47	67	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46964	UniProtKB	Topological domain	68	71	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46964	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46964	UniProtKB	Topological domain	93	109	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46964	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46964	UniProtKB	Mutagenesis	16	16	.	.	.	Note=In OST2-3%3B ts%3B reduced activity. S->P	
+P46964	UniProtKB	Mutagenesis	25	25	.	.	.	Note=In OST2-3%3B ts%3B reduced activity. E->G	
+P46964	UniProtKB	Mutagenesis	31	31	.	.	.	Note=In OST2-1%3B ts%3B reduced activity. K->M	
+P46964	UniProtKB	Mutagenesis	48	48	.	.	.	Note=In OST2-2%3B ts%3B reduced activity. D->V	
+P46964	UniProtKB	Mutagenesis	61	61	.	.	.	Note=In OST2-3%3B ts%3B reduced activity. Q->R	
+P46964	UniProtKB	Mutagenesis	62	62	.	.	.	Note=In OST2-1%3B ts%3B reduced activity. C->S	
+P46964	UniProtKB	Mutagenesis	69	69	.	.	.	Note=In OST2-6%3B ts%3B reduced activity. R->C	
+P46964	UniProtKB	Mutagenesis	80	80	.	.	.	Note=In OST2-1%3B ts%3B reduced activity. G->E	
+P46964	UniProtKB	Mutagenesis	86	86	.	.	.	Note=In OST2-4%3B ts%3B reduced activity. G->R	
+P46964	UniProtKB	Mutagenesis	112	112	.	.	.	Note=In OST2-6%3B ts%3B reduced activity. A->S	
+P46964	UniProtKB	Mutagenesis	113	113	.	.	.	Note=In OST2-6%3B ts%3B reduced activity. E->K	
+P46964	UniProtKB	Mutagenesis	113	113	.	.	.	Note=In OST2-5%3B ts%3B reduced activity. E->V	
+P46964	UniProtKB	Mutagenesis	119	119	.	.	.	Note=In OST2-2%3B ts%3B reduced activity. L->S	
+P46964	UniProtKB	Mutagenesis	123	123	.	.	.	Note=In OST2-2%3B ts%3B reduced activity. F->L	
+P46964	UniProtKB	Mutagenesis	127	127	.	.	.	Note=In OST2-1%3B ts%3B reduced activity. H->Y	
+##sequence-region Q08952 1 273
+Q08952	UniProtKB	Chain	1	273	.	.	.	ID=PRO_0000058123;Note=Oxidation resistance protein 1	
+Q08952	UniProtKB	Domain	100	273	.	.	.	Note=TLD	
+Q08952	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08952	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P41816 1 400
+P41816	UniProtKB	Chain	1	400	.	.	.	ID=PRO_0000194475;Note=NADPH dehydrogenase 3	
+P41816	UniProtKB	Active site	197	197	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41816	UniProtKB	Binding site	38	38	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41816	UniProtKB	Binding site	192	192	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41816	UniProtKB	Binding site	192	192	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41816	UniProtKB	Binding site	195	195	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41816	UniProtKB	Binding site	244	244	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41816	UniProtKB	Binding site	349	349	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41816	UniProtKB	Binding site	376	376	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41816	UniProtKB	Sequence conflict	78	78	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38725 1 120
+P38725	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38725	UniProtKB	Chain	26	120	.	.	.	ID=PRO_0000033245;Note=Seripauperin-13	
+##sequence-region P0CE91 1 120
+P0CE91	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE91	UniProtKB	Chain	21	120	.	.	.	ID=PRO_0000392930;Note=Seripauperin-18	
+##sequence-region P0CE87 1 164
+P0CE87	UniProtKB	Chain	1	164	.	.	.	ID=PRO_0000392932;Note=Seripauperin-22	
+P0CE87	UniProtKB	Alternative sequence	1	40	.	.	.	ID=VSP_038856;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25610 1 124
+P25610	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000203780;Note=Seripauperin-3	
+P25610	UniProtKB	Transmembrane	7	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25610	UniProtKB	Sequence conflict	64	64	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40091 1 420
+P40091	UniProtKB	Chain	1	420	.	.	.	ID=PRO_0000058300;Note=Protein PEA2	
+P40091	UniProtKB	Modified residue	230	230	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40091	UniProtKB	Natural variant	90	90	.	.	.	Note=In strain: CLIB 219. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	117	117	.	.	.	Note=In strain: CLIB 630. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	157	157	.	.	.	Note=In strain: CLIB 219. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	161	161	.	.	.	Note=In strain: CLIB 630. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	165	165	.	.	.	Note=In strain: CLIB 630. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	171	171	.	.	.	Note=In strain: CLIB 630. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	189	189	.	.	.	Note=In strain: CLIB 382. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	210	210	.	.	.	Note=In strain: CLIB 413 haplotype Ha2. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	249	249	.	.	.	Note=In strain: CLIB 556. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	253	253	.	.	.	Note=In strain: Sigma 1278B. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	325	325	.	.	.	Note=In strain: CLIB 219. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	355	355	.	.	.	Note=In strain: R12. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	384	384	.	.	.	Note=In strain: CLIB 219. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P40091	UniProtKB	Natural variant	409	409	.	.	.	Note=In strain: CLIB 410%2C CLIB 413 and Sigma 1278B. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+##sequence-region P25625 1 357
+P25625	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Chain	22	357	.	.	.	ID=PRO_0000202569;Note=Protein PER1	
+P25625	UniProtKB	Topological domain	23	113	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Topological domain	135	155	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Transmembrane	156	176	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Topological domain	177	189	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Transmembrane	190	210	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Topological domain	211	212	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Transmembrane	213	233	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Topological domain	234	248	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Transmembrane	249	269	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Topological domain	270	293	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Transmembrane	294	314	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Topological domain	315	324	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Transmembrane	325	345	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25625	UniProtKB	Topological domain	346	357	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12144 1 273
+Q12144	UniProtKB	Chain	1	273	.	.	.	ID=PRO_0000247231;Note=Pore and endoplasmic reticulum protein of 33 kDa	
+Q12144	UniProtKB	Topological domain	1	24	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Topological domain	46	56	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Transmembrane	57	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Topological domain	75	98	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Topological domain	120	126	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Transmembrane	127	147	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Topological domain	148	176	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Topological domain	198	199	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12144	UniProtKB	Topological domain	221	273	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q92316 1 86
+Q92316	UniProtKB	Chain	1	86	.	.	.	ID=PRO_0000058099;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST5	
+Q92316	UniProtKB	Topological domain	1	27	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q92316	UniProtKB	Transmembrane	28	48	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q92316	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q92316	UniProtKB	Topological domain	78	86	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q92316	UniProtKB	Sequence conflict	46	46	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40219 1 148
+P40219	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000203308;Note=Outer spore wall protein 5	
+P40219	UniProtKB	Topological domain	1	7	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40219	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40219	UniProtKB	Topological domain	29	29	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40219	UniProtKB	Transmembrane	30	50	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40219	UniProtKB	Topological domain	51	148	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40219	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P39952 1 402
+P39952	UniProtKB	Transit peptide	1	42	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9171337;Dbxref=PMID:9171337	
+P39952	UniProtKB	Chain	43	402	.	.	.	ID=PRO_0000020362;Note=Mitochondrial inner membrane protein OXA1	
+P39952	UniProtKB	Topological domain	43	118	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9171337;Dbxref=PMID:9171337	
+P39952	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39952	UniProtKB	Topological domain	140	199	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39952	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39952	UniProtKB	Topological domain	221	239	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39952	UniProtKB	Transmembrane	240	260	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39952	UniProtKB	Topological domain	261	275	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39952	UniProtKB	Transmembrane	276	292	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39952	UniProtKB	Topological domain	293	297	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39952	UniProtKB	Transmembrane	298	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39952	UniProtKB	Topological domain	317	402	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39952	UniProtKB	Mutagenesis	128	128	.	.	.	Note=Leads to respiratory deficiency. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673	
+P39952	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Leads to a defect in complex V assembly and subsequent respiratory deficiency. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673	
+P39952	UniProtKB	Mutagenesis	213	213	.	.	.	Note=Leads to a defect in complex V assembly and subsequent respiratory deficiency. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673	
+P39952	UniProtKB	Mutagenesis	229	229	.	.	.	Note=Leads to a defect in complexes IV and V assembly%2C and subsequent respiratory deficiency. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673	
+P39952	UniProtKB	Mutagenesis	240	240	.	.	.	Note=Leads to a defect in complex IV assembly and subsequent respiratory deficiency. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673	
+P39952	UniProtKB	Mutagenesis	249	249	.	.	.	Note=Leads to respiratory deficiency. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673	
+P39952	UniProtKB	Mutagenesis	250	250	.	.	.	Note=Leads to respiratory deficiency. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673	
+P39952	UniProtKB	Mutagenesis	300	300	.	.	.	Note=Leads to a defect in complex V assembly and subsequent respiratory deficiency. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673	
+P39952	UniProtKB	Mutagenesis	301	301	.	.	.	Note=Leads to respiratory deficiency. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673	
+P39952	UniProtKB	Sequence conflict	108	108	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03558 1 400
+Q03558	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8454584;Dbxref=PMID:8454584	
+Q03558	UniProtKB	Chain	2	400	.	.	.	ID=PRO_0000194474;Note=NADPH dehydrogenase 2	
+Q03558	UniProtKB	Active site	197	197	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03558	UniProtKB	Binding site	38	38	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03558	UniProtKB	Binding site	192	192	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03558	UniProtKB	Binding site	192	192	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03558	UniProtKB	Binding site	195	195	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03558	UniProtKB	Binding site	244	244	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03558	UniProtKB	Binding site	349	349	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03558	UniProtKB	Binding site	376	376	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03558	UniProtKB	Modified residue	353	353	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03558	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03558	UniProtKB	Sequence conflict	90	90	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04430 1 367
+Q04430	UniProtKB	Chain	1	367	.	.	.	ID=PRO_0000253828;Note=Pantothenate kinase CAB1	
+Q04430	UniProtKB	Mutagenesis	351	351	.	.	.	Note=Leads to thermo-sensitivity. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19266201;Dbxref=PMID:19266201	
+##sequence-region P25644 1 796
+P25644	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25644	UniProtKB	Chain	2	796	.	.	.	ID=PRO_0000058235;Note=DNA topoisomerase 2-associated protein PAT1	
+P25644	UniProtKB	Compositional bias	114	235	.	.	.	Note=Pro-rich	
+P25644	UniProtKB	Compositional bias	133	192	.	.	.	Note=Gln-rich	
+P25644	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25644	UniProtKB	Modified residue	456	456	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25644	UniProtKB	Modified residue	457	457	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25644	UniProtKB	Sequence conflict	688	688	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25644	UniProtKB	Helix	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRW	
+P25644	UniProtKB	Helix	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRW	
+P25644	UniProtKB	Helix	475	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	505	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Turn	511	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Beta strand	517	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	522	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	530	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	536	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	545	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	559	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	563	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Turn	570	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	578	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Beta strand	600	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	605	617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	621	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	628	642	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Turn	650	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJJ	
+P25644	UniProtKB	Helix	656	673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	677	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	684	693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	702	713	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	717	726	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Helix	728	749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Beta strand	751	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJJ	
+P25644	UniProtKB	Helix	756	782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Beta strand	785	788	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+P25644	UniProtKB	Beta strand	791	794	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP	
+##sequence-region P35994 1 123
+P35994	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35994	UniProtKB	Chain	21	123	.	.	.	ID=PRO_0000033247;Note=Seripauperin-16	
+##sequence-region P53427 1 120
+P53427	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000203781;Note=Seripauperin-4	
+P53427	UniProtKB	Transmembrane	7	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39545 1 55
+P39545	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39545	UniProtKB	Chain	21	55	.	.	.	ID=PRO_0000203784;Note=Seripauperin-7	
+##sequence-region Q12524 1 340
+Q12524	UniProtKB	Transit peptide	1	7	.	.	.	Note=Peroxisome;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10922370;Dbxref=PMID:10922370	
+Q12524	UniProtKB	Chain	8	340	.	.	.	ID=PRO_0000036186;Note=Peroxisomal coenzyme A diphosphatase 1%2C peroxisomal	
+Q12524	UniProtKB	Domain	37	199	.	.	.	Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794	
+Q12524	UniProtKB	Motif	77	99	.	.	.	Note=Nudix box	
+Q12524	UniProtKB	Metal binding	93	93	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12524	UniProtKB	Metal binding	97	97	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38126 1 564
+P38126	UniProtKB	Chain	1	564	.	.	.	ID=PRO_0000084789;Note=Pachytene checkpoint protein 2	
+P38126	UniProtKB	Nucleotide binding	314	321	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53124 1 433
+P53124	UniProtKB	Chain	1	433	.	.	.	ID=PRO_0000202740;Note=PHO85 cyclin-10	
+P53124	UniProtKB	Helix	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P53124	UniProtKB	Helix	262	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P53124	UniProtKB	Helix	291	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P53124	UniProtKB	Helix	310	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P53124	UniProtKB	Helix	325	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P53124	UniProtKB	Beta strand	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P53124	UniProtKB	Beta strand	348	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P53124	UniProtKB	Helix	356	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P53124	UniProtKB	Helix	359	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P53124	UniProtKB	Helix	381	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P53124	UniProtKB	Helix	392	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P53124	UniProtKB	Helix	415	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+##sequence-region P24867 1 279
+P24867	UniProtKB	Chain	1	279	.	.	.	ID=PRO_0000080499;Note=PHO85 cyclin-1	
+P24867	UniProtKB	Domain	19	152	.	.	.	Note=Cyclin N-terminal	
+P24867	UniProtKB	Region	29	36	.	.	.	Note=Required for degradation by DMA1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23264631;Dbxref=PMID:23264631	
+P24867	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23264631;Dbxref=PMID:23264631	
+P24867	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23264631;Dbxref=PMID:23264631	
+P24867	UniProtKB	Cross-link	82	82	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23264631;Dbxref=PMID:23264631	
+P24867	UniProtKB	Cross-link	121	121	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23264631;Dbxref=PMID:23264631	
+P24867	UniProtKB	Mutagenesis	33	33	.	.	.	Note=Stabilizes PCL1. P->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23264631;Dbxref=PMID:23264631	
+P24867	UniProtKB	Mutagenesis	39	39	.	.	.	Note=In pcl1-2A%3B stabilizes PCL1%3B when associated with A-43. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23264631;Dbxref=PMID:23264631	
+P24867	UniProtKB	Mutagenesis	43	43	.	.	.	Note=In pcl1-2A%3B stabilizes PCL1%3B when associated with A-39. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23264631;Dbxref=PMID:23264631	
+##sequence-region Q08966 1 492
+Q08966	UniProtKB	Chain	1	492	.	.	.	ID=PRO_0000271787;Note=PHO85 cyclin-8	
+Q08966	UniProtKB	Compositional bias	25	33	.	.	.	Note=Poly-Asp	
+Q08966	UniProtKB	Compositional bias	83	92	.	.	.	Note=Poly-Gln	
+Q08966	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08966	UniProtKB	Sequence conflict	234	234	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P15873 1 258
+P15873	UniProtKB	Chain	1	258	.	.	.	ID=PRO_0000149176;Note=Proliferating cell nuclear antigen	
+P15873	UniProtKB	DNA binding	61	80	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15873	UniProtKB	Cross-link	127	127	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219	
+P15873	UniProtKB	Cross-link	164	164	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15166219,ECO:0000269|PubMed:15542864;Dbxref=PMID:15166219,PMID:15542864	
+P15873	UniProtKB	Cross-link	164	164	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12226657;Dbxref=PMID:12226657	
+P15873	UniProtKB	Beta strand	2	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Helix	9	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Turn	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	24	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	34	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	44	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Helix	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE	
+P15873	UniProtKB	Beta strand	66	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Helix	72	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Turn	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	86	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	97	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	106	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	111	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Helix	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V62	
+P15873	UniProtKB	Beta strand	134	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Helix	141	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	156	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	166	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	177	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P15873	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V60	
+P15873	UniProtKB	Helix	191	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	195	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	203	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Helix	209	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Helix	216	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	223	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	231	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	235	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	244	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+P15873	UniProtKB	Beta strand	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ	
+##sequence-region P40345 1 661
+P40345	UniProtKB	Chain	1	661	.	.	.	ID=PRO_0000058268;Note=Phospholipid:diacylglycerol acyltransferase	
+P40345	UniProtKB	Topological domain	1	80	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40345	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40345	UniProtKB	Topological domain	102	661	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40345	UniProtKB	Active site	324	324	.	.	.	Note=Acyl-ester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40345	UniProtKB	Active site	567	567	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40345	UniProtKB	Active site	618	618	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P37254 1 787
+P37254	UniProtKB	Chain	1	787	.	.	.	ID=PRO_0000154142;Note=Aminodeoxychorismate synthase	
+P37254	UniProtKB	Domain	16	233	.	.	.	Note=Glutamine amidotransferase type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P37254	UniProtKB	Region	304	787	.	.	.	Note=PABB component	
+P37254	UniProtKB	Compositional bias	10	14	.	.	.	Note=Poly-Gln	
+P37254	UniProtKB	Active site	112	112	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P37254	UniProtKB	Active site	207	207	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P37254	UniProtKB	Active site	209	209	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605	
+P37254	UniProtKB	Sequence conflict	85	85	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37254	UniProtKB	Sequence conflict	171	171	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37254	UniProtKB	Sequence conflict	171	171	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37254	UniProtKB	Sequence conflict	533	533	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37254	UniProtKB	Sequence conflict	586	586	.	.	.	Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37254	UniProtKB	Sequence conflict	590	591	.	.	.	Note=CE->FV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37254	UniProtKB	Sequence conflict	721	721	.	.	.	Note=G->GL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37254	UniProtKB	Sequence conflict	722	722	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37254	UniProtKB	Sequence conflict	735	737	.	.	.	Note=NGD->FGF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38794 1 229
+P38794	UniProtKB	Chain	1	229	.	.	.	ID=PRO_0000080501;Note=PHO85 cyclin-5	
+##sequence-region P53259 1 346
+P53259	UniProtKB	Transit peptide	1	73	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53259	UniProtKB	Chain	74	346	.	.	.	ID=PRO_0000027392;Note=Rhomboid protein 1%2C mitochondrial	
+P53259	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53259	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53259	UniProtKB	Transmembrane	203	223	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53259	UniProtKB	Transmembrane	246	266	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53259	UniProtKB	Transmembrane	275	295	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53259	UniProtKB	Transmembrane	308	328	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53259	UniProtKB	Active site	256	256	.	.	.	Note=Nucleophile	
+P53259	UniProtKB	Active site	313	313	.	.	.	.	
+P53259	UniProtKB	Mutagenesis	202	202	.	.	.	Note=Abolishes protease activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12901865;Dbxref=PMID:12901865	
+P53259	UniProtKB	Mutagenesis	252	252	.	.	.	Note=Does not abolish protease activity. S->A%2CI;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12417197,ECO:0000269|PubMed:12901865;Dbxref=PMID:12417197,PMID:12901865	
+P53259	UniProtKB	Mutagenesis	254	256	.	.	.	Note=Abolishes protease activity. GAS->AAI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12417197;Dbxref=PMID:12417197	
+P53259	UniProtKB	Mutagenesis	256	256	.	.	.	Note=Abolishes protease activity. S->A%2CI%2CG;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12417197,ECO:0000269|PubMed:12774122,ECO:0000269|PubMed:12901865;Dbxref=PMID:12417197,PMID:12774122,PMID:12901865	
+P53259	UniProtKB	Mutagenesis	313	313	.	.	.	Note=Abolishes protease activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12901865;Dbxref=PMID:12901865	
+##sequence-region P26263 1 563
+P26263	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169	
+P26263	UniProtKB	Chain	2	563	.	.	.	ID=PRO_0000090772;Note=Pyruvate decarboxylase isozyme 3	
+P26263	UniProtKB	Region	390	476	.	.	.	Note=Thiamine pyrophosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26263	UniProtKB	Metal binding	444	444	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26263	UniProtKB	Metal binding	471	471	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26263	UniProtKB	Metal binding	473	473	.	.	.	Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26263	UniProtKB	Binding site	28	28	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26263	UniProtKB	Binding site	115	115	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26263	UniProtKB	Binding site	477	477	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26263	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169	
+P26263	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169	
+P26263	UniProtKB	Modified residue	266	266	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169	
+P26263	UniProtKB	Modified residue	353	353	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169	
+P26263	UniProtKB	Modified residue	522	522	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169	
+P26263	UniProtKB	Cross-link	212	212	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169	
+P26263	UniProtKB	Cross-link	233	233	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169	
+P26263	UniProtKB	Cross-link	269	269	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169	
+P26263	UniProtKB	Cross-link	505	505	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169	
+##sequence-region P22434 1 369
+P22434	UniProtKB	Chain	1	369	.	.	.	ID=PRO_0000206791;Note=3'%2C5'-cyclic-nucleotide phosphodiesterase 1	
+P22434	UniProtKB	Sequence conflict	94	94	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22434	UniProtKB	Beta strand	4	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	18	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	35	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	44	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	69	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	86	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	92	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Turn	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	102	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	110	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	121	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	135	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	141	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	153	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	159	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	170	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	186	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	200	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Turn	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	222	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Turn	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	238	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Turn	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	256	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	273	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	297	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Turn	314	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	321	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Helix	336	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	357	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+P22434	UniProtKB	Beta strand	365	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV	
+##sequence-region P06776 1 526
+P06776	UniProtKB	Chain	1	526	.	.	.	ID=PRO_0000198851;Note=3'%2C5'-cyclic-nucleotide phosphodiesterase 2	
+P06776	UniProtKB	Active site	265	265	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06776	UniProtKB	Metal binding	269	269	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06776	UniProtKB	Metal binding	302	302	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06776	UniProtKB	Metal binding	303	303	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06776	UniProtKB	Metal binding	303	303	.	.	.	Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06776	UniProtKB	Metal binding	400	400	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06776	UniProtKB	Sequence conflict	82	82	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06776	UniProtKB	Sequence conflict	349	350	.	.	.	Note=QL->LK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03266 1 374
+Q03266	UniProtKB	Chain	1	374	.	.	.	ID=PRO_0000203350;Note=Aminodeoxychorismate lyase	
+Q03266	UniProtKB	Beta strand	27	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	60	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	72	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	86	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	100	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	108	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	122	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	144	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	165	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	178	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	191	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	202	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	213	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	232	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	246	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	256	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	283	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	293	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Turn	310	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	313	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	329	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	339	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Helix	347	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	355	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Turn	361	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+Q03266	UniProtKB	Beta strand	364	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N	
+##sequence-region P53632 1 584
+P53632	UniProtKB	Chain	1	584	.	.	.	ID=PRO_0000120314;Note=Poly(A) RNA polymerase protein 2	
+P53632	UniProtKB	Domain	371	431	.	.	.	Note=PAP-associated	
+P53632	UniProtKB	Metal binding	236	236	.	.	.	Note=Magnesium or manganese%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53632	UniProtKB	Metal binding	238	238	.	.	.	Note=Magnesium or manganese%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53632	UniProtKB	Mutagenesis	131	133	.	.	.	Note=In TRF4-131%3B slow growth. EDE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	140	142	.	.	.	Note=In TRF4-140%3B slow growth. ERE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	182	185	.	.	.	Note=In TRF4-182%3B lethal. EIKD->AIAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	194	194	.	.	.	Note=In TRF4-194%3B lethal%3B when associated with A-195%3B A-196 and A-198. R->A	
+P53632	UniProtKB	Mutagenesis	195	198	.	.	.	Note=In TRF4-194%3B lethal. EEIE->AIAA	
+P53632	UniProtKB	Mutagenesis	217	219	.	.	.	Note=In TRF4-217%3B slow growth. DAD->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	224	225	.	.	.	Note=In TRF4-224%3B lethal. GS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	236	238	.	.	.	Note=In TRF4-236%3B lethal. DID->AIA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10926539,ECO:0000269|PubMed:11861546,ECO:0000269|PubMed:16431988;Dbxref=PMID:10926539,PMID:11861546,PMID:16431988	
+P53632	UniProtKB	Mutagenesis	275	277	.	.	.	Note=In TRF4-275%3B temperature sensitive. KAR->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	282	282	.	.	.	Note=In TRF4-282%3B lethal%3B when associated with A-285. K->A	
+P53632	UniProtKB	Mutagenesis	285	285	.	.	.	Note=In TRF4-282%3B lethal%3B when associated with A-282. E->A	
+P53632	UniProtKB	Mutagenesis	309	310	.	.	.	Note=In TRF4-309%3B lethal. RE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	332	333	.	.	.	Note=In TRF4-332%3B temperature sensitive. RR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	378	378	.	.	.	Note=In TRF4-378%3B lethal%3B when associated with A-381. E->A	
+P53632	UniProtKB	Mutagenesis	381	381	.	.	.	Note=In TRF4-378%3B lethal%3B when associated with A-378. E->A	
+P53632	UniProtKB	Mutagenesis	425	425	.	.	.	Note=In TRF4-425%3B lethal%3B when associated with A-428 and A-429. D->A	
+P53632	UniProtKB	Mutagenesis	428	429	.	.	.	Note=In TRF4-425%3B lethal%3B when associated with A-425. DE->AA	
+P53632	UniProtKB	Mutagenesis	444	445	.	.	.	Note=In TRF4-444%3B lethal. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	467	469	.	.	.	Note=In TRF4-467%3B temperature sensitive. KDR->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	486	487	.	.	.	Note=In TRF4-486%3B lethal. RD->AA	
+P53632	UniProtKB	Mutagenesis	490	492	.	.	.	Note=In TRF4-486%3B lethal. DER->AAA	
+P53632	UniProtKB	Mutagenesis	502	502	.	.	.	Note=In TRF4-502%3B lethal%3B when associated with A-504. E->A	
+P53632	UniProtKB	Mutagenesis	504	504	.	.	.	Note=In TRF4-502%3B lethal%3B when associated with A-502. E->A	
+P53632	UniProtKB	Mutagenesis	508	510	.	.	.	Note=In TRF4-508%3B lethal. KKR->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	559	560	.	.	.	Note=In TRF4-559%3B slow growth. KR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Mutagenesis	560	560	.	.	.	Note=In TRF4-559%3B slow growth%3B when associated with A-559. R->A	
+P53632	UniProtKB	Mutagenesis	572	574	.	.	.	Note=In TRF4-572%3B slow growth. EDD->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546	
+P53632	UniProtKB	Beta strand	122	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P53632	UniProtKB	Helix	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	175	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	194	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Beta strand	220	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Turn	225	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Beta strand	237	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	247	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	250	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Beta strand	271	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Beta strand	279	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Turn	286	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Beta strand	290	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	303	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	318	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	337	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	344	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	359	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	368	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	372	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Turn	389	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Beta strand	392	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Beta strand	401	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	406	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	410	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Beta strand	418	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Beta strand	423	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Beta strand	428	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Turn	433	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	440	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Helix	466	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+P53632	UniProtKB	Turn	476	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB	
+##sequence-region P29468 1 568
+P29468	UniProtKB	Chain	1	568	.	.	.	ID=PRO_0000051621;Note=Poly(A) polymerase	
+P29468	UniProtKB	Nucleotide binding	87	89	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751	
+P29468	UniProtKB	Nucleotide binding	99	102	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751	
+P29468	UniProtKB	Nucleotide binding	100	102	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751	
+P29468	UniProtKB	Nucleotide binding	233	234	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751	
+P29468	UniProtKB	Metal binding	100	100	.	.	.	Note=Magnesium 1%3B catalytic	
+P29468	UniProtKB	Metal binding	100	100	.	.	.	Note=Magnesium 2%3B catalytic	
+P29468	UniProtKB	Metal binding	102	102	.	.	.	Note=Magnesium 1%3B catalytic	
+P29468	UniProtKB	Metal binding	102	102	.	.	.	Note=Magnesium 2%3B catalytic	
+P29468	UniProtKB	Metal binding	154	154	.	.	.	Note=Magnesium 2%3B catalytic	
+P29468	UniProtKB	Binding site	154	154	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751	
+P29468	UniProtKB	Binding site	215	215	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751	
+P29468	UniProtKB	Binding site	224	224	.	.	.	Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751	
+P29468	UniProtKB	Site	140	140	.	.	.	Note=Interaction with RNA	
+P29468	UniProtKB	Site	145	145	.	.	.	Note=Interaction with RNA	
+P29468	UniProtKB	Site	294	294	.	.	.	Note=Interaction with RNA	
+P29468	UniProtKB	Site	314	314	.	.	.	Note=Interaction with RNA	
+P29468	UniProtKB	Site	315	315	.	.	.	Note=Interaction with RNA	
+P29468	UniProtKB	Site	387	387	.	.	.	Note=Interaction with RNA	
+P29468	UniProtKB	Site	392	392	.	.	.	Note=Interaction with RNA	
+P29468	UniProtKB	Site	487	487	.	.	.	Note=Interaction with RNA	
+P29468	UniProtKB	Modified residue	452	452	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P29468	UniProtKB	Modified residue	550	550	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P29468	UniProtKB	Mutagenesis	154	154	.	.	.	Note=Loss of enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751	
+P29468	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Slightly reduced rate of adenylyltransfer. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751	
+P29468	UniProtKB	Mutagenesis	215	215	.	.	.	Note=Reduces rate of adenylyltransfer about four-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751	
+P29468	UniProtKB	Mutagenesis	226	226	.	.	.	Note=Reduces rate of adenylyltransfer by half. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751	
+P29468	UniProtKB	Mutagenesis	485	485	.	.	.	Note=Abolishes interaction with FIP1%3B when associated with Y-489. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18537269;Dbxref=PMID:18537269	
+P29468	UniProtKB	Mutagenesis	489	489	.	.	.	Note=Abolishes interaction with FIP1%3B when associated with R-485. V->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18537269;Dbxref=PMID:18537269	
+P29468	UniProtKB	Helix	5	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Q66	
+P29468	UniProtKB	Helix	20	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	42	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	74	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	83	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	101	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	113	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	130	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	143	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	151	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	182	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	204	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	226	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	233	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	252	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	272	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	281	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FA0	
+P29468	UniProtKB	Turn	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	293	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	305	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Turn	312	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	318	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	345	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	354	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	359	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	372	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	399	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	409	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	417	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	420	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	428	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FA0	
+P29468	UniProtKB	Helix	431	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	435	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FA0	
+P29468	UniProtKB	Turn	444	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Q66	
+P29468	UniProtKB	Helix	451	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Q66	
+P29468	UniProtKB	Beta strand	458	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	475	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O1P	
+P29468	UniProtKB	Helix	482	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Turn	497	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Beta strand	502	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	514	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+P29468	UniProtKB	Helix	519	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP	
+##sequence-region Q12515 1 295
+Q12515	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12515	UniProtKB	Chain	2	295	.	.	.	ID=PRO_0000240879;Note=Protein PAR32	
+Q12515	UniProtKB	Compositional bias	54	58	.	.	.	Note=Poly-Asn	
+Q12515	UniProtKB	Compositional bias	274	283	.	.	.	Note=Poly-Lys	
+Q12515	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12515	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12515	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12515	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12515	UniProtKB	Modified residue	123	123	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12515	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12515	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12515	UniProtKB	Modified residue	147	147	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12515	UniProtKB	Modified residue	246	246	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12515	UniProtKB	Sequence conflict	135	135	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40186 1 285
+P40186	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12174291;Dbxref=PMID:12174291	
+P40186	UniProtKB	Chain	2	285	.	.	.	ID=PRO_0000202991;Note=PHO85 cyclin-7	
+P40186	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P17967 1 522
+P17967	UniProtKB	Signal peptide	1	28	.	.	.	Note=Or 22;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17967	UniProtKB	Chain	29	522	.	.	.	ID=PRO_0000034218;Note=Protein disulfide-isomerase	
+P17967	UniProtKB	Domain	29	141	.	.	.	Note=Thioredoxin 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P17967	UniProtKB	Domain	356	485	.	.	.	Note=Thioredoxin 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P17967	UniProtKB	Motif	519	522	.	.	.	Note=Prevents secretion from ER	
+P17967	UniProtKB	Active site	61	61	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17967	UniProtKB	Active site	64	64	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17967	UniProtKB	Active site	406	406	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17967	UniProtKB	Active site	409	409	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17967	UniProtKB	Site	62	62	.	.	.	Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17967	UniProtKB	Site	63	63	.	.	.	Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17967	UniProtKB	Site	126	126	.	.	.	Note=Lowers pKa of C-terminal Cys of first active site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17967	UniProtKB	Site	407	407	.	.	.	Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17967	UniProtKB	Site	408	408	.	.	.	Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17967	UniProtKB	Site	471	471	.	.	.	Note=Lowers pKa of C-terminal Cys of second active site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17967	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17967	UniProtKB	Glycosylation	117	117	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17967	UniProtKB	Glycosylation	155	155	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17967	UniProtKB	Glycosylation	174	174	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17967	UniProtKB	Glycosylation	425	425	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17967	UniProtKB	Disulfide bond	61	64	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00691,ECO:0000269|PubMed:16413482;Dbxref=PMID:16413482	
+P17967	UniProtKB	Disulfide bond	406	409	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00691,ECO:0000269|PubMed:16413482;Dbxref=PMID:16413482	
+P17967	UniProtKB	Sequence conflict	33	52	.	.	.	Note=AVVKLATDSFNEYIQSHDLV->LSLSWPPTLSMNTFSRTTWW;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	83	83	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	83	83	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	114	114	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	143	143	.	.	.	Note=V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	146	146	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	168	168	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	168	168	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	197	197	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	215	215	.	.	.	Note=V->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	226	226	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	226	226	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	333	333	.	.	.	Note=E->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	351	351	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	455	455	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	458	458	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	458	458	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	505	505	.	.	.	Note=A->AEADAEAEA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Sequence conflict	505	505	.	.	.	Note=A->AEADAEAEA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17967	UniProtKB	Turn	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	42	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	50	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	62	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Turn	78	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	84	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Turn	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	94	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	104	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	128	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	142	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	149	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	162	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	171	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Turn	184	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	189	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	201	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	209	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	220	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	226	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	246	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	259	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	267	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Turn	284	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	289	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	295	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	301	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	311	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Turn	319	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	323	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	332	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	346	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	377	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Turn	383	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	386	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	397	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	407	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	431	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	437	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Beta strand	448	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	473	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+P17967	UniProtKB	Helix	490	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E	
+##sequence-region P40530 1 394
+P40530	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40530	UniProtKB	Chain	21	394	.	.	.	ID=PRO_0000213686;Note=[Pyruvate dehydrogenase (acetyl-transferring)] kinase 1%2C mitochondrial	
+P40530	UniProtKB	Domain	126	386	.	.	.	Note=Histidine kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00107	
+P40530	UniProtKB	Nucleotide binding	267	274	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40530	UniProtKB	Nucleotide binding	323	324	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40530	UniProtKB	Nucleotide binding	347	352	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40530	UniProtKB	Binding site	304	304	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40530	UniProtKB	Modified residue	148	148	.	.	.	Note=Phosphohistidine%3B by autocatalysis;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00107	
+##sequence-region P12383 1 1068
+P12383	UniProtKB	Chain	1	1068	.	.	.	ID=PRO_0000114961;Note=Transcription factor PDR1	
+P12383	UniProtKB	DNA binding	46	72	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P12383	UniProtKB	Motif	1054	1062	.	.	.	Note=9aaTAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618436;Dbxref=PMID:27618436	
+P12383	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12383	UniProtKB	Modified residue	930	930	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P12383	UniProtKB	Modified residue	942	942	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P12383	UniProtKB	Modified residue	948	948	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P12383	UniProtKB	Sequence conflict	411	411	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12383	UniProtKB	Sequence conflict	411	411	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12383	UniProtKB	Sequence conflict	530	530	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12383	UniProtKB	Sequence conflict	820	820	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12383	UniProtKB	Sequence conflict	820	820	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12383	UniProtKB	Sequence conflict	921	921	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12383	UniProtKB	Sequence conflict	921	921	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12383	UniProtKB	Sequence conflict	981	981	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12383	UniProtKB	Sequence conflict	981	981	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12383	UniProtKB	Sequence conflict	1015	1019	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12383	UniProtKB	Sequence conflict	1015	1019	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33200 1 976
+P33200	UniProtKB	Chain	1	976	.	.	.	ID=PRO_0000114962;Note=Transcription factor PDR3	
+P33200	UniProtKB	DNA binding	15	41	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P33200	UniProtKB	Sequence conflict	355	355	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33302 1 1511
+P33302	UniProtKB	Chain	1	1511	.	.	.	ID=PRO_0000093442;Note=Pleiotropic ABC efflux transporter of multiple drugs	
+P33302	UniProtKB	Topological domain	1	517	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	518	542	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	543	558	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	559	579	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	580	611	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	612	628	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	629	631	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	632	650	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	651	665	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	666	685	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	686	774	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	775	793	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	794	1237	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	1238	1260	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	1261	1291	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	1292	1313	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	1314	1324	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	1325	1349	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	1350	1354	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	1355	1379	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	1380	1388	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	1389	1407	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	1408	1476	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Transmembrane	1477	1499	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Topological domain	1500	1511	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Domain	161	410	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P33302	UniProtKB	Domain	869	1112	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P33302	UniProtKB	Nucleotide binding	905	912	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P33302	UniProtKB	Compositional bias	784	787	.	.	.	Note=Poly-Phe	
+P33302	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33302	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P33302	UniProtKB	Modified residue	51	51	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33302	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P33302	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33302	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P33302	UniProtKB	Modified residue	837	837	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956	
+P33302	UniProtKB	Modified residue	840	840	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P33302	UniProtKB	Modified residue	841	841	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P33302	UniProtKB	Modified residue	849	849	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P33302	UniProtKB	Modified residue	850	850	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P33302	UniProtKB	Modified residue	854	854	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P33302	UniProtKB	Glycosylation	734	734	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Glycosylation	1447	1447	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33302	UniProtKB	Cross-link	825	825	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12872131,ECO:0000269|PubMed:14557538;Dbxref=PMID:12872131,PMID:14557538	
+P33302	UniProtKB	Mutagenesis	183	183	.	.	.	Note=Activates ER-associated degradation. L->P	
+P33302	UniProtKB	Mutagenesis	257	257	.	.	.	Note=Alters drug specificity. T->I	
+P33302	UniProtKB	Mutagenesis	302	302	.	.	.	Note=Confers generalized drug resistance. G->D	
+P33302	UniProtKB	Mutagenesis	648	648	.	.	.	Note=Alters drug specificity. S->F	
+P33302	UniProtKB	Mutagenesis	905	905	.	.	.	Note=Inactivates drug transport. G->S	
+P33302	UniProtKB	Mutagenesis	908	908	.	.	.	Note=Inactivates drug transport. G->S	
+P33302	UniProtKB	Mutagenesis	1009	1009	.	.	.	Note=Confers generalized drug resistance. G->C	
+P33302	UniProtKB	Mutagenesis	1040	1040	.	.	.	Note=Alters drug specificity. G->D	
+P33302	UniProtKB	Mutagenesis	1048	1048	.	.	.	Note=Alters drug specificity. S->V	
+P33302	UniProtKB	Mutagenesis	1289	1289	.	.	.	Note=Alters drug specificity. E->K	
+P33302	UniProtKB	Mutagenesis	1311	1311	.	.	.	Note=Alters drug specificity. Y->S	
+P33302	UniProtKB	Mutagenesis	1360	1360	.	.	.	Note=Alters drug specificity. S->F	
+P33302	UniProtKB	Mutagenesis	1393	1393	.	.	.	Note=Alters drug specificity. T->I	
+P33302	UniProtKB	Mutagenesis	1427	1427	.	.	.	Note=Activates ER-associated degradation. C->Y	
+P33302	UniProtKB	Sequence conflict	171	171	.	.	.	Note=N->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33302	UniProtKB	Sequence conflict	190	190	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33302	UniProtKB	Sequence conflict	214	214	.	.	.	Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33302	UniProtKB	Sequence conflict	308	308	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33302	UniProtKB	Sequence conflict	340	345	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33302	UniProtKB	Sequence conflict	476	476	.	.	.	Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33302	UniProtKB	Sequence conflict	648	648	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33302	UniProtKB	Sequence conflict	770	770	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53224 1 222
+P53224	UniProtKB	Chain	1	222	.	.	.	ID=PRO_0000215645;Note=Protein ORM1	
+P53224	UniProtKB	Topological domain	1	85	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53224	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53224	UniProtKB	Topological domain	107	109	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53224	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53224	UniProtKB	Topological domain	131	162	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53224	UniProtKB	Transmembrane	163	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53224	UniProtKB	Topological domain	184	184	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53224	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53224	UniProtKB	Topological domain	206	222	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53224	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53224	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53224	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53224	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Induces dysregulation of sphingolipid synthesis%3B when associated with 32-A--A-36 and 51-A--A-53. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505	
+P53224	UniProtKB	Mutagenesis	32	36	.	.	.	Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-29 and 51-A--A-53. SASSS->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505	
+P53224	UniProtKB	Mutagenesis	51	53	.	.	.	Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-29 and 32-A--A-36. SSS->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505	
+##sequence-region P35845 1 1188
+P35845	UniProtKB	Chain	1	1188	.	.	.	ID=PRO_0000100387;Note=Oxysterol-binding protein homolog 1	
+P35845	UniProtKB	Repeat	51	80	.	.	.	Note=ANK 1	
+P35845	UniProtKB	Repeat	96	125	.	.	.	Note=ANK 2	
+P35845	UniProtKB	Repeat	196	225	.	.	.	Note=ANK 3	
+P35845	UniProtKB	Domain	330	379	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P35845	UniProtKB	Motif	716	722	.	.	.	Note=FFAT	
+P35845	UniProtKB	Compositional bias	434	472	.	.	.	Note=Asn/Asp-rich	
+P35845	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P35845	UniProtKB	Modified residue	490	490	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P35845	UniProtKB	Modified residue	500	500	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P35845	UniProtKB	Modified residue	678	678	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P35845	UniProtKB	Modified residue	683	683	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35845	UniProtKB	Modified residue	691	691	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35845	UniProtKB	Modified residue	692	692	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35845	UniProtKB	Modified residue	694	694	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P35845	UniProtKB	Modified residue	708	708	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P35845	UniProtKB	Modified residue	712	712	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P35845	UniProtKB	Mutagenesis	719	719	.	.	.	Note=Abolishes function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12727870;Dbxref=PMID:12727870	
+P35845	UniProtKB	Sequence conflict	244	244	.	.	.	Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35845	UniProtKB	Sequence conflict	248	248	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35845	UniProtKB	Sequence conflict	248	248	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35845	UniProtKB	Sequence conflict	424	424	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35845	UniProtKB	Sequence conflict	464	464	.	.	.	Note=D->NNN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35845	UniProtKB	Sequence conflict	468	469	.	.	.	Note=YD->DY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35845	UniProtKB	Sequence conflict	495	496	.	.	.	Note=TP->AS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35845	UniProtKB	Helix	13	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	29	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	46	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	55	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	65	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	110	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	141	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	171	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Turn	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	200	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	210	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	233	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	249	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+P35845	UniProtKB	Helix	252	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28	
+##sequence-region P38713 1 996
+P38713	UniProtKB	Chain	1	996	.	.	.	ID=PRO_0000100389;Note=Oxysterol-binding protein homolog 3	
+P38713	UniProtKB	Domain	221	315	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P38713	UniProtKB	Motif	514	520	.	.	.	Note=FFAT	
+P38713	UniProtKB	Modified residue	190	190	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38713	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38713	UniProtKB	Modified residue	210	210	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38713	UniProtKB	Modified residue	323	323	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38713	UniProtKB	Modified residue	324	324	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38713	UniProtKB	Modified residue	325	325	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38713	UniProtKB	Modified residue	352	352	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38713	UniProtKB	Modified residue	605	605	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38713	UniProtKB	Beta strand	223	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Beta strand	240	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Turn	248	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Beta strand	252	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Beta strand	266	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Helix	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Beta strand	273	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Turn	279	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Beta strand	283	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Beta strand	292	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Helix	300	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Helix	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP	
+P38713	UniProtKB	Helix	643	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	650	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	655	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	662	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	665	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	670	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	676	678	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Turn	679	681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	682	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	693	703	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	704	708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	711	715	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	717	719	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	726	731	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	732	734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	736	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Turn	745	748	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	749	771	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	773	788	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Turn	789	791	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	794	798	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	802	805	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	807	810	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	813	816	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	818	824	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	829	834	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	838	841	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	846	852	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	862	867	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Turn	868	870	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	871	874	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Turn	875	877	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	880	883	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	891	893	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Turn	894	896	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	899	904	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Turn	909	914	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	920	922	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	924	930	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	934	953	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	961	967	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Beta strand	970	973	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+P38713	UniProtKB	Helix	980	985	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4	
+##sequence-region P38755 1 437
+P38755	UniProtKB	Chain	1	437	.	.	.	ID=PRO_0000100391;Note=Oxysterol-binding protein homolog 7	
+P38755	UniProtKB	Region	64	69	.	.	.	Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201	
+P38755	UniProtKB	Region	64	69	.	.	.	Note=Phosphatidylserine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201	
+P38755	UniProtKB	Region	126	129	.	.	.	Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201	
+P38755	UniProtKB	Region	157	158	.	.	.	Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201	
+P38755	UniProtKB	Binding site	129	129	.	.	.	Note=Phosphatidylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201	
+P38755	UniProtKB	Binding site	183	183	.	.	.	Note=Phosphatidylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201	
+P38755	UniProtKB	Binding site	351	351	.	.	.	Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201	
+P38755	UniProtKB	Binding site	355	355	.	.	.	Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201	
+P38755	UniProtKB	Binding site	359	359	.	.	.	Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201	
+P38755	UniProtKB	Cross-link	276	276	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P38747 1 307
+P38747	UniProtKB	Chain	1	307	.	.	.	ID=PRO_0000202883;Note=OTU domain-containing protein 2	
+P38747	UniProtKB	Domain	167	307	.	.	.	Note=OTU;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00139	
+##sequence-region P38787 1 379
+P38787	UniProtKB	Chain	1	379	.	.	.	ID=PRO_0000157328;Note=2-dehydropantoate 2-reductase	
+P38787	UniProtKB	Nucleotide binding	13	18	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38787	UniProtKB	Active site	224	224	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38787	UniProtKB	Binding site	119	119	.	.	.	Note=NADP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38787	UniProtKB	Binding site	119	119	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38787	UniProtKB	Binding site	228	228	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38787	UniProtKB	Binding site	232	232	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38787	UniProtKB	Binding site	316	316	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38787	UniProtKB	Binding site	328	328	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q07362 1 185
+Q07362	UniProtKB	Chain	1	185	.	.	.	ID=PRO_0000262746;Note=Protein PBP4	
+Q07362	UniProtKB	Compositional bias	56	62	.	.	.	Note=Poly-Gln	
+##sequence-region P08018 1 668
+P08018	UniProtKB	Chain	1	668	.	.	.	ID=PRO_0000086483;Note=MAP kinase kinase PBS2	
+P08018	UniProtKB	Domain	360	623	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P08018	UniProtKB	Nucleotide binding	366	374	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P08018	UniProtKB	Compositional bias	91	101	.	.	.	Note=Pro-rich	
+P08018	UniProtKB	Active site	485	485	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P08018	UniProtKB	Binding site	389	389	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P08018	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P08018	UniProtKB	Modified residue	269	269	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08018	UniProtKB	Modified residue	514	514	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:7624781;Dbxref=PMID:18407956,PMID:7624781	
+P08018	UniProtKB	Modified residue	518	518	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7624781;Dbxref=PMID:7624781	
+P08018	UniProtKB	Mutagenesis	96	96	.	.	.	Note=In PBS2-13%3B loss of SH3-domain interaction. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7624781;Dbxref=PMID:7624781	
+P08018	UniProtKB	Mutagenesis	389	389	.	.	.	Note=Loss of activity. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7624781;Dbxref=PMID:7624781	
+P08018	UniProtKB	Mutagenesis	514	514	.	.	.	Note=Loss of phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7624781;Dbxref=PMID:7624781	
+P08018	UniProtKB	Mutagenesis	518	518	.	.	.	Note=Loss of phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7624781;Dbxref=PMID:7624781	
+P08018	UniProtKB	Sequence conflict	222	223	.	.	.	Note=GL->AV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08018	UniProtKB	Sequence conflict	222	223	.	.	.	Note=GL->AV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25693 1 308
+P25693	UniProtKB	Chain	1	308	.	.	.	ID=PRO_0000080500;Note=PHO85 cyclin-2	
+P25693	UniProtKB	Domain	18	146	.	.	.	Note=Cyclin N-terminal	
+##sequence-region Q12477 1 304
+Q12477	UniProtKB	Chain	1	304	.	.	.	ID=PRO_0000271788;Note=PHO85 cyclin-9	
+Q12477	UniProtKB	Domain	19	146	.	.	.	Note=Cyclin N-terminal	
+##sequence-region P13259 1 424
+P13259	UniProtKB	Chain	1	424	.	.	.	ID=PRO_0000208460;Note=Choline-phosphate cytidylyltransferase	
+P13259	UniProtKB	Nucleotide binding	111	119	.	.	.	Note=CTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13259	UniProtKB	Nucleotide binding	195	196	.	.	.	Note=CTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13259	UniProtKB	Nucleotide binding	223	227	.	.	.	Note=CTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13259	UniProtKB	Binding site	149	149	.	.	.	Note=CTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13259	UniProtKB	Binding site	149	149	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13259	UniProtKB	Binding site	178	178	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13259	UniProtKB	Binding site	200	200	.	.	.	Note=CTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13259	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P13259	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P13259	UniProtKB	Modified residue	346	346	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198	
+P13259	UniProtKB	Modified residue	401	401	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13259	UniProtKB	Sequence conflict	90	90	.	.	.	Note=P->PG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13259	UniProtKB	Sequence conflict	105	105	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13259	UniProtKB	Sequence conflict	192	192	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32896 1 925
+P32896	UniProtKB	Chain	1	925	.	.	.	ID=PRO_0000126137;Note=Protein PDC2	
+P32896	UniProtKB	Domain	63	138	.	.	.	Note=HTH CENPB-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00583	
+P32896	UniProtKB	Compositional bias	538	562	.	.	.	Note=Asn/Ser-rich	
+P32896	UniProtKB	Compositional bias	890	895	.	.	.	Note=Poly-Ala	
+P32896	UniProtKB	Sequence conflict	113	113	.	.	.	Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32896	UniProtKB	Sequence conflict	113	113	.	.	.	Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32896	UniProtKB	Sequence conflict	174	174	.	.	.	Note=D->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32896	UniProtKB	Sequence conflict	174	174	.	.	.	Note=D->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99220 1 542
+Q99220	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99220	UniProtKB	Chain	22	542	.	.	.	ID=PRO_0000042758;Note=Protein OS-9 homolog	
+Q99220	UniProtKB	Domain	115	190	.	.	.	Note=PRKCSH	
+Q99220	UniProtKB	Motif	539	542	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138	
+Q99220	UniProtKB	Binding site	137	137	.	.	.	Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99220	UniProtKB	Binding site	194	194	.	.	.	Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99220	UniProtKB	Binding site	200	200	.	.	.	Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99220	UniProtKB	Binding site	223	223	.	.	.	Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99220	UniProtKB	Binding site	229	229	.	.	.	Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99220	UniProtKB	Glycosylation	52	52	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99220	UniProtKB	Glycosylation	74	74	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99220	UniProtKB	Glycosylation	380	380	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99220	UniProtKB	Disulfide bond	117	130	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99220	UniProtKB	Disulfide bond	193	227	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99220	UniProtKB	Disulfide bond	208	239	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99220	UniProtKB	Mutagenesis	127	127	.	.	.	Note=Decrease of ER lumenal misfolded protein degradation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16168372;Dbxref=PMID:16168372	
+Q99220	UniProtKB	Mutagenesis	137	137	.	.	.	Note=Decrease of ER lumenal misfolded protein degradation. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16168372;Dbxref=PMID:16168372	
+Q99220	UniProtKB	Mutagenesis	139	139	.	.	.	Note=Decrease of ER lumenal misfolded protein degradation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16168372;Dbxref=PMID:16168372	
+Q99220	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Decrease of ER lumenal misfolded protein degradation. No effect on interaction with CDC48%2C HRD3%2C KAR2%2C UBX2%2C HRD1 or EMP47. R->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16168370,ECO:0000269|PubMed:16168372,ECO:0000269|PubMed:16873065;Dbxref=PMID:16168370,PMID:16168372,PMID:16873065	
+Q99220	UniProtKB	Mutagenesis	223	223	.	.	.	Note=Decrease of ER lumenal misfolded protein degradation. E->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16168370,ECO:0000269|PubMed:16168372;Dbxref=PMID:16168370,PMID:16168372	
+Q99220	UniProtKB	Mutagenesis	229	229	.	.	.	Note=Decrease of ER lumenal misfolded protein degradation. Y->A%2CF;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16168370,ECO:0000269|PubMed:16168372;Dbxref=PMID:16168370,PMID:16168372	
+Q99220	UniProtKB	Sequence conflict	25	25	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q99220	UniProtKB	Beta strand	276	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA	
+Q99220	UniProtKB	Beta strand	286	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA	
+Q99220	UniProtKB	Beta strand	299	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA	
+Q99220	UniProtKB	Helix	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA	
+Q99220	UniProtKB	Beta strand	310	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA	
+Q99220	UniProtKB	Helix	315	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA	
+Q99220	UniProtKB	Beta strand	347	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA	
+Q99220	UniProtKB	Beta strand	361	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA	
+Q99220	UniProtKB	Beta strand	371	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA	
+Q99220	UniProtKB	Beta strand	375	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA	
+Q99220	UniProtKB	Beta strand	391	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA	
+##sequence-region P04147 1 577
+P04147	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P04147	UniProtKB	Chain	2	577	.	.	.	ID=PRO_0000081720;Note=Polyadenylate-binding protein%2C cytoplasmic and nuclear	
+P04147	UniProtKB	Domain	38	116	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P04147	UniProtKB	Domain	126	203	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P04147	UniProtKB	Domain	219	296	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P04147	UniProtKB	Domain	322	399	.	.	.	Note=RRM 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P04147	UniProtKB	Domain	489	568	.	.	.	Note=PABC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00641	
+P04147	UniProtKB	Region	9	61	.	.	.	Note=Required and sufficient for nuclear export;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04147	UniProtKB	Region	281	317	.	.	.	Note=Required and sufficient for nuclear import;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04147	UniProtKB	Region	473	577	.	.	.	Note=Interaction with SUP35	
+P04147	UniProtKB	Motif	12	17	.	.	.	Note=Nuclear export signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P04147	UniProtKB	Compositional bias	422	431	.	.	.	Note=Poly-Ala	
+P04147	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P04147	UniProtKB	Modified residue	107	107	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23865587;Dbxref=PMID:23865587	
+P04147	UniProtKB	Modified residue	249	249	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04147	UniProtKB	Modified residue	332	332	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04147	UniProtKB	Modified residue	405	405	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04147	UniProtKB	Cross-link	7	7	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P04147	UniProtKB	Cross-link	337	337	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P04147	UniProtKB	Mutagenesis	12	12	.	.	.	Note=Impairs nuclear export%3B when associated with A-15. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15630021;Dbxref=PMID:15630021	
+P04147	UniProtKB	Mutagenesis	15	15	.	.	.	Note=Impairs nuclear export%3B when associated with A-12. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15630021;Dbxref=PMID:15630021	
+P04147	UniProtKB	Mutagenesis	79	79	.	.	.	Note=In PAB1-14%3B fails to bind poly(U)%2C but not poly(A) RNA%3B when associated with Q-166%3B Q-259 and Q-362. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001	
+P04147	UniProtKB	Mutagenesis	83	83	.	.	.	Note=In PAB1-16%3B reduces affinity for oligo(A) about 100-fold%2C impairs poly(A)-dependent translation%2C but still interacts with eIF4G%3B when associated with V-170. In PAB1-15%3B fails to bind RNA%3B when associated with V-170%3B V-263 and V-366. Y->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9193001,ECO:0000269|PubMed:9418852;Dbxref=PMID:9193001,PMID:9418852	
+P04147	UniProtKB	Mutagenesis	134	136	.	.	.	Note=In PAB1-134. HPD->DKS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826	
+P04147	UniProtKB	Mutagenesis	148	148	.	.	.	Note=In PAB1-148%3B greatly reduces poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro%3B when associated with N-151. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826	
+P04147	UniProtKB	Mutagenesis	151	151	.	.	.	Note=In PAB1-148%3B greatly reduces poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro%3B when associated with A-148. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826	
+P04147	UniProtKB	Mutagenesis	157	159	.	.	.	Note=In PAB1-157%3B greatly reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. IAT->VVC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826	
+P04147	UniProtKB	Mutagenesis	166	166	.	.	.	Note=In PAB1-14%3B fails to bind poly(U)%2C but not poly(A) RNA%3B when associated with A-79%3B Q-259 and Q-362. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001	
+P04147	UniProtKB	Mutagenesis	170	170	.	.	.	Note=In PAB1-6%3B selectively reduces poly(A) RNA binding. In PAB1-16%3B reduces affinity for oligo(A) about 100-fold%2C impairs poly(A)-dependent translation%2C but still interacts with eIF4G%3B when associated with V-83. In PAB1-15%3B fails to bind RNA%3B when associated with V-83%3B V-263 and V-366. F->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9193001,ECO:0000269|PubMed:9418852;Dbxref=PMID:9193001,PMID:9418852	
+P04147	UniProtKB	Mutagenesis	175	177	.	.	.	Note=In PAB1-175%3B greatly reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. EEG->TQE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826	
+P04147	UniProtKB	Mutagenesis	180	181	.	.	.	Note=In PAB1-180%3B abolishes poly(A)-dependent translation and greatly reduces stimulation of cap-dependent translation in vitro. Impairs interaction with eIF4G. KE->ER;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826	
+P04147	UniProtKB	Mutagenesis	184	186	.	.	.	Note=In PAB1-184%3B abolishes poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro. Impairs interaction with eIF4G. DAL->EKM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826	
+P04147	UniProtKB	Mutagenesis	193	197	.	.	.	Note=In PAB1-193%3B moderately reduces stimulation of cap-dependent translation in vitro. GQEIY->DRKVF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826	
+P04147	UniProtKB	Mutagenesis	199	202	.	.	.	Note=In PAB1-199%3B moderately reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. APHL->GRFK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826	
+P04147	UniProtKB	Mutagenesis	259	259	.	.	.	Note=In PAB1-14%3B fails to bind poly(U)%2C but not poly(A) RNA%3B when associated with A-79%3B Q-166 and Q-362. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001	
+P04147	UniProtKB	Mutagenesis	263	263	.	.	.	Note=In PAB1-7. In PAB1-15%3B fails to bind RNA%3B when associated with V-83%3B V-170 and V-366. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001	
+P04147	UniProtKB	Mutagenesis	362	362	.	.	.	Note=In PAB1-14%3B fails to bind poly(U)%2C but not poly(A) RNA%3B when associated with A-79%3B Q-166 and Q-259. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001	
+P04147	UniProtKB	Mutagenesis	366	366	.	.	.	Note=In PAB1-8%3B selectively reduces poly(U) RNA binding. In PAB1-15%3B fails to bind RNA%3B when associated with V-83%3B V-170 and V-263. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001	
+P04147	UniProtKB	Sequence conflict	426	426	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04147	UniProtKB	Helix	503	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IFW	
+P04147	UniProtKB	Helix	518	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IFW	
+P04147	UniProtKB	Helix	524	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IFW	
+P04147	UniProtKB	Helix	539	546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IFW	
+P04147	UniProtKB	Helix	549	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IFW	
+##sequence-region P53343 1 120
+P53343	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000203786;Note=Seripauperin-12	
+P53343	UniProtKB	Transmembrane	7	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12370 1 124
+Q12370	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12370	UniProtKB	Chain	21	124	.	.	.	ID=PRO_0000033248;Note=Seripauperin-17	
+Q12370	UniProtKB	Sequence conflict	115	115	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08322 1 120
+Q08322	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000245258;Note=Seripauperin-20	
+Q08322	UniProtKB	Transmembrane	7	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38155 1 120
+P38155	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38155	UniProtKB	Chain	21	120	.	.	.	ID=PRO_0000033242;Note=Seripauperin-24	
+##sequence-region P0CE92 1 120
+P0CE92	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE92	UniProtKB	Chain	21	120	.	.	.	ID=PRO_0000203785;Note=Seripauperin-8	
+##sequence-region P25580 1 416
+P25580	UniProtKB	Chain	1	416	.	.	.	ID=PRO_0000058243;Note=Protein PBN1	
+P25580	UniProtKB	Topological domain	1	385	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25580	UniProtKB	Transmembrane	386	405	.	.	.	Note=Helical%3B Signal-anchor for type III membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25580	UniProtKB	Topological domain	406	416	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25580	UniProtKB	Glycosylation	24	24	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25580	UniProtKB	Glycosylation	85	85	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25580	UniProtKB	Glycosylation	120	120	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25580	UniProtKB	Glycosylation	212	212	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25580	UniProtKB	Glycosylation	365	365	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P10963 1 549
+P10963	UniProtKB	Chain	1	549	.	.	.	ID=PRO_0000203875;Note=Phosphoenolpyruvate carboxykinase (ATP)	
+P10963	UniProtKB	Nucleotide binding	250	257	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10963	UniProtKB	Sequence conflict	95	107	.	.	.	Note=PCSERTWSINRER->HVLKEHGLSTVK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10963	UniProtKB	Sequence conflict	123	123	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10963	UniProtKB	Sequence conflict	322	322	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10963	UniProtKB	Sequence conflict	357	357	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10963	UniProtKB	Sequence conflict	431	431	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10963	UniProtKB	Sequence conflict	544	549	.	.	.	Note=AGPQFE->DWSSIRVNETC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40038 1 420
+P40038	UniProtKB	Chain	1	420	.	.	.	ID=PRO_0000202631;Note=PHO85 cyclin-6	
+P40038	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40038	UniProtKB	Modified residue	281	281	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40038	UniProtKB	Modified residue	312	312	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40038	UniProtKB	Modified residue	317	317	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40550 1 1411
+P40550	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7629127;Dbxref=PMID:7629127	
+P40550	UniProtKB	Chain	2	1411	.	.	.	ID=PRO_0000093444;Note=ATP-dependent permease PDR11	
+P40550	UniProtKB	Topological domain	2	388	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	389	409	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	410	418	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	419	439	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	440	471	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	472	492	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	493	494	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	495	515	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	516	524	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	525	545	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	546	636	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	637	657	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	658	1090	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	1091	1111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	1112	1117	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	1118	1138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	1139	1175	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	1176	1196	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	1197	1204	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	1205	1225	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	1226	1230	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	1231	1251	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	1252	1355	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Transmembrane	1356	1376	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Topological domain	1377	1411	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Domain	31	273	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P40550	UniProtKB	Domain	751	979	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P40550	UniProtKB	Nucleotide binding	782	789	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P40550	UniProtKB	Compositional bias	708	713	.	.	.	Note=Poly-Ser	
+P40550	UniProtKB	Compositional bias	1046	1049	.	.	.	Note=Poly-Leu	
+P40550	UniProtKB	Glycosylation	595	595	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Glycosylation	1289	1289	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Glycosylation	1324	1324	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40550	UniProtKB	Glycosylation	1346	1346	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04182 1 1529
+Q04182	UniProtKB	Chain	1	1529	.	.	.	ID=PRO_0000093446;Note=ATP-dependent permease PDR15	
+Q04182	UniProtKB	Topological domain	1	531	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	532	552	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	553	567	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	568	588	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	589	617	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	618	638	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	639	642	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	643	663	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	664	699	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	700	720	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	721	783	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	784	804	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	805	1219	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	1220	1240	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	1241	1312	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	1313	1333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	1334	1340	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	1341	1361	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	1362	1368	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	1369	1389	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	1390	1396	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	1397	1417	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	1418	1492	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Transmembrane	1493	1513	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Topological domain	1514	1529	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Domain	171	420	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q04182	UniProtKB	Domain	884	1127	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q04182	UniProtKB	Nucleotide binding	920	927	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q04182	UniProtKB	Compositional bias	13	24	.	.	.	Note=Poly-Ser	
+Q04182	UniProtKB	Compositional bias	66	69	.	.	.	Note=Poly-Ser	
+Q04182	UniProtKB	Compositional bias	794	797	.	.	.	Note=Poly-Phe	
+Q04182	UniProtKB	Glycosylation	558	558	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04182	UniProtKB	Glycosylation	744	744	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53756 1 1333
+P53756	UniProtKB	Chain	1	1333	.	.	.	ID=PRO_0000093466;Note=ABC transporter ATP-binding protein/permease PDR18	
+P53756	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	392	412	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	425	445	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	474	494	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	499	519	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	534	554	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	642	662	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	1071	1091	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	1092	1112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	1150	1170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	1178	1198	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	1210	1230	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Transmembrane	1235	1255	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Domain	30	281	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P53756	UniProtKB	Domain	729	971	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P53756	UniProtKB	Nucleotide binding	765	772	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P53756	UniProtKB	Glycosylation	48	48	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Glycosylation	144	144	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Glycosylation	205	205	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Glycosylation	350	350	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Glycosylation	697	697	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Glycosylation	733	733	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Glycosylation	958	958	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53756	UniProtKB	Glycosylation	1320	1320	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04264 1 1277
+Q04264	UniProtKB	Chain	1	1277	.	.	.	ID=PRO_0000058280;Note=Sister chromatid cohesion protein PDS5	
+Q04264	UniProtKB	Repeat	393	429	.	.	.	Note=HEAT	
+Q04264	UniProtKB	Modified residue	1231	1231	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04264	UniProtKB	Modified residue	1233	1233	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04264	UniProtKB	Beta strand	19	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	25	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Beta strand	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	53	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	70	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	95	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	120	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	136	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	145	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	168	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	187	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	215	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	228	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	254	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	274	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	281	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	293	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	315	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	320	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	328	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	335	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	345	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	358	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	372	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	387	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	397	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	406	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	412	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Beta strand	437	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	440	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	449	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	456	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	462	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	483	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	499	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	527	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Turn	530	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Beta strand	535	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	540	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	561	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	577	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	593	607	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	626	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Beta strand	643	646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	648	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	662	678	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Turn	680	682	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	683	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q04264	UniProtKB	Helix	692	696	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+##sequence-region P36139 1 283
+P36139	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3	
+P36139	UniProtKB	Chain	2	283	.	.	.	ID=PRO_0000058317;Note=Protein PET10	
+P36139	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3	
+##sequence-region Q12462 1 236
+Q12462	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7721939,ECO:0000269|PubMed:7860627;Dbxref=PMID:7721939,PMID:7860627	
+Q12462	UniProtKB	Chain	2	236	.	.	.	ID=PRO_0000105974;Note=Peroxisomal membrane protein PMP27	
+##sequence-region P53112 1 341
+P53112	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53112	UniProtKB	Chain	2	341	.	.	.	ID=PRO_0000058329;Note=Peroxisomal membrane protein PEX14	
+P53112	UniProtKB	Motif	86	94	.	.	.	Note=SH3-binding	
+P53112	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53112	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53112	UniProtKB	Mutagenesis	87	90	.	.	.	Note=Loss of interaction with SH3 domain of PEX13. No effect on membrane association. PTLP->ATLA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10087260;Dbxref=PMID:10087260	
+##sequence-region P24004 1 1043
+P24004	UniProtKB	Chain	1	1043	.	.	.	ID=PRO_0000084606;Note=Peroxisomal ATPase PEX1	
+P24004	UniProtKB	Nucleotide binding	461	468	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24004	UniProtKB	Nucleotide binding	738	745	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24004	UniProtKB	Region	453	626	.	.	.	Note=AAA-cassette D1	
+P24004	UniProtKB	Region	733	926	.	.	.	Note=AAA-cassette D2	
+P24004	UniProtKB	Mutagenesis	467	467	.	.	.	Note=In PEX1pA1%3B no effect. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078,ECO:0000269|PubMed:7725796;Dbxref=PMID:15634331,PMID:16007078,PMID:7725796	
+P24004	UniProtKB	Mutagenesis	525	525	.	.	.	Note=In PEX1pB1%3B no effect. D->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078;Dbxref=PMID:15634331,PMID:16007078	
+P24004	UniProtKB	Mutagenesis	744	744	.	.	.	Note=In PEX1pA2%3B decreased binding to PEX6. Results in accumulation of PEX5 on peroxisomal membranes. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078,ECO:0000269|PubMed:7725796;Dbxref=PMID:15634331,PMID:16007078,PMID:7725796	
+P24004	UniProtKB	Mutagenesis	797	797	.	.	.	Note=In PEX1pB2%3B results in accumulation of PEX5 on peroxisomal membranes. D->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078;Dbxref=PMID:15634331,PMID:16007078	
+P24004	UniProtKB	Sequence conflict	354	354	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03370 1 554
+Q03370	UniProtKB	Chain	1	554	.	.	.	ID=PRO_0000252269;Note=Peroxisomal membrane protein PEX29	
+Q03370	UniProtKB	Topological domain	1	145	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03370	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03370	UniProtKB	Topological domain	167	172	.	.	.	Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03370	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03370	UniProtKB	Topological domain	194	264	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03370	UniProtKB	Transmembrane	265	285	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03370	UniProtKB	Topological domain	286	287	.	.	.	Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03370	UniProtKB	Transmembrane	288	308	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03370	UniProtKB	Topological domain	309	554	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39108 1 375
+P39108	UniProtKB	Chain	1	375	.	.	.	ID=PRO_0000051120;Note=Peroxisomal targeting signal 2 receptor	
+P39108	UniProtKB	Repeat	58	89	.	.	.	Note=WD 1	
+P39108	UniProtKB	Repeat	102	133	.	.	.	Note=WD 2	
+P39108	UniProtKB	Repeat	172	203	.	.	.	Note=WD 3	
+P39108	UniProtKB	Repeat	218	249	.	.	.	Note=WD 4	
+P39108	UniProtKB	Repeat	281	312	.	.	.	Note=WD 5	
+P39108	UniProtKB	Repeat	340	372	.	.	.	Note=WD 6	
+P39108	UniProtKB	Beta strand	2	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	9	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	23	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Helix	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	38	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	51	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	63	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	75	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	83	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	97	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	107	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	114	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	120	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	140	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Helix	148	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Helix	158	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	177	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	189	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	197	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	210	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	223	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	235	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	245	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	274	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	281	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	286	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	298	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	308	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Turn	326	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Turn	330	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	334	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	345	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	352	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	358	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P39108	UniProtKB	Beta strand	366	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+##sequence-region P48363 1 199
+P48363	UniProtKB	Chain	1	199	.	.	.	ID=PRO_0000153659;Note=Prefoldin subunit 3	
+P48363	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q04493 1 163
+Q04493	UniProtKB	Chain	1	163	.	.	.	ID=PRO_0000153668;Note=Prefoldin subunit 5	
+##sequence-region P53170 1 491
+P53170	UniProtKB	Domain	153	480	.	.	.	Note=Histidine kinase	
+P53170	UniProtKB	Nucleotide binding	300	307	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53170	UniProtKB	Nucleotide binding	359	360	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53170	UniProtKB	Nucleotide binding	383	446	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53170	UniProtKB	Binding site	341	341	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53170	UniProtKB	Sequence conflict	224	225	.	.	.	Note=SI->VY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53170	UniProtKB	Sequence conflict	224	225	.	.	.	Note=SI->VY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53860 1 351
+P53860	UniProtKB	Chain	1	351	.	.	.	ID=PRO_0000210745;Note=Phosphatidylinositol transfer protein PDR16	
+P53860	UniProtKB	Domain	135	295	.	.	.	Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056	
+P53860	UniProtKB	Beta strand	19	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	42	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Beta strand	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	79	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	87	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Turn	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8Z	
+P53860	UniProtKB	Helix	101	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	133	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	137	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Beta strand	144	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Beta strand	156	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	171	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Beta strand	195	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	221	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Beta strand	237	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	247	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	257	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Beta strand	268	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FMM	
+P53860	UniProtKB	Helix	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	285	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Beta strand	289	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	297	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+P53860	UniProtKB	Helix	330	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q	
+##sequence-region P38075 1 228
+P38075	UniProtKB	Chain	1	228	.	.	.	ID=PRO_0000167787;Note=Pyridoxamine 5'-phosphate oxidase	
+P38075	UniProtKB	Nucleotide binding	73	76	.	.	.	Note=FMN;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+P38075	UniProtKB	Nucleotide binding	88	89	.	.	.	Note=FMN;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+P38075	UniProtKB	Nucleotide binding	95	96	.	.	.	Note=FMN;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+P38075	UniProtKB	Nucleotide binding	153	154	.	.	.	Note=FMN;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+P38075	UniProtKB	Region	20	23	.	.	.	Note=Pyridoxal 5'-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFI7	
+P38075	UniProtKB	Region	205	207	.	.	.	Note=Pyridoxal 5'-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFI7	
+P38075	UniProtKB	Binding site	78	78	.	.	.	Note=Pyridoxal 5'-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NVS9	
+P38075	UniProtKB	Binding site	118	118	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFI7	
+P38075	UniProtKB	Binding site	136	136	.	.	.	Note=Pyridoxal 5'-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NVS9	
+P38075	UniProtKB	Binding site	140	140	.	.	.	Note=Pyridoxal 5'-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NVS9	
+P38075	UniProtKB	Binding site	144	144	.	.	.	Note=Pyridoxal 5'-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NVS9	
+P38075	UniProtKB	Binding site	199	199	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFI7	
+P38075	UniProtKB	Binding site	209	209	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFI7	
+P38075	UniProtKB	Cross-link	29	29	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P38075	UniProtKB	Helix	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Helix	35	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Beta strand	57	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Turn	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Beta strand	69	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Beta strand	82	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Helix	95	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Beta strand	105	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Turn	113	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Beta strand	117	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Helix	130	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Helix	142	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Beta strand	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Helix	160	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Beta strand	186	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Beta strand	208	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+P38075	UniProtKB	Beta strand	222	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0	
+##sequence-region P25362 1 215
+P25362	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000192043;Note=Protein PET18	
+P25362	UniProtKB	Sequence conflict	40	40	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25362	UniProtKB	Sequence conflict	104	104	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25362	UniProtKB	Sequence conflict	122	122	.	.	.	Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P80667 1 386
+P80667	UniProtKB	Chain	1	386	.	.	.	ID=PRO_0000058324;Note=Peroxisomal membrane protein PAS20	
+P80667	UniProtKB	Topological domain	1	263	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P80667	UniProtKB	Transmembrane	264	280	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P80667	UniProtKB	Topological domain	281	386	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P80667	UniProtKB	Domain	306	372	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P80667	UniProtKB	Helix	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R	
+P80667	UniProtKB	Beta strand	309	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R	
+P80667	UniProtKB	Turn	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R	
+P80667	UniProtKB	Beta strand	333	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R	
+P80667	UniProtKB	Beta strand	346	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R	
+P80667	UniProtKB	Turn	355	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NM7	
+P80667	UniProtKB	Beta strand	359	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R	
+P80667	UniProtKB	Helix	364	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R	
+P80667	UniProtKB	Beta strand	367	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R	
+##sequence-region P50091 1 288
+P50091	UniProtKB	Chain	1	288	.	.	.	ID=PRO_0000202855;Note=Peroxisomal membrane protein PEX21	
+P50091	UniProtKB	Helix	198	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P50091	UniProtKB	Helix	225	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P50091	UniProtKB	Helix	235	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P50091	UniProtKB	Beta strand	247	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P50091	UniProtKB	Beta strand	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P50091	UniProtKB	Turn	265	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+P50091	UniProtKB	Beta strand	269	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15	
+##sequence-region P25584 1 144
+P25584	UniProtKB	Chain	1	144	.	.	.	ID=PRO_0000202551;Note=Peroxisomal membrane protein PEX34	
+P25584	UniProtKB	Transmembrane	18	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25584	UniProtKB	Transmembrane	52	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25584	UniProtKB	Transmembrane	109	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47116 1 818
+P47116	UniProtKB	Chain	1	818	.	.	.	ID=PRO_0000086591;Note=Serine/threonine-protein kinase PTK2/STK2	
+P47116	UniProtKB	Domain	255	562	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P47116	UniProtKB	Nucleotide binding	261	269	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P47116	UniProtKB	Active site	388	388	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P47116	UniProtKB	Binding site	285	285	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P47116	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47116	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47116	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P47116	UniProtKB	Modified residue	623	623	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47116	UniProtKB	Modified residue	632	632	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47116	UniProtKB	Modified residue	694	694	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47116	UniProtKB	Modified residue	700	700	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47116	UniProtKB	Modified residue	711	711	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47116	UniProtKB	Modified residue	737	737	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P47116	UniProtKB	Modified residue	752	752	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47116	UniProtKB	Modified residue	755	755	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47116	UniProtKB	Modified residue	778	778	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47116	UniProtKB	Modified residue	781	781	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47116	UniProtKB	Sequence conflict	801	801	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P29461 1 750
+P29461	UniProtKB	Chain	1	750	.	.	.	ID=PRO_0000094856;Note=Tyrosine-protein phosphatase 2	
+P29461	UniProtKB	Domain	383	737	.	.	.	Note=Tyrosine-protein phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160	
+P29461	UniProtKB	Active site	666	666	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160,ECO:0000255|PROSITE-ProRule:PRU10044	
+P29461	UniProtKB	Modified residue	258	258	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P29461	UniProtKB	Modified residue	430	430	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P29461	UniProtKB	Sequence conflict	371	371	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29461	UniProtKB	Sequence conflict	474	475	.	.	.	Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29461	UniProtKB	Sequence conflict	660	661	.	.	.	Note=SP->GA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07244 1 802
+P07244	UniProtKB	Chain	1	802	.	.	.	ID=PRO_0000074941;Note=Bifunctional purine biosynthetic protein ADE5%2C7	
+P07244	UniProtKB	Domain	114	330	.	.	.	Note=ATP-grasp	
+P07244	UniProtKB	Nucleotide binding	140	203	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07244	UniProtKB	Region	1	450	.	.	.	Note=GARS	
+P07244	UniProtKB	Region	451	802	.	.	.	Note=AIRS	
+P07244	UniProtKB	Metal binding	298	298	.	.	.	Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07244	UniProtKB	Metal binding	300	300	.	.	.	Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07244	UniProtKB	Modified residue	455	455	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P07244	UniProtKB	Modified residue	458	458	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07244	UniProtKB	Sequence conflict	28	28	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P54113 1 591
+P54113	UniProtKB	Chain	1	591	.	.	.	ID=PRO_0000192159;Note=Bifunctional purine biosynthesis protein ADE16	
+##sequence-region P53294 1 404
+P53294	UniProtKB	Chain	1	404	.	.	.	ID=PRO_0000162757;Note=tRNA pseudouridine(31) synthase	
+P53294	UniProtKB	Active site	168	168	.	.	.	.	
+P53294	UniProtKB	Mutagenesis	168	168	.	.	.	Note=Loss of function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11406626;Dbxref=PMID:11406626	
+##sequence-region Q12069 1 462
+Q12069	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12069	UniProtKB	Chain	25	462	.	.	.	ID=PRO_0000162756;Note=tRNA pseudouridine(32) synthase%2C mitochondrial	
+Q12069	UniProtKB	Domain	127	188	.	.	.	Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182	
+Q12069	UniProtKB	Active site	238	238	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12069	UniProtKB	Sequence conflict	458	458	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P09368 1 476
+P09368	UniProtKB	Sequence conflict	50	50	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09368	UniProtKB	Sequence conflict	185	185	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P03962 1 267
+P03962	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P03962	UniProtKB	Chain	2	267	.	.	.	ID=PRO_0000134692;Note=Orotidine 5'-phosphate decarboxylase	
+P03962	UniProtKB	Region	59	61	.	.	.	Note=Substrate binding	
+P03962	UniProtKB	Region	91	100	.	.	.	Note=Substrate binding	
+P03962	UniProtKB	Active site	93	93	.	.	.	Note=Proton donor	
+P03962	UniProtKB	Binding site	37	37	.	.	.	Note=Substrate	
+P03962	UniProtKB	Binding site	217	217	.	.	.	Note=Substrate	
+P03962	UniProtKB	Binding site	235	235	.	.	.	Note=Substrate	
+P03962	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P03962	UniProtKB	Cross-link	93	93	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P03962	UniProtKB	Cross-link	209	209	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P03962	UniProtKB	Cross-link	253	253	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P03962	UniProtKB	Natural variant	160	160	.	.	.	Note=In strain: +D4. A->S	
+P03962	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Reduces Kcat 100-fold. Reduces substrate affinity 900-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278904;Dbxref=PMID:11278904	
+P03962	UniProtKB	Mutagenesis	91	91	.	.	.	Note=Reduces activity over 100000-fold. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278904;Dbxref=PMID:11278904	
+P03962	UniProtKB	Mutagenesis	93	93	.	.	.	Note=Reduces activity over 100000-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278904;Dbxref=PMID:11278904	
+P03962	UniProtKB	Mutagenesis	96	96	.	.	.	Note=Reduces Kcat over 100000-fold. Reduces substrate affinity 11-fold. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278904;Dbxref=PMID:11278904	
+P03962	UniProtKB	Mutagenesis	215	215	.	.	.	Note=No effect. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278904;Dbxref=PMID:11278904	
+P03962	UniProtKB	Sequence conflict	71	73	.	.	.	Note=EGT->RIR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03962	UniProtKB	Helix	6	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	16	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Beta strand	32	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	41	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Beta strand	56	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Turn	70	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	74	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Beta strand	87	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	98	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Turn	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	112	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Beta strand	117	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	128	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Beta strand	146	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	162	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Turn	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Beta strand	179	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	191	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Beta strand	198	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Beta strand	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Turn	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DQW	
+P03962	UniProtKB	Helix	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Beta strand	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	220	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Beta strand	229	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+P03962	UniProtKB	Helix	244	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM	
+##sequence-region Q9ZZX9 1 128
+Q9ZZX9	UniProtKB	Chain	1	128	.	.	.	ID=PRO_0000299678;Note=Putative uncharacterized protein Q0010%2C mitochondrial	
+##sequence-region Q9ZZW4 1 58
+Q9ZZW4	UniProtKB	Chain	1	58	.	.	.	ID=PRO_0000299682;Note=Putative uncharacterized protein Q0142%2C mitochondrial	
+##sequence-region Q9ZZW2 1 109
+Q9ZZW2	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299684;Note=Putative uncharacterized protein Q0144%2C mitochondrial	
+##sequence-region P43122 1 407
+P43122	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03179	
+P43122	UniProtKB	Chain	31	407	.	.	.	ID=PRO_0000096988;Note=tRNA N6-adenosine threonylcarbamoyltransferase%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03179	
+P43122	UniProtKB	Region	170	174	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372	
+P43122	UniProtKB	Region	328	329	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372	
+P43122	UniProtKB	Metal binding	145	145	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Metal binding	149	149	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Metal binding	361	361	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Binding site	203	203	.	.	.	Note=Substrate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372	
+P43122	UniProtKB	Binding site	217	217	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372	
+P43122	UniProtKB	Binding site	221	221	.	.	.	Note=Substrate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372	
+P43122	UniProtKB	Binding site	360	360	.	.	.	Note=Substrate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372	
+P43122	UniProtKB	Mutagenesis	39	39	.	.	.	Note=Severely impairs t(6)A37 formation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	43	43	.	.	.	Note=Severely impairs t(6)A37 formation. No effect on dimer formation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Severely impairs t(6)A37 formation. No effect on dimer formation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	77	77	.	.	.	Note=Severely impairs t(6)A37 formation. No effect on dimer formation. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Reduces enzyme activity by 35%25. Partially impairs dimer formation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Severely impairs t(6)A37 formation. Partially impairs dimer formation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	134	134	.	.	.	Note=Severely impairs t(6)A37 formation. Prevents dimerization. V->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	145	145	.	.	.	Note=Severely impairs t(6)A37 formation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Severely impairs t(6)A37 formation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	172	172	.	.	.	Note=Severely impairs t(6)A37 formation. S->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	207	207	.	.	.	Note=Severely impairs t(6)A37 formation. No effect on dimer formation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	258	258	.	.	.	Note=Severely impairs t(6)A37 formation. No effect on dimer formation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Mutagenesis	361	361	.	.	.	Note=Severely impairs t(6)A37 formation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P43122	UniProtKB	Beta strand	34	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	41	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	60	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Helix	82	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	109	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Helix	119	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	140	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Helix	145	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Helix	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Turn	155	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WUH	
+P43122	UniProtKB	Beta strand	164	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	176	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	187	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Helix	198	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Helix	216	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Helix	259	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Turn	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Helix	281	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Turn	311	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	320	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Helix	326	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Helix	330	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Turn	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	344	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	350	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WUH	
+P43122	UniProtKB	Helix	356	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Helix	364	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	379	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Turn	394	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+P43122	UniProtKB	Beta strand	402	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25	
+##sequence-region P41903 1 349
+P41903	UniProtKB	Chain	1	349	.	.	.	ID=PRO_0000202158;Note=Peroxisomal acyl-coenzyme A thioester hydrolase 1	
+P41903	UniProtKB	Motif	347	349	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41903	UniProtKB	Active site	259	259	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41903	UniProtKB	Active site	282	282	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41903	UniProtKB	Active site	333	333	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41903	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU	
+P41903	UniProtKB	Beta strand	21	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU	
+P41903	UniProtKB	Helix	42	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU	
+P41903	UniProtKB	Beta strand	62	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU	
+P41903	UniProtKB	Beta strand	81	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU	
+P41903	UniProtKB	Beta strand	91	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU	
+P41903	UniProtKB	Beta strand	105	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU	
+##sequence-region P25339 1 888
+P25339	UniProtKB	Chain	1	888	.	.	.	ID=PRO_0000075925;Note=Pumilio homology domain family member 4	
+P25339	UniProtKB	Domain	539	888	.	.	.	Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318	
+P25339	UniProtKB	Repeat	563	598	.	.	.	Note=Pumilio 1	
+P25339	UniProtKB	Repeat	599	634	.	.	.	Note=Pumilio 2	
+P25339	UniProtKB	Repeat	635	671	.	.	.	Note=Pumilio 3	
+P25339	UniProtKB	Repeat	672	707	.	.	.	Note=Pumilio 4	
+P25339	UniProtKB	Repeat	708	743	.	.	.	Note=Pumilio 5	
+P25339	UniProtKB	Repeat	744	783	.	.	.	Note=Pumilio 6	
+P25339	UniProtKB	Repeat	784	821	.	.	.	Note=Pumilio 7	
+P25339	UniProtKB	Repeat	823	861	.	.	.	Note=Pumilio 8	
+P25339	UniProtKB	Compositional bias	8	38	.	.	.	Note=Asp/Glu-rich (acidic)	
+P25339	UniProtKB	Compositional bias	471	542	.	.	.	Note=Asn-rich	
+P25339	UniProtKB	Compositional bias	521	535	.	.	.	Note=Poly-Asn	
+P25339	UniProtKB	Modified residue	205	205	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25339	UniProtKB	Modified residue	212	212	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P25339	UniProtKB	Modified residue	252	252	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25339	UniProtKB	Modified residue	256	256	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25339	UniProtKB	Sequence conflict	595	595	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25339	UniProtKB	Sequence conflict	595	595	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25339	UniProtKB	Turn	555	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	561	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Turn	564	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	568	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Beta strand	572	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DZS	
+P25339	UniProtKB	Helix	575	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	590	600	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	601	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	604	608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	613	623	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	626	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	637	639	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	640	645	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	649	659	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	663	673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	674	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	677	681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	686	696	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	699	711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	713	717	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	722	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	735	746	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	749	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	758	772	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	777	785	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	786	788	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	789	793	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	798	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	809	821	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	824	832	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	837	851	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	853	863	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	864	866	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	869	873	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Helix	875	881	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT	
+P25339	UniProtKB	Beta strand	883	885	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DZS	
+##sequence-region Q06991 1 263
+Q06991	UniProtKB	Chain	1	263	.	.	.	ID=PRO_0000247353;Note=Protein PUN1	
+Q06991	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06991	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06991	UniProtKB	Topological domain	28	143	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06991	UniProtKB	Transmembrane	144	164	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06991	UniProtKB	Topological domain	165	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06991	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06991	UniProtKB	Topological domain	194	223	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06991	UniProtKB	Transmembrane	224	244	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06991	UniProtKB	Topological domain	245	263	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06991	UniProtKB	Glycosylation	100	100	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06991	UniProtKB	Glycosylation	209	209	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06991	UniProtKB	Cross-link	260	260	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q06991	UniProtKB	Sequence conflict	42	42	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38972 1 1358
+P38972	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38972	UniProtKB	Chain	2	1358	.	.	.	ID=PRO_0000100405;Note=Phosphoribosylformylglycinamidine synthase	
+P38972	UniProtKB	Domain	1093	1358	.	.	.	Note=Glutamine amidotransferase type-1	
+P38972	UniProtKB	Nucleotide binding	345	356	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38972	UniProtKB	Nucleotide binding	424	426	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38972	UniProtKB	Active site	1187	1187	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38972	UniProtKB	Active site	1319	1319	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38972	UniProtKB	Active site	1321	1321	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38972	UniProtKB	Metal binding	720	720	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38972	UniProtKB	Metal binding	762	762	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38972	UniProtKB	Metal binding	766	766	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38972	UniProtKB	Metal binding	930	930	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38972	UniProtKB	Binding site	719	719	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38972	UniProtKB	Binding site	932	932	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38972	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38972	UniProtKB	Sequence conflict	84	84	.	.	.	Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38972	UniProtKB	Sequence conflict	219	220	.	.	.	Note=DS->EC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38972	UniProtKB	Sequence conflict	226	226	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38972	UniProtKB	Sequence conflict	492	492	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38972	UniProtKB	Sequence conflict	499	499	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38972	UniProtKB	Sequence conflict	551	551	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38972	UniProtKB	Sequence conflict	604	604	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38972	UniProtKB	Sequence conflict	1169	1170	.	.	.	Note=SQ->TSSK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38972	UniProtKB	Sequence conflict	1298	1298	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53167 1 370
+P53167	UniProtKB	Chain	1	370	.	.	.	ID=PRO_0000057532;Note=tRNA pseudouridine(27/28) synthase	
+P53167	UniProtKB	Active site	56	56	.	.	.	Note=Nucleophile	
+P53167	UniProtKB	Binding site	111	111	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53167	UniProtKB	Mutagenesis	56	56	.	.	.	Note=Abolishes catalytic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17684231;Dbxref=PMID:17684231	
+P53167	UniProtKB	Sequence conflict	136	136	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53167	UniProtKB	Sequence conflict	136	136	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11154 1 1178
+P11154	UniProtKB	Chain	1	1178	.	.	.	ID=PRO_0000146824;Note=Pyruvate carboxylase 1	
+P11154	UniProtKB	Domain	18	470	.	.	.	Note=Biotin carboxylation	
+P11154	UniProtKB	Domain	140	337	.	.	.	Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P11154	UniProtKB	Domain	557	824	.	.	.	Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151	
+P11154	UniProtKB	Domain	1094	1169	.	.	.	Note=Biotinyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066	
+P11154	UniProtKB	Region	565	569	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Active site	312	312	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Metal binding	566	566	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Metal binding	734	734	.	.	.	Note=Divalent metal cation%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Metal binding	764	764	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Metal binding	766	766	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Binding site	136	136	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Binding site	220	220	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Binding site	255	255	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Binding site	638	638	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Binding site	898	898	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Modified residue	734	734	.	.	.	Note=N6-carboxylysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11154	UniProtKB	Modified residue	1135	1135	.	.	.	Note=N6-biotinyllysine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01066,ECO:0000269|PubMed:3042770;Dbxref=PMID:3042770	
+P11154	UniProtKB	Sequence conflict	462	462	.	.	.	Note=T->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11154	UniProtKB	Sequence conflict	493	493	.	.	.	Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11154	UniProtKB	Sequence conflict	595	595	.	.	.	Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11154	UniProtKB	Sequence conflict	619	619	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11154	UniProtKB	Sequence conflict	664	664	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11154	UniProtKB	Sequence conflict	772	772	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11154	UniProtKB	Sequence conflict	879	879	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11154	UniProtKB	Sequence conflict	909	909	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P28272 1 314
+P28272	UniProtKB	Chain	1	314	.	.	.	ID=PRO_0000148506;Note=Dihydroorotate dehydrogenase (fumarate)	
+P28272	UniProtKB	Nucleotide binding	46	47	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Nucleotide binding	252	253	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Nucleotide binding	274	275	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Region	70	74	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Region	196	197	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Active site	133	133	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Binding site	46	46	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Binding site	130	130	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Binding site	130	130	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Binding site	167	167	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Binding site	195	195	.	.	.	Note=FMN%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Binding site	224	224	.	.	.	Note=FMN%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28272	UniProtKB	Cross-link	46	46	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P28272	UniProtKB	Natural variant	58	58	.	.	.	Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+##sequence-region Q9ZZV8 1 51
+Q9ZZV8	UniProtKB	Chain	1	51	.	.	.	ID=PRO_0000299686;Note=Putative uncharacterized protein Q0297%2C mitochondrial	
+##sequence-region Q12355 1 444
+Q12355	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Chain	20	419	.	.	.	ID=PRO_0000033193;Note=Cell wall mannoprotein PST1	
+Q12355	UniProtKB	Propeptide	420	444	.	.	.	ID=PRO_0000033194;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Compositional bias	22	26	.	.	.	Note=Poly-Ser	
+Q12355	UniProtKB	Compositional bias	356	416	.	.	.	Note=Ser-rich	
+Q12355	UniProtKB	Lipidation	419	419	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Glycosylation	57	57	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Glycosylation	76	76	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Glycosylation	83	83	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Glycosylation	86	86	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Glycosylation	196	196	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Glycosylation	210	210	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17024473;Dbxref=PMID:17024473	
+Q12355	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17024473;Dbxref=PMID:17024473	
+Q12355	UniProtKB	Glycosylation	235	235	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17024473;Dbxref=PMID:17024473	
+Q12355	UniProtKB	Glycosylation	242	242	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17024473;Dbxref=PMID:17024473	
+Q12355	UniProtKB	Glycosylation	263	263	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Glycosylation	268	268	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Glycosylation	280	280	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Glycosylation	292	292	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Glycosylation	305	305	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12355	UniProtKB	Glycosylation	329	329	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17024473;Dbxref=PMID:17024473	
+##sequence-region P39927 1 425
+P39927	UniProtKB	Chain	1	425	.	.	.	ID=PRO_0000076294;Note=Protein PTI1	
+P39927	UniProtKB	Modified residue	272	272	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39927	UniProtKB	Sequence conflict	300	300	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P27616 1 306
+P27616	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9551557;Dbxref=PMID:22814378,PMID:9551557	
+P27616	UniProtKB	Chain	2	306	.	.	.	ID=PRO_0000100929;Note=Phosphoribosylaminoimidazole-succinocarboxamide synthase	
+P27616	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9551557;Dbxref=PMID:22814378,PMID:9551557	
+P27616	UniProtKB	Sequence conflict	185	185	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27616	UniProtKB	Sequence conflict	185	185	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27616	UniProtKB	Beta strand	14	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Beta strand	19	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Beta strand	30	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Helix	53	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Turn	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Beta strand	72	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Helix	85	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Helix	91	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Helix	96	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Beta strand	105	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Beta strand	116	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Helix	127	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Beta strand	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Beta strand	153	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Helix	176	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Helix	185	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Beta strand	211	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Turn	224	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Beta strand	228	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Turn	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Beta strand	241	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Turn	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Turn	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNU	
+P27616	UniProtKB	Helix	261	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+P27616	UniProtKB	Helix	282	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ	
+##sequence-region Q05911 1 482
+Q05911	UniProtKB	Chain	1	482	.	.	.	ID=PRO_0000137899;Note=Adenylosuccinate lyase	
+Q05911	UniProtKB	Region	14	15	.	.	.	Note=Substrate binding%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05911	UniProtKB	Region	82	84	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05911	UniProtKB	Region	108	109	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05911	UniProtKB	Active site	156	156	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05911	UniProtKB	Active site	286	286	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05911	UniProtKB	Binding site	238	238	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05911	UniProtKB	Binding site	300	300	.	.	.	Note=Substrate%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05911	UniProtKB	Binding site	326	326	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05911	UniProtKB	Binding site	331	331	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05911	UniProtKB	Binding site	335	335	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q05911	UniProtKB	Cross-link	196	196	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region Q35811 1 46
+Q35811	UniProtKB	Chain	1	46	.	.	.	ID=PRO_0000299681;Note=Putative uncharacterized protein Q0092%2C mitochondrial	
+##sequence-region Q9ZZW1 1 134
+Q9ZZW1	UniProtKB	Chain	1	134	.	.	.	ID=PRO_0000299685;Note=Putative uncharacterized protein Q0182%2C mitochondrial	
+##sequence-region P04046 1 510
+P04046	UniProtKB	Chain	1	510	.	.	.	ID=PRO_0000139647;Note=Amidophosphoribosyltransferase	
+P04046	UniProtKB	Domain	2	239	.	.	.	Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609	
+P04046	UniProtKB	Active site	2	2	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609	
+P04046	UniProtKB	Metal binding	373	373	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04046	UniProtKB	Metal binding	374	374	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04046	UniProtKB	Sequence conflict	46	47	.	.	.	Note=IY->VC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04046	UniProtKB	Sequence conflict	46	47	.	.	.	Note=IY->VC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04046	UniProtKB	Sequence conflict	62	62	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04046	UniProtKB	Sequence conflict	62	62	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04046	UniProtKB	Sequence conflict	82	87	.	.	.	Note=GSSANS->PLRLIL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04046	UniProtKB	Sequence conflict	156	158	.	.	.	Note=VFH->GFSN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04046	UniProtKB	Sequence conflict	156	158	.	.	.	Note=VFH->GFSN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04046	UniProtKB	Sequence conflict	234	234	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04046	UniProtKB	Sequence conflict	234	234	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04046	UniProtKB	Sequence conflict	291	291	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04046	UniProtKB	Sequence conflict	291	291	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38009 1 592
+P38009	UniProtKB	Chain	1	592	.	.	.	ID=PRO_0000192160;Note=Bifunctional purine biosynthesis protein ADE17	
+P38009	UniProtKB	Sequence conflict	389	389	.	.	.	Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06244 1 254
+Q06244	UniProtKB	Chain	1	254	.	.	.	ID=PRO_0000162754;Note=21S rRNA pseudouridine(2819) synthase	
+Q06244	UniProtKB	Active site	71	71	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P25502 1 979
+P25502	UniProtKB	Chain	1	979	.	.	.	ID=PRO_0000114968;Note=Proline utilization trans-activator	
+P25502	UniProtKB	DNA binding	34	60	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P25502	UniProtKB	Metal binding	34	34	.	.	.	Note=Zinc 1	
+P25502	UniProtKB	Metal binding	34	34	.	.	.	Note=Zinc 2	
+P25502	UniProtKB	Metal binding	37	37	.	.	.	Note=Zinc 1	
+P25502	UniProtKB	Metal binding	44	44	.	.	.	Note=Zinc 1	
+P25502	UniProtKB	Metal binding	50	50	.	.	.	Note=Zinc 1	
+P25502	UniProtKB	Metal binding	50	50	.	.	.	Note=Zinc 2	
+P25502	UniProtKB	Metal binding	53	53	.	.	.	Note=Zinc 2	
+P25502	UniProtKB	Metal binding	60	60	.	.	.	Note=Zinc 2	
+P25502	UniProtKB	Helix	35	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZME	
+P25502	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZME	
+P25502	UniProtKB	Helix	51	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZME	
+P25502	UniProtKB	Beta strand	68	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZME	
+P25502	UniProtKB	Helix	73	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZME	
+##sequence-region P08525 1 94
+P08525	UniProtKB	Chain	1	94	.	.	.	ID=PRO_0000193551;Note=Cytochrome b-c1 complex subunit 8	
+P08525	UniProtKB	Beta strand	23	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08525	UniProtKB	Helix	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08525	UniProtKB	Beta strand	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PD4	
+P08525	UniProtKB	Turn	41	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08525	UniProtKB	Beta strand	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08525	UniProtKB	Helix	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08525	UniProtKB	Helix	56	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08525	UniProtKB	Helix	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P08525	UniProtKB	Helix	86	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+##sequence-region P38230 1 334
+P38230	UniProtKB	Chain	1	334	.	.	.	ID=PRO_0000160912;Note=Probable quinone oxidoreductase	
+P38230	UniProtKB	Beta strand	7	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	23	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	37	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	51	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	63	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	69	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	90	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	99	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	109	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	120	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	151	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	160	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	175	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	183	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	195	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Turn	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	205	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Turn	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	218	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	226	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	230	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	237	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	248	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWA	
+P38230	UniProtKB	Helix	258	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Turn	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	273	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	280	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	303	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	309	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Helix	312	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+P38230	UniProtKB	Beta strand	326	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB	
+##sequence-region P06838 1 210
+P06838	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000097149;Note=DNA repair protein RAD10	
+P06838	UniProtKB	DNA binding	133	153	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06838	UniProtKB	Motif	17	23	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32641 1 659
+P32641	UniProtKB	Chain	1	659	.	.	.	ID=PRO_0000209953;Note=Checkpoint protein RAD24	
+P32641	UniProtKB	Nucleotide binding	109	116	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32641	UniProtKB	Modified residue	652	652	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32641	UniProtKB	Modified residue	654	654	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32641	UniProtKB	Mutagenesis	115	115	.	.	.	Note=Reduces NTP-binding and hydrolysis. Shows DNA damage sensitivity. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10913172;Dbxref=PMID:10913172	
+P32641	UniProtKB	Mutagenesis	115	115	.	.	.	Note=No effect on NTP-binding and hydrolysis. Resistant to DNA damage. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10913172;Dbxref=PMID:10913172	
+##sequence-region Q00578 1 843
+Q00578	UniProtKB	Chain	1	843	.	.	.	ID=PRO_0000101994;Note=DNA repair helicase RAD25	
+Q00578	UniProtKB	Domain	373	535	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q00578	UniProtKB	Domain	589	743	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q00578	UniProtKB	Nucleotide binding	386	393	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q00578	UniProtKB	Motif	64	75	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q00578	UniProtKB	Motif	487	491	.	.	.	Note=DEVH box	
+Q00578	UniProtKB	Compositional bias	302	309	.	.	.	Note=Asp/Glu-rich (acidic)	
+Q00578	UniProtKB	Modified residue	752	752	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q00578	UniProtKB	Natural variant	427	427	.	.	.	Note=In suppressor mutant. W->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1318786;Dbxref=PMID:1318786	
+Q00578	UniProtKB	Sequence conflict	9	9	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00578	UniProtKB	Sequence conflict	48	48	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04231 1 177
+Q04231	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04231	UniProtKB	Chain	2	177	.	.	.	ID=PRO_0000203263;Note=DNA repair protein RAD33	
+Q04231	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04231	UniProtKB	Cross-link	19	19	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P14736 1 754
+P14736	UniProtKB	Chain	1	754	.	.	.	ID=PRO_0000218298;Note=DNA repair protein RAD4	
+P14736	UniProtKB	DNA binding	250	269	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14736	UniProtKB	Sequence conflict	223	223	.	.	.	Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14736	UniProtKB	Sequence conflict	225	225	.	.	.	Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14736	UniProtKB	Sequence conflict	225	225	.	.	.	Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14736	UniProtKB	Turn	91	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M14	
+P14736	UniProtKB	Helix	124	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSH	
+P14736	UniProtKB	Helix	134	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	165	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	177	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	193	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSH	
+P14736	UniProtKB	Helix	230	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Turn	236	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	248	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	262	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	280	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	306	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	314	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Turn	322	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	326	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	337	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Turn	352	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	362	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	372	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	376	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	383	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	388	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	392	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	396	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	416	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	436	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSH	
+P14736	UniProtKB	Helix	439	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	445	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	450	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	457	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	466	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	478	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	484	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	487	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	493	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Turn	498	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	501	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	510	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	529	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	534	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	537	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	564	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	571	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	579	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	591	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Beta strand	601	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YIR	
+P14736	UniProtKB	Beta strand	607	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	616	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSH	
+P14736	UniProtKB	Helix	619	627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P14736	UniProtKB	Helix	629	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+##sequence-region P06778 1 471
+P06778	UniProtKB	Chain	1	471	.	.	.	ID=PRO_0000173892;Note=DNA repair and recombination protein RAD52	
+P06778	UniProtKB	Alternative sequence	1	6	.	.	.	ID=VSP_019613;Note=In isoform 3. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06778	UniProtKB	Alternative sequence	1	4	.	.	.	ID=VSP_019612;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P22216 1 821
+P22216	UniProtKB	Chain	1	821	.	.	.	ID=PRO_0000086595;Note=Serine/threonine-protein kinase RAD53	
+P22216	UniProtKB	Domain	66	116	.	.	.	Note=FHA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+P22216	UniProtKB	Domain	198	466	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22216	UniProtKB	Domain	601	664	.	.	.	Note=FHA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+P22216	UniProtKB	Nucleotide binding	204	212	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22216	UniProtKB	Active site	319	319	.	.	.	Note=Proton acceptor	
+P22216	UniProtKB	Binding site	227	227	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22216	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22216	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22216	UniProtKB	Modified residue	547	547	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22216	UniProtKB	Modified residue	560	560	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22216	UniProtKB	Modified residue	774	774	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P22216	UniProtKB	Modified residue	793	793	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22216	UniProtKB	Sequence conflict	204	204	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22216	UniProtKB	Helix	16	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G	
+P22216	UniProtKB	Beta strand	31	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G	
+P22216	UniProtKB	Beta strand	46	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G	
+P22216	UniProtKB	Helix	52	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G	
+P22216	UniProtKB	Beta strand	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G	
+P22216	UniProtKB	Beta strand	64	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G	
+P22216	UniProtKB	Beta strand	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G	
+P22216	UniProtKB	Turn	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G	
+P22216	UniProtKB	Beta strand	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G	
+P22216	UniProtKB	Beta strand	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J4O	
+P22216	UniProtKB	Beta strand	99	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G	
+P22216	UniProtKB	Beta strand	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G	
+P22216	UniProtKB	Beta strand	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G	
+P22216	UniProtKB	Beta strand	120	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G	
+P22216	UniProtKB	Beta strand	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G	
+P22216	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G	
+P22216	UniProtKB	Beta strand	141	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G	
+P22216	UniProtKB	Helix	149	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G	
+P22216	UniProtKB	Beta strand	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K3N	
+P22216	UniProtKB	Helix	193	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Beta strand	197	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Beta strand	211	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Turn	218	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Beta strand	223	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	241	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Beta strand	259	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Beta strand	269	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	281	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	293	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Beta strand	325	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Turn	330	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Beta strand	334	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	359	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	364	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Turn	384	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	387	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	413	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	428	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	437	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	451	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	457	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Turn	464	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Helix	484	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP	
+P22216	UniProtKB	Beta strand	551	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5	
+P22216	UniProtKB	Helix	563	565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5	
+P22216	UniProtKB	Beta strand	572	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5	
+P22216	UniProtKB	Beta strand	578	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	586	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5	
+P22216	UniProtKB	Beta strand	592	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	601	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	609	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	620	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	636	638	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FHQ	
+P22216	UniProtKB	Beta strand	645	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	653	655	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5	
+P22216	UniProtKB	Beta strand	657	659	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FHQ	
+P22216	UniProtKB	Beta strand	662	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FHQ	
+P22216	UniProtKB	Beta strand	666	671	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	678	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Turn	684	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	688	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5	
+P22216	UniProtKB	Beta strand	692	695	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	703	707	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	710	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	716	718	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Helix	721	728	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ	
+P22216	UniProtKB	Beta strand	804	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YGV	
+P22216	UniProtKB	Helix	811	813	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YGV	
+##sequence-region P38953 1 406
+P38953	UniProtKB	Chain	1	406	.	.	.	ID=PRO_0000122954;Note=DNA repair protein RAD55	
+P38953	UniProtKB	Nucleotide binding	43	50	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38953	UniProtKB	Compositional bias	277	287	.	.	.	Note=Ser-rich	
+P38953	UniProtKB	Compositional bias	371	378	.	.	.	Note=Ser-rich	
+P38953	UniProtKB	Sequence conflict	110	110	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38953	UniProtKB	Sequence conflict	197	197	.	.	.	Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P06779 1 565
+P06779	UniProtKB	Chain	1	565	.	.	.	ID=PRO_0000097155;Note=DNA repair protein RAD7	
+P06779	UniProtKB	Region	1	200	.	.	.	Note=Hydrophilic	
+P06779	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06779	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06779	UniProtKB	Sequence conflict	278	279	.	.	.	Note=LL->FV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06779	UniProtKB	Sequence conflict	504	505	.	.	.	Note=AC->RP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32864 1 603
+P32864	UniProtKB	Chain	1	603	.	.	.	ID=PRO_0000056693;Note=Rab proteins geranylgeranyltransferase component A	
+P32864	UniProtKB	Modified residue	470	470	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950	
+P32864	UniProtKB	Sequence conflict	132	137	.	.	.	Note=DLSPKI->MIFPRV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32864	UniProtKB	Sequence conflict	300	300	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32864	UniProtKB	Sequence conflict	300	300	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32864	UniProtKB	Sequence conflict	300	300	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06891 1 181
+Q06891	UniProtKB	Chain	1	181	.	.	.	ID=PRO_0000283651;Note=Trans-acting factor D	
+Q06891	UniProtKB	Natural variant	33	33	.	.	.	Note=In strain: ATCC 7754. V->A	
+Q06891	UniProtKB	Natural variant	36	36	.	.	.	Note=In strain: ATCC 7754. K->R	
+Q06891	UniProtKB	Natural variant	46	51	.	.	.	Note=In strain: ATCC 7754. RIPRTI->KVPQTV	
+Q06891	UniProtKB	Natural variant	67	68	.	.	.	Note=In strain: ATCC 7754. RS->KF	
+Q06891	UniProtKB	Natural variant	104	104	.	.	.	Note=In strain: ATCC 7754. R->K	
+Q06891	UniProtKB	Natural variant	116	116	.	.	.	Note=In strain: ATCC 7754. L->S	
+Q06891	UniProtKB	Natural variant	125	125	.	.	.	Note=In strain: ATCC 7754. D->N	
+Q06891	UniProtKB	Natural variant	136	136	.	.	.	Note=In strain: ATCC 7754. I->T	
+Q06891	UniProtKB	Natural variant	137	137	.	.	.	Note=In strain: ATCC 4108. R->H	
+Q06891	UniProtKB	Natural variant	144	144	.	.	.	Note=In strain: ATCC 7754. N->D	
+Q06891	UniProtKB	Natural variant	152	157	.	.	.	Note=In strain: ATCC 7754. IYDRTC->NYGRTG	
+Q06891	UniProtKB	Natural variant	162	162	.	.	.	Note=In strain: ATCC 7754. N->D	
+Q06891	UniProtKB	Natural variant	171	171	.	.	.	Note=In strain: ATCC 7754. F->L	
+Q06891	UniProtKB	Natural variant	180	180	.	.	.	Note=In strain: ATCC 7754. P->S	
+##sequence-region P25635 1 923
+P25635	UniProtKB	Chain	1	923	.	.	.	ID=PRO_0000051179;Note=Periodic tryptophan protein 2	
+P25635	UniProtKB	Repeat	12	52	.	.	.	Note=WD 1	
+P25635	UniProtKB	Repeat	53	93	.	.	.	Note=WD 2	
+P25635	UniProtKB	Repeat	94	132	.	.	.	Note=WD 3	
+P25635	UniProtKB	Repeat	144	183	.	.	.	Note=WD 4	
+P25635	UniProtKB	Repeat	189	228	.	.	.	Note=WD 5	
+P25635	UniProtKB	Repeat	258	297	.	.	.	Note=WD 6	
+P25635	UniProtKB	Repeat	300	340	.	.	.	Note=WD 7	
+P25635	UniProtKB	Repeat	343	382	.	.	.	Note=WD 8	
+P25635	UniProtKB	Repeat	385	424	.	.	.	Note=WD 9	
+P25635	UniProtKB	Repeat	428	470	.	.	.	Note=WD 10	
+P25635	UniProtKB	Repeat	471	510	.	.	.	Note=WD 11	
+P25635	UniProtKB	Repeat	513	552	.	.	.	Note=WD 12	
+P25635	UniProtKB	Repeat	575	614	.	.	.	Note=WD 13	
+P25635	UniProtKB	Repeat	676	714	.	.	.	Note=WD 14	
+P25635	UniProtKB	Compositional bias	226	240	.	.	.	Note=Asp/Glu-rich (acidic)	
+P25635	UniProtKB	Compositional bias	862	923	.	.	.	Note=Asp/Glu-rich (acidic)	
+P25635	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25635	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25635	UniProtKB	Modified residue	651	651	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25635	UniProtKB	Modified residue	664	664	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25635	UniProtKB	Modified residue	912	912	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25635	UniProtKB	Modified residue	913	913	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P34230 1 853
+P34230	UniProtKB	Chain	1	853	.	.	.	ID=PRO_0000093315;Note=Peroxisomal long-chain fatty acid import protein 1	
+P34230	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P34230	UniProtKB	Transmembrane	166	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P34230	UniProtKB	Transmembrane	269	289	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P34230	UniProtKB	Transmembrane	364	384	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P34230	UniProtKB	Domain	127	417	.	.	.	Note=ABC transmembrane type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P34230	UniProtKB	Domain	472	747	.	.	.	Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P34230	UniProtKB	Nucleotide binding	505	512	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P34230	UniProtKB	Glycosylation	33	33	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34230	UniProtKB	Glycosylation	39	39	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34230	UniProtKB	Glycosylation	162	162	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34230	UniProtKB	Glycosylation	230	230	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34230	UniProtKB	Glycosylation	241	241	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34230	UniProtKB	Glycosylation	267	267	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34230	UniProtKB	Glycosylation	295	295	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34230	UniProtKB	Glycosylation	560	560	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34230	UniProtKB	Glycosylation	608	608	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34230	UniProtKB	Glycosylation	620	620	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34230	UniProtKB	Glycosylation	647	647	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34230	UniProtKB	Glycosylation	836	836	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32327 1 1180
+P32327	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32327	UniProtKB	Chain	2	1180	.	.	.	ID=PRO_0000146825;Note=Pyruvate carboxylase 2	
+P32327	UniProtKB	Domain	19	471	.	.	.	Note=Biotin carboxylation	
+P32327	UniProtKB	Domain	141	338	.	.	.	Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P32327	UniProtKB	Domain	558	825	.	.	.	Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151	
+P32327	UniProtKB	Domain	1095	1170	.	.	.	Note=Biotinyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066	
+P32327	UniProtKB	Region	566	570	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Active site	313	313	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Metal binding	567	567	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Metal binding	735	735	.	.	.	Note=Divalent metal cation%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Metal binding	765	765	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Metal binding	767	767	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Binding site	137	137	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Binding site	221	221	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Binding site	256	256	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Binding site	639	639	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Binding site	899	899	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32327	UniProtKB	Modified residue	735	735	.	.	.	Note=N6-carboxylysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32327	UniProtKB	Modified residue	1136	1136	.	.	.	Note=N6-biotinyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066	
+P32327	UniProtKB	Sequence conflict	15	15	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	132	132	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	238	238	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	268	268	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	546	546	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	642	642	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	771	773	.	.	.	Note=GTA->STR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	831	831	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	839	839	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	1001	1001	.	.	.	Note=Y->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	1155	1155	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	1178	1178	.	.	.	Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32327	UniProtKB	Sequence conflict	1180	1180	.	.	.	Note=K->KVIFTR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P13298 1 226
+P13298	UniProtKB	Chain	1	226	.	.	.	ID=PRO_0000110804;Note=Orotate phosphoribosyltransferase 1	
+P13298	UniProtKB	Region	38	39	.	.	.	Note=Orotate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13298	UniProtKB	Region	76	77	.	.	.	Note=5-phosphoribose 1-diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13298	UniProtKB	Region	132	140	.	.	.	Note=5-phosphoribose 1-diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13298	UniProtKB	Binding site	30	30	.	.	.	Note=5-phosphoribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13298	UniProtKB	Binding site	106	106	.	.	.	Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13298	UniProtKB	Binding site	107	107	.	.	.	Note=5-phosphoribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13298	UniProtKB	Binding site	110	110	.	.	.	Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13298	UniProtKB	Binding site	112	112	.	.	.	Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13298	UniProtKB	Binding site	136	136	.	.	.	Note=Orotate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13298	UniProtKB	Binding site	164	164	.	.	.	Note=Orotate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13298	UniProtKB	Modified residue	213	213	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13298	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13298	UniProtKB	Sequence conflict	150	150	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13298	UniProtKB	Helix	7	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Beta strand	21	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Beta strand	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WN3	
+P13298	UniProtKB	Beta strand	34	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Helix	47	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Beta strand	69	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Turn	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Helix	78	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Helix	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Beta strand	101	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Beta strand	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Beta strand	127	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WN3	
+P13298	UniProtKB	Helix	139	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Beta strand	154	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Beta strand	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Helix	178	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Beta strand	190	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Helix	196	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Turn	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+P13298	UniProtKB	Helix	209	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML	
+##sequence-region P37299 1 77
+P37299	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1325905;Dbxref=PMID:1325905	
+P37299	UniProtKB	Chain	2	77	.	.	.	ID=PRO_0000193563;Note=Cytochrome b-c1 complex subunit 10	
+P37299	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P07256 1 457
+P07256	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion	
+P07256	UniProtKB	Chain	27	457	.	.	.	ID=PRO_0000026788;Note=Cytochrome b-c1 complex subunit 1%2C mitochondrial	
+P07256	UniProtKB	Beta strand	30	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Beta strand	47	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Turn	64	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	69	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	80	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Beta strand	92	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Beta strand	102	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EZV	
+P07256	UniProtKB	Helix	113	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Turn	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	134	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	156	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Turn	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	182	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	190	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Beta strand	206	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	216	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Beta strand	247	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Beta strand	256	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	275	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Beta strand	287	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	295	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	302	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Turn	308	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Beta strand	313	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Beta strand	326	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	340	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	360	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	383	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	403	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Helix	415	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Turn	426	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Beta strand	432	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07256	UniProtKB	Beta strand	440	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PD4	
+P07256	UniProtKB	Helix	445	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+##sequence-region P06777 1 1100
+P06777	UniProtKB	Chain	1	1100	.	.	.	ID=PRO_0000198857;Note=DNA repair protein RAD1	
+P06777	UniProtKB	Domain	821	901	.	.	.	Note=ERCC4	
+P06777	UniProtKB	Compositional bias	1	110	.	.	.	Note=Asp/Glu-rich (acidic)	
+P06777	UniProtKB	Compositional bias	516	576	.	.	.	Note=Arg/Lys-rich (basic)	
+P06777	UniProtKB	Compositional bias	595	689	.	.	.	Note=Asp/Glu-rich (acidic)	
+P06777	UniProtKB	Compositional bias	1041	1100	.	.	.	Note=Asp/Glu-rich (acidic)	
+P06777	UniProtKB	Modified residue	613	613	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06777	UniProtKB	Modified residue	1071	1071	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06777	UniProtKB	Modified residue	1072	1072	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06777	UniProtKB	Sequence conflict	223	223	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06777	UniProtKB	Sequence conflict	883	883	.	.	.	Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06777	UniProtKB	Sequence conflict	886	886	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06777	UniProtKB	Sequence conflict	912	912	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06777	UniProtKB	Sequence conflict	924	924	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06777	UniProtKB	Sequence conflict	1016	1016	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32628 1 398
+P32628	UniProtKB	Chain	1	398	.	.	.	ID=PRO_0000114902;Note=UV excision repair protein RAD23	
+P32628	UniProtKB	Domain	1	77	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+P32628	UniProtKB	Domain	146	186	.	.	.	Note=UBA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
+P32628	UniProtKB	Domain	355	395	.	.	.	Note=UBA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
+P32628	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32628	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32628	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32628	UniProtKB	Cross-link	49	49	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32628	UniProtKB	Sequence conflict	277	277	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32628	UniProtKB	Sequence conflict	277	277	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32628	UniProtKB	Sequence conflict	277	277	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32628	UniProtKB	Sequence conflict	277	277	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32628	UniProtKB	Beta strand	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P32628	UniProtKB	Beta strand	9	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NBW	
+P32628	UniProtKB	Beta strand	13	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P32628	UniProtKB	Helix	24	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P32628	UniProtKB	Turn	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P32628	UniProtKB	Helix	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P32628	UniProtKB	Beta strand	43	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P32628	UniProtKB	Turn	57	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P32628	UniProtKB	Beta strand	67	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62	
+P32628	UniProtKB	Helix	259	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P32628	UniProtKB	Helix	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P32628	UniProtKB	Helix	276	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P32628	UniProtKB	Helix	290	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P32628	UniProtKB	Helix	298	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P32628	UniProtKB	Helix	355	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P32628	UniProtKB	Turn	366	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P32628	UniProtKB	Helix	371	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P32628	UniProtKB	Turn	381	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+P32628	UniProtKB	Helix	385	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF	
+##sequence-region P06839 1 778
+P06839	UniProtKB	Chain	1	778	.	.	.	ID=PRO_0000101983;Note=DNA repair helicase RAD3	
+P06839	UniProtKB	Domain	7	285	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P06839	UniProtKB	Nucleotide binding	42	49	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P06839	UniProtKB	Motif	235	238	.	.	.	Note=DEAH box	
+P06839	UniProtKB	Compositional bias	759	778	.	.	.	Note=Asp/Glu-rich (acidic)	
+P06839	UniProtKB	Metal binding	115	115	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06839	UniProtKB	Metal binding	133	133	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06839	UniProtKB	Metal binding	156	156	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06839	UniProtKB	Metal binding	191	191	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06839	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Abolishes ATPase and DNA helicase activities but not ATP-binding capacity. K->R%2CA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16973432,ECO:0000269|PubMed:1719538,ECO:0000269|PubMed:2846277;Dbxref=PMID:16973432,PMID:1719538,PMID:2846277	
+P06839	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Confers an UV-sensitive phenotype. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16973432;Dbxref=PMID:16973432	
+P06839	UniProtKB	Mutagenesis	115	115	.	.	.	Note=Confers an UV-sensitive phenotype. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16973432;Dbxref=PMID:16973432	
+P06839	UniProtKB	Sequence conflict	2	2	.	.	.	Note=K->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12270 1 262
+Q12270	UniProtKB	Chain	1	262	.	.	.	ID=PRO_0000206193;Note=Rhomboid protein 2	
+Q12270	UniProtKB	Topological domain	1	16	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Topological domain	38	57	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Transmembrane	58	78	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Topological domain	79	89	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Topological domain	111	112	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Topological domain	134	151	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Transmembrane	152	168	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Topological domain	169	174	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Transmembrane	175	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Topological domain	192	262	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12270	UniProtKB	Active site	124	124	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12270	UniProtKB	Active site	179	179	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P50086 1 228
+P50086	UniProtKB	Chain	1	228	.	.	.	ID=PRO_0000067048;Note=Probable 26S proteasome regulatory subunit p28	
+P50086	UniProtKB	Repeat	1	30	.	.	.	Note=ANK 1	
+P50086	UniProtKB	Repeat	35	64	.	.	.	Note=ANK 2	
+P50086	UniProtKB	Repeat	71	100	.	.	.	Note=ANK 3	
+P50086	UniProtKB	Repeat	106	135	.	.	.	Note=ANK 4	
+P50086	UniProtKB	Repeat	139	168	.	.	.	Note=ANK 5	
+P50086	UniProtKB	Repeat	173	203	.	.	.	Note=ANK 6	
+P50086	UniProtKB	Helix	5	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	15	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	39	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	49	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	75	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	85	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	110	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	120	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	143	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	153	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Turn	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	177	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	187	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	211	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P50086	UniProtKB	Helix	220	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+##sequence-region P53037 1 1138
+P53037	UniProtKB	Chain	1	1138	.	.	.	ID=PRO_0000045200;Note=Phosphatidylserine decarboxylase proenzyme 2	
+P53037	UniProtKB	Chain	1	1042	.	.	.	ID=PRO_0000045201;Note=Phosphatidylserine decarboxylase 2 beta chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03209	
+P53037	UniProtKB	Chain	1043	1138	.	.	.	ID=PRO_0000045202;Note=Phosphatidylserine decarboxylase 2 alpha chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03209	
+P53037	UniProtKB	Domain	14	87	.	.	.	Note=C2 1%3B degenerate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24366873;Dbxref=PMID:24366873	
+P53037	UniProtKB	Domain	500	583	.	.	.	Note=C2 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03209	
+P53037	UniProtKB	Compositional bias	108	159	.	.	.	Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016	
+P53037	UniProtKB	Active site	899	899	.	.	.	Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:B3L2V1,ECO:0000255|HAMAP-Rule:MF_03209	
+P53037	UniProtKB	Active site	956	956	.	.	.	Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:B3L2V1,ECO:0000255|HAMAP-Rule:MF_03209	
+P53037	UniProtKB	Active site	1043	1043	.	.	.	Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:B3L2V1,ECO:0000255|HAMAP-Rule:MF_03209	
+P53037	UniProtKB	Active site	1043	1043	.	.	.	Note=Schiff-base intermediate with substrate%3B via pyruvic acid%3B for decarboxylase activity;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A8K1,ECO:0000255|HAMAP-Rule:MF_03209	
+P53037	UniProtKB	Site	1042	1043	.	.	.	Note=Cleavage (non-hydrolytic)%3B by autocatalysis;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A8K1,ECO:0000255|HAMAP-Rule:MF_03209	
+P53037	UniProtKB	Modified residue	1043	1043	.	.	.	Note=Pyruvic acid (Ser)%3B by autocatalysis;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A8K1,ECO:0000255|HAMAP-Rule:MF_03209	
+P53037	UniProtKB	Mutagenesis	1041	1043	.	.	.	Note=No processing of the proenzyme%2C complete loss of activity. GGS->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20016005;Dbxref=PMID:20016005	
+P53037	UniProtKB	Sequence conflict	801	801	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53037	UniProtKB	Sequence conflict	974	974	.	.	.	Note=Y->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P31374 1 1356
+P31374	UniProtKB	Chain	1	1356	.	.	.	ID=PRO_0000086042;Note=Serine/threonine-protein kinase PSK1	
+P31374	UniProtKB	Domain	450	518	.	.	.	Note=PAS 1	
+P31374	UniProtKB	Domain	738	807	.	.	.	Note=PAS 2	
+P31374	UniProtKB	Domain	1096	1354	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P31374	UniProtKB	Nucleotide binding	1102	1110	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P31374	UniProtKB	Active site	1230	1230	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P31374	UniProtKB	Binding site	1125	1125	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P31374	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P31374	UniProtKB	Modified residue	192	192	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P31374	UniProtKB	Modified residue	202	202	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P31374	UniProtKB	Modified residue	255	255	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P31374	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P31374	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P31374	UniProtKB	Modified residue	926	926	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P31374	UniProtKB	Modified residue	1018	1018	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P31374	UniProtKB	Modified residue	1023	1023	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P31374	UniProtKB	Modified residue	1035	1035	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P31374	UniProtKB	Modified residue	1055	1055	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P31374	UniProtKB	Modified residue	1079	1079	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P31374	UniProtKB	Sequence conflict	73	73	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31374	UniProtKB	Sequence conflict	73	73	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31374	UniProtKB	Sequence conflict	73	73	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31374	UniProtKB	Sequence conflict	73	73	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02771 1 107
+##sequence-region P32606 1 800
+P32606	UniProtKB	Chain	1	800	.	.	.	ID=PRO_0000097082;Note=Putative mitochondrial translation system component PET127	
+##sequence-region P32522 1 965
+P32522	UniProtKB	Transmembrane	237	256	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32522	UniProtKB	Repeat	310	344	.	.	.	Note=PPR 1	
+P32522	UniProtKB	Repeat	345	379	.	.	.	Note=PPR 2	
+P32522	UniProtKB	Repeat	380	414	.	.	.	Note=PPR 3	
+P32522	UniProtKB	Repeat	415	450	.	.	.	Note=PPR 4	
+P32522	UniProtKB	Repeat	451	486	.	.	.	Note=PPR 5	
+P32522	UniProtKB	Repeat	487	523	.	.	.	Note=PPR 6	
+P32522	UniProtKB	Repeat	524	558	.	.	.	Note=PPR 7	
+P32522	UniProtKB	Repeat	559	595	.	.	.	Note=PPR 8	
+P32522	UniProtKB	Repeat	596	630	.	.	.	Note=PPR 9	
+P32522	UniProtKB	Repeat	680	714	.	.	.	Note=PPR 10	
+P32522	UniProtKB	Repeat	723	763	.	.	.	Note=PPR 11	
+P32522	UniProtKB	Repeat	774	808	.	.	.	Note=PPR 12	
+P32522	UniProtKB	Repeat	809	844	.	.	.	Note=PPR 13	
+##sequence-region Q01329 1 785
+Q01329	UniProtKB	Chain	1	785	.	.	.	ID=PRO_0000097086;Note=Pre-tRNA-processing protein PTA1	
+Q01329	UniProtKB	Modified residue	500	500	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q04373 1 656
+Q04373	UniProtKB	Chain	1	656	.	.	.	ID=PRO_0000075926;Note=Pumilio homology domain family member 6	
+Q04373	UniProtKB	Domain	133	483	.	.	.	Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318	
+Q04373	UniProtKB	Repeat	155	191	.	.	.	Note=Pumilio 1	
+Q04373	UniProtKB	Repeat	192	227	.	.	.	Note=Pumilio 2	
+Q04373	UniProtKB	Repeat	228	264	.	.	.	Note=Pumilio 3	
+Q04373	UniProtKB	Repeat	340	376	.	.	.	Note=Pumilio 4	
+Q04373	UniProtKB	Repeat	377	413	.	.	.	Note=Pumilio 5	
+Q04373	UniProtKB	Repeat	415	450	.	.	.	Note=Pumilio 6	
+Q04373	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18791219;Dbxref=PMID:18791219	
+Q04373	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18791219;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:18791219	
+Q04373	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18791219;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:18791219	
+Q04373	UniProtKB	Modified residue	35	35	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18791219;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:18791219	
+Q04373	UniProtKB	Modified residue	35	35	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18791219;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:18791219	
+Q04373	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Increases translation repression of ASH1 mRNA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18791219;Dbxref=PMID:18791219	
+Q04373	UniProtKB	Mutagenesis	34	34	.	.	.	Note=Increases translation repression of ASH1 mRNA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18791219;Dbxref=PMID:18791219	
+Q04373	UniProtKB	Mutagenesis	35	35	.	.	.	Note=Increases translation repression of ASH1 mRNA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18791219;Dbxref=PMID:18791219	
+##sequence-region P80210 1 433
+P80210	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10417315,ECO:0000269|PubMed:8376380;Dbxref=PMID:10417315,PMID:8376380	
+P80210	UniProtKB	Chain	2	433	.	.	.	ID=PRO_0000095138;Note=Adenylosuccinate synthetase	
+P80210	UniProtKB	Nucleotide binding	11	17	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Nucleotide binding	39	41	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Nucleotide binding	337	339	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Nucleotide binding	419	421	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Region	12	15	.	.	.	Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Region	37	40	.	.	.	Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Region	305	311	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Active site	12	12	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Active site	40	40	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Metal binding	12	12	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Metal binding	39	39	.	.	.	Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Binding site	134	134	.	.	.	Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Binding site	148	148	.	.	.	Note=IMP%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Binding site	230	230	.	.	.	Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Binding site	245	245	.	.	.	Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Binding site	309	309	.	.	.	Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Binding site	311	311	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125	
+P80210	UniProtKB	Sequence conflict	237	237	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02256 1 364
+Q02256	UniProtKB	Chain	1	364	.	.	.	ID=PRO_0000094854;Note=Tyrosine-protein phosphatase YVH1	
+Q02256	UniProtKB	Domain	1	172	.	.	.	Note=Tyrosine-protein phosphatase	
+Q02256	UniProtKB	Active site	117	117	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02256	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02256	UniProtKB	Sequence conflict	71	71	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P21304 1 576
+P21304	UniProtKB	Chain	1	576	.	.	.	ID=PRO_0000051173;Note=Periodic tryptophan protein 1	
+P21304	UniProtKB	Repeat	207	252	.	.	.	Note=WD 1	
+P21304	UniProtKB	Repeat	284	324	.	.	.	Note=WD 2	
+P21304	UniProtKB	Repeat	329	369	.	.	.	Note=WD 3	
+P21304	UniProtKB	Repeat	376	414	.	.	.	Note=WD 4	
+P21304	UniProtKB	Repeat	420	461	.	.	.	Note=WD 5	
+P21304	UniProtKB	Repeat	472	514	.	.	.	Note=WD 6	
+P21304	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P21304	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P30620 1 661
+P30620	UniProtKB	Chain	1	661	.	.	.	ID=PRO_0000209130;Note=DNA cross-link repair protein PSO2/SNM1	
+P30620	UniProtKB	Zinc finger	145	169	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30620	UniProtKB	Mutagenesis	252	252	.	.	.	Note=Abrogates exonuclease activity. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12509272,ECO:0000269|PubMed:15590324;Dbxref=PMID:12509272,PMID:15590324	
+P30620	UniProtKB	Mutagenesis	256	256	.	.	.	Note=In SNM1-2%3B increased sensitivity to DNA cross-linking agents at 36 degrees Celsius. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7526204;Dbxref=PMID:7526204	
+##sequence-region P50896 1 841
+P50896	UniProtKB	Chain	1	841	.	.	.	ID=PRO_0000097068;Note=Protein PSP1	
+P50896	UniProtKB	Domain	653	765	.	.	.	Note=PSP1 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00744	
+P50896	UniProtKB	Compositional bias	98	101	.	.	.	Note=Poly-Gln	
+P50896	UniProtKB	Compositional bias	139	144	.	.	.	Note=Poly-Asn	
+P50896	UniProtKB	Compositional bias	314	320	.	.	.	Note=Poly-Asn	
+P50896	UniProtKB	Compositional bias	348	359	.	.	.	Note=Poly-Gln	
+P50896	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P50896	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P50896	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50896	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50896	UniProtKB	Modified residue	334	334	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50896	UniProtKB	Modified residue	520	520	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P50896	UniProtKB	Sequence conflict	116	116	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50896	UniProtKB	Sequence conflict	122	133	.	.	.	Note=QMSSSNSEPMSA->KCLRLIQSCVP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50896	UniProtKB	Sequence conflict	198	210	.	.	.	Note=GSNFAAPSHSAGN->RAILLPHHTVLAT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50896	UniProtKB	Sequence conflict	732	732	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36082 1 127
+P36082	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000203169;Note=Putative platinum sensitivity protein 1	
+##sequence-region Q12318 1 242
+Q12318	UniProtKB	Chain	1	242	.	.	.	ID=PRO_0000262753;Note=Platinum sensitivity protein 3	
+Q12318	UniProtKB	Helix	2	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQ6	
+Q12318	UniProtKB	Helix	12	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Helix	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Beta strand	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Helix	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Beta strand	43	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Helix	55	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Beta strand	66	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Helix	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Beta strand	89	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Beta strand	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Helix	100	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Helix	114	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Beta strand	128	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Helix	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Helix	152	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Beta strand	174	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Helix	182	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Turn	189	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Helix	213	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+Q12318	UniProtKB	Beta strand	220	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9	
+##sequence-region P47065 1 347
+P47065	UniProtKB	Chain	1	347	.	.	.	ID=PRO_0000097083;Note=Protein PET130	
+##sequence-region Q02772 1 108
+Q02772	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000022178;Note=Mitochondrial protein PET191	
+Q02772	UniProtKB	Domain	18	64	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q02772	UniProtKB	Motif	21	32	.	.	.	Note=Cx10C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q02772	UniProtKB	Motif	46	56	.	.	.	Note=Cx9C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q02772	UniProtKB	Disulfide bond	21	56	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+Q02772	UniProtKB	Disulfide bond	32	46	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+##sequence-region P07390 1 489
+P07390	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000097085;Note=COX3 mRNA-specific translational activator PET494	
+P07390	UniProtKB	Sequence conflict	68	68	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P34222 1 208
+P34222	UniProtKB	Chain	1	208	.	.	.	ID=PRO_0000120284;Note=Peptidyl-tRNA hydrolase 2	
+P34222	UniProtKB	Cross-link	152	152	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P04161 1 214
+P04161	UniProtKB	Chain	1	214	.	.	.	ID=PRO_0000074954;Note=Phosphoribosylglycinamide formyltransferase	
+P04161	UniProtKB	Region	12	14	.	.	.	Note=5'-phosphoribosylglycinamide binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04161	UniProtKB	Region	105	108	.	.	.	Note=10-formyltetrahydrofolate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04161	UniProtKB	Active site	125	125	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04161	UniProtKB	Binding site	123	123	.	.	.	Note=10-formyltetrahydrofolate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04161	UniProtKB	Binding site	167	167	.	.	.	Note=10-formyltetrahydrofolate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04161	UniProtKB	Binding site	197	197	.	.	.	Note=5'-phosphoribosylglycinamide;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04161	UniProtKB	Site	167	167	.	.	.	Note=Raises pKa of active site His;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12488 1 208
+Q12488	UniProtKB	Chain	1	208	.	.	.	ID=PRO_0000219040;Note=DNA replication complex GINS protein PSF1	
+Q12488	UniProtKB	Mutagenesis	84	84	.	.	.	Note=In PSF1-1%3B temperature-sensitive mutant. Defective in DNA replication. Impaired chromatin binding of CDC45. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134	
+##sequence-region P31115 1 442
+P31115	UniProtKB	Chain	1	442	.	.	.	ID=PRO_0000057519;Note=tRNA pseudouridine(38/39) synthase	
+P31115	UniProtKB	Active site	151	151	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P31115	UniProtKB	Binding site	222	222	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q08647 1 676
+Q08647	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08647	UniProtKB	Chain	2	676	.	.	.	ID=PRO_0000152561;Note=Multisubstrate pseudouridine synthase 7	
+Q08647	UniProtKB	Domain	338	582	.	.	.	Note=TRUD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00342	
+Q08647	UniProtKB	Active site	256	256	.	.	.	Note=Nucleophile	
+Q08647	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08647	UniProtKB	Mutagenesis	256	256	.	.	.	Note=Abolishes enzymatic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561887;Dbxref=PMID:14561887	
+##sequence-region P39006 1 500
+P39006	UniProtKB	Transit peptide	1	44	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
+P39006	UniProtKB	Chain	45	500	.	.	.	ID=PRO_0000029843;Note=Phosphatidylserine decarboxylase proenzyme 1%2C mitochondrial	
+P39006	UniProtKB	Chain	45	462	.	.	.	ID=PRO_0000029844;Note=Phosphatidylserine decarboxylase 1 beta chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
+P39006	UniProtKB	Chain	463	500	.	.	.	ID=PRO_0000029845;Note=Phosphatidylserine decarboxylase 1 alpha chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
+P39006	UniProtKB	Topological domain	45	79	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03208,ECO:0000305|PubMed:22984266;Dbxref=PMID:22984266	
+P39006	UniProtKB	Transmembrane	80	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
+P39006	UniProtKB	Topological domain	99	500	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03208,ECO:0000305|PubMed:22984266;Dbxref=PMID:22984266	
+P39006	UniProtKB	Active site	210	210	.	.	.	Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
+P39006	UniProtKB	Active site	348	348	.	.	.	Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
+P39006	UniProtKB	Active site	463	463	.	.	.	Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
+P39006	UniProtKB	Active site	463	463	.	.	.	Note=Schiff-base intermediate with substrate%3B via pyruvic acid%3B for decarboxylase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
+P39006	UniProtKB	Site	462	463	.	.	.	Note=Cleavage (non-hydrolytic)%3B by autocatalysis;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
+P39006	UniProtKB	Modified residue	463	463	.	.	.	Note=Pyruvic acid (Ser)%3B by autocatalysis;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
+P39006	UniProtKB	Mutagenesis	81	100	.	.	.	Note=In PSD1deltaIM%3B Mislocalizes to the mitochondrial matrix. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22984266;Dbxref=PMID:22984266	
+P39006	UniProtKB	Mutagenesis	461	463	.	.	.	Note=No processing of the proenzyme%2C complete loss of activity. LGS->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18644857;Dbxref=PMID:18644857	
+P39006	UniProtKB	Mutagenesis	461	461	.	.	.	Note=No effect. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25829489;Dbxref=PMID:25829489	
+P39006	UniProtKB	Mutagenesis	462	462	.	.	.	Note=Significantly impairs processing of the proenzyme%2C retains some activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25829489;Dbxref=PMID:25829489	
+P39006	UniProtKB	Mutagenesis	463	463	.	.	.	Note=No processing of the proenzyme%2C complete loss of activity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22984266,ECO:0000269|PubMed:25829489;Dbxref=PMID:22984266,PMID:25829489	
+P39006	UniProtKB	Mutagenesis	464	464	.	.	.	Note=No effect. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25829489;Dbxref=PMID:25829489	
+##sequence-region P25044 1 335
+P25044	UniProtKB	Chain	1	335	.	.	.	ID=PRO_0000094855;Note=Tyrosine-protein phosphatase 1	
+P25044	UniProtKB	Domain	15	328	.	.	.	Note=Tyrosine-protein phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160	
+P25044	UniProtKB	Active site	252	252	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160,ECO:0000255|PROSITE-ProRule:PRU10044	
+P25044	UniProtKB	Modified residue	83	83	.	.	.	Note=Phosphoserine%3B by CLK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10480872;Dbxref=PMID:10480872	
+##sequence-region P40048 1 928
+P40048	UniProtKB	Chain	1	928	.	.	.	ID=PRO_0000094857;Note=Tyrosine-protein phosphatase 3	
+P40048	UniProtKB	Domain	111	232	.	.	.	Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+P40048	UniProtKB	Domain	502	878	.	.	.	Note=Tyrosine-protein phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160	
+P40048	UniProtKB	Compositional bias	308	311	.	.	.	Note=Poly-Ser	
+P40048	UniProtKB	Compositional bias	592	597	.	.	.	Note=Poly-Thr	
+P40048	UniProtKB	Compositional bias	702	715	.	.	.	Note=Poly-Asn	
+P40048	UniProtKB	Compositional bias	724	732	.	.	.	Note=Poly-Asp	
+P40048	UniProtKB	Active site	804	804	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160,ECO:0000255|PROSITE-ProRule:PRU10044	
+P40048	UniProtKB	Modified residue	75	75	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P40048	UniProtKB	Modified residue	248	248	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40048	UniProtKB	Modified residue	297	297	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40048	UniProtKB	Modified residue	368	368	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40048	UniProtKB	Sequence conflict	717	717	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40048	UniProtKB	Sequence conflict	717	717	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40048	UniProtKB	Sequence conflict	738	738	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40048	UniProtKB	Sequence conflict	738	738	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40048	UniProtKB	Sequence conflict	857	857	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40048	UniProtKB	Sequence conflict	857	857	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40454 1 393
+P40454	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000202955;Note=Serine/threonine-protein phosphatase 2A activator 1	
+P40454	UniProtKB	Modified residue	341	341	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40454	UniProtKB	Mutagenesis	205	205	.	.	.	Note=Abolishes PPIase activity and fails to activate PP2A phosphatases. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16380387;Dbxref=PMID:16380387	
+P40454	UniProtKB	Turn	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	23	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	33	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	65	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	97	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	119	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	125	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Turn	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	146	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	170	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXP	
+P40454	UniProtKB	Beta strand	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	210	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Beta strand	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Beta strand	226	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	230	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	236	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Turn	243	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	247	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	263	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	268	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	280	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Turn	295	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Helix	299	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+P40454	UniProtKB	Beta strand	309	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO	
+##sequence-region P32588 1 453
+P32588	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P32588	UniProtKB	Chain	2	453	.	.	.	ID=PRO_0000081745;Note=Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1	
+P32588	UniProtKB	Domain	75	152	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P32588	UniProtKB	Domain	162	240	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P32588	UniProtKB	Domain	341	413	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P32588	UniProtKB	Region	260	264	.	.	.	Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32588	UniProtKB	Compositional bias	8	16	.	.	.	Note=Gln-rich	
+P32588	UniProtKB	Compositional bias	243	288	.	.	.	Note=Asn-rich	
+P32588	UniProtKB	Compositional bias	442	453	.	.	.	Note=Gln-rich	
+P32588	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P32588	UniProtKB	Sequence conflict	268	268	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32588	UniProtKB	Sequence conflict	268	268	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32588	UniProtKB	Beta strand	76	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3	
+P32588	UniProtKB	Helix	88	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3	
+P32588	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3	
+P32588	UniProtKB	Beta strand	101	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3	
+P32588	UniProtKB	Beta strand	115	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3	
+P32588	UniProtKB	Helix	125	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3	
+P32588	UniProtKB	Beta strand	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3	
+P32588	UniProtKB	Beta strand	162	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1	
+P32588	UniProtKB	Helix	175	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1	
+P32588	UniProtKB	Beta strand	188	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1	
+P32588	UniProtKB	Turn	197	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1	
+P32588	UniProtKB	Beta strand	202	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1	
+P32588	UniProtKB	Helix	213	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1	
+P32588	UniProtKB	Beta strand	234	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1	
+P32588	UniProtKB	Beta strand	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4	
+P32588	UniProtKB	Helix	326	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4	
+P32588	UniProtKB	Beta strand	342	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4	
+P32588	UniProtKB	Helix	354	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4	
+P32588	UniProtKB	Beta strand	368	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4	
+P32588	UniProtKB	Turn	374	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4	
+P32588	UniProtKB	Beta strand	378	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4	
+P32588	UniProtKB	Helix	386	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4	
+##sequence-region Q12221 1 1075
+Q12221	UniProtKB	Chain	1	1075	.	.	.	ID=PRO_0000262754;Note=mRNA-binding protein PUF2	
+Q12221	UniProtKB	Domain	316	402	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q12221	UniProtKB	Domain	511	872	.	.	.	Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318	
+Q12221	UniProtKB	Repeat	574	611	.	.	.	Note=Pumilio 1	
+Q12221	UniProtKB	Repeat	612	647	.	.	.	Note=Pumilio 2	
+Q12221	UniProtKB	Repeat	649	683	.	.	.	Note=Pumilio 3	
+Q12221	UniProtKB	Repeat	684	719	.	.	.	Note=Pumilio 4	
+Q12221	UniProtKB	Repeat	722	758	.	.	.	Note=Pumilio 5	
+Q12221	UniProtKB	Repeat	760	800	.	.	.	Note=Pumilio 6	
+Q12221	UniProtKB	Compositional bias	910	1063	.	.	.	Note=Asn-rich	
+Q12221	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12221	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12221	UniProtKB	Modified residue	872	872	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12221	UniProtKB	Modified residue	876	876	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q07807 1 879
+Q07807	UniProtKB	Chain	1	879	.	.	.	ID=PRO_0000075924;Note=mRNA-binding protein PUF3	
+Q07807	UniProtKB	Domain	513	871	.	.	.	Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318	
+Q07807	UniProtKB	Repeat	538	573	.	.	.	Note=Pumilio 1	
+Q07807	UniProtKB	Repeat	574	609	.	.	.	Note=Pumilio 2	
+Q07807	UniProtKB	Repeat	610	645	.	.	.	Note=Pumilio 3	
+Q07807	UniProtKB	Repeat	646	681	.	.	.	Note=Pumilio 4	
+Q07807	UniProtKB	Repeat	682	717	.	.	.	Note=Pumilio 5	
+Q07807	UniProtKB	Repeat	718	759	.	.	.	Note=Pumilio 6	
+Q07807	UniProtKB	Repeat	760	795	.	.	.	Note=Pumilio 7	
+Q07807	UniProtKB	Repeat	807	844	.	.	.	Note=Pumilio 8	
+Q07807	UniProtKB	Compositional bias	398	409	.	.	.	Note=Poly-Gln	
+Q07807	UniProtKB	Compositional bias	412	418	.	.	.	Note=Poly-Gln	
+Q07807	UniProtKB	Modified residue	83	83	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q07807	UniProtKB	Modified residue	207	207	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q07807	UniProtKB	Modified residue	210	210	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07807	UniProtKB	Mutagenesis	553	553	.	.	.	Note=Prevents binding to COX17 mRNA and its rapid decay and increases affinity to HO mRNA%2C a PUF5 target. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16244132;Dbxref=PMID:16244132	
+Q07807	UniProtKB	Helix	516	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	536	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	543	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	550	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	565	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	576	578	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	579	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Turn	586	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	589	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	601	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	615	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	624	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	637	644	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	645	647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	651	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	660	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	673	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Turn	677	679	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	680	683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Turn	684	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	687	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	696	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	709	717	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Turn	718	721	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	723	728	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	732	740	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	748	762	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	765	769	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	774	784	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	787	794	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Turn	795	797	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	802	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	813	818	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	823	833	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	836	855	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+Q07807	UniProtKB	Helix	865	874	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49	
+##sequence-region P21264 1 571
+P21264	UniProtKB	Chain	1	571	.	.	.	ID=PRO_0000075028;Note=Phosphoribosylaminoimidazole carboxylase	
+P21264	UniProtKB	Domain	110	298	.	.	.	Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P21264	UniProtKB	Nucleotide binding	138	193	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409	
+P21264	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21264	UniProtKB	Sequence conflict	101	101	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21264	UniProtKB	Sequence conflict	186	186	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21264	UniProtKB	Sequence conflict	206	206	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21264	UniProtKB	Sequence conflict	241	253	.	.	.	Note=ENAIKSFPGCGIF->KMQSNFSRLWYI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21264	UniProtKB	Sequence conflict	387	387	.	.	.	Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21264	UniProtKB	Sequence conflict	407	407	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21264	UniProtKB	Sequence conflict	431	431	.	.	.	Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21264	UniProtKB	Sequence conflict	434	434	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21264	UniProtKB	Sequence conflict	502	502	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P41909 1 870
+P41909	UniProtKB	Chain	1	870	.	.	.	ID=PRO_0000093314;Note=Peroxisomal long-chain fatty acid import protein 2	
+P41909	UniProtKB	Transmembrane	60	80	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P41909	UniProtKB	Transmembrane	207	227	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P41909	UniProtKB	Transmembrane	247	267	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P41909	UniProtKB	Transmembrane	330	350	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P41909	UniProtKB	Transmembrane	353	373	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P41909	UniProtKB	Transmembrane	455	475	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P41909	UniProtKB	Domain	210	501	.	.	.	Note=ABC transmembrane type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P41909	UniProtKB	Domain	608	866	.	.	.	Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P41909	UniProtKB	Nucleotide binding	645	652	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P41909	UniProtKB	Glycosylation	142	142	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41909	UniProtKB	Glycosylation	281	281	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41909	UniProtKB	Glycosylation	403	403	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36166 1 706
+P36166	UniProtKB	Chain	1	706	.	.	.	ID=PRO_0000075893;Note=Paxillin-like protein 1	
+P36166	UniProtKB	Domain	556	612	.	.	.	Note=LIM zinc-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125	
+P36166	UniProtKB	Domain	621	672	.	.	.	Note=LIM zinc-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125	
+P36166	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36166	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P36166	UniProtKB	Sequence conflict	688	688	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53335 1 271
+P53335	UniProtKB	Chain	1	271	.	.	.	ID=PRO_0000202871;Note=Protein PXR1	
+P53335	UniProtKB	Domain	25	72	.	.	.	Note=G-patch;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00092	
+P53335	UniProtKB	Compositional bias	139	226	.	.	.	Note=Lys-rich	
+P53335	UniProtKB	Modified residue	230	230	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53335	UniProtKB	Sequence conflict	148	148	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53335	UniProtKB	Sequence conflict	151	151	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53335	UniProtKB	Sequence conflict	165	167	.	.	.	Note=DDK->ADQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53335	UniProtKB	Sequence conflict	193	193	.	.	.	Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P05737 1 244
+P05737	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:1544921,PMID:18782943	
+P05737	UniProtKB	Chain	2	244	.	.	.	ID=PRO_0000104651;Note=60S ribosomal protein L7-A	
+P05737	UniProtKB	Turn	23	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U51	
+P05737	UniProtKB	Helix	28	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Beta strand	82	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Helix	97	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Beta strand	113	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Helix	121	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Turn	129	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Beta strand	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Helix	141	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Beta strand	156	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Beta strand	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P05737	UniProtKB	Helix	166	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Helix	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Helix	181	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Helix	195	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Beta strand	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Beta strand	219	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Helix	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Beta strand	227	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Helix	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05737	UniProtKB	Helix	236	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P17076 1 256
+P17076	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921	
+P17076	UniProtKB	Chain	2	256	.	.	.	ID=PRO_0000136760;Note=60S ribosomal protein L8-A	
+P17076	UniProtKB	Sequence conflict	113	113	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17076	UniProtKB	Beta strand	35	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	54	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Turn	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	84	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	102	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Beta strand	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F	
+P17076	UniProtKB	Beta strand	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P17076	UniProtKB	Helix	136	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Beta strand	149	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	161	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	166	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Beta strand	177	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	183	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Turn	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Beta strand	196	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	205	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Turn	222	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	226	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P17076	UniProtKB	Helix	240	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P10622 1 106
+P10622	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8476850;Dbxref=PMID:8476850	
+P10622	UniProtKB	Chain	2	106	.	.	.	ID=PRO_0000157706;Note=60S acidic ribosomal protein P1-beta	
+P10622	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8476850;Dbxref=PMID:8476850	
+P10622	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53060 1 241
+P53060	UniProtKB	Chain	1	241	.	.	.	ID=PRO_0000202705;Note=Reduced meiotic recombination protein 1	
+##sequence-region P36159 1 838
+P36159	UniProtKB	Chain	1	838	.	.	.	ID=PRO_0000155837;Note=Ribonuclease Z	
+P36159	UniProtKB	Modified residue	824	824	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region P53118 1 685
+P53118	UniProtKB	Chain	1	685	.	.	.	ID=PRO_0000202735;Note=Putative lipase ROG1	
+P53118	UniProtKB	Active site	269	269	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037	
+P53118	UniProtKB	Sequence conflict	514	514	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P51862 1 1356
+P51862	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P51862	UniProtKB	Chain	2	1356	.	.	.	ID=PRO_0000080969;Note=RHO1 GDP-GTP exchange protein 2	
+P51862	UniProtKB	Domain	659	846	.	.	.	Note=DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00062	
+P51862	UniProtKB	Domain	1034	1336	.	.	.	Note=CNH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00795	
+P51862	UniProtKB	Compositional bias	252	265	.	.	.	Note=Poly-Asn	
+P51862	UniProtKB	Compositional bias	329	336	.	.	.	Note=Poly-His	
+P51862	UniProtKB	Compositional bias	632	635	.	.	.	Note=Poly-Asp	
+P51862	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P51862	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P51862	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P51862	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P51862	UniProtKB	Modified residue	566	566	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P51862	UniProtKB	Modified residue	628	628	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32529 1 125
+P32529	UniProtKB	Chain	1	125	.	.	.	ID=PRO_0000121465;Note=DNA-directed RNA polymerase I subunit RPA12	
+P32529	UniProtKB	Zinc finger	10	33	.	.	.	Note=C4-type	
+P32529	UniProtKB	Zinc finger	82	122	.	.	.	Note=TFIIS-type;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00472,ECO:0000269|PubMed:24153182,ECO:0000269|PubMed:24153184;Dbxref=PMID:24153182,PMID:24153184	
+P32529	UniProtKB	Region	1	69	.	.	.	Note=Necessary and sufficient for recruitment into Pol I	
+P32529	UniProtKB	Region	1	60	.	.	.	Note=Interaction with RPA2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11918799;Dbxref=PMID:11918799	
+P32529	UniProtKB	Region	79	125	.	.	.	Note=Required for RNA cleavage%2C but not essential for elongation activity	
+P32529	UniProtKB	Mutagenesis	10	10	.	.	.	Note=Severe growth defect. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11918799;Dbxref=PMID:11918799	
+P32529	UniProtKB	Mutagenesis	13	13	.	.	.	Note=No effect. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11918799;Dbxref=PMID:11918799	
+P32529	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Limited growth defect. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11918799;Dbxref=PMID:11918799	
+P32529	UniProtKB	Mutagenesis	33	33	.	.	.	Note=No effect. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11918799;Dbxref=PMID:11918799	
+P32529	UniProtKB	Beta strand	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Beta strand	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Helix	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Beta strand	24	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Turn	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Beta strand	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Beta strand	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Helix	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Helix	59	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Beta strand	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Beta strand	79	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Beta strand	92	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Beta strand	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Beta strand	109	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Turn	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P32529	UniProtKB	Beta strand	120	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+##sequence-region Q01080 1 415
+Q01080	UniProtKB	Chain	1	415	.	.	.	ID=PRO_0000073955;Note=DNA-directed RNA polymerase I subunit RPA49	
+Q01080	UniProtKB	Region	322	415	.	.	.	Note=Interaction with DNA	
+Q01080	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q01080	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q01080	UniProtKB	Mutagenesis	325	326	.	.	.	Note=No effect on DNA binding. ED->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630	
+Q01080	UniProtKB	Mutagenesis	356	356	.	.	.	Note=Loss of DNA binding%3B when associated with A-358. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630	
+Q01080	UniProtKB	Mutagenesis	358	358	.	.	.	Note=Loss of DNA binding%3B when associated with A-356. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630	
+Q01080	UniProtKB	Mutagenesis	359	359	.	.	.	Note=Loss of DNA binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630	
+Q01080	UniProtKB	Mutagenesis	365	365	.	.	.	Note=Loss of DNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630	
+Q01080	UniProtKB	Mutagenesis	393	393	.	.	.	Note=Loss of DNA binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630	
+Q01080	UniProtKB	Sequence conflict	66	66	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01080	UniProtKB	Sequence conflict	157	157	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01080	UniProtKB	Beta strand	11	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+Q01080	UniProtKB	Beta strand	22	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+Q01080	UniProtKB	Beta strand	37	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+Q01080	UniProtKB	Beta strand	51	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+Q01080	UniProtKB	Beta strand	58	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+Q01080	UniProtKB	Helix	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+Q01080	UniProtKB	Beta strand	74	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+Q01080	UniProtKB	Turn	83	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+Q01080	UniProtKB	Beta strand	87	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+Q01080	UniProtKB	Beta strand	95	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+Q01080	UniProtKB	Helix	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+Q01080	UniProtKB	Helix	173	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	210	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	219	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	227	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	242	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	256	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Turn	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	280	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	292	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Beta strand	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	309	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Beta strand	317	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	322	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Turn	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Beta strand	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	346	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	357	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Beta strand	370	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	376	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Helix	386	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+Q01080	UniProtKB	Beta strand	392	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI	
+##sequence-region P27999 1 122
+P27999	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000121474;Note=DNA-directed RNA polymerase II subunit RPB9	
+P27999	UniProtKB	Zinc finger	7	32	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27999	UniProtKB	Zinc finger	71	111	.	.	.	Note=TFIIS-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00472	
+P27999	UniProtKB	Metal binding	7	7	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499	
+P27999	UniProtKB	Metal binding	10	10	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499	
+P27999	UniProtKB	Metal binding	29	29	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499	
+P27999	UniProtKB	Metal binding	32	32	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499	
+P27999	UniProtKB	Metal binding	75	75	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499	
+P27999	UniProtKB	Metal binding	78	78	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499	
+P27999	UniProtKB	Metal binding	103	103	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499	
+P27999	UniProtKB	Metal binding	106	106	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499	
+P27999	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P27999	UniProtKB	Beta strand	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Beta strand	15	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Turn	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Beta strand	24	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Beta strand	30	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Beta strand	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Beta strand	41	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Turn	52	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P27999	UniProtKB	Helix	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Beta strand	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1N	
+P27999	UniProtKB	Turn	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Beta strand	83	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S16	
+P27999	UniProtKB	Beta strand	99	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Turn	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Beta strand	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P27999	UniProtKB	Beta strand	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVQ	
+##sequence-region P47076 1 161
+P47076	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000203077;Note=DNA-directed RNA polymerase III subunit RPC9	
+P47076	UniProtKB	Sequence conflict	159	159	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47076	UniProtKB	Sequence conflict	159	159	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47076	UniProtKB	Beta strand	2	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P47076	UniProtKB	Helix	13	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P47076	UniProtKB	Helix	31	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P47076	UniProtKB	Helix	53	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P47076	UniProtKB	Helix	100	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P47076	UniProtKB	Helix	117	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P47076	UniProtKB	Helix	131	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P47076	UniProtKB	Beta strand	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P47076	UniProtKB	Turn	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P47076	UniProtKB	Helix	147	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+##sequence-region P05738 1 191
+P05738	UniProtKB	Chain	1	191	.	.	.	ID=PRO_0000131111;Note=60S ribosomal protein L9-A	
+P05738	UniProtKB	Beta strand	3	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	17	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	24	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Turn	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P05738	UniProtKB	Beta strand	44	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	52	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Helix	62	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	86	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	100	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	111	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Helix	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	124	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	132	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	143	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Helix	151	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P05738	UniProtKB	Turn	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05738	UniProtKB	Beta strand	178	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region Q02204 1 264
+Q02204	UniProtKB	Transit peptide	1	75	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2060626,ECO:0000269|PubMed:7954901;Dbxref=PMID:2060626,PMID:7954901	
+Q02204	UniProtKB	Chain	76	264	.	.	.	ID=PRO_0000030571;Note=54S ribosomal protein L13%2C mitochondrial	
+Q02204	UniProtKB	Sequence conflict	108	108	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P22354 1 195
+P22354	UniProtKB	Transit peptide	1	18	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2183197;Dbxref=PMID:2183197	
+P22354	UniProtKB	Chain	19	195	.	.	.	ID=PRO_0000030573;Note=54S ribosomal protein L20%2C mitochondrial	
+P22354	UniProtKB	Compositional bias	113	129	.	.	.	Note=Arg/Lys-rich (basic)	
+P22354	UniProtKB	Sequence conflict	187	187	.	.	.	Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12508 1 421
+Q12508	UniProtKB	Chain	1	421	.	.	.	ID=PRO_0000097361;Note=Sporulation protein RMD5	
+Q12508	UniProtKB	Domain	176	236	.	.	.	Note=CTLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00058	
+##sequence-region P40993 1 198
+P40993	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000097366;Note=Ribonuclease MRP protein subunit SNM1	
+P40993	UniProtKB	Compositional bias	136	198	.	.	.	Note=Lys/Ser-rich	
+##sequence-region Q02933 1 434
+Q02933	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02933	UniProtKB	Chain	19	434	.	.	.	ID=PRO_0000042717;Note=Ribonuclease T2-like	
+Q02933	UniProtKB	Active site	87	87	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02933	UniProtKB	Active site	156	156	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02933	UniProtKB	Active site	160	160	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02933	UniProtKB	Glycosylation	37	37	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02933	UniProtKB	Glycosylation	70	70	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02933	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02933	UniProtKB	Glycosylation	123	123	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02933	UniProtKB	Disulfide bond	27	46	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02933	UniProtKB	Disulfide bond	35	94	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02933	UniProtKB	Disulfide bond	45	171	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02933	UniProtKB	Disulfide bond	102	163	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02933	UniProtKB	Disulfide bond	241	277	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02933	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Impairs cytosolic tRNA-cleaving activity%3B when associated with F-160. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19332891;Dbxref=PMID:19332891	
+Q02933	UniProtKB	Mutagenesis	160	160	.	.	.	Note=Impairs cytosolic tRNA-cleaving activity%3B when associated with F-87. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19332891;Dbxref=PMID:19332891	
+##sequence-region P25042 1 368
+P25042	UniProtKB	Chain	1	368	.	.	.	ID=PRO_0000048574;Note=Repressor ROX1	
+P25042	UniProtKB	DNA binding	10	83	.	.	.	Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267	
+P25042	UniProtKB	Compositional bias	102	123	.	.	.	Note=Gln-rich	
+##sequence-region P10964 1 1664
+P10964	UniProtKB	Chain	1	1664	.	.	.	ID=PRO_0000073930;Note=DNA-directed RNA polymerase I subunit RPA190	
+P10964	UniProtKB	Region	992	1004	.	.	.	Note=Bridging helix;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P10964	UniProtKB	Metal binding	62	62	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182	
+P10964	UniProtKB	Metal binding	65	65	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182	
+P10964	UniProtKB	Metal binding	72	72	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182	
+P10964	UniProtKB	Metal binding	75	75	.	.	.	Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182	
+P10964	UniProtKB	Metal binding	102	102	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182	
+P10964	UniProtKB	Metal binding	105	105	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182	
+P10964	UniProtKB	Metal binding	233	233	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182	
+P10964	UniProtKB	Metal binding	236	236	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182	
+P10964	UniProtKB	Metal binding	627	627	.	.	.	Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04050	
+P10964	UniProtKB	Metal binding	629	629	.	.	.	Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04050	
+P10964	UniProtKB	Metal binding	631	631	.	.	.	Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04050	
+P10964	UniProtKB	Modified residue	889	889	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P10964	UniProtKB	Modified residue	1636	1636	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P10964	UniProtKB	Sequence conflict	158	158	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10964	UniProtKB	Beta strand	10	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	21	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	77	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	91	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	112	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	130	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	175	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P10964	UniProtKB	Helix	210	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	242	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	247	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	251	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	258	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	267	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	317	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	332	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	352	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	356	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	371	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	376	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	381	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	408	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	415	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	440	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	456	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	462	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P10964	UniProtKB	Helix	466	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	472	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	488	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P10964	UniProtKB	Beta strand	494	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	499	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	506	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	513	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	516	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	526	528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	529	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	533	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	543	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	551	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	559	562	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	568	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	576	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	586	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	597	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	600	607	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	613	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	618	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	621	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	628	630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	632	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	641	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	653	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	660	662	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	672	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	686	688	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	689	700	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	703	705	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	708	711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P10964	UniProtKB	Beta strand	718	723	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	725	727	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	728	739	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	742	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P10964	UniProtKB	Beta strand	749	752	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	757	759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	768	772	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	775	778	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	783	786	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	793	824	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	830	833	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	837	847	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	848	850	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	853	861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	873	884	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	886	911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	912	915	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	916	918	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	920	922	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	924	930	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	937	944	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	976	979	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	986	988	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	992	1011	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1017	1027	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1036	1039	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P10964	UniProtKB	Beta strand	1045	1049	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1050	1052	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P10964	UniProtKB	Helix	1057	1059	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1066	1070	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1073	1080	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1082	1088	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1089	1092	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1093	1107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1109	1111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P10964	UniProtKB	Helix	1113	1115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1123	1126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	1129	1131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1138	1150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1152	1155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1157	1160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1163	1175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1185	1194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1196	1200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1218	1226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1237	1242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1244	1246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P10964	UniProtKB	Helix	1248	1258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1263	1266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1267	1275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1288	1296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1299	1306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1310	1318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1320	1335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1344	1346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P10964	UniProtKB	Helix	1364	1366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1369	1378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1382	1384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1389	1394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1442	1452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1454	1462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	1464	1466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1469	1476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1485	1493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1497	1499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1504	1508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P10964	UniProtKB	Beta strand	1518	1523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1526	1529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1530	1532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	1533	1535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1538	1540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1542	1544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1546	1553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1555	1572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1579	1589	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Turn	1590	1592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1600	1603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1609	1613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1618	1627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1637	1643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Helix	1650	1652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P10964	UniProtKB	Beta strand	1653	1661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+##sequence-region P40422 1 70
+P40422	UniProtKB	Chain	1	70	.	.	.	ID=PRO_0000159753;Note=DNA-directed RNA polymerases I%2C II%2C and III subunit RPABC4	
+P40422	UniProtKB	Zinc finger	31	51	.	.	.	Note=C4-type	
+P40422	UniProtKB	Metal binding	31	31	.	.	.	Note=Zinc	
+P40422	UniProtKB	Metal binding	34	34	.	.	.	Note=Zinc	
+P40422	UniProtKB	Metal binding	48	48	.	.	.	Note=Zinc	
+P40422	UniProtKB	Metal binding	51	51	.	.	.	Note=Zinc	
+P40422	UniProtKB	Beta strand	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P40422	UniProtKB	Beta strand	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P40422	UniProtKB	Beta strand	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q	
+P40422	UniProtKB	Beta strand	41	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P40422	UniProtKB	Beta strand	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q	
+P40422	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P40422	UniProtKB	Beta strand	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P40422	UniProtKB	Beta strand	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+##sequence-region P07703 1 335
+P07703	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07703	UniProtKB	Chain	2	335	.	.	.	ID=PRO_0000132742;Note=DNA-directed RNA polymerases I and III subunit RPAC1	
+P07703	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07703	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07703	UniProtKB	Helix	33	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	41	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	49	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	61	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	77	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	94	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P07703	UniProtKB	Helix	122	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Turn	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	132	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	153	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P07703	UniProtKB	Beta strand	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	175	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Turn	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	185	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	192	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	201	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Turn	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	222	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	242	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Turn	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Turn	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	264	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	278	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	283	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	289	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Beta strand	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P07703	UniProtKB	Helix	310	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+##sequence-region P38902 1 120
+P38902	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000149315;Note=DNA-directed RNA polymerase II subunit RPB11	
+P38902	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Transcript termination readthrough. E->G%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537912;Dbxref=PMID:16537912	
+P38902	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Transcript termination readthrough. Lethal. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537912;Dbxref=PMID:16537912	
+P38902	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Transcript termination readthrough. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537912;Dbxref=PMID:16537912	
+P38902	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Transcript termination readthrough. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537912;Dbxref=PMID:16537912	
+P38902	UniProtKB	Helix	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P38902	UniProtKB	Beta strand	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S2H	
+P38902	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P38902	UniProtKB	Beta strand	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P38902	UniProtKB	Beta strand	30	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P38902	UniProtKB	Helix	40	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P38902	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VUM	
+P38902	UniProtKB	Beta strand	56	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P38902	UniProtKB	Beta strand	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P38902	UniProtKB	Beta strand	70	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P38902	UniProtKB	Helix	83	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P38902	UniProtKB	Turn	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+##sequence-region P16370 1 318
+P16370	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P16370	UniProtKB	Chain	2	318	.	.	.	ID=PRO_0000132748;Note=DNA-directed RNA polymerase II subunit RPB3	
+P16370	UniProtKB	Metal binding	86	86	.	.	.	Note=Zinc	
+P16370	UniProtKB	Metal binding	88	88	.	.	.	Note=Zinc	
+P16370	UniProtKB	Metal binding	92	92	.	.	.	Note=Zinc	
+P16370	UniProtKB	Metal binding	95	95	.	.	.	Note=Zinc	
+P16370	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P16370	UniProtKB	Natural variant	30	30	.	.	.	Note=In mutant RPB3-1. A->D	
+P16370	UniProtKB	Mutagenesis	9	9	.	.	.	Note=Transcript termination readthrough. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537912;Dbxref=PMID:16537912	
+P16370	UniProtKB	Sequence conflict	175	175	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16370	UniProtKB	Beta strand	5	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P16370	UniProtKB	Beta strand	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	21	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Helix	27	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	43	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Helix	60	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Helix	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Turn	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	86	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Turn	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	96	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	111	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Helix	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	128	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P16370	UniProtKB	Beta strand	142	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	152	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Turn	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Helix	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	173	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Helix	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I3Q	
+P16370	UniProtKB	Helix	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Helix	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M3Y	
+P16370	UniProtKB	Beta strand	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	228	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Beta strand	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P16370	UniProtKB	Helix	240	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+##sequence-region P34087 1 171
+P34087	UniProtKB	Chain	1	171	.	.	.	ID=PRO_0000073993;Note=DNA-directed RNA polymerase II subunit RPB7	
+P34087	UniProtKB	Mutagenesis	108	113	.	.	.	Note=Lowers nucleic-acid binding of RPB4-RPB7 by 10-fold%3B no effect on association with Pol II core complex%3B abolishes transcriptional activity of Pol II. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11087726;Dbxref=PMID:11087726	
+P34087	UniProtKB	Mutagenesis	151	158	.	.	.	Note=No effect on nucleic-acid binding of RPB4-RPB7 and on association with Pol II core complex%3B abolishes transcriptional activity of Pol II. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11087726;Dbxref=PMID:11087726	
+P34087	UniProtKB	Beta strand	2	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Helix	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P34087	UniProtKB	Beta strand	19	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOU	
+P34087	UniProtKB	Helix	22	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Beta strand	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Turn	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Beta strand	43	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Helix	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Beta strand	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P34087	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P34087	UniProtKB	Beta strand	71	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Beta strand	86	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Beta strand	98	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Beta strand	106	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Helix	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Beta strand	117	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOY	
+P34087	UniProtKB	Beta strand	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Beta strand	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P34087	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOU	
+P34087	UniProtKB	Beta strand	142	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Beta strand	156	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P34087	UniProtKB	Beta strand	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VUM	
+##sequence-region Q12189 1 258
+Q12189	UniProtKB	Chain	1	258	.	.	.	ID=PRO_0000158524;Note=Ribose-5-phosphate isomerase	
+Q12189	UniProtKB	Helix	20	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Turn	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	41	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Helix	51	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Turn	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Helix	67	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	74	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Helix	80	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Turn	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	101	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Helix	126	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	136	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Helix	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	161	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Helix	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Helix	170	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	184	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Turn	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	195	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	206	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	213	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Helix	218	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	231	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	242	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+Q12189	UniProtKB	Beta strand	253	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ	
+##sequence-region P32496 1 274
+P32496	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+P32496	UniProtKB	Chain	2	274	.	.	.	ID=PRO_0000173851;Note=26S proteasome regulatory subunit RPN12	
+P32496	UniProtKB	Helix	8	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Helix	20	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Helix	52	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Helix	75	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Helix	101	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Helix	119	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Turn	138	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Helix	143	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Helix	157	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Helix	174	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Beta strand	198	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Helix	202	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Helix	215	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Beta strand	232	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P32496	UniProtKB	Helix	259	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+##sequence-region Q12250 1 445
+Q12250	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+Q12250	UniProtKB	Chain	2	445	.	.	.	ID=PRO_0000173865;Note=26S proteasome regulatory subunit RPN5	
+Q12250	UniProtKB	Domain	231	404	.	.	.	Note=PCI	
+Q12250	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+Q12250	UniProtKB	Helix	32	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	37	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	49	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Turn	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	72	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	94	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	111	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	135	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	153	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Turn	161	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Turn	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	173	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	194	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	205	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	211	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	235	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	248	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	254	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	275	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	295	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	311	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Turn	326	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Beta strand	331	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	337	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Beta strand	357	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	362	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	373	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Beta strand	392	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Turn	395	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Beta strand	399	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12250	UniProtKB	Helix	408	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+##sequence-region Q06103 1 429
+Q06103	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+Q06103	UniProtKB	Chain	2	429	.	.	.	ID=PRO_0000173845;Note=26S proteasome regulatory subunit RPN7	
+Q06103	UniProtKB	Repeat	131	164	.	.	.	Note=TPR	
+Q06103	UniProtKB	Domain	221	392	.	.	.	Note=PCI	
+Q06103	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06103	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06103	UniProtKB	Sequence conflict	8	8	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06103	UniProtKB	Helix	25	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Beta strand	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	40	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Turn	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	60	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	96	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	127	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	147	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	164	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	169	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	184	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	204	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	224	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Turn	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	246	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	263	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	276	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Beta strand	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	286	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	301	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Turn	315	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Turn	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	323	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	326	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Beta strand	345	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	350	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	361	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	372	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Beta strand	379	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Turn	383	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Beta strand	387	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q06103	UniProtKB	Helix	396	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+##sequence-region Q04062 1 393
+Q04062	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000173870;Note=26S proteasome regulatory subunit RPN9	
+Q04062	UniProtKB	Domain	282	352	.	.	.	Note=PCI	
+Q04062	UniProtKB	Helix	7	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	24	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	38	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	58	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	75	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	92	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Turn	115	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	122	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	143	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	165	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	185	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	207	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	231	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	239	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	249	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	263	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	278	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	284	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Beta strand	306	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR3	
+Q04062	UniProtKB	Helix	310	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Turn	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Helix	324	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Beta strand	336	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Beta strand	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR3	
+Q04062	UniProtKB	Turn	343	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Beta strand	347	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR3	
+Q04062	UniProtKB	Helix	360	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q04062	UniProtKB	Turn	385	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+##sequence-region P38061 1 130
+P38061	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P38061	UniProtKB	Chain	2	130	.	.	.	ID=PRO_0000131145;Note=60S ribosomal protein L32	
+P38061	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38061	UniProtKB	Turn	20	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38061	UniProtKB	Beta strand	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U55	
+P38061	UniProtKB	Turn	41	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38061	UniProtKB	Helix	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38061	UniProtKB	Turn	61	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38061	UniProtKB	Beta strand	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U53	
+P38061	UniProtKB	Beta strand	72	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38061	UniProtKB	Helix	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38061	UniProtKB	Helix	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38061	UniProtKB	Turn	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38061	UniProtKB	Beta strand	92	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38061	UniProtKB	Helix	102	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38061	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38061	UniProtKB	Turn	122	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P51998 1 286
+P51998	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P51998	UniProtKB	Chain	27	286	.	.	.	ID=PRO_0000030541;Note=54S ribosomal protein YmL6%2C mitochondrial	
+P51998	UniProtKB	Sequence conflict	30	30	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P51998	UniProtKB	Sequence conflict	35	35	.	.	.	Note=A->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P51998	UniProtKB	Sequence conflict	53	53	.	.	.	Note=E->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P51998	UniProtKB	Sequence conflict	121	121	.	.	.	Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P51998	UniProtKB	Sequence conflict	156	156	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P51998	UniProtKB	Sequence conflict	249	249	.	.	.	Note=E->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P05319 1 106
+P05319	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000157681;Note=60S acidic ribosomal protein P2-alpha	
+P05319	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P05319	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P05319	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P05319	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P05319	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P05319	UniProtKB	Cross-link	2	2	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05319	UniProtKB	Cross-link	48	48	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P02400 1 110
+P02400	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000157682;Note=60S acidic ribosomal protein P2-beta	
+P02400	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P02400	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P02400	UniProtKB	Cross-link	49	49	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P02400	UniProtKB	Sequence conflict	75	78	.	.	.	Note=AAGA->GPAS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02400	UniProtKB	Sequence conflict	86	87	.	.	.	Note=DA->GD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02400	UniProtKB	Sequence conflict	89	89	.	.	.	Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12495 1 606
+Q12495	UniProtKB	Chain	1	606	.	.	.	ID=PRO_0000089272;Note=Chromatin assembly factor 1 subunit p90	
+Q12495	UniProtKB	Coiled coil	128	240	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12495	UniProtKB	Compositional bias	122	236	.	.	.	Note=Arg/Glu/Lys-rich (highly charged)	
+Q12495	UniProtKB	Compositional bias	166	169	.	.	.	Note=Poly-Lys	
+Q12495	UniProtKB	Compositional bias	383	436	.	.	.	Note=Asp/Glu-rich (acidic)	
+Q12495	UniProtKB	Compositional bias	393	398	.	.	.	Note=Poly-Glu	
+Q12495	UniProtKB	Compositional bias	406	412	.	.	.	Note=Poly-Glu	
+Q12495	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12495	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12495	UniProtKB	Modified residue	509	509	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12495	UniProtKB	Helix	527	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO	
+Q12495	UniProtKB	Helix	544	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO	
+Q12495	UniProtKB	Helix	560	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO	
+Q12495	UniProtKB	Beta strand	571	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO	
+Q12495	UniProtKB	Beta strand	577	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JBM	
+Q12495	UniProtKB	Beta strand	584	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO	
+Q12495	UniProtKB	Helix	589	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO	
+##sequence-region Q03195 1 608
+Q03195	UniProtKB	Chain	1	608	.	.	.	ID=PRO_0000268703;Note=Translation initiation factor RLI1	
+Q03195	UniProtKB	Domain	7	39	.	.	.	Note=4Fe-4S ferredoxin-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00711	
+Q03195	UniProtKB	Domain	46	75	.	.	.	Note=4Fe-4S ferredoxin-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00711	
+Q03195	UniProtKB	Domain	70	320	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q03195	UniProtKB	Domain	345	568	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q03195	UniProtKB	Nucleotide binding	110	117	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q03195	UniProtKB	Nucleotide binding	385	392	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q03195	UniProtKB	Modified residue	349	349	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03195	UniProtKB	Mutagenesis	224	224	.	.	.	Note=Lethal%3B when associated with D-225. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15277527;Dbxref=PMID:15277527	
+Q03195	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Lethal%3B when associated with D-224. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15277527;Dbxref=PMID:15277527	
+Q03195	UniProtKB	Mutagenesis	470	470	.	.	.	Note=Lethal%3B when associated with D-471. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15277527;Dbxref=PMID:15277527	
+Q03195	UniProtKB	Mutagenesis	471	471	.	.	.	Note=Lethal%3B when associated with D-470. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15277527;Dbxref=PMID:15277527	
+Q03195	UniProtKB	Mutagenesis	493	493	.	.	.	Note=Lethal. Inhibits translation in vitro. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15277527;Dbxref=PMID:15277527	
+##sequence-region Q12224 1 676
+Q12224	UniProtKB	Chain	1	676	.	.	.	ID=PRO_0000199440;Note=Transcription factor RLM1	
+Q12224	UniProtKB	Domain	3	57	.	.	.	Note=MADS-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00251	
+Q12224	UniProtKB	DNA binding	58	87	.	.	.	Note=Mef2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12224	UniProtKB	Compositional bias	129	134	.	.	.	Note=Poly-Asp	
+Q12224	UniProtKB	Compositional bias	207	212	.	.	.	Note=Poly-Gln	
+Q12224	UniProtKB	Compositional bias	229	236	.	.	.	Note=Poly-Ser	
+Q12224	UniProtKB	Compositional bias	414	417	.	.	.	Note=Poly-Asn	
+Q12224	UniProtKB	Compositional bias	567	579	.	.	.	Note=Poly-Asn	
+Q12224	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12224	UniProtKB	Modified residue	164	164	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12224	UniProtKB	Modified residue	374	374	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12224	UniProtKB	Modified residue	377	377	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P36520 1 322
+P36520	UniProtKB	Transit peptide	1	57	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P36520	UniProtKB	Chain	58	322	.	.	.	ID=PRO_0000030468;Note=54S ribosomal protein L10%2C mitochondrial	
+P36520	UniProtKB	Sequence conflict	68	68	.	.	.	Note=D->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36520	UniProtKB	Sequence conflict	71	71	.	.	.	Note=T->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36520	UniProtKB	Sequence conflict	182	182	.	.	.	Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36520	UniProtKB	Sequence conflict	188	188	.	.	.	Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P23369 1 157
+P23369	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2017142;Dbxref=PMID:2017142	
+P23369	UniProtKB	Chain	2	157	.	.	.	ID=PRO_0000087690;Note=54S ribosomal protein L25%2C mitochondrial	
+P23369	UniProtKB	Sequence conflict	14	14	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23369	UniProtKB	Sequence conflict	27	27	.	.	.	Note=Y->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36531 1 177
+P36531	UniProtKB	Transit peptide	1	14	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P36531	UniProtKB	Chain	15	177	.	.	.	ID=PRO_0000030580;Note=54S ribosomal protein L36%2C mitochondrial	
+P36531	UniProtKB	Region	36	118	.	.	.	Note=Sufficient for general mitochondrial translation	
+P36531	UniProtKB	Region	87	177	.	.	.	Note=Sufficient for dosage suppression of COX2 mutation	
+##sequence-region P36533 1 70
+P36533	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P36533	UniProtKB	Chain	2	70	.	.	.	ID=PRO_0000087693;Note=54S ribosomal protein L39%2C mitochondrial	
+P36533	UniProtKB	Sequence conflict	29	29	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36533	UniProtKB	Sequence conflict	38	38	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36533	UniProtKB	Sequence conflict	47	47	.	.	.	Note=V->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36534 1 297
+P36534	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36534	UniProtKB	Chain	2	297	.	.	.	ID=PRO_0000030582;Note=54S ribosomal protein L40%2C mitochondrial	
+P36534	UniProtKB	Domain	63	96	.	.	.	Note=KOW	
+P36534	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36534	UniProtKB	Sequence conflict	179	179	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06090 1 140
+Q06090	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000030590;Note=54S ribosomal protein L51%2C mitochondrial	
+##sequence-region P43620 1 662
+P43620	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P43620	UniProtKB	Chain	2	662	.	.	.	ID=PRO_0000202698;Note=Sporulation protein RMD8	
+P43620	UniProtKB	Transmembrane	630	647	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43620	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P49166 1 88
+P49166	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3	
+P49166	UniProtKB	Chain	2	88	.	.	.	ID=PRO_0000139722;Note=60S ribosomal protein L37-A	
+P49166	UniProtKB	Zinc finger	19	37	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49166	UniProtKB	Metal binding	19	19	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102	
+P49166	UniProtKB	Metal binding	22	22	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102	
+P49166	UniProtKB	Metal binding	34	34	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102	
+P49166	UniProtKB	Metal binding	37	37	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102	
+P49166	UniProtKB	Sequence conflict	73	73	.	.	.	Note=R->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P49166	UniProtKB	Helix	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49166	UniProtKB	Beta strand	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49166	UniProtKB	Turn	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49166	UniProtKB	Beta strand	24	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49166	UniProtKB	Turn	29	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49166	UniProtKB	Turn	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49166	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49166	UniProtKB	Helix	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U55	
+P49166	UniProtKB	Helix	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49166	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49166	UniProtKB	Helix	70	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49166	UniProtKB	Turn	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P04650 1 51
+P04650	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P04650	UniProtKB	Chain	2	51	.	.	.	ID=PRO_0000127044;Note=60S ribosomal protein L39	
+P04650	UniProtKB	Helix	7	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04650	UniProtKB	Helix	25	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04650	UniProtKB	Turn	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P25348 1 183
+P25348	UniProtKB	Transit peptide	1	71	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P25348	UniProtKB	Chain	72	183	.	.	.	ID=PRO_0000030518;Note=54S ribosomal protein L32%2C mitochondrial	
+##sequence-region Q04598 1 105
+Q04598	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04598	UniProtKB	Chain	17	105	.	.	.	ID=PRO_0000030523;Note=54S ribosomal protein L34%2C mitochondrial	
+##sequence-region P32387 1 263
+P32387	UniProtKB	Transit peptide	1	45	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P32387	UniProtKB	Chain	46	263	.	.	.	ID=PRO_0000030488;Note=54S ribosomal protein L41%2C mitochondrial	
+P32387	UniProtKB	Sequence conflict	52	52	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32387	UniProtKB	Sequence conflict	155	155	.	.	.	Note=P->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32387	UniProtKB	Sequence conflict	253	253	.	.	.	Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32387	UniProtKB	Sequence conflict	259	259	.	.	.	Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32338 1 300
+P32338	UniProtKB	Chain	1	300	.	.	.	ID=PRO_0000046848;Note=Zinc finger protein RME1	
+P32338	UniProtKB	Zinc finger	178	199	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P32338	UniProtKB	Zinc finger	206	234	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P32338	UniProtKB	Zinc finger	256	281	.	.	.	Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P32338	UniProtKB	Mutagenesis	183	183	.	.	.	Note=Inactivates RME1. C->S	
+P32338	UniProtKB	Mutagenesis	213	213	.	.	.	Note=Inactivates RME1. C->S	
+P32338	UniProtKB	Mutagenesis	263	263	.	.	.	Note=Inactivates RME1. C->S	
+##sequence-region Q02685 1 241
+Q02685	UniProtKB	Chain	1	241	.	.	.	ID=PRO_0000270571;Note=RecQ-mediated genome instability protein 1	
+##sequence-region P40525 1 121
+P40525	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000131846;Note=60S ribosomal protein L34-B	
+##sequence-region P49167 1 78
+P49167	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P49167	UniProtKB	Chain	2	78	.	.	.	ID=PRO_0000215445;Note=60S ribosomal protein L38	
+P49167	UniProtKB	Beta strand	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49167	UniProtKB	Helix	8	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49167	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49167	UniProtKB	Beta strand	22	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49167	UniProtKB	Beta strand	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49167	UniProtKB	Beta strand	37	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49167	UniProtKB	Beta strand	51	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49167	UniProtKB	Helix	59	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P49167	UniProtKB	Beta strand	73	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX87 1 25
+P0CX87	UniProtKB	Chain	1	25	.	.	.	ID=PRO_0000410448;Note=60S ribosomal protein L41-B	
+P0CX87	UniProtKB	Compositional bias	2	23	.	.	.	Note=Arg-rich	
+##sequence-region P0CX26 1 92
+P0CX26	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894	
+P0CX26	UniProtKB	Chain	2	92	.	.	.	ID=PRO_0000409759;Note=60S ribosomal protein L43-B	
+P0CX26	UniProtKB	Zinc finger	39	60	.	.	.	Note=C4-type	
+P0CX26	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P0CX28 1 106
+P0CX28	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:365584;Dbxref=PMID:365584	
+P0CX28	UniProtKB	Chain	2	106	.	.	.	ID=PRO_0000409760;Note=60S ribosomal protein L42-B	
+P0CX28	UniProtKB	Modified residue	40	40	.	.	.	Note=N6-methyllysine%3B by RKM3;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342;Dbxref=PMID:18957409,PMID:22522802,PMID:24517342	
+P0CX28	UniProtKB	Modified residue	55	55	.	.	.	Note=N6-methyllysine%3B by RKM4;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:24517342;Dbxref=PMID:18957409,PMID:24517342	
+P0CX28	UniProtKB	Natural variant	56	56	.	.	.	Note=Confers resistance to cycloheximide%2C an inhibitor of polypeptide elongation. P->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729213;Dbxref=PMID:1729213	
+P0CX28	UniProtKB	Sequence conflict	40	41	.	.	.	Note=KR->RK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CX28	UniProtKB	Sequence conflict	88	89	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02326 1 176
+Q02326	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+Q02326	UniProtKB	Chain	2	176	.	.	.	ID=PRO_0000171017;Note=60S ribosomal protein L6-A	
+Q02326	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+Q02326	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02326	UniProtKB	Cross-link	128	128	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05739	
+Q02326	UniProtKB	Beta strand	38	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Turn	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Beta strand	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Beta strand	63	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Helix	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Beta strand	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Helix	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Beta strand	84	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Turn	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Helix	113	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Helix	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Helix	132	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Helix	155	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+Q02326	UniProtKB	Turn	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS	
+##sequence-region P51401 1 191
+P51401	UniProtKB	Chain	1	191	.	.	.	ID=PRO_0000131112;Note=60S ribosomal protein L9-B	
+##sequence-region P05317 1 312
+P05317	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000154786;Note=60S acidic ribosomal protein P0	
+P05317	UniProtKB	Region	199	230	.	.	.	Note=Interaction with P1A-P2B	
+P05317	UniProtKB	Region	231	258	.	.	.	Note=Interaction with P1B-P2A	
+P05317	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P05317	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:9843429;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:9843429	
+P05317	UniProtKB	Cross-link	14	14	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05317	UniProtKB	Cross-link	97	97	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05317	UniProtKB	Cross-link	144	144	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05317	UniProtKB	Sequence conflict	83	83	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05317	UniProtKB	Sequence conflict	83	83	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05317	UniProtKB	Sequence conflict	83	83	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05317	UniProtKB	Helix	4	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Beta strand	23	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Helix	35	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Beta strand	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P05317	UniProtKB	Beta strand	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Helix	56	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Beta strand	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Helix	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Helix	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Beta strand	82	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Helix	93	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Beta strand	186	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Beta strand	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P05317	UniProtKB	Turn	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Helix	210	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05317	UniProtKB	Turn	214	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region Q07915 1 199
+Q07915	UniProtKB	Chain	1	199	.	.	.	ID=PRO_0000136910;Note=Ribosome biogenesis protein RLP24	
+Q07915	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P12687 1 371
+P12687	UniProtKB	Transit peptide	1	27	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2060626,ECO:0000269|PubMed:2693936;Dbxref=PMID:2060626,PMID:2693936	
+P12687	UniProtKB	Chain	28	371	.	.	.	ID=PRO_0000030503;Note=54S ribosomal protein L2%2C mitochondrial	
+P12687	UniProtKB	Sequence conflict	28	29	.	.	.	Note=AT->SG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12687	UniProtKB	Sequence conflict	350	350	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36516 1 390
+P36516	UniProtKB	Transit peptide	1	59	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3060376;Dbxref=PMID:3060376	
+P36516	UniProtKB	Chain	60	390	.	.	.	ID=PRO_0000030569;Note=54S ribosomal protein L3%2C mitochondrial	
+P36516	UniProtKB	Domain	139	205	.	.	.	Note=RNase III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00177	
+P36516	UniProtKB	Domain	302	372	.	.	.	Note=DRBM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00266	
+P36516	UniProtKB	Sequence conflict	60	60	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P22353 1 238
+P22353	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2183197;Dbxref=PMID:2183197	
+P22353	UniProtKB	Chain	2	238	.	.	.	ID=PRO_0000175550;Note=54S ribosomal protein L8%2C mitochondrial	
+P22353	UniProtKB	Sequence conflict	2	2	.	.	.	Note=T->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22353	UniProtKB	Sequence conflict	82	82	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32388 1 137
+P32388	UniProtKB	Chain	1	137	.	.	.	ID=PRO_0000030583;Note=54S ribosomal protein MRP49%2C mitochondrial	
+##sequence-region P53724 1 139
+P53724	UniProtKB	Chain	1	139	.	.	.	ID=PRO_0000030584;Note=54S ribosomal protein L50%2C mitochondrial	
+##sequence-region P38330 1 731
+P38330	UniProtKB	Modified residue	132	132	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P25299 1 296
+P25299	UniProtKB	Chain	1	296	.	.	.	ID=PRO_0000081807;Note=mRNA 3'-end-processing protein RNA15	
+P25299	UniProtKB	Domain	18	96	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P25299	UniProtKB	Compositional bias	104	109	.	.	.	Note=Poly-Gln	
+P25299	UniProtKB	Compositional bias	111	128	.	.	.	Note=Asn-rich	
+P25299	UniProtKB	Beta strand	18	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F	
+P25299	UniProtKB	Helix	31	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F	
+P25299	UniProtKB	Beta strand	44	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F	
+P25299	UniProtKB	Turn	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F	
+P25299	UniProtKB	Beta strand	60	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F	
+P25299	UniProtKB	Helix	69	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F	
+P25299	UniProtKB	Beta strand	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM8	
+P25299	UniProtKB	Beta strand	90	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F	
+P25299	UniProtKB	Helix	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F	
+P25299	UniProtKB	Helix	139	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+P25299	UniProtKB	Turn	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+P25299	UniProtKB	Helix	161	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+P25299	UniProtKB	Helix	174	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+P25299	UniProtKB	Helix	192	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+P25299	UniProtKB	Helix	203	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+P25299	UniProtKB	Beta strand	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+P25299	UniProtKB	Helix	221	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+P25299	UniProtKB	Turn	225	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+##sequence-region P11745 1 407
+P11745	UniProtKB	Chain	1	407	.	.	.	ID=PRO_0000056742;Note=Ran GTPase-activating protein 1	
+P11745	UniProtKB	Repeat	11	39	.	.	.	Note=LRR 1	
+P11745	UniProtKB	Repeat	40	67	.	.	.	Note=LRR 2	
+P11745	UniProtKB	Repeat	68	101	.	.	.	Note=LRR 3	
+P11745	UniProtKB	Repeat	102	133	.	.	.	Note=LRR 4	
+P11745	UniProtKB	Repeat	134	166	.	.	.	Note=LRR 5	
+P11745	UniProtKB	Repeat	167	197	.	.	.	Note=LRR 6	
+P11745	UniProtKB	Repeat	198	226	.	.	.	Note=LRR 7	
+P11745	UniProtKB	Repeat	227	256	.	.	.	Note=LRR 8	
+P11745	UniProtKB	Repeat	257	285	.	.	.	Note=LRR 9	
+P11745	UniProtKB	Repeat	286	315	.	.	.	Note=LRR 10	
+P11745	UniProtKB	Repeat	316	346	.	.	.	Note=LRR 11	
+P11745	UniProtKB	Compositional bias	348	375	.	.	.	Note=Asp/Glu-rich (acidic)	
+P11745	UniProtKB	Modified residue	360	360	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P11745	UniProtKB	Natural variant	17	17	.	.	.	Note=In mutant RNA1-1. S->F	
+P11745	UniProtKB	Natural variant	194	194	.	.	.	Note=In mutant RNA1-1. A->V	
+P11745	UniProtKB	Sequence conflict	42	42	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11745	UniProtKB	Sequence conflict	222	222	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05635 1 350
+Q05635	UniProtKB	Chain	1	350	.	.	.	ID=PRO_0000248383;Note=Ribonuclease H2 subunit B	
+Q05635	UniProtKB	Sequence conflict	83	83	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P05747 1 59
+P05747	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943	
+P05747	UniProtKB	Chain	2	59	.	.	.	ID=PRO_0000219141;Note=60S ribosomal protein L29	
+P05747	UniProtKB	Cross-link	52	52	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05747	UniProtKB	Helix	12	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05747	UniProtKB	Helix	37	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05747	UniProtKB	Helix	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX27 1 106
+P0CX27	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:365584;Dbxref=PMID:365584	
+P0CX27	UniProtKB	Chain	2	106	.	.	.	ID=PRO_0000149147;Note=60S ribosomal protein L42-A	
+P0CX27	UniProtKB	Modified residue	40	40	.	.	.	Note=N6-methyllysine%3B by RKM3;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342;Dbxref=PMID:18957409,PMID:22522802,PMID:24517342	
+P0CX27	UniProtKB	Modified residue	55	55	.	.	.	Note=N6-methyllysine%3B by RKM4;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:24517342;Dbxref=PMID:18957409,PMID:24517342	
+P0CX27	UniProtKB	Natural variant	56	56	.	.	.	Note=Confers resistance to cycloheximide%2C an inhibitor of polypeptide elongation. P->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729213;Dbxref=PMID:1729213	
+P0CX27	UniProtKB	Sequence conflict	40	41	.	.	.	Note=KR->RK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CX27	UniProtKB	Sequence conflict	88	89	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CX27	UniProtKB	Beta strand	6	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX27	UniProtKB	Turn	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX27	UniProtKB	Beta strand	19	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX27	UniProtKB	Helix	38	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX27	UniProtKB	Beta strand	48	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX27	UniProtKB	Beta strand	66	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX27	UniProtKB	Turn	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX27	UniProtKB	Beta strand	80	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX27	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region Q12213 1 244
+Q12213	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000104652;Note=60S ribosomal protein L7-B	
+##sequence-region P38064 1 232
+P38064	UniProtKB	Transit peptide	1	41	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38064	UniProtKB	Chain	42	232	.	.	.	ID=PRO_0000030469;Note=54S ribosomal protein L16%2C mitochondrial	
+P38064	UniProtKB	Sequence conflict	55	55	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38064	UniProtKB	Sequence conflict	119	119	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38064	UniProtKB	Sequence conflict	209	209	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36527 1 147
+P36527	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P36527	UniProtKB	Chain	27	147	.	.	.	ID=PRO_0000030575;Note=54S ribosomal protein L28%2C mitochondrial	
+P36527	UniProtKB	Sequence conflict	28	29	.	.	.	Note=RT->IF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36527	UniProtKB	Sequence conflict	33	37	.	.	.	Note=SSLSP->VILVI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36527	UniProtKB	Sequence conflict	49	49	.	.	.	Note=M->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36527	UniProtKB	Sequence conflict	53	53	.	.	.	Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P20084 1 86
+P20084	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P20084	UniProtKB	Chain	2	86	.	.	.	ID=PRO_0000104619;Note=54S ribosomal protein L33%2C mitochondrial	
+P20084	UniProtKB	Sequence conflict	81	86	.	.	.	Note=EKRTID->GEENHRLKQRNKALDFLSS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36532 1 105
+P36532	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P36532	UniProtKB	Chain	25	105	.	.	.	ID=PRO_0000030581;Note=54S ribosomal protein L37%2C mitochondrial	
+P36532	UniProtKB	Sequence conflict	27	27	.	.	.	Note=V->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36532	UniProtKB	Sequence conflict	30	30	.	.	.	Note=C->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36532	UniProtKB	Sequence conflict	35	35	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36532	UniProtKB	Sequence conflict	41	41	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36532	UniProtKB	Sequence conflict	54	54	.	.	.	Note=E->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35996 1 138
+P35996	UniProtKB	Chain	1	138	.	.	.	ID=PRO_0000030464;Note=54S ribosomal protein L38%2C mitochondrial	
+P35996	UniProtKB	Chain	58	138	.	.	.	ID=PRO_0000030465;Note=54S ribosomal protein L34%2C mitochondrial	
+P35996	UniProtKB	Sequence conflict	60	60	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35996	UniProtKB	Sequence conflict	69	70	.	.	.	Note=CH->DI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P02406 1 149
+P02406	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P02406	UniProtKB	Chain	2	149	.	.	.	ID=PRO_0000104904;Note=60S ribosomal protein L28	
+P02406	UniProtKB	Motif	7	13	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2104804;Dbxref=PMID:2104804	
+P02406	UniProtKB	Motif	24	30	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2104804;Dbxref=PMID:2104804	
+P02406	UniProtKB	Cross-link	96	96	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P02406	UniProtKB	Natural variant	38	38	.	.	.	Note=Confers resistance to cycloheximide%2C an inhibitor of polypeptide elongation. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6304624;Dbxref=PMID:6304624	
+P02406	UniProtKB	Helix	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Helix	7	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Beta strand	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Helix	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Turn	33	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Helix	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Turn	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Turn	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Turn	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Helix	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Helix	84	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Beta strand	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Turn	104	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Beta strand	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Beta strand	124	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Helix	132	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02406	UniProtKB	Beta strand	144	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX85 1 120
+P0CX85	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894	
+P0CX85	UniProtKB	Chain	2	120	.	.	.	ID=PRO_0000410447;Note=60S ribosomal protein L35-B	
+P0CX85	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX85	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P14126 1 387
+P14126	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:6355773;Dbxref=PMID:1544921,PMID:6355773	
+P14126	UniProtKB	Chain	2	387	.	.	.	ID=PRO_0000077251;Note=60S ribosomal protein L3	
+P14126	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P14126	UniProtKB	Modified residue	103	103	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P14126	UniProtKB	Modified residue	156	156	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P14126	UniProtKB	Modified residue	243	243	.	.	.	Note=Pros-methylhistidine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20864530;Dbxref=PMID:20864530	
+P14126	UniProtKB	Modified residue	297	297	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14126	UniProtKB	Cross-link	39	39	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14126	UniProtKB	Cross-link	136	136	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14126	UniProtKB	Sequence conflict	255	255	.	.	.	Note=W->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14126	UniProtKB	Helix	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U52	
+P14126	UniProtKB	Beta strand	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U53	
+P14126	UniProtKB	Beta strand	44	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Turn	66	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	70	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	84	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Helix	112	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Helix	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Turn	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Turn	129	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Helix	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Helix	142	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	156	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Helix	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	178	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F	
+P14126	UniProtKB	Helix	188	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Turn	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P14126	UniProtKB	Helix	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	214	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	223	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Helix	229	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	255	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	268	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	274	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Turn	291	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Turn	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Turn	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	321	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	335	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Turn	349	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Beta strand	356	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Turn	364	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P14126	UniProtKB	Helix	373	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CH09 1 128
+P0CH09	UniProtKB	Chain	1	76	.	.	.	ID=PRO_0000396455;Note=Ubiquitin	
+P0CH09	UniProtKB	Chain	77	128	.	.	.	ID=PRO_0000396456;Note=60S ribosomal protein L40-B	
+P0CH09	UniProtKB	Domain	1	76	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+P0CH09	UniProtKB	Cross-link	76	76	.	.	.	Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)	
+P0CH09	UniProtKB	Cross-link	93	93	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CH09	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P0CH09	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P0CH09	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+##sequence-region P0CX86 1 25
+P0CX86	UniProtKB	Chain	1	25	.	.	.	ID=PRO_0000198074;Note=60S ribosomal protein L41-A	
+P0CX86	UniProtKB	Compositional bias	2	23	.	.	.	Note=Arg-rich	
+P0CX86	UniProtKB	Helix	3	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+##sequence-region P10664 1 362
+P10664	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921	
+P10664	UniProtKB	Chain	2	362	.	.	.	ID=PRO_0000129367;Note=60S ribosomal protein L4-A	
+P10664	UniProtKB	Region	277	362	.	.	.	Note=C-terminal-extended nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P10664	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921	
+P10664	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Leads to a slower growth at higher temperatures but allows RPL4 assembly into the 60S subunit%3B when associated with E-98. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P10664	UniProtKB	Mutagenesis	98	98	.	.	.	Note=Leads to a slower growth at higher temperatures but allows RPL4 assembly into the 60S subunit%3B when associated with E-95. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P10664	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-290 and A-295. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P10664	UniProtKB	Mutagenesis	290	290	.	.	.	Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-289 and A-295. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P10664	UniProtKB	Mutagenesis	295	295	.	.	.	Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-289 and A-290. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P10664	UniProtKB	Mutagenesis	314	314	.	.	.	Note=Significantly diminished nuclear localization%3B when associated with A-315 and A-319. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P10664	UniProtKB	Mutagenesis	315	315	.	.	.	Note=Significantly diminished nuclear localization%3B when associated with A-314 and A-319. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P10664	UniProtKB	Mutagenesis	319	319	.	.	.	Note=Significantly diminished nuclear localization%3B when associated with A-314 and A-315. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P10664	UniProtKB	Mutagenesis	332	332	.	.	.	Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-334. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P10664	UniProtKB	Mutagenesis	334	334	.	.	.	Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with e-332. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P10664	UniProtKB	Sequence conflict	38	38	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10664	UniProtKB	Sequence conflict	144	144	.	.	.	Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10664	UniProtKB	Sequence conflict	157	157	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10664	UniProtKB	Sequence conflict	224	224	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10664	UniProtKB	Sequence conflict	241	241	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10664	UniProtKB	Beta strand	6	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N	
+P10664	UniProtKB	Beta strand	15	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F	
+P10664	UniProtKB	Helix	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	32	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Turn	43	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Turn	54	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F	
+P10664	UniProtKB	Beta strand	67	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	81	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	94	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56	
+P10664	UniProtKB	Helix	115	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	132	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	143	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	148	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	154	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	162	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	175	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	206	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	215	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Turn	219	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N	
+P10664	UniProtKB	Beta strand	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P10664	UniProtKB	Beta strand	226	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	235	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	248	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	252	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	265	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	286	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Turn	292	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Beta strand	317	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	321	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	331	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P10664	UniProtKB	Helix	339	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U51	
+P10664	UniProtKB	Helix	353	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P36517 1 319
+P36517	UniProtKB	Transit peptide	1	14	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3060376;Dbxref=PMID:3060376	
+P36517	UniProtKB	Chain	15	319	.	.	.	ID=PRO_0000030570;Note=54S ribosomal protein L4%2C mitochondrial	
+P36517	UniProtKB	Sequence conflict	168	168	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36519 1 292
+P36519	UniProtKB	Transit peptide	1	19	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P36519	UniProtKB	Chain	20	292	.	.	.	ID=PRO_0000030545;Note=54S ribosomal protein L7%2C mitochondrial	
+P36519	UniProtKB	Sequence conflict	23	23	.	.	.	Note=C->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36519	UniProtKB	Sequence conflict	33	33	.	.	.	Note=V->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36519	UniProtKB	Sequence conflict	85	85	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36528 1 281
+P36528	UniProtKB	Transit peptide	1	19	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P36528	UniProtKB	Chain	20	281	.	.	.	ID=PRO_0000030578;Note=54S ribosomal protein L17%2C mitochondrial	
+##sequence-region P53881 1 309
+P53881	UniProtKB	Transit peptide	1	25	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53881	UniProtKB	Chain	26	309	.	.	.	ID=PRO_0000030487;Note=54S ribosomal protein L22%2C mitochondrial	
+P53881	UniProtKB	Sequence conflict	151	151	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12487 1 163
+Q12487	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12487	UniProtKB	Propeptide	2	4	.	.	.	ID=PRO_0000030462;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978	
+Q12487	UniProtKB	Chain	5	163	.	.	.	ID=PRO_0000030463;Note=54S ribosomal protein L23%2C mitochondrial	
+Q12487	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12487	UniProtKB	Sequence conflict	5	5	.	.	.	Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39975 1 231
+P39975	UniProtKB	Chain	1	231	.	.	.	ID=PRO_0000202600;Note=Sporulation protein RMD6	
+P39975	UniProtKB	Sequence conflict	28	28	.	.	.	Note=Y->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CX42 1 137
+P0CX42	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16096273;Dbxref=PMID:22814378,PMID:16096273	
+P0CX42	UniProtKB	Chain	2	137	.	.	.	ID=PRO_0000409767;Note=60S ribosomal protein L23-B	
+P0CX42	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16096273;Dbxref=PMID:22814378,PMID:16096273	
+P0CX42	UniProtKB	Modified residue	106	106	.	.	.	Note=N6%2CN6-dimethyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17327221;Dbxref=PMID:17327221	
+P0CX42	UniProtKB	Modified residue	110	110	.	.	.	Note=N6%2CN6-dimethyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17327221;Dbxref=PMID:17327221	
+##sequence-region P04456 1 142
+P04456	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921	
+P04456	UniProtKB	Chain	2	142	.	.	.	ID=PRO_0000129483;Note=60S ribosomal protein L25	
+P04456	UniProtKB	Cross-link	61	61	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542864;Dbxref=PMID:15542864	
+P04456	UniProtKB	Sequence conflict	106	112	.	.	.	Note=DVLKVNT->NI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04456	UniProtKB	Beta strand	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P04456	UniProtKB	Beta strand	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04456	UniProtKB	Helix	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04456	UniProtKB	Beta strand	63	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04456	UniProtKB	Helix	70	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04456	UniProtKB	Beta strand	81	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04456	UniProtKB	Helix	92	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04456	UniProtKB	Beta strand	107	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04456	UniProtKB	Turn	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U55	
+P04456	UniProtKB	Beta strand	120	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04456	UniProtKB	Helix	132	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0C2H9 1 113
+P0C2H9	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000278968;Note=60S ribosomal protein L31-B	
+##sequence-region P29453 1 256
+P29453	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921	
+P29453	UniProtKB	Chain	2	256	.	.	.	ID=PRO_0000136761;Note=60S ribosomal protein L8-B	
+P29453	UniProtKB	Sequence conflict	114	115	.	.	.	Note=AA->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P05318 1 106
+P05318	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:8476850;Dbxref=PMID:10601260,PMID:8476850	
+P05318	UniProtKB	Chain	2	106	.	.	.	ID=PRO_0000157705;Note=60S acidic ribosomal protein P1-alpha	
+P05318	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:8476850;Dbxref=PMID:10601260,PMID:8476850	
+P05318	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P05318	UniProtKB	Sequence conflict	37	37	.	.	.	Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05318	UniProtKB	Sequence conflict	37	37	.	.	.	Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05318	UniProtKB	Sequence conflict	37	37	.	.	.	Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region O14455 1 100
+O14455	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943	
+O14455	UniProtKB	Chain	2	100	.	.	.	ID=PRO_0000195021;Note=60S ribosomal protein L36-B	
+O14455	UniProtKB	Sequence conflict	35	35	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CH08 1 128
+P0CH08	UniProtKB	Chain	1	76	.	.	.	ID=PRO_0000396454;Note=Ubiquitin	
+P0CH08	UniProtKB	Chain	77	128	.	.	.	ID=PRO_0000138775;Note=60S ribosomal protein L40-A	
+P0CH08	UniProtKB	Domain	1	76	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+P0CH08	UniProtKB	Cross-link	76	76	.	.	.	Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)	
+P0CH08	UniProtKB	Cross-link	93	93	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CH08	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P0CH08	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P0CH08	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P0CH08	UniProtKB	Helix	80	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CH08	UniProtKB	Beta strand	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CH08	UniProtKB	Turn	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CH08	UniProtKB	Turn	113	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CH08	UniProtKB	Beta strand	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX25 1 92
+P0CX25	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894	
+P0CX25	UniProtKB	Chain	2	92	.	.	.	ID=PRO_0000139838;Note=60S ribosomal protein L43-A	
+P0CX25	UniProtKB	Zinc finger	39	60	.	.	.	Note=C4-type	
+P0CX25	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX25	UniProtKB	Helix	9	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX25	UniProtKB	Turn	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX25	UniProtKB	Helix	20	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX25	UniProtKB	Turn	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX25	UniProtKB	Beta strand	44	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX25	UniProtKB	Beta strand	54	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX25	UniProtKB	Turn	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX25	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX25	UniProtKB	Beta strand	68	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX25	UniProtKB	Helix	74	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P26321 1 297
+P26321	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:393511;Dbxref=PMID:393511	
+P26321	UniProtKB	Chain	2	297	.	.	.	ID=PRO_0000131454;Note=60S ribosomal protein L5	
+P26321	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P26321	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P26321	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P26321	UniProtKB	Cross-link	164	164	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P26321	UniProtKB	Sequence conflict	18	18	.	.	.	Note=T->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P26321	UniProtKB	Sequence conflict	112	112	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P26321	UniProtKB	Sequence conflict	112	112	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P26321	UniProtKB	Beta strand	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P26321	UniProtKB	Helix	10	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	30	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Beta strand	50	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Beta strand	59	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Beta strand	71	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	80	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P26321	UniProtKB	Helix	95	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Beta strand	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Beta strand	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	159	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P26321	UniProtKB	Beta strand	180	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P26321	UniProtKB	Turn	185	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	192	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	202	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	216	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	224	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	236	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	262	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Beta strand	271	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Helix	279	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26321	UniProtKB	Turn	293	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P05739 1 176
+P05739	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943	
+P05739	UniProtKB	Chain	2	176	.	.	.	ID=PRO_0000171018;Note=60S ribosomal protein L6-B	
+P05739	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02326	
+P05739	UniProtKB	Cross-link	128	128	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05739	UniProtKB	Sequence conflict	68	68	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38144 1 1129
+P38144	UniProtKB	Chain	1	1129	.	.	.	ID=PRO_0000074330;Note=ISWI chromatin-remodeling complex ATPase ISW1	
+P38144	UniProtKB	Domain	208	373	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P38144	UniProtKB	Domain	506	657	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P38144	UniProtKB	Domain	882	935	.	.	.	Note=SANT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624	
+P38144	UniProtKB	Domain	988	1052	.	.	.	Note=SANT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624	
+P38144	UniProtKB	Nucleotide binding	221	228	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P38144	UniProtKB	Motif	324	327	.	.	.	Note=DEAH box	
+P38144	UniProtKB	Modified residue	694	694	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38144	UniProtKB	Modified residue	846	846	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38144	UniProtKB	Mutagenesis	227	227	.	.	.	Note=Abolishes ATPase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10090725;Dbxref=PMID:10090725	
+P38144	UniProtKB	Helix	814	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Turn	828	830	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	835	838	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Turn	839	841	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Turn	848	850	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	851	862	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Beta strand	866	868	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	870	882	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	889	902	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	907	911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Beta strand	917	919	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	920	932	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Turn	941	943	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	944	968	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	974	977	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	994	1007	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	1015	1024	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	1027	1029	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	1032	1035	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Helix	1039	1054	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P38144	UniProtKB	Turn	1055	1058	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+##sequence-region Q08773 1 1120
+Q08773	UniProtKB	Chain	1	1120	.	.	.	ID=PRO_0000240453;Note=ISWI chromatin-remodeling complex ATPase ISW2	
+Q08773	UniProtKB	Domain	196	361	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q08773	UniProtKB	Domain	494	645	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q08773	UniProtKB	Domain	886	938	.	.	.	Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624	
+Q08773	UniProtKB	Nucleotide binding	209	216	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q08773	UniProtKB	Motif	312	315	.	.	.	Note=DEAH box	
+Q08773	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08773	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08773	UniProtKB	Modified residue	831	831	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08773	UniProtKB	Modified residue	1079	1079	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08773	UniProtKB	Modified residue	1082	1082	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08773	UniProtKB	Mutagenesis	215	215	.	.	.	Note=Abolishes ATPase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10090725;Dbxref=PMID:10090725	
+##sequence-region Q03419 1 316
+Q03419	UniProtKB	Chain	1	316	.	.	.	ID=PRO_0000240373;Note=ADIPOR-like receptor IZH1	
+Q03419	UniProtKB	Topological domain	1	89	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03419	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03419	UniProtKB	Topological domain	111	117	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03419	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03419	UniProtKB	Topological domain	139	156	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03419	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03419	UniProtKB	Topological domain	178	181	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03419	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03419	UniProtKB	Topological domain	203	218	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03419	UniProtKB	Transmembrane	219	239	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03419	UniProtKB	Topological domain	240	245	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03419	UniProtKB	Transmembrane	246	266	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03419	UniProtKB	Topological domain	267	279	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03419	UniProtKB	Transmembrane	280	300	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03419	UniProtKB	Topological domain	301	316	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03419	UniProtKB	Glycosylation	79	79	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03419	UniProtKB	Glycosylation	207	207	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03419	UniProtKB	Sequence conflict	139	139	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99393 1 312
+Q99393	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000240376;Note=ADIPOR-like receptor IZH4	
+Q99393	UniProtKB	Topological domain	1	64	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Topological domain	86	101	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Transmembrane	102	122	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Topological domain	123	141	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Topological domain	163	165	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Transmembrane	166	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Topological domain	187	201	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Topological domain	223	231	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Topological domain	253	277	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Transmembrane	278	298	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Topological domain	299	312	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99393	UniProtKB	Sequence conflict	211	211	.	.	.	Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40358 1 645
+P40358	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40358	UniProtKB	Chain	23	645	.	.	.	ID=PRO_0000043353;Note=DnaJ-like chaperone JEM1	
+P40358	UniProtKB	Topological domain	23	190	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9148890;Dbxref=PMID:9148890	
+P40358	UniProtKB	Transmembrane	191	211	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40358	UniProtKB	Topological domain	212	645	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9148890;Dbxref=PMID:9148890	
+P40358	UniProtKB	Domain	538	608	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P40358	UniProtKB	Compositional bias	493	525	.	.	.	Note=Gln-rich	
+##sequence-region P36224 1 373
+P36224	UniProtKB	Chain	1	373	.	.	.	ID=PRO_0000084289;Note=Nuclear migration protein JNM1	
+P36224	UniProtKB	Coiled coil	114	139	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36224	UniProtKB	Coiled coil	200	245	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36224	UniProtKB	Coiled coil	331	367	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36224	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36224	UniProtKB	Sequence conflict	92	92	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36224	UniProtKB	Sequence conflict	114	114	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36224	UniProtKB	Sequence conflict	193	193	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36224	UniProtKB	Sequence conflict	201	201	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36224	UniProtKB	Sequence conflict	264	264	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07170 1 222
+P07170	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07170	UniProtKB	Propeptide	2	2	.	.	.	ID=PRO_0000016550;Note=Removed in mature form;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:3004985;Dbxref=PMID:3004985	
+P07170	UniProtKB	Chain	3	222	.	.	.	ID=PRO_0000016551;Note=Adenylate kinase	
+P07170	UniProtKB	Nucleotide binding	16	21	.	.	.	Note=ATP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369,ECO:0000269|PubMed:8594191;Dbxref=PMID:7635152,PMID:7670369,PMID:8594191	
+P07170	UniProtKB	Nucleotide binding	63	65	.	.	.	Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369	
+P07170	UniProtKB	Nucleotide binding	92	95	.	.	.	Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369	
+P07170	UniProtKB	Nucleotide binding	143	144	.	.	.	Note=ATP;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369,ECO:0000269|PubMed:8594191;Dbxref=PMID:7635152,PMID:7670369,PMID:8594191	
+P07170	UniProtKB	Region	36	65	.	.	.	Note=NMPbind;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369	
+P07170	UniProtKB	Region	133	170	.	.	.	Note=LID;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369	
+P07170	UniProtKB	Binding site	37	37	.	.	.	Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369	
+P07170	UniProtKB	Binding site	42	42	.	.	.	Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369	
+P07170	UniProtKB	Binding site	99	99	.	.	.	Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369	
+P07170	UniProtKB	Binding site	134	134	.	.	.	Note=ATP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369,ECO:0000269|PubMed:8594191;Dbxref=PMID:7635152,PMID:7670369,PMID:8594191	
+P07170	UniProtKB	Binding site	167	167	.	.	.	Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369	
+P07170	UniProtKB	Binding site	178	178	.	.	.	Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369	
+P07170	UniProtKB	Binding site	206	206	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369,ECO:0000269|PubMed:8594191;Dbxref=PMID:7635152,PMID:7670369,PMID:8594191	
+P07170	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07170	UniProtKB	Modified residue	3	3	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:3004985;Dbxref=PMID:3004985	
+P07170	UniProtKB	Sequence conflict	95	95	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07170	UniProtKB	Sequence conflict	139	139	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07170	UniProtKB	Sequence conflict	222	222	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07170	UniProtKB	Beta strand	8	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Helix	19	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Beta strand	33	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Helix	37	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Helix	50	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Helix	67	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Helix	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Beta strand	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Helix	97	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Beta strand	116	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Helix	124	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Beta strand	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Turn	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Beta strand	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Turn	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Turn	158	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Helix	172	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Helix	188	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Beta strand	199	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+P07170	UniProtKB	Helix	208	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY	
+##sequence-region Q12055 1 197
+Q12055	UniProtKB	Chain	1	197	.	.	.	ID=PRO_0000153902;Note=Adenylate kinase isoenzyme 6 homolog FAP7	
+Q12055	UniProtKB	Nucleotide binding	17	22	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173	
+Q12055	UniProtKB	Region	38	61	.	.	.	Note=NMPbind;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173	
+Q12055	UniProtKB	Region	113	123	.	.	.	Note=LID;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173	
+Q12055	UniProtKB	Motif	28	35	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12055	UniProtKB	Binding site	44	44	.	.	.	Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173	
+Q12055	UniProtKB	Binding site	84	84	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173	
+Q12055	UniProtKB	Binding site	110	110	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173	
+Q12055	UniProtKB	Binding site	114	114	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173	
+Q12055	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12055	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12055	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12055	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Sensitive to hydrogen peroxide. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10692169;Dbxref=PMID:10692169	
+Q12055	UniProtKB	Mutagenesis	20	20	.	.	.	Note=Decreases the processing of 20S rRNA. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16287850;Dbxref=PMID:16287850	
+Q12055	UniProtKB	Mutagenesis	21	21	.	.	.	Note=Sensitive to hydrogen peroxide. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10692169;Dbxref=PMID:10692169	
+Q12055	UniProtKB	Mutagenesis	82	82	.	.	.	Note=Decreases the processing of 20S rRNA%3B when associated with A-84. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16287850;Dbxref=PMID:16287850	
+Q12055	UniProtKB	Mutagenesis	84	84	.	.	.	Note=Decreases the processing of 20S rRNA%3B when associated with A-82. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16287850;Dbxref=PMID:16287850	
+Q12055	UniProtKB	Sequence conflict	80	80	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P06245 1 380
+P06245	UniProtKB	Chain	1	380	.	.	.	ID=PRO_0000086048;Note=cAMP-dependent protein kinase type 2	
+P06245	UniProtKB	Domain	70	324	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06245	UniProtKB	Domain	325	380	.	.	.	Note=AGC-kinase C-terminal	
+P06245	UniProtKB	Nucleotide binding	76	84	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06245	UniProtKB	Active site	193	193	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P06245	UniProtKB	Binding site	99	99	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06245	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P06245	UniProtKB	Modified residue	224	224	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P06245	UniProtKB	Sequence conflict	214	220	.	.	.	Note=FAKEVQT->LRQRGTN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06245	UniProtKB	Sequence conflict	260	260	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06245	UniProtKB	Sequence conflict	289	289	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04746 1 504
+Q04746	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04746	UniProtKB	Chain	20	504	.	.	.	ID=PRO_0000203279;Note=Nuclear fusion protein KAR5	
+Q04746	UniProtKB	Topological domain	20	452	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9382856;Dbxref=PMID:9382856	
+Q04746	UniProtKB	Transmembrane	453	470	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04746	UniProtKB	Topological domain	471	481	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9382856;Dbxref=PMID:9382856	
+Q04746	UniProtKB	Transmembrane	482	502	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04746	UniProtKB	Topological domain	503	504	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9382856;Dbxref=PMID:9382856	
+Q04746	UniProtKB	Glycosylation	159	159	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04746	UniProtKB	Glycosylation	206	206	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04746	UniProtKB	Glycosylation	313	313	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04746	UniProtKB	Glycosylation	404	404	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39962 1 524
+P39962	UniProtKB	Chain	1	524	.	.	.	ID=PRO_0000192858;Note=Casein kinase I homolog 3	
+P39962	UniProtKB	Domain	14	319	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P39962	UniProtKB	Nucleotide binding	20	28	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P39962	UniProtKB	Motif	444	447	.	.	.	Note=YXXZ targeting signal	
+P39962	UniProtKB	Active site	150	150	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P39962	UniProtKB	Binding site	60	60	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P39962	UniProtKB	Lipidation	517	517	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479	
+P39962	UniProtKB	Lipidation	518	518	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479	
+P39962	UniProtKB	Lipidation	519	519	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479	
+P39962	UniProtKB	Lipidation	520	520	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479	
+P39962	UniProtKB	Lipidation	522	522	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479	
+P39962	UniProtKB	Lipidation	523	523	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479	
+P39962	UniProtKB	Lipidation	524	524	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479	
+P39962	UniProtKB	Mutagenesis	444	444	.	.	.	Note=Impaired vacuolar targeting. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14668479;Dbxref=PMID:14668479	
+P39962	UniProtKB	Mutagenesis	446	446	.	.	.	Note=Impaired vacuolar targeting. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14668479;Dbxref=PMID:14668479	
+P39962	UniProtKB	Mutagenesis	447	447	.	.	.	Note=Impaired vacuolar targeting. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14668479;Dbxref=PMID:14668479	
+##sequence-region P27466 1 446
+P27466	UniProtKB	Chain	1	446	.	.	.	ID=PRO_0000086090;Note=Calcium/calmodulin-dependent protein kinase I	
+P27466	UniProtKB	Domain	37	299	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P27466	UniProtKB	Nucleotide binding	43	51	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P27466	UniProtKB	Region	312	323	.	.	.	Note=Calmodulin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27466	UniProtKB	Active site	161	161	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P27466	UniProtKB	Binding site	66	66	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P27466	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22517	
+P27466	UniProtKB	Modified residue	357	357	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22517	
+P27466	UniProtKB	Modified residue	417	417	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P27466	UniProtKB	Modified residue	418	418	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27466	UniProtKB	Modified residue	420	420	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P27466	UniProtKB	Modified residue	429	429	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P27466	UniProtKB	Sequence conflict	53	54	.	.	.	Note=QA->VR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27466	UniProtKB	Sequence conflict	68	68	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27466	UniProtKB	Sequence conflict	188	188	.	.	.	Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27466	UniProtKB	Sequence conflict	199	202	.	.	.	Note=PAGS->AGTA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27466	UniProtKB	Sequence conflict	237	243	.	.	.	Note=SAFRAER->ATIDRK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P27466	UniProtKB	Sequence conflict	271	271	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P34167 1 436
+P34167	UniProtKB	Chain	1	436	.	.	.	ID=PRO_0000081618;Note=Eukaryotic translation initiation factor 4B	
+P34167	UniProtKB	Domain	101	183	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P34167	UniProtKB	Repeat	190	210	.	.	.	Note=1%3B approximate	
+P34167	UniProtKB	Repeat	211	232	.	.	.	Note=2	
+P34167	UniProtKB	Repeat	233	258	.	.	.	Note=3	
+P34167	UniProtKB	Repeat	259	284	.	.	.	Note=4	
+P34167	UniProtKB	Repeat	285	310	.	.	.	Note=5	
+P34167	UniProtKB	Repeat	311	340	.	.	.	Note=6	
+P34167	UniProtKB	Repeat	341	350	.	.	.	Note=7%3B truncated	
+P34167	UniProtKB	Region	190	350	.	.	.	Note=7 X approximate tandem repeats	
+P34167	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P34167	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P34167	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Retention of function. N->G%2CV%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8404866;Dbxref=PMID:8404866	
+P34167	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Loss of function. N->S%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8404866;Dbxref=PMID:8404866	
+P34167	UniProtKB	Mutagenesis	150	150	.	.	.	Note=Retention of function. A->S%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8404866;Dbxref=PMID:8404866	
+P34167	UniProtKB	Mutagenesis	150	150	.	.	.	Note=Loss of function. A->Y%2CF%2CN%2CL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8404866;Dbxref=PMID:8404866	
+##sequence-region P38431 1 405
+P38431	UniProtKB	Chain	1	405	.	.	.	ID=PRO_0000007791;Note=Eukaryotic translation initiation factor 5	
+P38431	UniProtKB	Domain	241	402	.	.	.	Note=W2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00695	
+P38431	UniProtKB	Nucleotide binding	27	34	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38431	UniProtKB	Compositional bias	152	156	.	.	.	Note=Poly-Lys	
+P38431	UniProtKB	Compositional bias	396	405	.	.	.	Note=Asp/Glu-rich (acidic)	
+P38431	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38431	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38431	UniProtKB	Modified residue	191	191	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38431	UniProtKB	Modified residue	228	228	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38431	UniProtKB	Modified residue	317	317	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38431	UniProtKB	Modified residue	397	397	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38431	UniProtKB	Alternative sequence	1	17	.	.	.	ID=VSP_018724;Note=In isoform Short. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38431	UniProtKB	Mutagenesis	343	364	.	.	.	Note=In TIF5-12A%3B Abolishes binding to SUI3 and NIP1. LPKILVQLYNNDIISEEEIMRF->APKAAVQAANNDAASAAEAARA	
+P38431	UniProtKB	Mutagenesis	388	398	.	.	.	Note=In TIF5-7A%3B Abolishes binding to SUI3 and NIP1. FITWLETAESD->AATAAETAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937	
+P38431	UniProtKB	Helix	244	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+P38431	UniProtKB	Helix	269	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+P38431	UniProtKB	Helix	287	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+P38431	UniProtKB	Helix	300	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+P38431	UniProtKB	Helix	308	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+P38431	UniProtKB	Helix	318	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+P38431	UniProtKB	Helix	337	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+P38431	UniProtKB	Helix	343	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+P38431	UniProtKB	Helix	358	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+P38431	UniProtKB	Beta strand	370	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+P38431	UniProtKB	Helix	375	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+P38431	UniProtKB	Helix	386	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL	
+##sequence-region P53897 1 168
+P53897	UniProtKB	Chain	1	168	.	.	.	ID=PRO_0000203416;Note=mRNA stability protein IGO1	
+P53897	UniProtKB	Compositional bias	155	160	.	.	.	Note=Poly-Ser	
+P53897	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53897	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:20471941;Dbxref=PMID:17330950,PMID:19779198,PMID:20471941	
+##sequence-region P50094 1 524
+P50094	UniProtKB	Chain	1	524	.	.	.	ID=PRO_0000093684;Note=Inosine-5'-monophosphate dehydrogenase 4	
+P50094	UniProtKB	Domain	122	183	.	.	.	Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Domain	185	241	.	.	.	Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Nucleotide binding	279	281	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Nucleotide binding	329	331	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Region	369	371	.	.	.	Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Region	392	393	.	.	.	Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Region	416	420	.	.	.	Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Active site	336	336	.	.	.	Note=Thioimidate intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Active site	438	438	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Metal binding	331	331	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Metal binding	333	333	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Metal binding	336	336	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Metal binding	509	509	.	.	.	Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Metal binding	510	510	.	.	.	Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Metal binding	511	511	.	.	.	Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Binding site	334	334	.	.	.	Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Binding site	450	450	.	.	.	Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P50094	UniProtKB	Modified residue	125	125	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q06704 1 911
+Q06704	UniProtKB	Chain	1	911	.	.	.	ID=PRO_0000240370;Note=Golgin IMH1	
+Q06704	UniProtKB	Domain	861	909	.	.	.	Note=GRIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00250	
+Q06704	UniProtKB	Coiled coil	101	280	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06704	UniProtKB	Coiled coil	312	735	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06704	UniProtKB	Coiled coil	766	814	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06704	UniProtKB	Modified residue	308	308	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06704	UniProtKB	Modified residue	660	660	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06704	UniProtKB	Modified residue	827	827	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+Q06704	UniProtKB	Modified residue	830	830	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06704	UniProtKB	Mutagenesis	870	870	.	.	.	Note=Impairs interaction with ARL1 and Golgi localization. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12620189;Dbxref=PMID:12620189	
+##sequence-region P47031 1 731
+P47031	UniProtKB	Chain	1	731	.	.	.	ID=PRO_0000203051;Note=Mitochondrial outer membrane protein IML2	
+P47031	UniProtKB	Transmembrane	297	317	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47031	UniProtKB	Transmembrane	339	359	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47031	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47031	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47031	UniProtKB	Modified residue	378	378	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36114	
+P47031	UniProtKB	Modified residue	380	380	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47031	UniProtKB	Modified residue	383	383	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47031	UniProtKB	Modified residue	392	392	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32351 1 346
+P32351	UniProtKB	Chain	1	346	.	.	.	ID=PRO_0000084187;Note=Sugar utilization regulatory protein IMP2	
+P32351	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32351	UniProtKB	Sequence conflict	181	181	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32351	UniProtKB	Sequence conflict	279	279	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32351	UniProtKB	Sequence conflict	282	282	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11986 1 533
+P11986	UniProtKB	Chain	1	533	.	.	.	ID=PRO_0000195185;Note=Inositol-3-phosphate synthase	
+P11986	UniProtKB	Modified residue	368	368	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P11986	UniProtKB	Sequence conflict	14	14	.	.	.	Note=V->RL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	14	14	.	.	.	Note=V->RL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	60	60	.	.	.	Note=L->FE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	60	60	.	.	.	Note=L->FE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	66	93	.	.	.	Note=LGIMLIGLGGNNGSTLVASVLANKHNVE->TRNYAHWVRWLQQWLTLWPRYWRISTMWS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	66	93	.	.	.	Note=LGIMLIGLGGNNGSTLVASVLANKHNVE->TRNYAHWVRWLQQWLTLWPRYWRISTMWS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	98	98	.	.	.	Note=E->AK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	98	98	.	.	.	Note=E->AK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	140	141	.	.	.	Note=ND->KH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	140	141	.	.	.	Note=ND->KH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	201	201	.	.	.	Note=N->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	201	201	.	.	.	Note=N->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	444	444	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	444	444	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	476	497	.	.	.	Note=NFYPVLTFLSYWLKAPLTRPGF->ELLSSFNLLELLVKSSINKNQDL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Sequence conflict	524	533	.	.	.	Note=NELRFEERLL->KRTKIRREIVVISFQRLSFSFSAYL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11986	UniProtKB	Beta strand	11	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	25	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	43	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	64	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Turn	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	76	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	109	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	114	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1H	
+P11986	UniProtKB	Beta strand	125	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	142	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	154	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	166	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	193	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JKI	
+P11986	UniProtKB	Helix	216	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	239	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Turn	255	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	261	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	277	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	292	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1H	
+P11986	UniProtKB	Helix	303	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	316	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	325	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	342	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	355	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	363	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	378	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Turn	385	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Turn	390	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	397	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	406	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	411	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	423	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	427	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	438	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	459	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	466	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1H	
+P11986	UniProtKB	Helix	482	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Beta strand	488	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	503	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+P11986	UniProtKB	Helix	528	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J	
+##sequence-region P13902 1 151
+P13902	UniProtKB	Chain	1	151	.	.	.	ID=PRO_0000127254;Note=Protein INO4	
+P13902	UniProtKB	Domain	45	97	.	.	.	Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981	
+##sequence-region P53115 1 1489
+P53115	UniProtKB	Chain	1	1489	.	.	.	ID=PRO_0000074329;Note=Putative DNA helicase INO80	
+P53115	UniProtKB	Domain	476	601	.	.	.	Note=DBINO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00746	
+P53115	UniProtKB	Domain	718	890	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53115	UniProtKB	Domain	1303	1467	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P53115	UniProtKB	Nucleotide binding	731	738	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53115	UniProtKB	Motif	841	844	.	.	.	Note=DEAQ box	
+P53115	UniProtKB	Compositional bias	188	193	.	.	.	Note=Poly-Ala	
+P53115	UniProtKB	Compositional bias	259	268	.	.	.	Note=Poly-Glu	
+P53115	UniProtKB	Compositional bias	300	306	.	.	.	Note=Poly-Ser	
+P53115	UniProtKB	Compositional bias	568	573	.	.	.	Note=Poly-Glu	
+P53115	UniProtKB	Compositional bias	675	682	.	.	.	Note=Poly-Glu	
+P53115	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53115	UniProtKB	Modified residue	115	115	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53115	UniProtKB	Modified residue	133	133	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53115	UniProtKB	Modified residue	610	610	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53115	UniProtKB	Mutagenesis	737	737	.	.	.	Note=Reduced ATPase activity of the INO80 complex. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10952318;Dbxref=PMID:10952318	
+##sequence-region Q08227 1 384
+Q08227	UniProtKB	Chain	1	384	.	.	.	ID=PRO_0000268682;Note=Phosphatidylinositol 4%2C5-bisphosphate 5-phosphatase INP54	
+##sequence-region P40015 1 477
+P40015	UniProtKB	Chain	1	477	.	.	.	ID=PRO_0000075695;Note=Inositol phosphosphingolipids phospholipase C	
+P40015	UniProtKB	Topological domain	1	398	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40015	UniProtKB	Transmembrane	399	417	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40015	UniProtKB	Topological domain	418	424	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40015	UniProtKB	Transmembrane	425	449	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40015	UniProtKB	Topological domain	450	477	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40015	UniProtKB	Active site	334	334	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40015	UniProtKB	Metal binding	100	100	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40015	UniProtKB	Site	233	233	.	.	.	Note=Important for substrate recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12479 1 156
+Q12479	UniProtKB	Chain	1	156	.	.	.	ID=PRO_0000299700;Note=Putative increased recombination centers protein 11	
+Q12479	UniProtKB	Transmembrane	20	42	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07843 1 230
+Q07843	UniProtKB	Chain	1	230	.	.	.	ID=PRO_0000247128;Note=Increased recombination centers protein 19	
+##sequence-region Q08416 1 157
+Q08416	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000237647;Note=Increased recombination centers protein 23	
+Q08416	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08416	UniProtKB	Transmembrane	7	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08416	UniProtKB	Topological domain	30	33	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08416	UniProtKB	Transmembrane	34	56	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08416	UniProtKB	Topological domain	57	157	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06683 1 689
+Q06683	UniProtKB	Chain	1	689	.	.	.	ID=PRO_0000253816;Note=Putative ATP-dependent helicase IRC3	
+Q06683	UniProtKB	Domain	46	211	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q06683	UniProtKB	Domain	265	438	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q06683	UniProtKB	Nucleotide binding	59	66	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q06683	UniProtKB	Motif	158	161	.	.	.	Note=DEAH box	
+##sequence-region Q07821 1 250
+Q07821	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000077034;Note=Iron-sulfur assembly protein 1	
+Q07821	UniProtKB	Metal binding	178	178	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8	
+Q07821	UniProtKB	Metal binding	242	242	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8	
+Q07821	UniProtKB	Metal binding	244	244	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8	
+##sequence-region P32645 1 267
+P32645	UniProtKB	Chain	1	267	.	.	.	ID=PRO_0000084242;Note=Meiosis-specific protein ISC10	
+##sequence-region P53193 1 184
+P53193	UniProtKB	Transit peptide	1	10	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171977;Dbxref=PMID:11171977	
+P53193	UniProtKB	Chain	11	184	.	.	.	ID=PRO_0000071163;Note=J-type co-chaperone JAC1%2C mitochondrial	
+P53193	UniProtKB	Domain	13	82	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P53193	UniProtKB	Region	71	184	.	.	.	Note=Interaction with ISU1	
+P53193	UniProtKB	Mutagenesis	32	32	.	.	.	Note=In JAC1-1%3B temperature sensitive%3B causes growth defect at high temperatures. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9813017;Dbxref=PMID:9813017	
+P53193	UniProtKB	Mutagenesis	48	50	.	.	.	Note=In JAC1-A3%3B temperature sensitive%3B causes growth defect at high temperatures. HPD->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171977;Dbxref=PMID:11171977	
+P53193	UniProtKB	Mutagenesis	104	117	.	.	.	Note=In JAC1(LKDDEQ)%3B impairs interaction with ISU1%2C but does not affect stimulation of SSQ1 ATPase activity. LLLKVLDIHDELSQ->ALLAVLAIHAALSA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16551614;Dbxref=PMID:16551614	
+P53193	UniProtKB	Helix	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3	
+P53193	UniProtKB	Turn	19	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3	
+P53193	UniProtKB	Helix	33	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3	
+P53193	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3	
+P53193	UniProtKB	Helix	62	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3	
+P53193	UniProtKB	Helix	72	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3	
+P53193	UniProtKB	Helix	91	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3	
+P53193	UniProtKB	Helix	102	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3	
+P53193	UniProtKB	Helix	121	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3	
+P53193	UniProtKB	Helix	151	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3	
+##sequence-region P47156 1 728
+P47156	UniProtKB	Chain	1	728	.	.	.	ID=PRO_0000203116;Note=Histone demethylase JHD2	
+P47156	UniProtKB	Domain	4	47	.	.	.	Note=JmjN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00537	
+P47156	UniProtKB	Domain	381	549	.	.	.	Note=JmjC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538	
+P47156	UniProtKB	Zinc finger	235	285	.	.	.	Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+P47156	UniProtKB	Metal binding	427	427	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47156	UniProtKB	Metal binding	430	430	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538	
+P47156	UniProtKB	Metal binding	517	517	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538	
+P47156	UniProtKB	Mutagenesis	427	427	.	.	.	Note=Abolishes enzymatic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17310255;Dbxref=PMID:17310255	
+##sequence-region O13555 1 125
+O13555	UniProtKB	Chain	1	125	.	.	.	ID=PRO_0000299775;Note=Uncharacterized protein JIP3	
+O13555	UniProtKB	Compositional bias	2	91	.	.	.	Note=Glu-rich	
+##sequence-region P07278 1 416
+P07278	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1339314,ECO:0000269|PubMed:3037314,ECO:0000269|PubMed:6243658;Dbxref=PMID:1339314,PMID:3037314,PMID:6243658	
+P07278	UniProtKB	Chain	2	416	.	.	.	ID=PRO_0000205418;Note=cAMP-dependent protein kinase regulatory subunit	
+P07278	UniProtKB	Nucleotide binding	184	301	.	.	.	Note=cAMP 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946	
+P07278	UniProtKB	Nucleotide binding	302	416	.	.	.	Note=cAMP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946	
+P07278	UniProtKB	Region	2	183	.	.	.	Note=Dimerization and phosphorylation	
+P07278	UniProtKB	Region	8	45	.	.	.	Note=Dimerization/docking domain (D/D)	
+P07278	UniProtKB	Motif	142	146	.	.	.	Note=Inhibitor sequence (IS)	
+P07278	UniProtKB	Binding site	249	249	.	.	.	Note=cAMP 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946	
+P07278	UniProtKB	Binding site	258	258	.	.	.	Note=cAMP 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946	
+P07278	UniProtKB	Binding site	368	368	.	.	.	Note=cAMP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946	
+P07278	UniProtKB	Binding site	377	377	.	.	.	Note=cAMP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946	
+P07278	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07278	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07278	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07278	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	83	83	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:20702584;Dbxref=PMID:19779198,PMID:20702584	
+P07278	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	130	130	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	145	145	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:20702584,ECO:0000269|PubMed:3037314;Dbxref=PMID:18407956,PMID:19779198,PMID:20702584,PMID:3037314	
+P07278	UniProtKB	Modified residue	147	147	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:20702584;Dbxref=PMID:19779198,PMID:20702584	
+P07278	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Confers increased sensitivity to rapamycin and enhanced accumulation of glycogen upon TORC1 inhibition. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584	
+P07278	UniProtKB	Sequence conflict	264	264	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07278	UniProtKB	Helix	173	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Turn	183	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Helix	190	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	201	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	220	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	229	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Helix	249	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	259	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	268	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Helix	275	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Turn	281	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Helix	288	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Helix	294	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Helix	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Helix	308	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	319	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	328	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	338	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	346	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Turn	352	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	355	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Helix	368	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	378	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Beta strand	387	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Helix	394	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Turn	402	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+P07278	UniProtKB	Helix	405	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1	
+##sequence-region P23292 1 546
+P23292	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P23292	UniProtKB	Chain	2	546	.	.	.	ID=PRO_0000192857;Note=Casein kinase I homolog 2	
+P23292	UniProtKB	Domain	76	360	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23292	UniProtKB	Nucleotide binding	82	90	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23292	UniProtKB	Active site	195	195	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P23292	UniProtKB	Binding site	105	105	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23292	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P23292	UniProtKB	Modified residue	455	455	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P23292	UniProtKB	Lipidation	545	545	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12370247,ECO:0000269|PubMed:15105419;Dbxref=PMID:12370247,PMID:15105419	
+P23292	UniProtKB	Lipidation	546	546	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12370247,ECO:0000269|PubMed:15105419;Dbxref=PMID:12370247,PMID:15105419	
+P23292	UniProtKB	Cross-link	465	465	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P23292	UniProtKB	Mutagenesis	545	545	.	.	.	Note=Impaired palmitoylation and plasma membrane localization. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15105419;Dbxref=PMID:15105419	
+P23292	UniProtKB	Mutagenesis	546	546	.	.	.	Note=Impaired palmitoylation and plasma membrane localization. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15105419;Dbxref=PMID:15105419	
+##sequence-region P19158 1 3079
+P19158	UniProtKB	Chain	1	3079	.	.	.	ID=PRO_0000056658;Note=Inhibitory regulator protein IRA2	
+P19158	UniProtKB	Domain	1701	1890	.	.	.	Note=Ras-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00167	
+P19158	UniProtKB	Compositional bias	399	409	.	.	.	Note=Poly-Ser	
+P19158	UniProtKB	Compositional bias	412	416	.	.	.	Note=Poly-Ser	
+P19158	UniProtKB	Compositional bias	520	528	.	.	.	Note=Poly-Ala	
+P19158	UniProtKB	Compositional bias	2469	2472	.	.	.	Note=Poly-Leu	
+P19158	UniProtKB	Modified residue	635	635	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19158	UniProtKB	Sequence conflict	2309	2309	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19158	UniProtKB	Sequence conflict	2317	2317	.	.	.	Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12056 1 156
+Q12056	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12056	UniProtKB	Chain	27	156	.	.	.	ID=PRO_0000019701;Note=Iron sulfur cluster assembly protein 2%2C mitochondrial	
+##sequence-region P47119 1 197
+P47119	UniProtKB	Chain	1	197	.	.	.	ID=PRO_0000178279;Note=Inosine triphosphate pyrophosphatase	
+P47119	UniProtKB	Region	10	15	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148	
+P47119	UniProtKB	Region	76	77	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148	
+P47119	UniProtKB	Region	151	154	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148	
+P47119	UniProtKB	Region	180	181	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148	
+P47119	UniProtKB	Metal binding	45	45	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148	
+P47119	UniProtKB	Metal binding	76	76	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148	
+P47119	UniProtKB	Binding site	58	58	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148	
+P47119	UniProtKB	Binding site	175	175	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148	
+##sequence-region P30605 1 584
+P30605	UniProtKB	Chain	1	584	.	.	.	ID=PRO_0000050455;Note=Myo-inositol transporter 1	
+P30605	UniProtKB	Topological domain	1	81	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	103	129	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	130	150	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	151	163	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	185	186	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	208	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	216	236	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	237	246	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	247	267	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	268	349	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	350	370	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	371	376	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	377	397	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	398	400	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	401	421	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	422	441	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	442	462	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	463	486	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	487	507	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	508	510	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Transmembrane	511	531	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Topological domain	532	584	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P30605	UniProtKB	Modified residue	26	26	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P30605	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P30605	UniProtKB	Modified residue	35	35	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P30605	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P30605	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P30605	UniProtKB	Glycosylation	371	371	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30605	UniProtKB	Cross-link	573	573	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P30605	UniProtKB	Sequence conflict	43	44	.	.	.	Note=TL->HI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07959 1 543
+Q07959	UniProtKB	Chain	1	543	.	.	.	ID=PRO_0000240375;Note=ADIPOR-like receptor IZH3	
+Q07959	UniProtKB	Topological domain	1	259	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Transmembrane	260	280	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Topological domain	281	295	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Transmembrane	296	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Topological domain	317	330	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Transmembrane	331	353	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Topological domain	354	357	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Transmembrane	358	378	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Topological domain	379	395	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Transmembrane	396	416	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Topological domain	417	425	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Transmembrane	426	446	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Topological domain	447	505	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Transmembrane	506	526	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Topological domain	527	543	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Compositional bias	125	150	.	.	.	Note=Ser-rich	
+Q07959	UniProtKB	Glycosylation	45	45	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Glycosylation	123	123	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Glycosylation	153	153	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Glycosylation	256	256	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07959	UniProtKB	Glycosylation	319	319	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40034 1 492
+P40034	UniProtKB	Chain	1	492	.	.	.	ID=PRO_0000202630;Note=JmjC domain-containing histone demethylation protein 1	
+P40034	UniProtKB	Domain	254	409	.	.	.	Note=JmjC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538	
+P40034	UniProtKB	Zinc finger	4	72	.	.	.	Note=PHD-type%3B atypical	
+P40034	UniProtKB	Metal binding	305	305	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40034	UniProtKB	Metal binding	307	307	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538	
+P40034	UniProtKB	Metal binding	377	377	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538	
+P40034	UniProtKB	Binding site	302	302	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40034	UniProtKB	Binding site	322	322	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40034	UniProtKB	Mutagenesis	305	305	.	.	.	Note=Abolishes histone demethylase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16362057;Dbxref=PMID:16362057	
+##sequence-region P53863 1 590
+P53863	UniProtKB	Chain	1	590	.	.	.	ID=PRO_0000071162;Note=J protein JJJ1	
+P53863	UniProtKB	Domain	3	72	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P53863	UniProtKB	Zinc finger	338	362	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P53863	UniProtKB	Zinc finger	549	573	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P53863	UniProtKB	Modified residue	393	393	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53863	UniProtKB	Modified residue	504	504	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P32767 1 1081
+P32767	UniProtKB	Chain	1	1081	.	.	.	ID=PRO_0000058276;Note=Importin beta-like protein KAP122	
+##sequence-region P22517 1 447
+P22517	UniProtKB	Chain	1	447	.	.	.	ID=PRO_0000086105;Note=Calcium/calmodulin-dependent protein kinase II	
+P22517	UniProtKB	Domain	47	309	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22517	UniProtKB	Nucleotide binding	53	61	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22517	UniProtKB	Region	323	334	.	.	.	Note=Calmodulin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22517	UniProtKB	Active site	171	171	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P22517	UniProtKB	Binding site	76	76	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22517	UniProtKB	Modified residue	316	316	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22517	UniProtKB	Modified residue	353	353	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22517	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22517	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P22517	UniProtKB	Modified residue	371	371	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P22517	UniProtKB	Modified residue	387	387	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22517	UniProtKB	Modified residue	443	443	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P22517	UniProtKB	Sequence conflict	282	282	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12494 1 1050
+Q12494	UniProtKB	Chain	1	1050	.	.	.	ID=PRO_0000255955;Note=Inositol hexakisphosphate kinase 1	
+Q12494	UniProtKB	Region	772	780	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12494	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12494	UniProtKB	Modified residue	396	396	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12494	UniProtKB	Modified residue	469	469	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12494	UniProtKB	Modified residue	537	537	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+Q12494	UniProtKB	Modified residue	539	539	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12494	UniProtKB	Modified residue	566	566	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q12494	UniProtKB	Modified residue	583	583	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12494	UniProtKB	Modified residue	589	589	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q12494	UniProtKB	Modified residue	646	646	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12494	UniProtKB	Modified residue	664	664	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12494	UniProtKB	Modified residue	670	670	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q08295 1 589
+Q08295	UniProtKB	Chain	1	589	.	.	.	ID=PRO_0000245259;Note=Oligo-1%2C6-glucosidase IMA2	
+Q08295	UniProtKB	Active site	215	215	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08295	UniProtKB	Active site	277	277	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08295	UniProtKB	Site	352	352	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P40884 1 581
+P40884	UniProtKB	Chain	1	581	.	.	.	ID=PRO_0000054331;Note=Oligo-1%2C6-glucosidase IMA5	
+P40884	UniProtKB	Active site	210	210	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40884	UniProtKB	Active site	272	272	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40884	UniProtKB	Site	347	347	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q06142 1 861
+Q06142	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06142	UniProtKB	Chain	2	861	.	.	.	ID=PRO_0000120764;Note=Importin subunit beta-1	
+Q06142	UniProtKB	Repeat	3	35	.	.	.	Note=HEAT 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Domain	25	106	.	.	.	Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115	
+Q06142	UniProtKB	Repeat	37	66	.	.	.	Note=HEAT 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	90	129	.	.	.	Note=HEAT 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	134	164	.	.	.	Note=HEAT 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	177	208	.	.	.	Note=HEAT 5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	219	255	.	.	.	Note=HEAT 6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	260	306	.	.	.	Note=HEAT 7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	317	362	.	.	.	Note=HEAT 8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	367	395	.	.	.	Note=HEAT 9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	402	442	.	.	.	Note=HEAT 10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	452	484	.	.	.	Note=HEAT 11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	496	530	.	.	.	Note=HEAT 12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	536	586	.	.	.	Note=HEAT 13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	592	629	.	.	.	Note=HEAT 14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	634	669	.	.	.	Note=HEAT 15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	675	713	.	.	.	Note=HEAT 16;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	718	764	.	.	.	Note=HEAT 17;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	773	812	.	.	.	Note=HEAT 18;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Repeat	819	859	.	.	.	Note=HEAT 19;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174	
+Q06142	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06142	UniProtKB	Modified residue	836	836	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06142	UniProtKB	Helix	3	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	19	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	37	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	55	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Turn	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	74	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	90	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	109	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	134	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	149	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Beta strand	166	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EA5	
+Q06142	UniProtKB	Helix	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	177	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	195	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	213	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	219	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	238	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	260	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	267	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	280	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	317	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	346	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	363	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	367	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	383	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Beta strand	397	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	402	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	419	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	425	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	443	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Turn	448	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	452	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	467	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Beta strand	485	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	491	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	496	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Beta strand	509	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ND2	
+Q06142	UniProtKB	Helix	513	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	516	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	533	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	536	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	558	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	563	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	588	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	592	594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	595	607	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Beta strand	608	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EA5	
+Q06142	UniProtKB	Helix	611	613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	615	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	630	633	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	634	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	654	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	671	674	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	675	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	698	713	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	714	717	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	718	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Beta strand	737	740	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	741	764	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Turn	765	767	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	769	772	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	773	775	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	776	788	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	790	793	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	796	812	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Beta strand	816	818	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKU	
+Q06142	UniProtKB	Helix	819	821	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	825	836	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Beta strand	838	840	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+Q06142	UniProtKB	Helix	842	859	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT	
+##sequence-region P32337 1 1089
+P32337	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32337	UniProtKB	Chain	2	1089	.	.	.	ID=PRO_0000120774;Note=Importin subunit beta-3	
+P32337	UniProtKB	Repeat	6	39	.	.	.	Note=HEAT 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	44	78	.	.	.	Note=HEAT 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	96	129	.	.	.	Note=HEAT 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	138	165	.	.	.	Note=HEAT 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	175	207	.	.	.	Note=HEAT 5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	216	252	.	.	.	Note=HEAT 6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	260	295	.	.	.	Note=HEAT 7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	304	359	.	.	.	Note=HEAT 8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	361	395	.	.	.	Note=HEAT 9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	399	439	.	.	.	Note=HEAT 10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	441	481	.	.	.	Note=HEAT 11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	484	524	.	.	.	Note=HEAT 12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	526	568	.	.	.	Note=HEAT 13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	571	613	.	.	.	Note=HEAT 14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	615	689	.	.	.	Note=HEAT 15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	692	735	.	.	.	Note=HEAT 16;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	742	781	.	.	.	Note=HEAT 17;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	788	849	.	.	.	Note=HEAT 18;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	852	890	.	.	.	Note=HEAT 19;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	898	930	.	.	.	Note=HEAT 20;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	938	978	.	.	.	Note=HEAT 21;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	986	1017	.	.	.	Note=HEAT 22;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	1028	1063	.	.	.	Note=HEAT 23;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Repeat	1066	1089	.	.	.	Note=HEAT 24;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588	
+P32337	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32337	UniProtKB	Modified residue	830	830	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32337	UniProtKB	Sequence conflict	65	65	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32337	UniProtKB	Sequence conflict	65	65	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32337	UniProtKB	Sequence conflict	1077	1077	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32337	UniProtKB	Sequence conflict	1077	1077	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32337	UniProtKB	Helix	6	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	25	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Beta strand	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZJ7	
+P32337	UniProtKB	Turn	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	44	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	61	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	96	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	116	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Beta strand	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H2V	
+P32337	UniProtKB	Helix	138	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	153	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	168	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	175	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	191	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	210	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	220	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	228	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	236	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	254	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	261	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	279	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	297	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	304	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	329	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	343	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	361	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	381	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Turn	395	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	399	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	406	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	414	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	422	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Turn	439	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	442	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	465	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	484	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	488	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	491	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	507	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	525	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	532	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	551	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	570	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Turn	574	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	577	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	597	613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	614	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	621	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Beta strand	638	641	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Beta strand	646	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	649	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Beta strand	655	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	669	689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	690	693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	694	703	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	705	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	715	734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	742	757	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Turn	758	760	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	764	781	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	788	809	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	829	849	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Turn	850	853	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	854	857	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	858	860	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	861	868	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Beta strand	870	872	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H2V	
+P32337	UniProtKB	Helix	873	887	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	891	893	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3U	
+P32337	UniProtKB	Helix	895	909	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	914	930	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Turn	933	935	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	936	949	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	958	960	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	961	977	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Turn	978	980	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	987	993	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	1002	1013	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Beta strand	1023	1027	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H2V	
+P32337	UniProtKB	Helix	1029	1041	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	1053	1062	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	1066	1071	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	1072	1075	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+P32337	UniProtKB	Helix	1078	1085	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W	
+##sequence-region P53067 1 1004
+P53067	UniProtKB	Chain	1	1004	.	.	.	ID=PRO_0000120778;Note=Importin subunit beta-5	
+P53067	UniProtKB	Domain	21	100	.	.	.	Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115	
+P53067	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P25642 1 146
+P25642	UniProtKB	Transit peptide	1	38	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25642	UniProtKB	Chain	39	146	.	.	.	ID=PRO_0000030537;Note=54S ribosomal protein IMG2%2C mitochondrial	
+P25642	UniProtKB	Sequence conflict	120	121	.	.	.	Note=SV->LW;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38265 1 245
+P38265	UniProtKB	Chain	1	245	.	.	.	ID=PRO_0000084182;Note=Central kinetochore subunit IML3	
+P38265	UniProtKB	Beta strand	3	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Helix	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IT3	
+P38265	UniProtKB	Helix	21	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	31	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	46	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	72	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	85	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Helix	95	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Helix	118	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	145	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Helix	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	160	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Helix	167	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Helix	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Helix	188	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Turn	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	205	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Turn	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	214	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Beta strand	221	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+P38265	UniProtKB	Helix	230	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3	
+##sequence-region P28627 1 190
+P28627	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132591;Dbxref=PMID:8132591	
+P28627	UniProtKB	Chain	2	190	.	.	.	ID=PRO_0000109537;Note=Mitochondrial inner membrane protease subunit 1	
+P28627	UniProtKB	Active site	40	40	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28627	UniProtKB	Active site	84	84	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P28627	UniProtKB	Mutagenesis	40	40	.	.	.	Note=Abolishes enzymatic activity. S->A%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835	
+P28627	UniProtKB	Mutagenesis	84	84	.	.	.	Note=Abolishes enzymatic activity. K->H%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835	
+P28627	UniProtKB	Mutagenesis	85	85	.	.	.	Note=Reduces enzymatic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835	
+P28627	UniProtKB	Mutagenesis	88	88	.	.	.	Note=In pet ts2858%3B temperature-sensitive%3B abolishes processing of CYB2 and presence of SOM1 in the IMP complex. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15118906,ECO:0000269|PubMed:1886606;Dbxref=PMID:15118906,PMID:1886606	
+P28627	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Abolishes processing of CYB2 and COX2 and presence of SOM1 in the IMP complex. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15118906;Dbxref=PMID:15118906	
+P28627	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Reduces enzymatic activity. D->E%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835	
+P28627	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Abolishes enzymatic activity. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835	
+P28627	UniProtKB	Mutagenesis	138	138	.	.	.	Note=Abolishes enzymatic activity. D->N%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835	
+P28627	UniProtKB	Sequence conflict	178	178	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P26798 1 304
+P26798	UniProtKB	Chain	1	304	.	.	.	ID=PRO_0000127253;Note=Protein INO2	
+P26798	UniProtKB	Domain	236	290	.	.	.	Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981	
+##sequence-region Q06098 1 443
+Q06098	UniProtKB	Chain	1	443	.	.	.	ID=PRO_0000086038;Note=Serine/threonine-protein kinase ISR1	
+Q06098	UniProtKB	Domain	135	415	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q06098	UniProtKB	Nucleotide binding	141	149	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q06098	UniProtKB	Active site	280	280	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q06098	UniProtKB	Binding site	169	169	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region Q04638 1 464
+Q04638	UniProtKB	Chain	1	464	.	.	.	ID=PRO_0000056340;Note=Translation termination inhibitor protein ITT1	
+Q04638	UniProtKB	Zinc finger	180	232	.	.	.	Note=RING-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q04638	UniProtKB	Zinc finger	272	338	.	.	.	Note=IBR-type	
+Q04638	UniProtKB	Zinc finger	402	431	.	.	.	Note=RING-type 2%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q04638	UniProtKB	Active site	415	415	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y4X5	
+##sequence-region Q06214 1 492
+Q06214	UniProtKB	Chain	1	492	.	.	.	ID=PRO_0000257817;Note=WD repeat-containing protein JIP5	
+Q06214	UniProtKB	Repeat	127	166	.	.	.	Note=WD 1	
+Q06214	UniProtKB	Repeat	178	217	.	.	.	Note=WD 2	
+Q06214	UniProtKB	Repeat	236	274	.	.	.	Note=WD 3	
+Q06214	UniProtKB	Repeat	276	317	.	.	.	Note=WD 4	
+Q06214	UniProtKB	Repeat	365	405	.	.	.	Note=WD 5	
+Q06214	UniProtKB	Compositional bias	449	488	.	.	.	Note=Lys-rich	
+##sequence-region P40206 1 208
+P40206	UniProtKB	Chain	1	208	.	.	.	ID=PRO_0000203301;Note=Protein JLP2	
+##sequence-region P47135 1 1091
+P47135	UniProtKB	Chain	1	1091	.	.	.	ID=PRO_0000075922;Note=Protein JSN1	
+P47135	UniProtKB	Domain	340	426	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P47135	UniProtKB	Domain	557	913	.	.	.	Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318	
+P47135	UniProtKB	Repeat	617	652	.	.	.	Note=Pumilio 1	
+P47135	UniProtKB	Repeat	653	689	.	.	.	Note=Pumilio 2	
+P47135	UniProtKB	Repeat	690	724	.	.	.	Note=Pumilio 3	
+P47135	UniProtKB	Repeat	725	760	.	.	.	Note=Pumilio 4	
+P47135	UniProtKB	Repeat	801	837	.	.	.	Note=Pumilio 5	
+P47135	UniProtKB	Compositional bias	507	510	.	.	.	Note=Poly-Asn	
+P47135	UniProtKB	Compositional bias	515	518	.	.	.	Note=Poly-Asn	
+P47135	UniProtKB	Compositional bias	923	927	.	.	.	Note=Poly-Gln	
+P47135	UniProtKB	Compositional bias	967	970	.	.	.	Note=Poly-Thr	
+P47135	UniProtKB	Compositional bias	1065	1076	.	.	.	Note=Poly-Asn	
+P47135	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47135	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47135	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47135	UniProtKB	Modified residue	168	168	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47135	UniProtKB	Modified residue	913	913	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q02932 1 1032
+Q02932	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q02932	UniProtKB	Chain	2	1032	.	.	.	ID=PRO_0000255954;Note=Importin beta-like protein KAP120	
+Q02932	UniProtKB	Domain	31	103	.	.	.	Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115	
+Q02932	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P36132 1 386
+P36132	UniProtKB	Chain	1	386	.	.	.	ID=PRO_0000096989;Note=tRNA N6-adenosine threonylcarbamoyltransferase	
+P36132	UniProtKB	Region	162	166	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180	
+P36132	UniProtKB	Metal binding	141	141	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180	
+P36132	UniProtKB	Metal binding	145	145	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180	
+P36132	UniProtKB	Metal binding	162	162	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180	
+P36132	UniProtKB	Metal binding	344	344	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180	
+P36132	UniProtKB	Binding site	194	194	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180	
+P36132	UniProtKB	Binding site	209	209	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180	
+P36132	UniProtKB	Binding site	213	213	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180	
+P36132	UniProtKB	Binding site	315	315	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180	
+##sequence-region P38697 1 523
+P38697	UniProtKB	Chain	1	523	.	.	.	ID=PRO_0000093682;Note=Inosine-5'-monophosphate dehydrogenase 2	
+P38697	UniProtKB	Domain	121	183	.	.	.	Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Domain	184	240	.	.	.	Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Nucleotide binding	278	280	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Nucleotide binding	328	330	.	.	.	Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Region	368	370	.	.	.	Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Region	391	392	.	.	.	Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Region	415	419	.	.	.	Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Active site	335	335	.	.	.	Note=Thioimidate intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Active site	437	437	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Metal binding	330	330	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Metal binding	332	332	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Metal binding	335	335	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Metal binding	508	508	.	.	.	Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Metal binding	509	509	.	.	.	Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Metal binding	510	510	.	.	.	Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Binding site	333	333	.	.	.	Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Binding site	449	449	.	.	.	Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156	
+P38697	UniProtKB	Mutagenesis	253	253	.	.	.	Note=Reduces drug-resistance to MPA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16278936;Dbxref=PMID:16278936	
+P38697	UniProtKB	Mutagenesis	335	335	.	.	.	Note=Inactivates the proteins ability to provide drug-resistance in vivo. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292516;Dbxref=PMID:15292516	
+##sequence-region P40576 1 216
+P40576	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40576	UniProtKB	Chain	27	216	.	.	.	ID=PRO_0000203007;Note=Inner membrane assembly complex subunit 22;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40576	UniProtKB	Topological domain	27	43	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24942160;Dbxref=PMID:24942160	
+P40576	UniProtKB	Transmembrane	44	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40576	UniProtKB	Topological domain	64	216	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24942160;Dbxref=PMID:24942160	
+P40576	UniProtKB	Coiled coil	64	93	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08118 1 586
+Q08118	UniProtKB	Chain	1	586	.	.	.	ID=PRO_0000245270;Note=Uncharacterized protein IRC10	
+##sequence-region Q6B0V8 1 119
+Q6B0V8	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000299816;Note=Putative increased recombination centers protein 16	
+Q6B0V8	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6B0V8	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43615 1 237
+P43615	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000202696;Note=Increased recombination centers protein 6	
+P43615	UniProtKB	Beta strand	9	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Helix	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Helix	19	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Beta strand	39	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Beta strand	51	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Helix	64	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Helix	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Helix	77	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Beta strand	83	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Helix	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Helix	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Helix	101	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Beta strand	113	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Helix	125	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Beta strand	138	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Beta strand	143	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+P43615	UniProtKB	Helix	165	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9	
+##sequence-region Q03020 1 165
+Q03020	UniProtKB	Transit peptide	1	27	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03020	UniProtKB	Chain	28	165	.	.	.	ID=PRO_0000019700;Note=Iron sulfur cluster assembly protein 1%2C mitochondrial	
+Q03020	UniProtKB	Mutagenesis	63	63	.	.	.	Note=In ISU1(LVF/SSS)%3B no growth and abolishes interaction with both JAC1 and NFS1%3B when associated with S-72 and S-94. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895	
+Q03020	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Fails to complement an isu1 deletion mutation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895	
+Q03020	UniProtKB	Mutagenesis	72	72	.	.	.	Note=In ISU1(LVF/SSS)%3B no growth and abolishes interaction with both JAC1 and NFS1%3B when associated with S-63 and S-94. V->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895	
+Q03020	UniProtKB	Mutagenesis	94	94	.	.	.	Note=In ISU1(LVF/SSS)%3B no growth and abolishes interaction with both JAC1 and NFS1%3B when associated with S-63 and S-72. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895	
+Q03020	UniProtKB	Mutagenesis	96	96	.	.	.	Note=Fails to complement an isu1 deletion mutation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895	
+Q03020	UniProtKB	Mutagenesis	132	132	.	.	.	Note=No growth. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15123690;Dbxref=PMID:15123690	
+Q03020	UniProtKB	Mutagenesis	133	133	.	.	.	Note=Wild-type growth. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15123690;Dbxref=PMID:15123690	
+Q03020	UniProtKB	Mutagenesis	134	136	.	.	.	Note=No growth%3B no interaction with frataxin and SSQ1. PVK->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15123690,ECO:0000269|PubMed:25228696;Dbxref=PMID:15123690,PMID:25228696	
+Q03020	UniProtKB	Mutagenesis	134	134	.	.	.	Note=Slow growth%3B no interaction with SSQ1. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15123690;Dbxref=PMID:15123690	
+Q03020	UniProtKB	Mutagenesis	135	135	.	.	.	Note=Wild-type growth%3B no interaction with SSQ1. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15123690;Dbxref=PMID:15123690	
+Q03020	UniProtKB	Mutagenesis	136	136	.	.	.	Note=No growth%3B no interaction with SSQ1. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15123690;Dbxref=PMID:15123690	
+Q03020	UniProtKB	Mutagenesis	139	139	.	.	.	Note=Fails to complement an isu1 deletion mutation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895	
+##sequence-region P38710 1 295
+P38710	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000142585;Note=Inositol monophosphatase 1	
+P38710	UniProtKB	Region	94	97	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38710	UniProtKB	Metal binding	73	73	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38710	UniProtKB	Metal binding	92	92	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38710	UniProtKB	Metal binding	92	92	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38710	UniProtKB	Metal binding	94	94	.	.	.	Note=Magnesium 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38710	UniProtKB	Metal binding	95	95	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38710	UniProtKB	Metal binding	231	231	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38710	UniProtKB	Binding site	73	73	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38710	UniProtKB	Binding site	231	231	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P40559 1 946
+P40559	UniProtKB	Chain	1	946	.	.	.	ID=PRO_0000209741;Note=Phosphatidylinositol 4%2C5-bisphosphate 5-phosphatase INP51	
+P40559	UniProtKB	Domain	151	480	.	.	.	Note=SAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00183	
+##sequence-region P01094 1 68
+P01094	UniProtKB	Chain	1	68	.	.	.	ID=PRO_0000195901;Note=Protease A inhibitor 3	
+P01094	UniProtKB	Region	1	32	.	.	.	Note=Inhibitory domain	
+P01094	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.1	
+P01094	UniProtKB	Helix	4	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ	
+##sequence-region P38803 1 334
+P38803	UniProtKB	Chain	1	334	.	.	.	ID=PRO_0000202904;Note=Pre-rRNA-processing protein IPI1	
+##sequence-region P53877 1 555
+P53877	UniProtKB	Chain	1	555	.	.	.	ID=PRO_0000051484;Note=Pre-rRNA-processing protein IPI3	
+P53877	UniProtKB	Repeat	90	133	.	.	.	Note=WD 1	
+P53877	UniProtKB	Repeat	137	176	.	.	.	Note=WD 2	
+P53877	UniProtKB	Repeat	187	234	.	.	.	Note=WD 3	
+P53877	UniProtKB	Repeat	342	383	.	.	.	Note=WD 4	
+P53877	UniProtKB	Modified residue	388	388	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P18963 1 3092
+P18963	UniProtKB	Chain	1	3092	.	.	.	ID=PRO_0000056657;Note=Inhibitory regulator protein IRA1	
+P18963	UniProtKB	Domain	1709	1898	.	.	.	Note=Ras-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00167	
+P18963	UniProtKB	Compositional bias	326	331	.	.	.	Note=Poly-Ser	
+P18963	UniProtKB	Compositional bias	379	383	.	.	.	Note=Poly-Ser	
+P18963	UniProtKB	Compositional bias	475	484	.	.	.	Note=Poly-Asn	
+P18963	UniProtKB	Compositional bias	1433	1437	.	.	.	Note=Poly-Ile	
+P18963	UniProtKB	Compositional bias	2039	2042	.	.	.	Note=Poly-Glu	
+P18963	UniProtKB	Modified residue	497	497	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P18963	UniProtKB	Modified residue	915	915	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P18963	UniProtKB	Modified residue	1342	1342	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P18963	UniProtKB	Modified residue	1753	1753	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18963	UniProtKB	Modified residue	3004	3004	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18963	UniProtKB	Sequence conflict	361	361	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08522 1 113
+Q08522	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000299715;Note=Putative increased recombination centers protein 14	
+##sequence-region P47056 1 224
+P47056	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47056	UniProtKB	Chain	27	224	.	.	.	ID=PRO_0000203069;Note=Outer spore wall protein 6	
+P47056	UniProtKB	Topological domain	27	174	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47055	
+P47056	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47056	UniProtKB	Topological domain	196	199	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47055	
+P47056	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47056	UniProtKB	Topological domain	221	224	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47055	
+P47056	UniProtKB	Glycosylation	74	74	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P47056	UniProtKB	Glycosylation	104	104	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+##sequence-region Q12425 1 185
+Q12425	UniProtKB	Chain	1	185	.	.	.	ID=PRO_0000077035;Note=Iron-sulfur assembly protein 2	
+Q12425	UniProtKB	Metal binding	89	89	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8	
+Q12425	UniProtKB	Metal binding	175	175	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8	
+Q12425	UniProtKB	Metal binding	177	177	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8	
+##sequence-region Q6Q560 1 94
+Q6Q560	UniProtKB	Chain	1	94	.	.	.	ID=PRO_0000245364;Note=Protein ISD11	
+##sequence-region P21374 1 235
+P21374	UniProtKB	Chain	1	235	.	.	.	ID=PRO_0000192976;Note=Pre-mRNA-splicing factor ISY1	
+P21374	UniProtKB	Helix	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P21374	UniProtKB	Helix	11	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P21374	UniProtKB	Beta strand	29	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P21374	UniProtKB	Helix	44	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P21374	UniProtKB	Helix	72	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P53125 1 1264
+P53125	UniProtKB	Chain	1	1264	.	.	.	ID=PRO_0000084270;Note=Imitation switch two complex protein 1	
+P53125	UniProtKB	Domain	23	130	.	.	.	Note=WAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00475	
+P53125	UniProtKB	Domain	423	483	.	.	.	Note=DDT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00063	
+##sequence-region Q06667 1 281
+Q06667	UniProtKB	Chain	1	281	.	.	.	ID=PRO_0000110528;Note=Inositol-pentakisphosphate 2-kinase	
+Q06667	UniProtKB	Motif	123	127	.	.	.	Note=EXKPK motif	
+##sequence-region P00817 1 287
+P00817	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:340461;Dbxref=PMID:340461	
+P00817	UniProtKB	Chain	2	287	.	.	.	ID=PRO_0000137588;Note=Inorganic pyrophosphatase	
+P00817	UniProtKB	Active site	90	90	.	.	.	Note=Proton donor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1322842;Dbxref=PMID:1322842	
+P00817	UniProtKB	Metal binding	116	116	.	.	.	Note=Magnesium 1	
+P00817	UniProtKB	Metal binding	121	121	.	.	.	Note=Magnesium 1	
+P00817	UniProtKB	Metal binding	121	121	.	.	.	Note=Magnesium 2	
+P00817	UniProtKB	Metal binding	153	153	.	.	.	Note=Magnesium 1	
+P00817	UniProtKB	Binding site	79	79	.	.	.	Note=Diphosphate	
+P00817	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00817	UniProtKB	Modified residue	251	251	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950	
+P00817	UniProtKB	Modified residue	266	266	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P00817	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P00817	UniProtKB	Cross-link	239	239	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00817	UniProtKB	Cross-link	279	279	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00817	UniProtKB	Sequence conflict	41	41	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00817	UniProtKB	Sequence conflict	72	72	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00817	UniProtKB	Sequence conflict	75	75	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00817	UniProtKB	Sequence conflict	124	124	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00817	UniProtKB	Sequence conflict	137	137	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00817	UniProtKB	Sequence conflict	187	187	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00817	UniProtKB	Sequence conflict	225	225	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00817	UniProtKB	Sequence conflict	267	267	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00817	UniProtKB	Beta strand	3	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPP	
+P00817	UniProtKB	Beta strand	17	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Turn	29	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Turn	39	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	43	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IK1	
+P00817	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYP	
+P00817	UniProtKB	Beta strand	91	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Turn	109	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IHP	
+P00817	UniProtKB	Beta strand	121	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M38	
+P00817	UniProtKB	Beta strand	135	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	155	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYP	
+P00817	UniProtKB	Helix	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Helix	172	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Helix	182	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Helix	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Helix	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6A	
+P00817	UniProtKB	Helix	213	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	245	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Helix	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Turn	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Beta strand	266	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+P00817	UniProtKB	Helix	275	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G	
+##sequence-region Q12280 1 1495
+Q12280	UniProtKB	Chain	1	1495	.	.	.	ID=PRO_0000056652;Note=Ras GTPase-activating-like protein IQG1	
+Q12280	UniProtKB	Domain	108	217	.	.	.	Note=Calponin-homology (CH);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044	
+Q12280	UniProtKB	Domain	447	467	.	.	.	Note=IQ 1	
+Q12280	UniProtKB	Domain	538	567	.	.	.	Note=IQ 2	
+Q12280	UniProtKB	Domain	568	597	.	.	.	Note=IQ 3	
+Q12280	UniProtKB	Domain	599	628	.	.	.	Note=IQ 4	
+Q12280	UniProtKB	Domain	629	658	.	.	.	Note=IQ 5	
+Q12280	UniProtKB	Domain	687	716	.	.	.	Note=IQ 6	
+Q12280	UniProtKB	Domain	717	746	.	.	.	Note=IQ 7	
+Q12280	UniProtKB	Domain	860	1071	.	.	.	Note=Ras-GAP	
+Q12280	UniProtKB	Coiled coil	759	798	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12280	UniProtKB	Compositional bias	37	76	.	.	.	Note=Ser-rich	
+Q12280	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12280	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12280	UniProtKB	Modified residue	299	299	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12280	UniProtKB	Mutagenesis	457	457	.	.	.	Note=In IQG1-1%3B causes a defect in cytokinesis at 37 degrees Celsius. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11082046;Dbxref=PMID:11082046	
+##sequence-region P40006 1 225
+P40006	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40006	UniProtKB	Chain	25	225	.	.	.	ID=PRO_0000014315;Note=Increased recombination centers protein 22	
+P40006	UniProtKB	Topological domain	25	169	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40006	UniProtKB	Transmembrane	170	190	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40006	UniProtKB	Topological domain	191	225	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32488 1 338
+P32488	UniProtKB	Chain	1	338	.	.	.	ID=PRO_0000096272;Note=Increasing suppression factor 1	
+P32488	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53843 1 298
+P53843	UniProtKB	Chain	1	298	.	.	.	ID=PRO_0000076227;Note=Vacuolar protein sorting-associated protein IST1	
+P53843	UniProtKB	Region	251	298	.	.	.	Note=Interaction with VPS4	
+P53843	UniProtKB	Motif	286	296	.	.	.	Note=MIT-interacting motif	
+P53843	UniProtKB	Compositional bias	190	196	.	.	.	Note=Poly-Ser	
+P53843	UniProtKB	Helix	8	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+P53843	UniProtKB	Helix	50	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+P53843	UniProtKB	Helix	84	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+P53843	UniProtKB	Helix	93	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+P53843	UniProtKB	Beta strand	100	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+P53843	UniProtKB	Helix	105	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+P53843	UniProtKB	Helix	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+P53843	UniProtKB	Helix	125	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+P53843	UniProtKB	Helix	138	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+P53843	UniProtKB	Helix	153	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+P53843	UniProtKB	Helix	166	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+P53843	UniProtKB	Helix	184	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY	
+##sequence-region Q07532 1 353
+Q07532	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q07532	UniProtKB	Chain	2	353	.	.	.	ID=PRO_0000255269;Note=RNA polymerase II nuclear localization protein IWR1	
+Q07532	UniProtKB	Motif	10	43	.	.	.	Note=Bipartite nuclear localization signal	
+Q07532	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P33417 1 597
+P33417	UniProtKB	Chain	1	597	.	.	.	ID=PRO_0000048573;Note=Intrastrand cross-link recognition protein	
+P33417	UniProtKB	DNA binding	361	429	.	.	.	Note=HMG box 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267	
+P33417	UniProtKB	DNA binding	434	502	.	.	.	Note=HMG box 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267	
+P33417	UniProtKB	Compositional bias	52	118	.	.	.	Note=Gln-rich	
+P33417	UniProtKB	Compositional bias	281	336	.	.	.	Note=Gln-rich	
+P33417	UniProtKB	Compositional bias	565	580	.	.	.	Note=Gln-rich	
+P33417	UniProtKB	Modified residue	532	532	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P33417	UniProtKB	Sequence conflict	73	73	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33417	UniProtKB	Sequence conflict	93	93	.	.	.	Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33417	UniProtKB	Sequence conflict	114	118	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33417	UniProtKB	Sequence conflict	207	207	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33417	UniProtKB	Sequence conflict	220	221	.	.	.	Note=AA->TT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12442 1 317
+Q12442	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000218834;Note=ADIPOR-like receptor IZH2	
+Q12442	UniProtKB	Topological domain	1	78	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Transmembrane	79	99	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Topological domain	100	110	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Topological domain	132	153	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Transmembrane	154	174	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Topological domain	175	176	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Topological domain	198	212	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Transmembrane	213	233	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Topological domain	234	242	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Topological domain	264	276	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Transmembrane	277	297	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12442	UniProtKB	Topological domain	298	317	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43596 1 787
+P43596	UniProtKB	Chain	1	787	.	.	.	ID=PRO_0000202685;Note=ISWI one complex protein 3	
+P43596	UniProtKB	Helix	144	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	179	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	192	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	198	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	205	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Beta strand	219	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Beta strand	224	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Beta strand	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	238	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	245	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	266	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	284	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	293	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	306	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	313	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Beta strand	326	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	369	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	373	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	380	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	385	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	404	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	432	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	437	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	454	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	462	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	470	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	473	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	483	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	491	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	500	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	506	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Beta strand	514	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	525	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	529	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Beta strand	539	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	544	546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Beta strand	547	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Beta strand	557	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	569	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	586	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	594	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Beta strand	604	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	608	617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Beta strand	627	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	634	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	645	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	694	696	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	697	726	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Beta strand	727	729	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Helix	735	739	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+P43596	UniProtKB	Turn	740	743	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y	
+##sequence-region P0CT04 1 75
+P0CT04	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:387783;Dbxref=PMID:387783	
+P0CT04	UniProtKB	Chain	2	75	.	.	.	ID=PRO_0000212790;Note=Protease B inhibitor 2	
+P0CT04	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P0CT04	UniProtKB	Sequence conflict	33	33	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43610 1 853
+P43610	UniProtKB	Chain	1	853	.	.	.	ID=PRO_0000074385;Note=Uncharacterized ATP-dependent helicase IRC5	
+P43610	UniProtKB	Domain	234	401	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P43610	UniProtKB	Domain	607	758	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P43610	UniProtKB	Nucleotide binding	247	254	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P43610	UniProtKB	Coiled coil	548	580	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43610	UniProtKB	Motif	352	355	.	.	.	Note=DEGH box	
+P43610	UniProtKB	Compositional bias	41	91	.	.	.	Note=Asp-rich	
+##sequence-region P36115 1 615
+P36115	UniProtKB	Chain	1	615	.	.	.	ID=PRO_0000203199;Note=Increased rDNA silencing protein 4	
+P36115	UniProtKB	Domain	460	571	.	.	.	Note=EH	
+P36115	UniProtKB	Compositional bias	122	282	.	.	.	Note=Ser-rich	
+P36115	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q99312 1 450
+Q99312	UniProtKB	Chain	1	450	.	.	.	ID=PRO_0000084257;Note=IMP-specific 5'-nucleotidase 1	
+##sequence-region Q12358 1 412
+Q12358	UniProtKB	Chain	1	412	.	.	.	ID=PRO_0000194022;Note=Alpha-ketoglutarate-dependent sulfonate dioxygenase	
+Q12358	UniProtKB	Metal binding	218	218	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12358	UniProtKB	Metal binding	220	220	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12358	UniProtKB	Metal binding	367	367	.	.	.	Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12358	UniProtKB	Binding site	245	245	.	.	.	Note=2-oxoglutarate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12358	UniProtKB	Binding site	352	352	.	.	.	Note=2-oxoglutarate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12358	UniProtKB	Binding site	379	379	.	.	.	Note=2-oxoglutarate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12358	UniProtKB	Binding site	383	383	.	.	.	Note=2-oxoglutarate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12358	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P05986 1 398
+P05986	UniProtKB	Chain	1	398	.	.	.	ID=PRO_0000086071;Note=cAMP-dependent protein kinase type 3	
+P05986	UniProtKB	Domain	88	342	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P05986	UniProtKB	Domain	343	398	.	.	.	Note=AGC-kinase C-terminal	
+P05986	UniProtKB	Nucleotide binding	94	102	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P05986	UniProtKB	Active site	211	211	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P05986	UniProtKB	Binding site	117	117	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P05986	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P05986	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P05986	UniProtKB	Sequence conflict	4	4	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05986	UniProtKB	Sequence conflict	208	208	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11927 1 433
+P11927	UniProtKB	Chain	1	433	.	.	.	ID=PRO_0000084295;Note=Cell division control protein KAR1	
+P11927	UniProtKB	Modified residue	233	233	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P11927	UniProtKB	Sequence conflict	95	95	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11927	UniProtKB	Sequence conflict	199	199	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11927	UniProtKB	Helix	240	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OQP	
+##sequence-region P17119 1 729
+P17119	UniProtKB	Chain	1	729	.	.	.	ID=PRO_0000125391;Note=Kinesin-like protein KAR3	
+P17119	UniProtKB	Domain	386	723	.	.	.	Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P17119	UniProtKB	Nucleotide binding	474	481	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P17119	UniProtKB	Region	1	109	.	.	.	Note=Globular	
+P17119	UniProtKB	Coiled coil	110	357	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17119	UniProtKB	Natural variant	378	378	.	.	.	Note=In KAR3-894. N->K	
+P17119	UniProtKB	Natural variant	462	462	.	.	.	Note=In KAR3-891. S->L	
+P17119	UniProtKB	Natural variant	521	521	.	.	.	Note=In KAR3-893. E->D	
+P17119	UniProtKB	Natural variant	550	550	.	.	.	Note=In KAR3-899. R->S	
+P17119	UniProtKB	Natural variant	558	558	.	.	.	Note=In KAR3-8912. T->A	
+P17119	UniProtKB	Natural variant	650	650	.	.	.	Note=In KAR3-898. N->K	
+P17119	UniProtKB	Natural variant	659	659	.	.	.	Note=In KAR3-897. V->L	
+P17119	UniProtKB	Mutagenesis	479	479	.	.	.	Note=Poisons nuclear fusion. G->E	
+P17119	UniProtKB	Helix	348	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ETP	
+P17119	UniProtKB	Beta strand	386	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Turn	398	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Beta strand	406	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Turn	415	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Beta strand	419	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Beta strand	433	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	448	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	460	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Beta strand	468	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	480	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Turn	487	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	491	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	507	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Beta strand	512	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Beta strand	526	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Beta strand	549	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Turn	553	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Beta strand	557	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Beta strand	566	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KAR	
+P17119	UniProtKB	Helix	571	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	574	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	596	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Beta strand	599	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Turn	612	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9U	
+P17119	UniProtKB	Beta strand	617	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	635	637	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	640	663	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Turn	668	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ETP	
+P17119	UniProtKB	Helix	675	677	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	679	688	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Beta strand	693	700	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	704	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Helix	707	720	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+P17119	UniProtKB	Turn	723	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V	
+##sequence-region P32526 1 644
+P32526	UniProtKB	Chain	1	644	.	.	.	ID=PRO_0000084296;Note=Karyogamy protein KAR9	
+P32526	UniProtKB	Modified residue	496	496	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32526	UniProtKB	Sequence conflict	641	641	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P23291 1 538
+P23291	UniProtKB	Chain	1	538	.	.	.	ID=PRO_0000192856;Note=Casein kinase I homolog 1	
+P23291	UniProtKB	Domain	69	353	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23291	UniProtKB	Nucleotide binding	75	83	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23291	UniProtKB	Active site	188	188	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P23291	UniProtKB	Binding site	98	98	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23291	UniProtKB	Modified residue	522	522	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P23291	UniProtKB	Modified residue	523	523	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P23291	UniProtKB	Modified residue	527	527	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P23291	UniProtKB	Lipidation	537	537	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23291	UniProtKB	Lipidation	538	538	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23291	UniProtKB	Sequence conflict	201	201	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23291	UniProtKB	Sequence conflict	367	367	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P15700 1 204
+P15700	UniProtKB	Chain	1	204	.	.	.	ID=PRO_0000158947;Note=Uridylate kinase	
+P15700	UniProtKB	Nucleotide binding	26	31	.	.	.	Note=ATP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116	
+P15700	UniProtKB	Nucleotide binding	74	76	.	.	.	Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116	
+P15700	UniProtKB	Nucleotide binding	104	107	.	.	.	Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116	
+P15700	UniProtKB	Region	46	76	.	.	.	Note=NMPbind;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116	
+P15700	UniProtKB	Region	141	151	.	.	.	Note=LID;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116	
+P15700	UniProtKB	Binding site	52	52	.	.	.	Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116	
+P15700	UniProtKB	Binding site	111	111	.	.	.	Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116	
+P15700	UniProtKB	Binding site	142	142	.	.	.	Note=ATP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116	
+P15700	UniProtKB	Binding site	148	148	.	.	.	Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116	
+P15700	UniProtKB	Binding site	159	159	.	.	.	Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116	
+P15700	UniProtKB	Binding site	187	187	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116	
+P15700	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Abolishes catalytic activity. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1655742;Dbxref=PMID:1655742	
+P15700	UniProtKB	Turn	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Beta strand	17	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Helix	29	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Beta strand	43	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Helix	47	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Helix	63	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Helix	78	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Beta strand	99	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Helix	109	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Beta strand	123	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Helix	132	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Helix	153	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Helix	168	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Turn	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Beta strand	180	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+P15700	UniProtKB	Helix	189	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ	
+##sequence-region P43614 1 200
+P43614	UniProtKB	Chain	1	200	.	.	.	ID=PRO_0000202695;Note=Beta-1%2C6-glucan synthesis-associated protein KEG1	
+P43614	UniProtKB	Topological domain	1	15	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43614	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43614	UniProtKB	Topological domain	37	44	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43614	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43614	UniProtKB	Topological domain	66	82	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43614	UniProtKB	Transmembrane	83	103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43614	UniProtKB	Topological domain	104	145	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43614	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43614	UniProtKB	Topological domain	167	173	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43614	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43614	UniProtKB	Topological domain	195	200	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43614	UniProtKB	Natural variant	3	3	.	.	.	Note=In strain: KA31a. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17893149;Dbxref=PMID:17893149	
+P43614	UniProtKB	Natural variant	55	55	.	.	.	Note=In strain: KA31a. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17893149;Dbxref=PMID:17893149	
+P43614	UniProtKB	Natural variant	84	84	.	.	.	Note=In strain: KA31a. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17893149;Dbxref=PMID:17893149	
+P43614	UniProtKB	Mutagenesis	124	124	.	.	.	Note=In KEG1-1%3B temperature-sensitive. Increased sensitivity to chitin-binding dye Calcofluor white and zymolyase. Shows K1 killer toxin resistance%2C and reduced content of the cell wall beta-1%2C6-glucan. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17893149;Dbxref=PMID:17893149	
+##sequence-region P35844 1 434
+P35844	UniProtKB	Chain	1	434	.	.	.	ID=PRO_0000100386;Note=Oxysterol-binding protein homolog 4	
+P35844	UniProtKB	Region	24	29	.	.	.	Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133	
+P35844	UniProtKB	Region	109	112	.	.	.	Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133	
+P35844	UniProtKB	Region	143	144	.	.	.	Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133	
+P35844	UniProtKB	Binding site	96	96	.	.	.	Note=Sterol;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1ZHT,ECO:0000244|PDB:1ZHW,ECO:0000244|PDB:1ZHX,ECO:0000244|PDB:1ZHY,ECO:0000244|PDB:1ZHZ,ECO:0000244|PDB:4FES,ECO:0000269|PubMed:16136145,ECO:0000269|PubMed:23756172;Dbxref=PMID:16136145,PMID:23756172	
+P35844	UniProtKB	Binding site	336	336	.	.	.	Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133	
+P35844	UniProtKB	Binding site	340	340	.	.	.	Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133	
+P35844	UniProtKB	Binding site	344	344	.	.	.	Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133	
+P35844	UniProtKB	Modified residue	370	370	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35844	UniProtKB	Modified residue	389	389	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P35844	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Abolishes both cholesterol binding and biological function. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16136145;Dbxref=PMID:16136145	
+P35844	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Strong reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16136145,ECO:0000269|PubMed:22162133;Dbxref=PMID:16136145,PMID:22162133	
+P35844	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Abolishes both cholesterol binding and biological function. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16136145;Dbxref=PMID:16136145	
+P35844	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Abolishes binding to phosphatidylinositol 4-phosphate. N->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133	
+P35844	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Abolishes both cholesterol binding and biological function. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16136145;Dbxref=PMID:16136145	
+P35844	UniProtKB	Mutagenesis	143	144	.	.	.	Note=Reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. HH->AA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16136145,ECO:0000269|PubMed:22162133,ECO:0000269|PubMed:26206936;Dbxref=PMID:16136145,PMID:22162133,PMID:26206936	
+P35844	UniProtKB	Mutagenesis	168	168	.	.	.	Note=Slight reduction in cholesterol transport. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16136145;Dbxref=PMID:16136145	
+P35844	UniProtKB	Mutagenesis	168	168	.	.	.	Note=Strong reduction in cholesterol transport. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16136145;Dbxref=PMID:16136145	
+P35844	UniProtKB	Mutagenesis	202	204	.	.	.	Note=Strong reduction in cholesterol binding without affecting phosphatidylinositol 4-phosphate binding. HIE->AIA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133	
+P35844	UniProtKB	Mutagenesis	336	336	.	.	.	Note=Strong reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16136145,ECO:0000269|PubMed:22162133;Dbxref=PMID:16136145,PMID:22162133	
+P35844	UniProtKB	Mutagenesis	340	340	.	.	.	Note=Abolishes binding to phosphatidylinositol 4-phosphate. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133	
+P35844	UniProtKB	Mutagenesis	344	344	.	.	.	Note=Slight reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16136145,ECO:0000269|PubMed:22162133;Dbxref=PMID:16136145,PMID:22162133	
+P35844	UniProtKB	Sequence conflict	355	355	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35844	UniProtKB	Turn	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	8	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Turn	16	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	34	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	39	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZI7	
+P35844	UniProtKB	Helix	50	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	55	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Turn	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	77	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	118	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Turn	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	134	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Turn	143	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	147	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Turn	155	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	159	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZI7	
+P35844	UniProtKB	Beta strand	177	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	185	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	192	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	201	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Turn	206	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	212	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	217	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	228	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	236	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	241	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	264	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	273	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	287	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Turn	292	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	313	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	318	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	329	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	357	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZI7	
+P35844	UniProtKB	Beta strand	360	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	368	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	383	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	396	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	407	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Beta strand	417	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+P35844	UniProtKB	Helix	423	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX	
+##sequence-region P13134 1 814
+P13134	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13134	UniProtKB	Propeptide	20	109	.	.	.	ID=PRO_0000027043	
+P13134	UniProtKB	Propeptide	110	113	.	.	.	ID=PRO_0000027044;Note=Removed by dipeptidylpeptidase STE13	
+P13134	UniProtKB	Chain	114	814	.	.	.	ID=PRO_0000027045;Note=Kexin	
+P13134	UniProtKB	Topological domain	114	678	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13134	UniProtKB	Transmembrane	679	699	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13134	UniProtKB	Topological domain	700	814	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13134	UniProtKB	Domain	171	453	.	.	.	Note=Peptidase S8	
+P13134	UniProtKB	Domain	462	596	.	.	.	Note=P/Homo B;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01173	
+P13134	UniProtKB	Compositional bias	625	642	.	.	.	Note=Ser/Thr-rich	
+P13134	UniProtKB	Active site	175	175	.	.	.	Note=Charge relay system	
+P13134	UniProtKB	Active site	213	213	.	.	.	Note=Charge relay system	
+P13134	UniProtKB	Active site	385	385	.	.	.	Note=Charge relay system	
+P13134	UniProtKB	Metal binding	135	135	.	.	.	Note=Calcium 1	
+P13134	UniProtKB	Metal binding	184	184	.	.	.	Note=Calcium 1	
+P13134	UniProtKB	Metal binding	227	227	.	.	.	Note=Calcium 1	
+P13134	UniProtKB	Metal binding	277	277	.	.	.	Note=Calcium 2	
+P13134	UniProtKB	Metal binding	320	320	.	.	.	Note=Calcium 2	
+P13134	UniProtKB	Metal binding	350	350	.	.	.	Note=Calcium 2	
+P13134	UniProtKB	Glycosylation	42	42	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13134	UniProtKB	Glycosylation	163	163	.	.	.	Note=N-linked (GlcNAc...) asparagine	
+P13134	UniProtKB	Glycosylation	404	404	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13134	UniProtKB	Glycosylation	480	480	.	.	.	Note=N-linked (GlcNAc...) asparagine	
+P13134	UniProtKB	Disulfide bond	230	377	.	.	.	.	
+P13134	UniProtKB	Disulfide bond	322	352	.	.	.	.	
+P13134	UniProtKB	Helix	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Turn	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	157	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	170	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Turn	183	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	191	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Turn	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Turn	209	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	213	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	225	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Turn	234	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	238	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R64	
+P13134	UniProtKB	Helix	252	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Turn	259	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	267	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	278	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	287	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	307	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	316	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Turn	326	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	333	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	355	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	368	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	377	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	384	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	407	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	425	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	433	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Turn	440	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	449	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	465	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	477	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	486	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	494	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	502	518	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	519	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	522	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	533	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	549	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Turn	558	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	566	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Beta strand	581	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+P13134	UniProtKB	Helix	597	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4	
+##sequence-region P38692 1 1080
+P38692	UniProtKB	Chain	1	1080	.	.	.	ID=PRO_0000086127;Note=Serine/threonine-protein kinase KIC1	
+P38692	UniProtKB	Domain	23	276	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38692	UniProtKB	Nucleotide binding	29	37	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38692	UniProtKB	Active site	144	144	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P38692	UniProtKB	Binding site	52	52	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38692	UniProtKB	Modified residue	735	735	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38991 1 367
+P38991	UniProtKB	Chain	1	367	.	.	.	ID=PRO_0000086029;Note=Spindle assembly checkpoint kinase	
+P38991	UniProtKB	Domain	104	355	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38991	UniProtKB	Nucleotide binding	110	118	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38991	UniProtKB	Active site	227	227	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P38991	UniProtKB	Binding site	133	133	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38991	UniProtKB	Modified residue	5	5	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861	
+P38991	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861	
+P38991	UniProtKB	Modified residue	260	260	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861	
+P38991	UniProtKB	Mutagenesis	260	260	.	.	.	Note=In IPL1-4%3B causes missegregation of chromosomes at 37 degrees Celsius. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8007975;Dbxref=PMID:8007975	
+P38991	UniProtKB	Mutagenesis	340	340	.	.	.	Note=In IPL1-1%3B causes missegregation of chromosomes at 37 degrees Celsius. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8007975;Dbxref=PMID:8007975	
+P38991	UniProtKB	Mutagenesis	352	352	.	.	.	Note=In IPL1-2%3B causes missegregation of chromosomes at 37 degrees Celsius. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8007975;Dbxref=PMID:8007975	
+##sequence-region P38250 1 946
+P38250	UniProtKB	Chain	1	946	.	.	.	ID=PRO_0000084261;Note=Increased sodium tolerance protein 2	
+P38250	UniProtKB	Topological domain	1	121	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Topological domain	143	153	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Transmembrane	154	174	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Topological domain	175	217	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Transmembrane	218	238	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Topological domain	239	253	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Transmembrane	254	274	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Topological domain	275	302	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Transmembrane	303	323	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Topological domain	324	447	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Transmembrane	448	468	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Topological domain	469	505	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Transmembrane	506	526	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Topological domain	527	563	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Transmembrane	564	584	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Topological domain	585	946	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38250	UniProtKB	Modified residue	638	638	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38250	UniProtKB	Modified residue	701	701	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38250	UniProtKB	Modified residue	704	704	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38250	UniProtKB	Modified residue	720	720	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38250	UniProtKB	Modified residue	726	726	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38250	UniProtKB	Modified residue	729	729	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38250	UniProtKB	Modified residue	730	730	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38250	UniProtKB	Modified residue	757	757	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956	
+P38250	UniProtKB	Modified residue	793	793	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38250	UniProtKB	Modified residue	844	844	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38250	UniProtKB	Modified residue	847	847	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38250	UniProtKB	Modified residue	850	850	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38250	UniProtKB	Sequence conflict	243	243	.	.	.	Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38250	UniProtKB	Sequence conflict	243	243	.	.	.	Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38250	UniProtKB	Sequence conflict	243	243	.	.	.	Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25389 1 1037
+P25389	UniProtKB	Chain	1	1037	.	.	.	ID=PRO_0000086109;Note=Probable serine/threonine-protein kinase KCC4	
+P25389	UniProtKB	Domain	21	285	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P25389	UniProtKB	Nucleotide binding	27	35	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P25389	UniProtKB	Compositional bias	388	499	.	.	.	Note=Ser-rich	
+P25389	UniProtKB	Active site	152	152	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P25389	UniProtKB	Binding site	50	50	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P25389	UniProtKB	Modified residue	396	396	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25389	UniProtKB	Modified residue	675	675	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25389	UniProtKB	Modified residue	707	707	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25389	UniProtKB	Modified residue	777	777	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25389	UniProtKB	Modified residue	822	822	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25389	UniProtKB	Modified residue	825	825	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25389	UniProtKB	Modified residue	871	871	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25389	UniProtKB	Helix	921	924	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Helix	925	927	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Beta strand	930	933	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Beta strand	938	942	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Helix	944	956	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Helix	959	961	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Beta strand	963	969	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Turn	970	973	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Beta strand	974	979	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Beta strand	984	986	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Beta strand	990	998	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Beta strand	1004	1013	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+P25389	UniProtKB	Helix	1015	1031	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST	
+##sequence-region P17423 1 357
+P17423	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2165904;Dbxref=PMID:2165904	
+P17423	UniProtKB	Chain	2	357	.	.	.	ID=PRO_0000156656;Note=Homoserine kinase	
+P17423	UniProtKB	Nucleotide binding	104	114	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17423	UniProtKB	Cross-link	133	133	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P17423	UniProtKB	Sequence conflict	87	87	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07277 1 443
+P07277	UniProtKB	Chain	1	443	.	.	.	ID=PRO_0000156662;Note=Mevalonate kinase	
+P07277	UniProtKB	Nucleotide binding	141	151	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07277	UniProtKB	Active site	202	202	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07277	UniProtKB	Binding site	138	138	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P13185 1 1064
+P13185	UniProtKB	Chain	1	1064	.	.	.	ID=PRO_0000086131;Note=Serine/threonine protein kinase KIN1	
+P13185	UniProtKB	Domain	120	398	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P13185	UniProtKB	Domain	1015	1064	.	.	.	Note=KA1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00565	
+P13185	UniProtKB	Nucleotide binding	126	134	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P13185	UniProtKB	Active site	269	269	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P13185	UniProtKB	Binding site	149	149	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P13185	UniProtKB	Modified residue	534	534	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P13185	UniProtKB	Modified residue	593	593	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P13185	UniProtKB	Modified residue	646	646	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P13185	UniProtKB	Modified residue	764	764	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P13185	UniProtKB	Modified residue	986	986	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P13185	UniProtKB	Sequence conflict	25	25	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13185	UniProtKB	Sequence conflict	453	453	.	.	.	Note=T->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13185	UniProtKB	Sequence conflict	455	455	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13185	UniProtKB	Sequence conflict	718	718	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13185	UniProtKB	Sequence conflict	920	921	.	.	.	Note=NI->IN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13185	UniProtKB	Sequence conflict	976	976	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13185	UniProtKB	Sequence conflict	979	980	.	.	.	Note=SI->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13185	UniProtKB	Sequence conflict	984	985	.	.	.	Note=KT->NS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P06242 1 306
+P06242	UniProtKB	Chain	1	306	.	.	.	ID=PRO_0000086132;Note=Serine/threonine-protein kinase KIN28	
+P06242	UniProtKB	Domain	7	290	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06242	UniProtKB	Nucleotide binding	13	21	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06242	UniProtKB	Active site	129	129	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P06242	UniProtKB	Binding site	36	36	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06242	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphothreonine%3B by CAK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10373527,ECO:0000269|PubMed:11839796,ECO:0000269|PubMed:9774652;Dbxref=PMID:10373527,PMID:11839796,PMID:9774652	
+P06242	UniProtKB	Mutagenesis	17	18	.	.	.	Note=No effect on phosphorylation%3B no effect on kinase activity. TY->AF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373527;Dbxref=PMID:10373527	
+P06242	UniProtKB	Mutagenesis	17	17	.	.	.	Note=Slow growth. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839796;Dbxref=PMID:11839796	
+P06242	UniProtKB	Mutagenesis	17	17	.	.	.	Note=Normal growth. T->E%2CQ%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839796;Dbxref=PMID:11839796	
+P06242	UniProtKB	Mutagenesis	36	36	.	.	.	Note=Slow growth. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839796;Dbxref=PMID:11839796	
+P06242	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Non-viable. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839796;Dbxref=PMID:11839796	
+P06242	UniProtKB	Mutagenesis	147	147	.	.	.	Note=Abolishes kinase activity. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10373527,ECO:0000269|PubMed:11839796;Dbxref=PMID:10373527,PMID:11839796	
+P06242	UniProtKB	Mutagenesis	162	162	.	.	.	Note=Diminishes phosphorylation%3B 75-80%25 loss in kinase activity%3B no effect on survival. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10373527,ECO:0000269|PubMed:11839796,ECO:0000269|PubMed:9774652;Dbxref=PMID:10373527,PMID:11839796,PMID:9774652	
+P06242	UniProtKB	Mutagenesis	162	162	.	.	.	Note=No effect on kinase activity. T->S%2CD%2CE;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10373527,ECO:0000269|PubMed:11839796,ECO:0000269|PubMed:9774652;Dbxref=PMID:10373527,PMID:11839796,PMID:9774652	
+P06242	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Normal growth. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839796;Dbxref=PMID:11839796	
+##sequence-region P24583 1 1151
+P24583	UniProtKB	Chain	1	1151	.	.	.	ID=PRO_0000055738;Note=Protein kinase C-like 1	
+P24583	UniProtKB	Repeat	5	77	.	.	.	Note=REM 1	
+P24583	UniProtKB	Repeat	118	193	.	.	.	Note=REM 2	
+P24583	UniProtKB	Domain	196	288	.	.	.	Note=C2	
+P24583	UniProtKB	Domain	824	1083	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P24583	UniProtKB	Domain	1084	1151	.	.	.	Note=AGC-kinase C-terminal	
+P24583	UniProtKB	Zinc finger	414	461	.	.	.	Note=Phorbol-ester/DAG-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226	
+P24583	UniProtKB	Zinc finger	481	531	.	.	.	Note=Phorbol-ester/DAG-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226	
+P24583	UniProtKB	Nucleotide binding	830	838	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P24583	UniProtKB	Active site	949	949	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P24583	UniProtKB	Binding site	853	853	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P24583	UniProtKB	Modified residue	226	226	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P24583	UniProtKB	Modified residue	761	761	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P24583	UniProtKB	Natural variant	958	958	.	.	.	Note=In cly5%3B temperature-sensitive mutation that cause cell lysis at high temperature. T->I	
+P24583	UniProtKB	Natural variant	1023	1023	.	.	.	Note=In cly7%3B temperature-sensitive mutation that cause cell lysis at high temperature. P->S	
+P24583	UniProtKB	Sequence conflict	81	81	.	.	.	Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24583	UniProtKB	Sequence conflict	81	81	.	.	.	Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24583	UniProtKB	Sequence conflict	244	244	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24583	UniProtKB	Sequence conflict	606	606	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24583	UniProtKB	Sequence conflict	621	621	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24583	UniProtKB	Sequence conflict	621	621	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24583	UniProtKB	Sequence conflict	621	621	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24583	UniProtKB	Sequence conflict	623	623	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24583	UniProtKB	Sequence conflict	789	789	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P24583	UniProtKB	Sequence conflict	789	789	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40565 1 148
+P40565	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000081621;Note=U2 snRNP component IST3	
+P40565	UniProtKB	Domain	31	109	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P40565	UniProtKB	Beta strand	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UQT	
+P40565	UniProtKB	Beta strand	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC	
+P40565	UniProtKB	Helix	44	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC	
+P40565	UniProtKB	Helix	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC	
+P40565	UniProtKB	Beta strand	57	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC	
+P40565	UniProtKB	Beta strand	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC	
+P40565	UniProtKB	Beta strand	71	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC	
+P40565	UniProtKB	Helix	82	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC	
+P40565	UniProtKB	Beta strand	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC	
+P40565	UniProtKB	Helix	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MY3	
+P40565	UniProtKB	Helix	116	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC	
+##sequence-region Q06505 1 410
+Q06505	UniProtKB	Chain	1	410	.	.	.	ID=PRO_0000083366;Note=Transcription factor SPN1	
+Q06505	UniProtKB	Domain	219	296	.	.	.	Note=TFIIS N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00649	
+Q06505	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06505	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q06505	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06505	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06505	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06505	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12242279;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198,PMID:12242279	
+Q06505	UniProtKB	Mutagenesis	192	192	.	.	.	Note=Suppresses postrecruitment-defective SPT15/TBP alleles. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12524336;Dbxref=PMID:12524336	
+Q06505	UniProtKB	Helix	150	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ	
+Q06505	UniProtKB	Helix	191	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ	
+Q06505	UniProtKB	Helix	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ	
+Q06505	UniProtKB	Helix	209	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ	
+Q06505	UniProtKB	Helix	217	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ	
+Q06505	UniProtKB	Helix	236	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ	
+Q06505	UniProtKB	Helix	253	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ	
+Q06505	UniProtKB	Helix	261	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ	
+Q06505	UniProtKB	Beta strand	272	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OAK	
+Q06505	UniProtKB	Helix	276	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ	
+##sequence-region Q12350 1 301
+Q12350	UniProtKB	Chain	1	301	.	.	.	ID=PRO_0000240378;Note=J domain-containing protein 1	
+Q12350	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12350	UniProtKB	Domain	58	150	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+##sequence-region Q03361 1 876
+Q03361	UniProtKB	Chain	1	876	.	.	.	ID=PRO_0000253825;Note=Uncharacterized protein JIP4	
+Q03361	UniProtKB	Compositional bias	685	854	.	.	.	Note=Ser-rich	
+Q03361	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03361	UniProtKB	Modified residue	51	51	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03361	UniProtKB	Modified residue	360	360	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03361	UniProtKB	Modified residue	510	510	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03361	UniProtKB	Modified residue	552	552	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03361	UniProtKB	Modified residue	577	577	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q03361	UniProtKB	Modified residue	775	775	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03361	UniProtKB	Sequence conflict	708	708	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02196 1 202
+Q02196	UniProtKB	Chain	1	202	.	.	.	ID=PRO_0000105936;Note=Adenylyl-sulfate kinase	
+Q02196	UniProtKB	Nucleotide binding	31	38	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02196	UniProtKB	Active site	105	105	.	.	.	Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P25583 1 335
+P25583	UniProtKB	Chain	1	335	.	.	.	ID=PRO_0000207635;Note=Karyogamy protein KAR4	
+##sequence-region P00549 1 500
+P00549	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00549	UniProtKB	Chain	2	500	.	.	.	ID=PRO_0000112121;Note=Pyruvate kinase 1	
+P00549	UniProtKB	Region	402	407	.	.	.	Note=Allosteric activator binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Metal binding	51	51	.	.	.	Note=Potassium;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Metal binding	53	53	.	.	.	Note=Potassium;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Metal binding	84	84	.	.	.	Note=Potassium;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Metal binding	85	85	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Metal binding	242	242	.	.	.	Note=Manganese;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Metal binding	266	266	.	.	.	Note=Manganese;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Binding site	49	49	.	.	.	Note=Substrate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Binding site	240	240	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Binding site	265	265	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Binding site	266	266	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Binding site	298	298	.	.	.	Note=Substrate;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Binding site	337	337	.	.	.	Note=ADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00549	UniProtKB	Binding site	452	452	.	.	.	Note=Allosteric activator;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Binding site	459	459	.	.	.	Note=Allosteric activator;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Binding site	484	484	.	.	.	Note=Allosteric activator%3B via amide nitrogen;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410	
+P00549	UniProtKB	Site	240	240	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10413488;Dbxref=PMID:10413488	
+P00549	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00549	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P00549	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P00549	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00549	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00549	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00549	UniProtKB	Modified residue	213	213	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00549	UniProtKB	Modified residue	316	316	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00549	UniProtKB	Modified residue	450	450	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00549	UniProtKB	Modified residue	478	478	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P00549	UniProtKB	Cross-link	204	204	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00549	UniProtKB	Cross-link	255	255	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00549	UniProtKB	Cross-link	446	446	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00549	UniProtKB	Mutagenesis	240	240	.	.	.	Note=Reduces activity 1000-fold. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10413488;Dbxref=PMID:10413488	
+P00549	UniProtKB	Sequence conflict	382	386	.	.	.	Note=VAASA->SLPR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00549	UniProtKB	Helix	3	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	21	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3X	
+P00549	UniProtKB	Helix	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	34	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	57	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	96	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	108	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Turn	116	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	126	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	133	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	142	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Turn	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3X	
+P00549	UniProtKB	Beta strand	163	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	193	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	208	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	218	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	235	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	245	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	250	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	264	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	276	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	294	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	302	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	312	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	327	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Turn	333	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	341	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	357	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3X	
+P00549	UniProtKB	Helix	361	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	378	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	398	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	403	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	406	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	420	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	429	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	433	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	439	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Turn	452	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Helix	455	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	478	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Turn	487	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+P00549	UniProtKB	Beta strand	494	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W	
+##sequence-region P14681 1 368
+P14681	UniProtKB	Chain	1	368	.	.	.	ID=PRO_0000186333;Note=Mitogen-activated protein kinase KSS1	
+P14681	UniProtKB	Domain	13	313	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P14681	UniProtKB	Nucleotide binding	19	27	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P14681	UniProtKB	Motif	183	185	.	.	.	Note=TXY	
+P14681	UniProtKB	Compositional bias	345	349	.	.	.	Note=Poly-Glu	
+P14681	UniProtKB	Active site	143	143	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P14681	UniProtKB	Binding site	42	42	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P14681	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P14681	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P50090 1 882
+P50090	UniProtKB	Chain	1	882	.	.	.	ID=PRO_0000119097;Note=Kelch repeat-containing protein 2	
+P50090	UniProtKB	Repeat	99	143	.	.	.	Note=Kelch 1	
+P50090	UniProtKB	Repeat	153	207	.	.	.	Note=Kelch 2	
+P50090	UniProtKB	Repeat	213	267	.	.	.	Note=Kelch 3	
+P50090	UniProtKB	Repeat	268	317	.	.	.	Note=Kelch 4	
+P50090	UniProtKB	Repeat	319	369	.	.	.	Note=Kelch 5	
+P50090	UniProtKB	Repeat	371	417	.	.	.	Note=Kelch 6	
+P50090	UniProtKB	Coiled coil	550	685	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50090	UniProtKB	Coiled coil	728	881	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50090	UniProtKB	Modified residue	455	455	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P50090	UniProtKB	Modified residue	509	509	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P13186 1 1147
+P13186	UniProtKB	Chain	1	1147	.	.	.	ID=PRO_0000086133;Note=Serine/threonine-protein kinase KIN2	
+P13186	UniProtKB	Domain	99	377	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P13186	UniProtKB	Domain	1098	1147	.	.	.	Note=KA1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00565	
+P13186	UniProtKB	Nucleotide binding	105	113	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P13186	UniProtKB	Compositional bias	527	536	.	.	.	Note=Poly-Gln	
+P13186	UniProtKB	Active site	248	248	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P13186	UniProtKB	Binding site	128	128	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P13186	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13186	UniProtKB	Modified residue	146	146	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P13186	UniProtKB	Modified residue	549	549	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P13186	UniProtKB	Modified residue	609	609	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P13186	UniProtKB	Modified residue	888	888	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P13186	UniProtKB	Sequence conflict	216	217	.	.	.	Note=QH->HD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13186	UniProtKB	Sequence conflict	675	707	.	.	.	Note=QEPLPEREPPTYMSKSNEISIKVPKSHSRTISD->SGTYSSKENLQHICQNQMKFPSKYRKAIVVLYQT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13186	UniProtKB	Sequence conflict	756	758	.	.	.	Note=NAE->KRQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13186	UniProtKB	Sequence conflict	805	805	.	.	.	Note=P->PLSVP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13186	UniProtKB	Sequence conflict	1034	1037	.	.	.	Note=ATNT->TTNSI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13186	UniProtKB	Sequence conflict	1041	1042	.	.	.	Note=NS->KT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q01919 1 800
+Q01919	UniProtKB	Chain	1	800	.	.	.	ID=PRO_0000086135;Note=Serine/threonine-protein kinase KIN4	
+Q01919	UniProtKB	Domain	46	313	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q01919	UniProtKB	Nucleotide binding	52	60	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q01919	UniProtKB	Active site	175	175	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q01919	UniProtKB	Binding site	80	80	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q01919	UniProtKB	Modified residue	365	365	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q01919	UniProtKB	Modified residue	388	388	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q01919	UniProtKB	Modified residue	521	521	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q01919	UniProtKB	Modified residue	748	748	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P28743 1 706
+P28743	UniProtKB	Chain	1	706	.	.	.	ID=PRO_0000125453;Note=Kinesin-like protein KIP2	
+P28743	UniProtKB	Domain	102	493	.	.	.	Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P28743	UniProtKB	Nucleotide binding	202	209	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P28743	UniProtKB	Coiled coil	507	541	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28743	UniProtKB	Coiled coil	569	589	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28743	UniProtKB	Coiled coil	612	689	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38063 1 326
+P38063	UniProtKB	Chain	1	326	.	.	.	ID=PRO_0000141089;Note=Ribose-phosphate pyrophosphokinase 4	
+P38063	UniProtKB	Metal binding	140	140	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38063	UniProtKB	Metal binding	142	142	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38063	UniProtKB	Metal binding	151	151	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38063	UniProtKB	Metal binding	155	155	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38063	UniProtKB	Sequence conflict	90	90	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38063	UniProtKB	Sequence conflict	169	169	.	.	.	Note=T->AR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P52489 1 506
+P52489	UniProtKB	Chain	1	506	.	.	.	ID=PRO_0000112122;Note=Pyruvate kinase 2	
+P52489	UniProtKB	Metal binding	53	53	.	.	.	Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52489	UniProtKB	Metal binding	55	55	.	.	.	Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52489	UniProtKB	Metal binding	86	86	.	.	.	Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52489	UniProtKB	Metal binding	87	87	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52489	UniProtKB	Metal binding	244	244	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52489	UniProtKB	Metal binding	268	268	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52489	UniProtKB	Binding site	51	51	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52489	UniProtKB	Binding site	267	267	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52489	UniProtKB	Binding site	268	268	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52489	UniProtKB	Binding site	300	300	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52489	UniProtKB	Binding site	339	339	.	.	.	Note=ADP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52489	UniProtKB	Site	242	242	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52489	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P42846 1 591
+P42846	UniProtKB	Chain	1	591	.	.	.	ID=PRO_0000203368;Note=Protein KRI1	
+P42846	UniProtKB	Compositional bias	53	475	.	.	.	Note=Glu-rich	
+P42846	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P42846	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P42846	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P42846	UniProtKB	Modified residue	486	486	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P54070 1 446
+P54070	UniProtKB	Chain	1	446	.	.	.	ID=PRO_0000208247;Note=Mannosyltransferase KTR6	
+P54070	UniProtKB	Topological domain	1	8	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54070	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54070	UniProtKB	Topological domain	30	446	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54070	UniProtKB	Region	30	114	.	.	.	Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54070	UniProtKB	Region	115	446	.	.	.	Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P54070	UniProtKB	Active site	334	334	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54070	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54070	UniProtKB	Glycosylation	98	98	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q02733 1 499
+Q02733	UniProtKB	Chain	1	499	.	.	.	ID=PRO_0000268179;Note=Increased recombination centers protein 15	
+Q02733	UniProtKB	Nucleotide binding	47	56	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q06554 1 1556
+Q06554	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06554	UniProtKB	Chain	2	1556	.	.	.	ID=PRO_0000268181;Note=Uncharacterized ATP-dependent helicase IRC20	
+Q06554	UniProtKB	Domain	378	583	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q06554	UniProtKB	Domain	1363	1531	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q06554	UniProtKB	Nucleotide binding	391	398	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q06554	UniProtKB	Zinc finger	1239	1277	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q06554	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06554	UniProtKB	Modified residue	810	810	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region A0A023PXB5 1 102
+A0A023PXB5	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000430978;Note=Putative uncharacterized membrane protein IRC2	
+A0A023PXB5	UniProtKB	Transmembrane	21	43	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PXB5	UniProtKB	Transmembrane	58	80	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03036 1 179
+Q03036	UniProtKB	Chain	1	179	.	.	.	ID=PRO_0000253886;Note=Uncharacterized protein IRC4	
+Q03036	UniProtKB	Helix	7	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Helix	24	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Helix	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Helix	44	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Beta strand	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Helix	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Helix	83	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Helix	99	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Helix	122	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Beta strand	127	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Helix	133	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Helix	142	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+Q03036	UniProtKB	Helix	151	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG	
+##sequence-region P47010 1 130
+P47010	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000203035;Note=Putative uncharacterized protein IRC9	
+P47010	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47010	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47010	UniProtKB	Transmembrane	83	103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32361 1 1115
+P32361	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32361	UniProtKB	Chain	19	1115	.	.	.	ID=PRO_0000024338;Note=Serine/threonine-protein kinase/endoribonuclease IRE1	
+P32361	UniProtKB	Topological domain	19	526	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32361	UniProtKB	Transmembrane	527	555	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32361	UniProtKB	Topological domain	556	1115	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32361	UniProtKB	Domain	674	980	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32361	UniProtKB	Domain	983	1115	.	.	.	Note=KEN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00725	
+P32361	UniProtKB	Nucleotide binding	680	688	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32361	UniProtKB	Active site	797	797	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P32361	UniProtKB	Binding site	702	702	.	.	.	Note=ATP	
+P32361	UniProtKB	Modified residue	840	840	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8670804;Dbxref=PMID:8670804	
+P32361	UniProtKB	Modified residue	841	841	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8670804;Dbxref=PMID:8670804	
+P32361	UniProtKB	Glycosylation	111	111	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32361	UniProtKB	Glycosylation	213	213	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32361	UniProtKB	Glycosylation	298	298	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32361	UniProtKB	Glycosylation	397	397	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32361	UniProtKB	Mutagenesis	702	702	.	.	.	Note=Loss of autophosphorylation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663458;Dbxref=PMID:8663458	
+P32361	UniProtKB	Sequence conflict	368	368	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32361	UniProtKB	Sequence conflict	625	626	.	.	.	Note=ND->KH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32361	UniProtKB	Beta strand	116	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	132	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Turn	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	142	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Helix	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Turn	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	165	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Turn	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	178	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Turn	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	187	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Helix	195	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	203	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	222	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	228	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Turn	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	243	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	277	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	300	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Turn	308	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Helix	311	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	326	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Turn	330	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	333	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	344	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	355	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Turn	365	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	369	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	390	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	400	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Turn	405	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Helix	409	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Helix	419	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Helix	424	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Helix	429	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Helix	435	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Beta strand	444	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1	
+P32361	UniProtKB	Turn	666	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LJ2	
+P32361	UniProtKB	Beta strand	674	682	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Turn	684	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV	
+P32361	UniProtKB	Beta strand	688	705	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	706	708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	709	722	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Beta strand	731	736	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Beta strand	738	745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Beta strand	749	751	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	752	757	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	765	769	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV	
+P32361	UniProtKB	Helix	774	790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	800	802	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Beta strand	803	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	809	812	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Beta strand	823	826	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Turn	836	838	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV	
+P32361	UniProtKB	Helix	851	855	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV	
+P32361	UniProtKB	Helix	858	861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	900	914	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Turn	924	926	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	927	933	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	947	960	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	965	967	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	971	975	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	978	980	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	983	998	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Turn	1002	1005	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	1007	1013	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	1016	1019	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	1025	1028	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	1031	1035	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV	
+P32361	UniProtKB	Beta strand	1038	1041	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV	
+P32361	UniProtKB	Helix	1048	1060	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	1062	1064	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	1067	1072	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	1078	1087	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	1091	1102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Turn	1107	1109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+P32361	UniProtKB	Helix	1110	1114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO	
+##sequence-region P30606 1 609
+P30606	UniProtKB	Chain	1	609	.	.	.	ID=PRO_0000050458;Note=Myo-inositol transporter 2	
+P30606	UniProtKB	Topological domain	1	104	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	126	152	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	174	179	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	180	200	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	201	209	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	210	230	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	231	240	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	262	269	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	270	290	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	291	359	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	360	380	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	381	396	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	397	417	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	418	423	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	424	444	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	445	465	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	466	486	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	487	506	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	507	527	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	528	533	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Transmembrane	534	554	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Topological domain	555	609	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30606	UniProtKB	Glycosylation	394	394	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04934 1 453
+Q04934	UniProtKB	Chain	1	453	.	.	.	ID=PRO_0000084277;Note=Protein IVY1	
+Q04934	UniProtKB	Coiled coil	102	122	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04934	UniProtKB	Coiled coil	230	257	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04934	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q04934	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04934	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04934	UniProtKB	Modified residue	335	335	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P36035 1 616
+P36035	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12872131;Dbxref=PMID:17761666,PMID:22814378,PMID:12872131	
+P36035	UniProtKB	Chain	2	616	.	.	.	ID=PRO_0000050460;Note=Carboxylic acid transporter protein homolog	
+P36035	UniProtKB	Topological domain	2	140	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	162	176	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	198	205	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	206	226	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	227	230	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	231	251	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	252	263	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	264	284	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	285	296	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	297	317	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	318	363	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	364	384	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	385	402	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	403	423	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	424	432	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	433	453	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	454	457	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	458	478	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	479	489	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	490	510	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	511	535	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Transmembrane	536	556	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Topological domain	557	616	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36035	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:22814378;Dbxref=PMID:17761666,PMID:22814378	
+P36035	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P36035	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P36035	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36035	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36035	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36035	UniProtKB	Modified residue	584	584	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P36035	UniProtKB	Modified residue	603	603	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36035	UniProtKB	Modified residue	606	606	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:19779198	
+P36035	UniProtKB	Cross-link	9	9	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P36035	UniProtKB	Cross-link	338	338	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region P46997 1 583
+P46997	UniProtKB	Chain	1	583	.	.	.	ID=PRO_0000071142;Note=J protein JJJ2	
+P46997	UniProtKB	Domain	11	79	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P46997	UniProtKB	Compositional bias	232	236	.	.	.	Note=Poly-Glu	
+P46997	UniProtKB	Compositional bias	240	252	.	.	.	Note=Poly-Gln	
+P46997	UniProtKB	Modified residue	229	229	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P26364 1 225
+P26364	UniProtKB	Chain	1	225	.	.	.	ID=PRO_0000158907;Note=GTP:AMP phosphotransferase%2C mitochondrial	
+P26364	UniProtKB	Nucleotide binding	24	29	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Nucleotide binding	72	74	.	.	.	Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Nucleotide binding	103	106	.	.	.	Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Nucleotide binding	154	155	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Region	45	74	.	.	.	Note=NMPbind;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Region	144	181	.	.	.	Note=LID;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Binding site	46	46	.	.	.	Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Binding site	51	51	.	.	.	Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Binding site	110	110	.	.	.	Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Binding site	145	145	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Binding site	178	178	.	.	.	Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Binding site	189	189	.	.	.	Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+P26364	UniProtKB	Binding site	218	218	.	.	.	Note=GTP%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169	
+##sequence-region P06244 1 397
+P06244	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P06244	UniProtKB	Chain	2	397	.	.	.	ID=PRO_0000086046;Note=cAMP-dependent protein kinase type 1	
+P06244	UniProtKB	Domain	87	341	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06244	UniProtKB	Domain	342	397	.	.	.	Note=AGC-kinase C-terminal	
+P06244	UniProtKB	Nucleotide binding	93	101	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06244	UniProtKB	Active site	210	210	.	.	.	Note=Proton acceptor	
+P06244	UniProtKB	Binding site	116	116	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06244	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P06244	UniProtKB	Sequence conflict	79	86	.	.	.	Note=SGKYSLQD->VGSIVYKN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06244	UniProtKB	Sequence conflict	79	86	.	.	.	Note=SGKYSLQD->VGSIVYKN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06244	UniProtKB	Sequence conflict	164	171	.	.	.	Note=MDYIEGGE->ILKVER;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06244	UniProtKB	Sequence conflict	180	181	.	.	.	Note=QR->KD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06244	UniProtKB	Sequence conflict	188	190	.	.	.	Note=KFY->QIF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06244	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Beta strand	87	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Beta strand	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Turn	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Beta strand	112	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	120	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	129	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Beta strand	150	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Beta strand	157	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	172	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	184	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Turn	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Beta strand	216	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Beta strand	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Turn	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	251	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	263	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	287	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	307	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Turn	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Turn	329	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	333	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	339	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	346	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+P06244	UniProtKB	Helix	391	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT	
+##sequence-region Q07551 1 312
+Q07551	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000262755;Note=NADPH-dependent alpha-keto amide reductase	
+Q07551	UniProtKB	Nucleotide binding	208	268	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07551	UniProtKB	Active site	64	64	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07551	UniProtKB	Binding site	122	122	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07551	UniProtKB	Site	89	89	.	.	.	Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07551	UniProtKB	Modified residue	123	123	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q08979 1 651
+Q08979	UniProtKB	Chain	1	651	.	.	.	ID=PRO_0000119098;Note=Kelch repeat-containing protein 3	
+Q08979	UniProtKB	Repeat	94	148	.	.	.	Note=Kelch 1	
+Q08979	UniProtKB	Repeat	150	199	.	.	.	Note=Kelch 2	
+Q08979	UniProtKB	Repeat	208	259	.	.	.	Note=Kelch 3	
+Q08979	UniProtKB	Repeat	262	310	.	.	.	Note=Kelch 4	
+Q08979	UniProtKB	Repeat	334	383	.	.	.	Note=Kelch 5	
+Q08979	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q04066 1 261
+Q04066	UniProtKB	Chain	1	261	.	.	.	ID=PRO_0000234660;Note=Kynurenine formamidase	
+Q04066	UniProtKB	Motif	36	40	.	.	.	Note=HGGXW	
+Q04066	UniProtKB	Active site	110	110	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03014	
+Q04066	UniProtKB	Active site	211	211	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03014	
+Q04066	UniProtKB	Active site	243	243	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03014	
+Q04066	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q04066	UniProtKB	Helix	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Beta strand	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Beta strand	30	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Turn	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	51	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Beta strand	66	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Turn	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	83	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Beta strand	104	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	111	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	121	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Turn	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	132	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Beta strand	144	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	156	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	167	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	185	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Beta strand	202	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	217	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Beta strand	233	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	243	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+Q04066	UniProtKB	Helix	250	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH	
+##sequence-region P36005 1 433
+P36005	UniProtKB	Chain	1	433	.	.	.	ID=PRO_0000086150;Note=Serine/threonine-protein kinase KDX1	
+P36005	UniProtKB	Domain	23	318	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P36005	UniProtKB	Nucleotide binding	29	37	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P36005	UniProtKB	Active site	153	153	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P36005	UniProtKB	Binding site	55	55	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region P38853 1 1164
+P38853	UniProtKB	Chain	1	1164	.	.	.	ID=PRO_0000119096;Note=Kelch repeat-containing protein 1	
+P38853	UniProtKB	Repeat	139	186	.	.	.	Note=Kelch 1	
+P38853	UniProtKB	Repeat	253	307	.	.	.	Note=Kelch 2	
+P38853	UniProtKB	Repeat	308	357	.	.	.	Note=Kelch 3	
+P38853	UniProtKB	Repeat	359	409	.	.	.	Note=Kelch 4	
+P38853	UniProtKB	Repeat	411	460	.	.	.	Note=Kelch 5	
+P38853	UniProtKB	Coiled coil	777	931	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38853	UniProtKB	Coiled coil	974	1163	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38853	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38853	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38853	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38853	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P38853	UniProtKB	Modified residue	467	467	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38853	UniProtKB	Modified residue	477	477	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38853	UniProtKB	Modified residue	503	503	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38853	UniProtKB	Modified residue	604	604	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38853	UniProtKB	Modified residue	613	613	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P38853	UniProtKB	Modified residue	626	626	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38853	UniProtKB	Modified residue	689	689	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38853	UniProtKB	Modified residue	691	691	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38853	UniProtKB	Modified residue	717	717	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38853	UniProtKB	Modified residue	748	748	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38853	UniProtKB	Modified residue	837	837	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38853	UniProtKB	Modified residue	848	848	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38853	UniProtKB	Modified residue	958	958	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38853	UniProtKB	Modified residue	997	997	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38853	UniProtKB	Modified residue	1003	1003	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38853	UniProtKB	Modified residue	1022	1022	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38853	UniProtKB	Sequence conflict	447	447	.	.	.	Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40309 1 873
+P40309	UniProtKB	Chain	1	873	.	.	.	ID=PRO_0000196618;Note=K(+)/H(+) antiporter 1	
+P40309	UniProtKB	Topological domain	1	23	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	24	44	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	45	51	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	73	82	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	83	103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	104	116	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	138	154	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	155	175	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	176	188	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	210	220	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	221	241	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	242	267	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	268	288	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	289	316	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	317	337	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	338	341	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	342	362	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	363	375	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	376	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	397	404	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	405	425	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	426	726	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Transmembrane	727	747	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Topological domain	748	873	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40309	UniProtKB	Modified residue	557	557	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40309	UniProtKB	Cross-link	562	562	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P22209 1 435
+P22209	UniProtKB	Chain	1	435	.	.	.	ID=PRO_0000086134;Note=Serine/threonine-protein kinase KIN3	
+P22209	UniProtKB	Domain	25	343	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22209	UniProtKB	Nucleotide binding	31	39	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22209	UniProtKB	Active site	174	174	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P22209	UniProtKB	Binding site	54	54	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22209	UniProtKB	Sequence conflict	92	92	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22209	UniProtKB	Sequence conflict	98	98	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22209	UniProtKB	Sequence conflict	121	121	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22209	UniProtKB	Sequence conflict	130	130	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22209	UniProtKB	Sequence conflict	235	238	.	.	.	Note=AKSL->SQIS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22209	UniProtKB	Sequence conflict	358	358	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25341 1 720
+P25341	UniProtKB	Chain	1	720	.	.	.	ID=PRO_0000086136;Note=Serine/threonine-protein kinase KIN82	
+P25341	UniProtKB	Domain	324	602	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P25341	UniProtKB	Nucleotide binding	330	338	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P25341	UniProtKB	Active site	449	449	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P25341	UniProtKB	Binding site	353	353	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P25341	UniProtKB	Modified residue	203	203	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25341	UniProtKB	Sequence conflict	341	341	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25341	UniProtKB	Sequence conflict	341	341	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53086 1 805
+P53086	UniProtKB	Chain	1	805	.	.	.	ID=PRO_0000125404;Note=Kinesin-like protein KIP3	
+P53086	UniProtKB	Domain	10	438	.	.	.	Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P53086	UniProtKB	Nucleotide binding	192	199	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P53086	UniProtKB	Coiled coil	449	481	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGJ3 1 72
+Q8TGJ3	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q8TGJ3	UniProtKB	Chain	27	72	.	.	.	ID=PRO_0000247775;Note=Protein kish	
+Q8TGJ3	UniProtKB	Topological domain	27	53	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q8TGJ3	UniProtKB	Transmembrane	54	72	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P50112 1 268
+P50112	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50112	UniProtKB	Chain	21	268	.	.	.	ID=PRO_0000016851;Note=Cell wall synthesis protein KNH1	
+P50112	UniProtKB	Sequence conflict	238	238	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38873 1 1557
+P38873	UniProtKB	Chain	1	1557	.	.	.	ID=PRO_0000051476;Note=Target of rapamycin complex 1 subunit KOG1	
+P38873	UniProtKB	Repeat	548	586	.	.	.	Note=HEAT 1	
+P38873	UniProtKB	Repeat	588	625	.	.	.	Note=HEAT 2	
+P38873	UniProtKB	Repeat	777	814	.	.	.	Note=HEAT 3	
+P38873	UniProtKB	Repeat	888	925	.	.	.	Note=HEAT 4	
+P38873	UniProtKB	Repeat	1207	1248	.	.	.	Note=WD 1	
+P38873	UniProtKB	Repeat	1252	1293	.	.	.	Note=WD 2	
+P38873	UniProtKB	Repeat	1296	1346	.	.	.	Note=WD 3	
+P38873	UniProtKB	Repeat	1350	1390	.	.	.	Note=WD 4	
+P38873	UniProtKB	Repeat	1400	1440	.	.	.	Note=WD 5	
+P38873	UniProtKB	Repeat	1452	1492	.	.	.	Note=WD 6	
+P38873	UniProtKB	Repeat	1517	1557	.	.	.	Note=WD 7	
+P38873	UniProtKB	Compositional bias	513	525	.	.	.	Note=Poly-Gln	
+P38873	UniProtKB	Compositional bias	846	855	.	.	.	Note=Poly-Gln	
+##sequence-region P40504 1 517
+P40504	UniProtKB	Chain	1	517	.	.	.	ID=PRO_0000208248;Note=Probable mannosyltransferase KTR7	
+P40504	UniProtKB	Topological domain	1	23	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40504	UniProtKB	Transmembrane	24	44	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P40504	UniProtKB	Topological domain	45	517	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40504	UniProtKB	Region	45	85	.	.	.	Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40504	UniProtKB	Region	86	517	.	.	.	Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40504	UniProtKB	Active site	367	367	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40504	UniProtKB	Glycosylation	89	89	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40504	UniProtKB	Glycosylation	144	144	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36146 1 502
+P36146	UniProtKB	Chain	1	502	.	.	.	ID=PRO_0000211561;Note=Protein LAS1	
+P36146	UniProtKB	Sequence conflict	97	97	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39518 1 744
+P39518	UniProtKB	Chain	1	744	.	.	.	ID=PRO_0000193120;Note=Long-chain-fatty-acid--CoA ligase 2	
+P39518	UniProtKB	Mutagenesis	1	1	.	.	.	Note=In FAM1-1. M->MWKNAGYKKRIRTNLFRNM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7988550;Dbxref=PMID:7988550	
+##sequence-region P09620 1 729
+P09620	UniProtKB	Signal peptide	1	22	.	.	.	.	
+P09620	UniProtKB	Chain	23	729	.	.	.	ID=PRO_0000004287;Note=Pheromone-processing carboxypeptidase KEX1	
+P09620	UniProtKB	Topological domain	23	616	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P09620	UniProtKB	Transmembrane	617	637	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P09620	UniProtKB	Topological domain	638	729	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P09620	UniProtKB	Compositional bias	526	531	.	.	.	Note=Poly-Glu	
+P09620	UniProtKB	Compositional bias	545	561	.	.	.	Note=Poly-Asp	
+P09620	UniProtKB	Compositional bias	567	578	.	.	.	Note=Poly-Asp	
+P09620	UniProtKB	Compositional bias	597	607	.	.	.	Note=Poly-Glu	
+P09620	UniProtKB	Compositional bias	703	711	.	.	.	Note=Poly-Lys	
+P09620	UniProtKB	Active site	198	198	.	.	.	.	
+P09620	UniProtKB	Active site	405	405	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09620	UniProtKB	Active site	470	470	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09620	UniProtKB	Modified residue	660	660	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P09620	UniProtKB	Glycosylation	81	81	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P09620	UniProtKB	Glycosylation	459	459	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1469044;Dbxref=PMID:1469044	
+P09620	UniProtKB	Glycosylation	467	467	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1469044;Dbxref=PMID:1469044	
+P09620	UniProtKB	Mutagenesis	198	198	.	.	.	Note=Inactivates enzyme. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3301004;Dbxref=PMID:3301004	
+P09620	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	50	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	72	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	91	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Turn	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	104	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	110	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	133	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	166	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	190	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	200	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	226	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	239	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	246	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	263	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	283	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	287	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	291	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	296	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	314	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	320	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Turn	327	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	337	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	350	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Turn	358	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	369	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	383	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	387	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	396	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	410	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	425	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	433	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	452	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	460	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	472	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Helix	477	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	492	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+P09620	UniProtKB	Beta strand	499	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5	
+##sequence-region P15454 1 187
+P15454	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2551688;Dbxref=PMID:2551688	
+P15454	UniProtKB	Chain	2	187	.	.	.	ID=PRO_0000170655;Note=Guanylate kinase	
+P15454	UniProtKB	Domain	2	184	.	.	.	Note=Guanylate kinase-like	
+P15454	UniProtKB	Nucleotide binding	9	16	.	.	.	Note=ATP	
+P15454	UniProtKB	Nucleotide binding	35	82	.	.	.	Note=GMP	
+P15454	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1314905,ECO:0000269|PubMed:2551688;Dbxref=PMID:1314905,PMID:2551688	
+P15454	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P15454	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P15454	UniProtKB	Beta strand	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Helix	15	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Turn	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Beta strand	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Beta strand	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GKY	
+P15454	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Beta strand	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GKY	
+P15454	UniProtKB	Helix	56	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Beta strand	68	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Beta strand	77	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Helix	83	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Beta strand	94	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Helix	102	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Helix	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Beta strand	117	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Helix	126	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Helix	141	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Beta strand	163	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+P15454	UniProtKB	Helix	172	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7	
+##sequence-region P17260 1 313
+P17260	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17260	UniProtKB	Chain	27	288	.	.	.	ID=PRO_0000021561;Note=Protein KRE1	
+P17260	UniProtKB	Propeptide	289	313	.	.	.	ID=PRO_0000021562;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17260	UniProtKB	Repeat	72	86	.	.	.	Note=1	
+P17260	UniProtKB	Repeat	127	141	.	.	.	Note=2	
+P17260	UniProtKB	Region	72	141	.	.	.	Note=2 X approximate repeats	
+P17260	UniProtKB	Compositional bias	52	58	.	.	.	Note=Poly-Ala	
+P17260	UniProtKB	Compositional bias	95	100	.	.	.	Note=Poly-Thr	
+P17260	UniProtKB	Compositional bias	106	109	.	.	.	Note=Poly-Thr	
+P17260	UniProtKB	Compositional bias	158	169	.	.	.	Note=Poly-Ser	
+P17260	UniProtKB	Lipidation	288	288	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38691 1 1029
+P38691	UniProtKB	Chain	1	1029	.	.	.	ID=PRO_0000086228;Note=Serine/threonine-protein kinase KSP1	
+P38691	UniProtKB	Domain	18	351	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38691	UniProtKB	Nucleotide binding	27	35	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38691	UniProtKB	Active site	207	207	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P38691	UniProtKB	Binding site	47	47	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38691	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38691	UniProtKB	Modified residue	419	419	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38691	UniProtKB	Modified residue	501	501	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38691	UniProtKB	Modified residue	504	504	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38691	UniProtKB	Modified residue	526	526	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P38691	UniProtKB	Modified residue	529	529	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38691	UniProtKB	Modified residue	646	646	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38691	UniProtKB	Modified residue	845	845	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38691	UniProtKB	Modified residue	884	884	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38691	UniProtKB	Modified residue	1005	1005	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38691	UniProtKB	Modified residue	1014	1014	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P38130 1 404
+P38130	UniProtKB	Chain	1	404	.	.	.	ID=PRO_0000208244;Note=Probable mannosyltransferase KTR3	
+P38130	UniProtKB	Topological domain	1	27	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38130	UniProtKB	Transmembrane	28	44	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P38130	UniProtKB	Topological domain	45	404	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38130	UniProtKB	Region	45	83	.	.	.	Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38130	UniProtKB	Region	84	404	.	.	.	Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38130	UniProtKB	Active site	295	295	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38130	UniProtKB	Sequence conflict	100	100	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38800 1 1345
+P38800	UniProtKB	Chain	1	1345	.	.	.	ID=PRO_0000202901;Note=Membrane-anchored lipid-binding protein LAM4	
+P38800	UniProtKB	Topological domain	1	1197	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38800	UniProtKB	Transmembrane	1198	1218	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38800	UniProtKB	Topological domain	1219	1345	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38800	UniProtKB	Domain	549	616	.	.	.	Note=GRAM;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38800	UniProtKB	Domain	758	930	.	.	.	Note=VASt 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114	
+P38800	UniProtKB	Domain	967	1139	.	.	.	Note=VASt 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114	
+P38800	UniProtKB	Compositional bias	679	711	.	.	.	Note=Asp-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00004	
+P38800	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38800	UniProtKB	Modified residue	747	747	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P38800	UniProtKB	Mutagenesis	1119	1119	.	.	.	Note=Abolishes the ability to bind sterol. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26001273;Dbxref=PMID:26001273	
+##sequence-region P38210 1 180
+P38210	UniProtKB	Chain	1	180	.	.	.	ID=PRO_0000076230;Note=Chromatin structure-remodeling complex protein RSC14	
+##sequence-region P20485 1 582
+P20485	UniProtKB	Chain	1	582	.	.	.	ID=PRO_0000206226;Note=Choline kinase	
+P20485	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105205;Dbxref=PMID:12105205	
+P20485	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P20485	UniProtKB	Modified residue	51	51	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P20485	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P20485	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105205;Dbxref=PMID:12105205	
+P20485	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Decrease in activity and in phosphorylation by PKA. No phosphorylation by PKA%2C and strong decrease in activity%3B when associated with A-85. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105205;Dbxref=PMID:12105205	
+P20485	UniProtKB	Mutagenesis	85	85	.	.	.	Note=No phosphorylation by PKA%2C and strong decrease in activity%3B when associated with A-30. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105205;Dbxref=PMID:12105205	
+##sequence-region P38689 1 320
+P38689	UniProtKB	Chain	1	320	.	.	.	ID=PRO_0000141088;Note=Ribose-phosphate pyrophosphokinase 3	
+P38689	UniProtKB	Metal binding	131	131	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38689	UniProtKB	Metal binding	133	133	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38689	UniProtKB	Metal binding	142	142	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38689	UniProtKB	Metal binding	146	146	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04431 1 385
+Q04431	UniProtKB	Chain	1	385	.	.	.	ID=PRO_0000253889;Note=Spindle pole body component KRE28	
+Q04431	UniProtKB	Coiled coil	128	167	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04431	UniProtKB	Coiled coil	229	258	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04431	UniProtKB	Sequence conflict	263	263	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P22023 1 1365
+P22023	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Chain	18	1365	.	.	.	ID=PRO_0000021563;Note=Killer toxin-resistance protein 5	
+P22023	UniProtKB	Motif	1362	1365	.	.	.	Note=Prevents secretion from ER	
+P22023	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Glycosylation	228	228	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Glycosylation	293	293	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Glycosylation	457	457	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Glycosylation	519	519	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Glycosylation	523	523	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Glycosylation	644	644	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Glycosylation	870	870	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Glycosylation	1091	1091	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Glycosylation	1150	1150	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Glycosylation	1195	1195	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22023	UniProtKB	Sequence conflict	582	582	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22023	UniProtKB	Sequence conflict	780	794	.	.	.	Note=HLDQNEVPETEHFEA->ILIKMKCQKQNISKAK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33550 1 425
+P33550	UniProtKB	Chain	1	425	.	.	.	ID=PRO_0000208243;Note=Probable mannosyltransferase KTR2	
+P33550	UniProtKB	Topological domain	1	13	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33550	UniProtKB	Transmembrane	14	33	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P33550	UniProtKB	Topological domain	34	425	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33550	UniProtKB	Region	34	89	.	.	.	Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33550	UniProtKB	Region	90	425	.	.	.	Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33550	UniProtKB	Active site	313	313	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33550	UniProtKB	Glycosylation	65	65	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33550	UniProtKB	Glycosylation	81	81	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33550	UniProtKB	Glycosylation	92	92	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33550	UniProtKB	Glycosylation	167	167	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43560 1 674
+P43560	UniProtKB	Chain	1	674	.	.	.	ID=PRO_0000202673;Note=Membrane-anchored lipid-binding protein LAM5	
+P43560	UniProtKB	Topological domain	1	633	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43560	UniProtKB	Transmembrane	634	654	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43560	UniProtKB	Topological domain	655	674	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43560	UniProtKB	Domain	198	264	.	.	.	Note=GRAM;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43560	UniProtKB	Domain	409	582	.	.	.	Note=VASt;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114	
+P43560	UniProtKB	Compositional bias	81	140	.	.	.	Note=Ser-rich	
+P43560	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P43560	UniProtKB	Modified residue	113	113	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P43560	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P43560	UniProtKB	Modified residue	143	143	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P43560	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q06346 1 221
+Q06346	UniProtKB	Chain	1	221	.	.	.	ID=PRO_0000253846;Note=Inositol phosphorylceramide synthase regulatory subunit KEI1	
+Q06346	UniProtKB	Chain	1	135	.	.	.	ID=PRO_0000409445;Note=KEI1N	
+Q06346	UniProtKB	Chain	136	221	.	.	.	ID=PRO_0000409446;Note=KEI1C	
+Q06346	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06346	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06346	UniProtKB	Transmembrane	79	99	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06346	UniProtKB	Transmembrane	154	174	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06346	UniProtKB	Region	176	221	.	.	.	Note=COPI vesicle-binding	
+Q06346	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Decreases ICP synthase activity. F->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19726565;Dbxref=PMID:19726565	
+Q06346	UniProtKB	Mutagenesis	135	135	.	.	.	Note=Impairs cleavage by KEX2. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19726565;Dbxref=PMID:19726565	
+##sequence-region P36004 1 724
+P36004	UniProtKB	Chain	1	724	.	.	.	ID=PRO_0000086151;Note=Probable serine/threonine-protein kinase KKQ8	
+P36004	UniProtKB	Domain	412	712	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P36004	UniProtKB	Nucleotide binding	418	426	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P36004	UniProtKB	Active site	563	563	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P36004	UniProtKB	Binding site	455	455	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P36004	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P36004	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P36004	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P36004	UniProtKB	Modified residue	241	241	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P32350 1 737
+P32350	UniProtKB	Chain	1	737	.	.	.	ID=PRO_0000086155;Note=Dual specificity protein kinase KNS1	
+P32350	UniProtKB	Domain	313	720	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32350	UniProtKB	Nucleotide binding	319	327	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32350	UniProtKB	Compositional bias	143	146	.	.	.	Note=Poly-Ser	
+P32350	UniProtKB	Compositional bias	148	152	.	.	.	Note=Poly-Asn	
+P32350	UniProtKB	Compositional bias	673	679	.	.	.	Note=Ser/Thr-rich	
+P32350	UniProtKB	Active site	440	440	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P32350	UniProtKB	Binding site	343	343	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32350	UniProtKB	Modified residue	562	562	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32350	UniProtKB	Sequence conflict	411	421	.	.	.	Note=RFPGSHIQAIA->GSPALISGHC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32895 1 427
+P32895	UniProtKB	Chain	1	427	.	.	.	ID=PRO_0000141086;Note=Ribose-phosphate pyrophosphokinase 1	
+P32895	UniProtKB	Metal binding	128	128	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32895	UniProtKB	Metal binding	130	130	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32895	UniProtKB	Metal binding	143	143	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32895	UniProtKB	Modified residue	199	199	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P32895	UniProtKB	Modified residue	218	218	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32895	UniProtKB	Modified residue	271	271	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32895	UniProtKB	Modified residue	295	295	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53158 1 218
+P53158	UniProtKB	Chain	1	218	.	.	.	ID=PRO_0000202759;Note=Biogenesis of lysosome-related organelles complex 1 subunit KXD1	
+P53158	UniProtKB	Coiled coil	142	192	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53158	UniProtKB	Motif	175	179	.	.	.	Note=KxDL	
+P53158	UniProtKB	Compositional bias	16	64	.	.	.	Note=Ser-rich	
+##sequence-region P40970 1 561
+P40970	UniProtKB	Chain	1	561	.	.	.	ID=PRO_0000163862;Note=Serine palmitoyltransferase 2	
+P40970	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40970	UniProtKB	Transmembrane	443	463	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40970	UniProtKB	Modified residue	366	366	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40970	UniProtKB	Mutagenesis	334	334	.	.	.	Note=Loss of activity. No effect on interaction with LCB1. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11781309;Dbxref=PMID:11781309	
+P40970	UniProtKB	Mutagenesis	366	366	.	.	.	Note=Loss of activity. No effect on interaction with LCB1. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11781309;Dbxref=PMID:11781309	
+P40970	UniProtKB	Sequence conflict	5	6	.	.	.	Note=AN->PH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40970	UniProtKB	Sequence conflict	23	23	.	.	.	Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40970	UniProtKB	Sequence conflict	236	236	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40970	UniProtKB	Sequence conflict	441	441	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39002 1 694
+P39002	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39002	UniProtKB	Chain	2	694	.	.	.	ID=PRO_0000193121;Note=Long-chain-fatty-acid--CoA ligase 3	
+P39002	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P40079 1 357
+P40079	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40079	UniProtKB	Chain	2	357	.	.	.	ID=PRO_0000084370;Note=U3 small nucleolar ribonucleoprotein protein LCP5	
+P40079	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P25587 1 256
+P25587	UniProtKB	Chain	1	256	.	.	.	ID=PRO_0000202538;Note=Protein LDB16	
+P25587	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25587	UniProtKB	Transmembrane	22	42	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25587	UniProtKB	Topological domain	43	75	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25587	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25587	UniProtKB	Topological domain	97	256	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25587	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25587	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25587	UniProtKB	Modified residue	241	241	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+##sequence-region Q02799 1 301
+Q02799	UniProtKB	Chain	1	301	.	.	.	ID=PRO_0000213909;Note=Zinc finger protein LEE1	
+Q02799	UniProtKB	Zinc finger	87	114	.	.	.	Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q02799	UniProtKB	Zinc finger	123	145	.	.	.	Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+Q02799	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02799	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02799	UniProtKB	Modified residue	282	282	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02799	UniProtKB	Sequence conflict	198	198	.	.	.	Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12166 1 604
+Q12166	UniProtKB	Transit peptide	1	50	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12166	UniProtKB	Chain	51	604	.	.	.	ID=PRO_0000255958;Note=2-isopropylmalate synthase 2%2C mitochondrial	
+Q12166	UniProtKB	Domain	60	335	.	.	.	Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151	
+##sequence-region P50107 1 326
+P50107	UniProtKB	Chain	1	326	.	.	.	ID=PRO_0000168087;Note=Lactoylglutathione lyase	
+P50107	UniProtKB	Domain	22	167	.	.	.	Note=VOC 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01163	
+P50107	UniProtKB	Domain	182	322	.	.	.	Note=VOC 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01163	
+P50107	UniProtKB	Active site	163	163	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50107	UniProtKB	Metal binding	25	25	.	.	.	Note=Zinc%3B via tele nitrogen%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50107	UniProtKB	Metal binding	89	89	.	.	.	Note=Zinc%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50107	UniProtKB	Metal binding	117	117	.	.	.	Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50107	UniProtKB	Metal binding	163	163	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50107	UniProtKB	Binding site	29	29	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50107	UniProtKB	Binding site	93	93	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50107	UniProtKB	Binding site	113	113	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50107	UniProtKB	Binding site	117	117	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P50107	UniProtKB	Sequence conflict	36	36	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50107	UniProtKB	Sequence conflict	156	156	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50107	UniProtKB	Sequence conflict	156	156	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50107	UniProtKB	Sequence conflict	322	322	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06005 1 328
+Q06005	UniProtKB	Domain	108	312	.	.	.	Note=BPL/LPL catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01067	
+Q06005	UniProtKB	Region	162	169	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06005	UniProtKB	Region	241	243	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06005	UniProtKB	Region	254	256	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06005	UniProtKB	Active site	272	272	.	.	.	Note=Acyl-thioester intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06005	UniProtKB	Site	238	238	.	.	.	Note=Lowers pKa of active site Cys;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38878 1 278
+P38878	UniProtKB	Chain	1	278	.	.	.	ID=PRO_0000202936;Note=Protein lunapark	
+P38878	UniProtKB	Topological domain	1	45	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38878	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38878	UniProtKB	Topological domain	67	77	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38878	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38878	UniProtKB	Topological domain	99	278	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38878	UniProtKB	Zinc finger	223	247	.	.	.	Note=C4-type%3B plays a role in ER morphology	
+P38878	UniProtKB	Coiled coil	107	183	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38878	UniProtKB	Mutagenesis	223	223	.	.	.	Note=In lnp1-1%3B causes aberrant ER morphology%3B when associaetd with A-226%2C A-244 and A-247. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22729086;Dbxref=PMID:22729086	
+P38878	UniProtKB	Mutagenesis	226	226	.	.	.	Note=In lnp1-1%3B causes aberrant ER morphology%3B when associaetd with A-223%2C A-244 and A-247. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22729086;Dbxref=PMID:22729086	
+P38878	UniProtKB	Mutagenesis	244	244	.	.	.	Note=In lnp1-1%3B causes aberrant ER morphology%3B when associaetd with A-223%2C A-226 and A-247. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22729086;Dbxref=PMID:22729086	
+P38878	UniProtKB	Mutagenesis	247	247	.	.	.	Note=In lnp1-1%3B causes aberrant ER morphology%3B when associaetd with A-223%2C A-226 and A-244. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22729086;Dbxref=PMID:22729086	
+##sequence-region Q04396 1 274
+Q04396	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000220919;Note=Lipid phosphate phosphatase 1	
+Q04396	UniProtKB	Topological domain	1	15	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Transmembrane	16	33	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Topological domain	34	69	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Transmembrane	70	87	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Topological domain	88	117	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Transmembrane	118	139	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Topological domain	140	189	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Transmembrane	190	203	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Topological domain	204	214	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Transmembrane	215	231	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Topological domain	232	237	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Transmembrane	238	255	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Topological domain	256	274	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04396	UniProtKB	Region	136	144	.	.	.	Note=Phosphatase sequence motif I	
+Q04396	UniProtKB	Region	186	189	.	.	.	Note=Phosphatase sequence motif II	
+Q04396	UniProtKB	Region	228	239	.	.	.	Note=Phosphatase sequence motif III	
+##sequence-region P53281 1 241
+P53281	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53281	UniProtKB	Chain	2	241	.	.	.	ID=PRO_0000202825;Note=LAS seventeen-binding protein 1	
+P53281	UniProtKB	Domain	53	112	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P53281	UniProtKB	Motif	135	138	.	.	.	Note=PY motif	
+P53281	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53281	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53281	UniProtKB	Modified residue	114	114	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53281	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53281	UniProtKB	Cross-link	41	41	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P53281	UniProtKB	Cross-link	79	79	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P53281	UniProtKB	Cross-link	118	118	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P53281	UniProtKB	Cross-link	219	219	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P53281	UniProtKB	Mutagenesis	90	90	.	.	.	Note=Abolishes interaction with LAS17%2C but not with SUP35. Blocks colocalization with actin. W->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21777813;Dbxref=PMID:21777813	
+##sequence-region P42838 1 414
+P42838	UniProtKB	Chain	1	414	.	.	.	ID=PRO_0000207671;Note=Alkylphosphocholine resistance protein LEM3	
+P42838	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42838	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42838	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P42838	UniProtKB	Glycosylation	113	113	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42838	UniProtKB	Glycosylation	240	240	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42838	UniProtKB	Glycosylation	256	256	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42838	UniProtKB	Glycosylation	279	279	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42838	UniProtKB	Glycosylation	298	298	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42838	UniProtKB	Glycosylation	332	332	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P06208 1 619
+P06208	UniProtKB	Chain	1	619	.	.	.	ID=PRO_0000001046;Note=2-isopropylmalate synthase	
+P06208	UniProtKB	Domain	61	336	.	.	.	Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151	
+P06208	UniProtKB	Alternative sequence	1	30	.	.	.	ID=VSP_018640;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32875 1 414
+P32875	UniProtKB	Transit peptide	1	18	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123	
+P32875	UniProtKB	Chain	19	414	.	.	.	ID=PRO_0000017726;Note=Lipoyl synthase%2C mitochondrial	
+P32875	UniProtKB	Metal binding	150	150	.	.	.	Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123	
+P32875	UniProtKB	Metal binding	155	155	.	.	.	Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123	
+P32875	UniProtKB	Metal binding	161	161	.	.	.	Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123	
+P32875	UniProtKB	Metal binding	181	181	.	.	.	Note=Iron-sulfur 2 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123	
+P32875	UniProtKB	Metal binding	185	185	.	.	.	Note=Iron-sulfur 2 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123	
+P32875	UniProtKB	Metal binding	188	188	.	.	.	Note=Iron-sulfur 2 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123	
+##sequence-region P36775 1 1133
+P36775	UniProtKB	Transit peptide	1	37	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03120	
+P36775	UniProtKB	Propeptide	38	98	.	.	.	ID=PRO_0000395761;Note=Removed in mature form%3B by autocatalysis;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03120,ECO:0000269|PubMed:9405361,ECO:0000269|PubMed:9724747;Dbxref=PMID:9405361,PMID:9724747	
+P36775	UniProtKB	Chain	99	1133	.	.	.	ID=PRO_0000026733;Note=Lon protease homolog%2C mitochondrial	
+P36775	UniProtKB	Domain	182	478	.	.	.	Note=Lon N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01123	
+P36775	UniProtKB	Domain	923	1109	.	.	.	Note=Lon proteolytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01122	
+P36775	UniProtKB	Nucleotide binding	632	639	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03120	
+P36775	UniProtKB	Active site	1015	1015	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03120	
+P36775	UniProtKB	Active site	1058	1058	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03120	
+P36775	UniProtKB	Mutagenesis	638	638	.	.	.	Note=Abolishes ATP-binding. K->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8810243,ECO:0000269|PubMed:9405361;Dbxref=PMID:8810243,PMID:9405361	
+P36775	UniProtKB	Mutagenesis	1015	1015	.	.	.	Note=Abolishes peptidase activity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8810243,ECO:0000269|PubMed:9405361;Dbxref=PMID:8810243,PMID:9405361	
+P36775	UniProtKB	Sequence conflict	509	509	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38131 1 464
+P38131	UniProtKB	Chain	1	464	.	.	.	ID=PRO_0000208245;Note=Probable mannosyltransferase KTR4	
+P38131	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38131	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38131	UniProtKB	Topological domain	33	464	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38131	UniProtKB	Region	33	130	.	.	.	Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38131	UniProtKB	Region	131	464	.	.	.	Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38131	UniProtKB	Active site	352	352	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38131	UniProtKB	Helix	71	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	95	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Turn	128	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	133	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	146	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	168	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	178	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	194	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	212	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Turn	228	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	233	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	256	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	275	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	286	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	291	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	302	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	314	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	323	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	333	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	345	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	351	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	356	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	362	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	376	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	384	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	398	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	401	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Beta strand	429	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	440	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	448	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+P38131	UniProtKB	Helix	458	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07	
+##sequence-region Q08218 1 356
+Q08218	UniProtKB	Chain	1	356	.	.	.	ID=PRO_0000235923;Note=Outer spore wall protein LDS2	
+Q08218	UniProtKB	Topological domain	1	92	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31379	
+Q08218	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08218	UniProtKB	Topological domain	114	115	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31379	
+Q08218	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08218	UniProtKB	Topological domain	137	213	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31379	
+Q08218	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08218	UniProtKB	Topological domain	235	294	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31379	
+Q08218	UniProtKB	Transmembrane	295	315	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08218	UniProtKB	Topological domain	316	356	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31379	
+##sequence-region P28742 1 1111
+P28742	UniProtKB	Chain	1	1111	.	.	.	ID=PRO_0000125369;Note=Kinesin-like protein KIP1	
+P28742	UniProtKB	Domain	52	410	.	.	.	Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P28742	UniProtKB	Nucleotide binding	141	148	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P28742	UniProtKB	Coiled coil	424	510	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28742	UniProtKB	Coiled coil	648	670	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28742	UniProtKB	Coiled coil	710	780	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28742	UniProtKB	Coiled coil	808	828	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38169 1 460
+P38169	UniProtKB	Chain	1	460	.	.	.	ID=PRO_0000020823;Note=Kynurenine 3-monooxygenase	
+P38169	UniProtKB	Beta strand	4	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	12	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	27	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	50	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	56	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	67	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Turn	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	82	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	92	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J34	
+P38169	UniProtKB	Beta strand	104	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	109	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Turn	121	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	126	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	131	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	143	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Turn	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	156	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	173	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	185	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	194	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Turn	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	220	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	230	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	241	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	249	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	259	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	271	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Turn	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	279	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	295	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	302	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J36	
+P38169	UniProtKB	Turn	305	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Beta strand	309	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	314	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Turn	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	326	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Turn	344	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Helix	348	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+P38169	UniProtKB	Turn	384	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33	
+##sequence-region P38620 1 318
+P38620	UniProtKB	Chain	1	318	.	.	.	ID=PRO_0000141087;Note=Ribose-phosphate pyrophosphokinase 2	
+P38620	UniProtKB	Metal binding	132	132	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38620	UniProtKB	Metal binding	134	134	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38620	UniProtKB	Metal binding	143	143	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38620	UniProtKB	Metal binding	147	147	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12265 1 496
+Q12265	UniProtKB	Chain	1	496	.	.	.	ID=PRO_0000141090;Note=Ribose-phosphate pyrophosphokinase 5	
+Q12265	UniProtKB	Metal binding	242	242	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12265	UniProtKB	Metal binding	244	244	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12265	UniProtKB	Metal binding	253	253	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12265	UniProtKB	Metal binding	257	257	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12265	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12265	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12265	UniProtKB	Modified residue	123	123	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12265	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q12265	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358;Dbxref=PMID:15665377,PMID:17287358	
+Q12265	UniProtKB	Modified residue	332	332	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P34253 1 313
+P34253	UniProtKB	Chain	1	313	.	.	.	ID=PRO_0000084335;Note=Protein KTI12	
+P34253	UniProtKB	Nucleotide binding	8	15	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34253	UniProtKB	Sequence conflict	103	103	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P34253	UniProtKB	Sequence conflict	150	150	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P27810 1 393
+P27810	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000208242;Note=Alpha-1%2C2 mannosyltransferase KTR1	
+P27810	UniProtKB	Topological domain	1	16	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27810	UniProtKB	Transmembrane	17	34	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27810	UniProtKB	Topological domain	35	393	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27810	UniProtKB	Region	35	68	.	.	.	Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27810	UniProtKB	Region	69	393	.	.	.	Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27810	UniProtKB	Active site	280	280	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27810	UniProtKB	Glycosylation	120	120	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q92325 1 660
+Q92325	UniProtKB	Chain	1	660	.	.	.	ID=PRO_0000084352;Note=Cullin-associated NEDD8-dissociated protein 1 homolog	
+Q92325	UniProtKB	Compositional bias	344	393	.	.	.	Note=Asp-rich	
+Q92325	UniProtKB	Cross-link	16	16	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)	
+Q92325	UniProtKB	Mutagenesis	16	16	.	.	.	Note=Does not affect interaction with CDC53. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19942853;Dbxref=PMID:19942853	
+Q92325	UniProtKB	Mutagenesis	17	23	.	.	.	Note=Decreased interaction with CDC53. DNDLKYM->ANALKAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19942853;Dbxref=PMID:19942853	
+Q92325	UniProtKB	Mutagenesis	551	552	.	.	.	Note=Decreased interaction with CDC53. GN->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19942853;Dbxref=PMID:19942853	
+Q92325	UniProtKB	Sequence conflict	13	13	.	.	.	Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q92325	UniProtKB	Sequence conflict	156	157	.	.	.	Note=QL->HV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q92325	UniProtKB	Sequence conflict	486	491	.	.	.	Note=CTLAHT->VSYAI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12446 1 633
+Q12446	UniProtKB	Chain	1	633	.	.	.	ID=PRO_0000084361;Note=Proline-rich protein LAS17	
+Q12446	UniProtKB	Domain	16	127	.	.	.	Note=WH1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00410	
+Q12446	UniProtKB	Domain	547	567	.	.	.	Note=WH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00406	
+Q12446	UniProtKB	Compositional bias	185	529	.	.	.	Note=Pro-rich	
+Q12446	UniProtKB	Compositional bias	185	190	.	.	.	Note=Poly-Pro	
+Q12446	UniProtKB	Compositional bias	323	329	.	.	.	Note=Poly-Pro	
+Q12446	UniProtKB	Compositional bias	342	348	.	.	.	Note=Poly-Pro	
+Q12446	UniProtKB	Compositional bias	352	358	.	.	.	Note=Poly-Pro	
+Q12446	UniProtKB	Compositional bias	385	391	.	.	.	Note=Poly-Pro	
+Q12446	UniProtKB	Compositional bias	427	431	.	.	.	Note=Poly-Pro	
+Q12446	UniProtKB	Compositional bias	470	474	.	.	.	Note=Poly-Pro	
+Q12446	UniProtKB	Compositional bias	503	507	.	.	.	Note=Poly-Pro	
+Q12446	UniProtKB	Compositional bias	520	526	.	.	.	Note=Poly-Pro	
+Q12446	UniProtKB	Modified residue	334	334	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12446	UniProtKB	Modified residue	337	337	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12446	UniProtKB	Modified residue	588	588	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P00572 1 216
+P00572	UniProtKB	Chain	1	216	.	.	.	ID=PRO_0000155214;Note=Thymidylate kinase	
+P00572	UniProtKB	Nucleotide binding	12	19	.	.	.	Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00572	UniProtKB	Sequence conflict	57	57	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00572	UniProtKB	Sequence conflict	188	188	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00572	UniProtKB	Beta strand	7	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Beta strand	14	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Helix	18	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Beta strand	31	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Helix	44	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Helix	62	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Helix	77	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Beta strand	89	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Helix	96	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Helix	113	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Beta strand	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2TMK	
+P00572	UniProtKB	Beta strand	127	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Helix	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Beta strand	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Helix	154	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Beta strand	178	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+P00572	UniProtKB	Helix	189	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK	
+##sequence-region P31379 1 325
+P31379	UniProtKB	Chain	1	325	.	.	.	ID=PRO_0000202413;Note=Outer spore wall protein LDS1	
+P31379	UniProtKB	Topological domain	1	91	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P31379	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31379	UniProtKB	Topological domain	113	118	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P31379	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31379	UniProtKB	Topological domain	140	208	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P31379	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31379	UniProtKB	Topological domain	230	263	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P31379	UniProtKB	Transmembrane	264	284	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31379	UniProtKB	Topological domain	285	325	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+##sequence-region P04173 1 364
+P04173	UniProtKB	Chain	1	364	.	.	.	ID=PRO_0000083623;Note=3-isopropylmalate dehydrogenase	
+P04173	UniProtKB	Nucleotide binding	79	90	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04173	UniProtKB	Nucleotide binding	289	300	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04173	UniProtKB	Metal binding	225	225	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04173	UniProtKB	Metal binding	250	250	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04173	UniProtKB	Metal binding	254	254	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04173	UniProtKB	Binding site	97	97	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04173	UniProtKB	Binding site	107	107	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04173	UniProtKB	Binding site	136	136	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04173	UniProtKB	Binding site	225	225	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04173	UniProtKB	Site	143	143	.	.	.	Note=Important for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04173	UniProtKB	Site	192	192	.	.	.	Note=Important for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04173	UniProtKB	Sequence conflict	69	69	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04173	UniProtKB	Sequence conflict	69	69	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04173	UniProtKB	Sequence conflict	69	69	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04173	UniProtKB	Sequence conflict	300	300	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04173	UniProtKB	Sequence conflict	300	300	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38702 1 357
+P38702	UniProtKB	Chain	1	357	.	.	.	ID=PRO_0000090683;Note=Mitochondrial carrier protein LEU5	
+P38702	UniProtKB	Transmembrane	31	47	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38702	UniProtKB	Transmembrane	103	119	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38702	UniProtKB	Transmembrane	136	153	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38702	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38702	UniProtKB	Transmembrane	269	285	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38702	UniProtKB	Transmembrane	325	347	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38702	UniProtKB	Repeat	31	122	.	.	.	Note=Solcar 1	
+P38702	UniProtKB	Repeat	130	231	.	.	.	Note=Solcar 2	
+P38702	UniProtKB	Repeat	262	354	.	.	.	Note=Solcar 3	
+##sequence-region P07264 1 779
+P07264	UniProtKB	Chain	1	779	.	.	.	ID=PRO_0000076894;Note=3-isopropylmalate dehydratase	
+P07264	UniProtKB	Metal binding	360	360	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07264	UniProtKB	Metal binding	421	421	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07264	UniProtKB	Metal binding	424	424	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07264	UniProtKB	Modified residue	488	488	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P07264	UniProtKB	Modified residue	494	494	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07264	UniProtKB	Modified residue	495	495	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07264	UniProtKB	Sequence conflict	291	291	.	.	.	Note=N->TLKH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07264	UniProtKB	Sequence conflict	423	423	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07264	UniProtKB	Sequence conflict	459	459	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07264	UniProtKB	Sequence conflict	744	744	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07264	UniProtKB	Sequence conflict	744	744	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02796 1 332
+Q02796	UniProtKB	Chain	1	332	.	.	.	ID=PRO_0000076234;Note=Transcriptional regulatory protein LGE1	
+Q02796	UniProtKB	Coiled coil	284	328	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02796	UniProtKB	Sequence conflict	28	28	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53966 1 522
+P53966	UniProtKB	Chain	1	522	.	.	.	ID=PRO_0000208246;Note=Probable mannosyltransferase KTR5	
+P53966	UniProtKB	Topological domain	1	16	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53966	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53966	UniProtKB	Topological domain	38	522	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53966	UniProtKB	Region	38	82	.	.	.	Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53966	UniProtKB	Region	83	522	.	.	.	Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53966	UniProtKB	Active site	363	363	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53966	UniProtKB	Glycosylation	86	86	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32807 1 602
+P32807	UniProtKB	Chain	1	602	.	.	.	ID=PRO_0000210184;Note=ATP-dependent DNA helicase II subunit 1	
+P32807	UniProtKB	Domain	268	483	.	.	.	Note=Ku	
+P32807	UniProtKB	Modified residue	370	370	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32807	UniProtKB	Modified residue	371	371	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32807	UniProtKB	Modified residue	372	372	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32807	UniProtKB	Natural variant	21	21	.	.	.	Note=In strain: ABYS 60 and SK1. T->K	
+P32807	UniProtKB	Natural variant	50	50	.	.	.	Note=In strain: ABYS 60%2C DBVPG6044%2C SK1 and YPS128. E->D	
+P32807	UniProtKB	Natural variant	230	230	.	.	.	Note=In strain: DBVPG6044. T->A	
+P32807	UniProtKB	Natural variant	368	368	.	.	.	Note=In strain: YPS128. F->I	
+P32807	UniProtKB	Natural variant	562	562	.	.	.	Note=In strain: ABYS 60%2C DBVPG6044%2C SK1 and YPS128. I->T	
+P32807	UniProtKB	Sequence conflict	3	3	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32807	UniProtKB	Sequence conflict	87	87	.	.	.	Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25045 1 558
+P25045	UniProtKB	Chain	1	558	.	.	.	ID=PRO_0000163856;Note=Serine palmitoyltransferase 1	
+P25045	UniProtKB	Topological domain	1	49	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Transmembrane	50	84	.	.	.	Note=Helical	
+P25045	UniProtKB	Topological domain	85	341	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Transmembrane	342	371	.	.	.	Note=Helical	
+P25045	UniProtKB	Topological domain	372	424	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Transmembrane	425	457	.	.	.	Note=Helical	
+P25045	UniProtKB	Topological domain	458	558	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P25045	UniProtKB	Mutagenesis	24	26	.	.	.	Note=No effect on stability. No effect on LCB2 stabilization. YLW->DRS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Mutagenesis	50	85	.	.	.	Note=No effect on stability. No effect on LCB2 stabilization. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Mutagenesis	66	68	.	.	.	Note=No effect on stability. No effect on LCB2 stabilization. YGI->DVK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Mutagenesis	180	180	.	.	.	Note=Loss of activity. No effect on interaction with LCB2. C->W%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11781309;Dbxref=PMID:11781309	
+P25045	UniProtKB	Mutagenesis	191	191	.	.	.	Note=Loss of activity. No effect on interaction with LCB2. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11781309;Dbxref=PMID:11781309	
+P25045	UniProtKB	Mutagenesis	342	371	.	.	.	Note=Unstable. Destabilizes LCB2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Mutagenesis	371	386	.	.	.	Note=No effect on stability. Destabilizes LCB2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Mutagenesis	386	416	.	.	.	Note=Unstable. Destabilizes LCB2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Mutagenesis	416	425	.	.	.	Note=No effect on stability. Destabilizes LCB2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Mutagenesis	433	458	.	.	.	Note=Unstable. Destabilizes LCB2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Mutagenesis	549	550	.	.	.	Note=No effect on stability. Partially stabilizes LCB2. IL->AS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Mutagenesis	549	550	.	.	.	Note=No effect on stability. Partially stabilizes LCB2. IL->PR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854	
+P25045	UniProtKB	Sequence conflict	443	443	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06147 1 687
+Q06147	UniProtKB	Chain	1	687	.	.	.	ID=PRO_0000255957;Note=Sphingoid long chain base kinase 5	
+Q06147	UniProtKB	Domain	266	405	.	.	.	Note=DAGKc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q06147	UniProtKB	Nucleotide binding	276	278	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q06147	UniProtKB	Nucleotide binding	366	368	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q06147	UniProtKB	Nucleotide binding	652	654	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q06147	UniProtKB	Region	333	336	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06147	UniProtKB	Active site	335	335	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06147	UniProtKB	Binding site	308	308	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q06147	UniProtKB	Binding site	340	340	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q06147	UniProtKB	Binding site	434	434	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q06147	UniProtKB	Binding site	440	440	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q06147	UniProtKB	Lipidation	91	91	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06147	UniProtKB	Lipidation	94	94	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53153 1 274
+P53153	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000215285;Note=Probable endonuclease LCL3	
+P53153	UniProtKB	Transmembrane	15	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53153	UniProtKB	Domain	53	261	.	.	.	Note=TNase-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00272	
+P53153	UniProtKB	Active site	151	151	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00272	
+P53153	UniProtKB	Active site	159	159	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00272	
+P53153	UniProtKB	Active site	199	199	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00272	
+P53153	UniProtKB	Metal binding	156	156	.	.	.	Note=Calcium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00272	
+##sequence-region Q04081 1 328
+Q04081	UniProtKB	Chain	1	328	.	.	.	ID=PRO_0000226135;Note=Leucine carboxyl methyltransferase 1	
+Q04081	UniProtKB	Region	175	177	.	.	.	Note=S-adenosyl-L-methionine binding	
+Q04081	UniProtKB	Binding site	81	81	.	.	.	Note=S-adenosyl-L-methionine	
+Q04081	UniProtKB	Binding site	105	105	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen	
+Q04081	UniProtKB	Binding site	128	128	.	.	.	Note=S-adenosyl-L-methionine	
+Q04081	UniProtKB	Binding site	201	201	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen	
+Q04081	UniProtKB	Helix	3	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	8	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Turn	28	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	35	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	57	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	72	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Beta strand	97	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	112	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Beta strand	122	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	130	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	144	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Beta strand	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Beta strand	167	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Beta strand	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJG	
+Q04081	UniProtKB	Helix	179	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Beta strand	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJE	
+Q04081	UniProtKB	Beta strand	196	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	209	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Beta strand	224	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	243	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Turn	260	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	268	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Beta strand	278	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	286	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	296	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Helix	311	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+Q04081	UniProtKB	Beta strand	321	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD	
+##sequence-region P08638 1 886
+P08638	UniProtKB	Chain	1	886	.	.	.	ID=PRO_0000114954;Note=Regulatory protein LEU3	
+P08638	UniProtKB	DNA binding	37	67	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P08638	UniProtKB	Motif	874	882	.	.	.	Note=9aaTAD	
+P08638	UniProtKB	Compositional bias	678	697	.	.	.	Note=Asp/Glu-rich (acidic)	
+P08638	UniProtKB	Sequence conflict	504	504	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08638	UniProtKB	Helix	38	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ER8	
+P08638	UniProtKB	Helix	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ER8	
+P08638	UniProtKB	Helix	58	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ER8	
+P08638	UniProtKB	Helix	78	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ER8	
+##sequence-region P36016 1 881
+P36016	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36016	UniProtKB	Chain	21	881	.	.	.	ID=PRO_0000013556;Note=Heat shock protein 70 homolog LHS1	
+P36016	UniProtKB	Motif	878	881	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138	
+P36016	UniProtKB	Glycosylation	128	128	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36016	UniProtKB	Glycosylation	458	458	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36016	UniProtKB	Glycosylation	474	474	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36016	UniProtKB	Glycosylation	481	481	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36016	UniProtKB	Glycosylation	489	489	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36016	UniProtKB	Glycosylation	527	527	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36016	UniProtKB	Glycosylation	844	844	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36016	UniProtKB	Mutagenesis	239	239	.	.	.	Note=In allele LHS1-1%3B constitutive ATPase activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14704430;Dbxref=PMID:14704430	
+##sequence-region Q04005 1 294
+Q04005	UniProtKB	Chain	1	294	.	.	.	ID=PRO_0000076239;Note=Protein ATC1/LIC4	
+Q04005	UniProtKB	Sequence conflict	204	204	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39946 1 494
+P39946	UniProtKB	Chain	1	494	.	.	.	ID=PRO_0000051113;Note=Nuclear distribution protein PAC1	
+P39946	UniProtKB	Domain	14	46	.	.	.	Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03141	
+P39946	UniProtKB	Repeat	153	192	.	.	.	Note=WD 1	
+P39946	UniProtKB	Repeat	196	244	.	.	.	Note=WD 2	
+P39946	UniProtKB	Repeat	251	292	.	.	.	Note=WD 3	
+P39946	UniProtKB	Repeat	295	334	.	.	.	Note=WD 4	
+P39946	UniProtKB	Repeat	347	395	.	.	.	Note=WD 5	
+P39946	UniProtKB	Repeat	415	454	.	.	.	Note=WD 6	
+P39946	UniProtKB	Repeat	457	492	.	.	.	Note=WD 7	
+P39946	UniProtKB	Coiled coil	90	123	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03141	
+##sequence-region Q10740 1 671
+Q10740	UniProtKB	Chain	1	671	.	.	.	ID=PRO_0000095129;Note=Leukotriene A-4 hydrolase homolog	
+Q10740	UniProtKB	Region	184	186	.	.	.	Note=Substrate binding	
+Q10740	UniProtKB	Region	311	316	.	.	.	Note=Substrate binding	
+Q10740	UniProtKB	Active site	341	341	.	.	.	Note=Proton acceptor	
+Q10740	UniProtKB	Active site	429	429	.	.	.	Note=Proton donor	
+Q10740	UniProtKB	Metal binding	340	340	.	.	.	Note=Zinc%3B catalytic	
+Q10740	UniProtKB	Metal binding	344	344	.	.	.	Note=Zinc%3B catalytic	
+Q10740	UniProtKB	Metal binding	363	363	.	.	.	Note=Zinc%3B catalytic	
+Q10740	UniProtKB	Mutagenesis	244	244	.	.	.	Note=Reduces strongly the substrate affinity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16597475;Dbxref=PMID:16597475	
+Q10740	UniProtKB	Mutagenesis	316	316	.	.	.	Note=Abolishes the aminopeptidase activity. E->A%2CQ%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16024909;Dbxref=PMID:16024909	
+Q10740	UniProtKB	Mutagenesis	340	340	.	.	.	Note=Abolishes the epoxide hydrolase and aminopeptidase activities. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994	
+Q10740	UniProtKB	Mutagenesis	341	341	.	.	.	Note=Abolishes aminopeptidase activity. No effect on the epoxide hydrolase activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994	
+Q10740	UniProtKB	Mutagenesis	344	344	.	.	.	Note=Abolishes the epoxide hydrolase and aminopeptidase activities. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994	
+Q10740	UniProtKB	Mutagenesis	363	363	.	.	.	Note=Abolishes the epoxide hydrolase activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994	
+Q10740	UniProtKB	Mutagenesis	424	424	.	.	.	Note=Increases the aminopeptidase activity and decreases the epoxide hydrolase activity. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994	
+Q10740	UniProtKB	Mutagenesis	429	429	.	.	.	Note=Abolishes the aminopeptidase activity and decreases the epoxide hydrolase activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994	
+Q10740	UniProtKB	Mutagenesis	627	627	.	.	.	Note=Abolishes the aminopeptidase activity. R->K%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16024909;Dbxref=PMID:16024909	
+Q10740	UniProtKB	Helix	43	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	67	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Turn	80	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	84	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XPY	
+Q10740	UniProtKB	Beta strand	105	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	111	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Turn	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	140	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	147	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	164	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Turn	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	175	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XPY	
+Q10740	UniProtKB	Beta strand	180	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Turn	186	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	204	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	216	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	232	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	243	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	248	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	254	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	262	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	268	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Turn	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	282	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XPZ	
+Q10740	UniProtKB	Beta strand	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	312	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	330	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	336	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Turn	348	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	351	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	356	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	360	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	380	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	401	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XPZ	
+Q10740	UniProtKB	Helix	404	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	416	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	420	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	427	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	446	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Turn	460	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	463	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	467	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	482	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	490	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	508	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Turn	524	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	530	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	539	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	547	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Beta strand	562	565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XPZ	
+Q10740	UniProtKB	Helix	572	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	576	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	587	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	596	608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	612	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	615	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Turn	622	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	628	639	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	643	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	654	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+Q10740	UniProtKB	Helix	659	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0	
+##sequence-region P40026 1 464
+P40026	UniProtKB	Chain	1	464	.	.	.	ID=PRO_0000084329;Note=DNA repair protein KRE29	
+P40026	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40026	UniProtKB	Modified residue	101	101	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P27809 1 442
+P27809	UniProtKB	Chain	1	442	.	.	.	ID=PRO_0000208241;Note=Glycolipid 2-alpha-mannosyltransferase	
+P27809	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27809	UniProtKB	Transmembrane	12	30	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P27809	UniProtKB	Topological domain	31	442	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27809	UniProtKB	Region	31	118	.	.	.	Note=Stem region	
+P27809	UniProtKB	Region	119	442	.	.	.	Note=Catalytic	
+P27809	UniProtKB	Active site	329	329	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27809	UniProtKB	Glycosylation	197	197	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1550992;Dbxref=PMID:1550992	
+P27809	UniProtKB	Helix	106	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Beta strand	123	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	134	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Turn	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Beta strand	156	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	166	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Beta strand	180	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	198	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Turn	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Turn	213	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	218	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	231	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Beta strand	241	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	260	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Beta strand	271	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Beta strand	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	281	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	287	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	299	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	308	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Beta strand	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Beta strand	328	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	333	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	339	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	353	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	361	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	375	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Beta strand	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Beta strand	386	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Beta strand	391	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	398	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	410	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	422	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+P27809	UniProtKB	Helix	437	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N	
+##sequence-region P39005 1 276
+P39005	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39005	UniProtKB	Chain	22	276	.	.	.	ID=PRO_0000016849;Note=Cell wall synthesis protein KRE9	
+##sequence-region P25586 1 316
+P25586	UniProtKB	Chain	1	316	.	.	.	ID=PRO_0000202553;Note=KRR1 small subunit processome component	
+P25586	UniProtKB	Domain	122	192	.	.	.	Note=KH	
+P25586	UniProtKB	Mutagenesis	20	20	.	.	.	Note=In temperature-sensitive mutant KRR1-17%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with N-66%3B R-162 and A-261. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267	
+P25586	UniProtKB	Mutagenesis	45	45	.	.	.	Note=In temperature-sensitive mutant KRR1-18%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with S-95 and G-207. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267	
+P25586	UniProtKB	Mutagenesis	66	66	.	.	.	Note=In temperature-sensitive mutant KRR1-17%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with E-20%3B R-162 and A-261. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267	
+P25586	UniProtKB	Mutagenesis	95	95	.	.	.	Note=In temperature-sensitive mutant KRR1-18%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with L-45 and G-207. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267	
+P25586	UniProtKB	Mutagenesis	162	162	.	.	.	Note=In temperature-sensitive mutant KRR1-17%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with E-20%3B N-66 and A-261. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267	
+P25586	UniProtKB	Mutagenesis	207	207	.	.	.	Note=In temperature-sensitive mutant KRR1-18%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with L-45 and S-95. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267	
+P25586	UniProtKB	Mutagenesis	261	261	.	.	.	Note=In temperature-sensitive mutant KRR1-17%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with E-20%3B N-66 and R-162. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267	
+P25586	UniProtKB	Beta strand	40	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Helix	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Helix	50	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Turn	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Beta strand	70	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Turn	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Beta strand	79	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Helix	93	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Helix	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Helix	114	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Beta strand	122	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Beta strand	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Helix	136	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Helix	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Helix	151	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Beta strand	163	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Beta strand	170	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Helix	177	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+P25586	UniProtKB	Helix	197	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF	
+##sequence-region P30624 1 700
+P30624	UniProtKB	Chain	1	700	.	.	.	ID=PRO_0000193119;Note=Long-chain-fatty-acid--CoA ligase 1	
+P30624	UniProtKB	Cross-link	189	189	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P32486 1 720
+P32486	UniProtKB	Chain	1	720	.	.	.	ID=PRO_0000084331;Note=Beta-glucan synthesis-associated protein KRE6	
+P32486	UniProtKB	Topological domain	1	252	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32486	UniProtKB	Transmembrane	253	273	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32486	UniProtKB	Topological domain	274	720	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32486	UniProtKB	Domain	289	664	.	.	.	Note=GH16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01098	
+P32486	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32486	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32486	UniProtKB	Modified residue	133	133	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32486	UniProtKB	Modified residue	134	134	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32486	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32486	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32486	UniProtKB	Glycosylation	374	374	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32486	UniProtKB	Glycosylation	461	461	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32486	UniProtKB	Glycosylation	538	538	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32486	UniProtKB	Glycosylation	563	563	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32486	UniProtKB	Glycosylation	691	691	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32486	UniProtKB	Sequence conflict	310	310	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32486	UniProtKB	Sequence conflict	310	310	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32486	UniProtKB	Sequence conflict	483	483	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32486	UniProtKB	Sequence conflict	483	483	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39526 1 2014
+P39526	UniProtKB	Chain	1	2014	.	.	.	ID=PRO_0000203015;Note=AP-1 accessory protein LAA1	
+##sequence-region P47912 1 694
+P47912	UniProtKB	Chain	1	694	.	.	.	ID=PRO_0000193122;Note=Long-chain-fatty-acid--CoA ligase 4	
+P47912	UniProtKB	Sequence conflict	552	552	.	.	.	Note=N->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47912	UniProtKB	Sequence conflict	631	631	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33399 1 275
+P33399	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P33399	UniProtKB	Chain	2	275	.	.	.	ID=PRO_0000207608;Note=La protein homolog	
+P33399	UniProtKB	Domain	23	112	.	.	.	Note=HTH La-type RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00332	
+P33399	UniProtKB	Domain	123	216	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P33399	UniProtKB	Motif	240	256	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33399	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P33399	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:11720288;Dbxref=PMID:17287358,PMID:18407956,PMID:11720288	
+P33399	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:11720288;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198,PMID:11720288	
+P33399	UniProtKB	Modified residue	104	104	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23865587;Dbxref=PMID:23865587	
+P33399	UniProtKB	Modified residue	230	230	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P33399	UniProtKB	Modified residue	233	233	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P33399	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000269|PubMed:11720288;Dbxref=PMID:17287358,PMID:11720288	
+P33399	UniProtKB	Mutagenesis	15	15	.	.	.	Note=Prevents phosphorylation%3B when associated with A-19 and A-235. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11720288;Dbxref=PMID:11720288	
+P33399	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Prevents phosphorylation%3B when associated with A-15 and A-235. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11720288;Dbxref=PMID:11720288	
+P33399	UniProtKB	Mutagenesis	235	235	.	.	.	Note=Prevents phosphorylation%3B when associated with A-15 and A-19. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11720288;Dbxref=PMID:11720288	
+##sequence-region Q03579 1 150
+Q03579	UniProtKB	Chain	1	150	.	.	.	ID=PRO_0000203352;Note=Ceramide synthase subunit LIP1	
+Q03579	UniProtKB	Topological domain	1	20	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15692566;Dbxref=PMID:15692566	
+Q03579	UniProtKB	Transmembrane	21	40	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03579	UniProtKB	Topological domain	41	150	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15692566;Dbxref=PMID:15692566	
+##sequence-region Q05979 1 453
+Q05979	UniProtKB	Chain	1	453	.	.	.	ID=PRO_0000218665;Note=Kynureninase	
+Q05979	UniProtKB	Region	139	142	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017	
+Q05979	UniProtKB	Binding site	111	111	.	.	.	Note=Pyridoxal phosphate%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017	
+Q05979	UniProtKB	Binding site	112	112	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017	
+Q05979	UniProtKB	Binding site	196	196	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017	
+Q05979	UniProtKB	Binding site	226	226	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017	
+Q05979	UniProtKB	Binding site	229	229	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017	
+Q05979	UniProtKB	Binding site	251	251	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017	
+Q05979	UniProtKB	Binding site	286	286	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017	
+Q05979	UniProtKB	Binding site	314	314	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017	
+Q05979	UniProtKB	Modified residue	252	252	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017	
+##sequence-region P28496 1 418
+P28496	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P28496	UniProtKB	Chain	2	418	.	.	.	ID=PRO_0000185535;Note=Sphingosine N-acyltransferase LAC1	
+P28496	UniProtKB	Topological domain	2	81	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Topological domain	103	134	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Transmembrane	135	155	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Topological domain	156	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Topological domain	194	221	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Transmembrane	222	242	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Topological domain	243	259	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Transmembrane	260	280	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Topological domain	281	296	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Transmembrane	297	317	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Topological domain	318	355	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Transmembrane	356	376	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Topological domain	377	418	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28496	UniProtKB	Domain	168	384	.	.	.	Note=TLC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00205	
+P28496	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P28496	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38703	
+P28496	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38703	
+P28496	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38703 1 411
+P38703	UniProtKB	Chain	1	411	.	.	.	ID=PRO_0000185527;Note=Sphingosine N-acyltransferase LAG1	
+P38703	UniProtKB	Topological domain	1	81	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Topological domain	103	134	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Transmembrane	135	155	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Topological domain	156	176	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Topological domain	198	211	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Transmembrane	212	232	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Topological domain	233	251	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Transmembrane	252	272	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Topological domain	273	296	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Transmembrane	297	317	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Topological domain	318	355	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Transmembrane	356	376	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Topological domain	377	411	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38703	UniProtKB	Domain	168	384	.	.	.	Note=TLC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00205	
+P38703	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38703	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38703	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38851 1 1228
+P38851	UniProtKB	Chain	1	1228	.	.	.	ID=PRO_0000202927;Note=Membrane-anchored lipid-binding protein LAM1	
+P38851	UniProtKB	Topological domain	1	1062	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26001273;Dbxref=PMID:26001273	
+P38851	UniProtKB	Transmembrane	1063	1083	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38851	UniProtKB	Topological domain	1084	1228	.	.	.	Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38717	
+P38851	UniProtKB	Domain	308	421	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P38851	UniProtKB	Domain	773	978	.	.	.	Note=VASt;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114	
+P38851	UniProtKB	Glycosylation	1205	1205	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+##sequence-region Q08001 1 693
+Q08001	UniProtKB	Chain	1	693	.	.	.	ID=PRO_0000247247;Note=Membrane-anchored lipid-binding protein LAM6	
+Q08001	UniProtKB	Topological domain	1	630	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08001	UniProtKB	Transmembrane	631	651	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08001	UniProtKB	Topological domain	652	693	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08001	UniProtKB	Domain	164	230	.	.	.	Note=GRAM;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08001	UniProtKB	Domain	403	576	.	.	.	Note=VASt;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114	
+Q08001	UniProtKB	Compositional bias	347	360	.	.	.	Note=Poly-Ser	
+Q08001	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08001	UniProtKB	Modified residue	591	591	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08001	UniProtKB	Modified residue	593	593	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08001	UniProtKB	Modified residue	594	594	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q08001	UniProtKB	Modified residue	597	597	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q04377 1 747
+Q04377	UniProtKB	Chain	1	747	.	.	.	ID=PRO_0000227715;Note=DNA damage checkpoint protein LCD1	
+Q04377	UniProtKB	Coiled coil	62	139	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04377	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04377	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04377	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04377	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Impairs dsDNA and ssDNA binding of the MEC1-LCD1 complex. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983176;Dbxref=PMID:11983176	
+Q04377	UniProtKB	Mutagenesis	179	179	.	.	.	Note=Impairs dsDNA and ssDNA binding of the MEC1-LCD1 complex. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983176;Dbxref=PMID:11983176	
+##sequence-region Q02786 1 101
+Q02786	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02786	UniProtKB	Chain	18	81	.	.	.	ID=PRO_0000238639;Note=Long chronological lifespan protein 1	
+Q02786	UniProtKB	Propeptide	82	101	.	.	.	ID=PRO_0000238640;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02786	UniProtKB	Lipidation	81	81	.	.	.	Note=GPI-anchor amidated serine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08045 1 131
+Q08045	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08045	UniProtKB	Chain	25	131	.	.	.	ID=PRO_0000247350;Note=Long chronological lifespan protein 2	
+Q08045	UniProtKB	Compositional bias	32	40	.	.	.	Note=Poly-Gln	
+##sequence-region Q07887 1 179
+Q07887	UniProtKB	Chain	1	179	.	.	.	ID=PRO_0000240386;Note=Protein LDB18	
+##sequence-region P38139 1 375
+P38139	UniProtKB	Chain	1	375	.	.	.	ID=PRO_0000090373;Note=Lipid droplet hydrolase 1	
+P38139	UniProtKB	Domain	88	358	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38139	UniProtKB	Motif	373	375	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38139	UniProtKB	Active site	177	177	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38139	UniProtKB	Active site	351	351	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38139	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Abolishes serine hydrolase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21478434;Dbxref=PMID:21478434	
+P38139	UniProtKB	Sequence conflict	63	63	.	.	.	Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38139	UniProtKB	Sequence conflict	63	63	.	.	.	Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38439 1 464
+P38439	UniProtKB	Chain	1	464	.	.	.	ID=PRO_0000084406;Note=RNA polymerase-associated protein LEO1	
+P38439	UniProtKB	Compositional bias	68	74	.	.	.	Note=Poly-Asp	
+P38439	UniProtKB	Compositional bias	383	464	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P38439	UniProtKB	Modified residue	105	105	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38439	UniProtKB	Modified residue	132	132	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38439	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38439	UniProtKB	Modified residue	358	358	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38439	UniProtKB	Modified residue	372	372	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38439	UniProtKB	Sequence conflict	134	134	.	.	.	Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38439	UniProtKB	Sequence conflict	320	320	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38852 1 340
+P38852	UniProtKB	Chain	1	340	.	.	.	ID=PRO_0000195038;Note=Protein LIN1	
+P38852	UniProtKB	Domain	282	340	.	.	.	Note=GYF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00101	
+##sequence-region Q12342 1 491
+Q12342	UniProtKB	Chain	1	491	.	.	.	ID=PRO_0000240385;Note=Protein LDB17	
+Q12342	UniProtKB	Compositional bias	475	483	.	.	.	Note=Poly-Pro	
+Q12342	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12342	UniProtKB	Modified residue	463	463	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12342	UniProtKB	Modified residue	466	466	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P53150 1 421
+P53150	UniProtKB	Chain	1	421	.	.	.	ID=PRO_0000084419;Note=Ligase-interacting factor 1	
+P53150	UniProtKB	Sequence conflict	44	44	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47055 1 219
+P47055	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47055	UniProtKB	Chain	20	219	.	.	.	ID=PRO_0000203068;Note=Outer spore wall protein 4	
+P47055	UniProtKB	Topological domain	20	170	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P47055	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47055	UniProtKB	Topological domain	192	193	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P47055	UniProtKB	Transmembrane	194	214	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47055	UniProtKB	Topological domain	215	219	.	.	.	Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P47055	UniProtKB	Glycosylation	42	42	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P47055	UniProtKB	Glycosylation	62	62	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P47055	UniProtKB	Glycosylation	136	136	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+##sequence-region P25579 1 583
+P25579	UniProtKB	Chain	1	583	.	.	.	ID=PRO_0000084482;Note=Laminarase-resistance protein LRE1	
+P25579	UniProtKB	Modified residue	393	393	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25579	UniProtKB	Modified residue	398	398	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25579	UniProtKB	Modified residue	516	516	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25579	UniProtKB	Modified residue	552	552	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53237 1 242
+P53237	UniProtKB	Chain	1	242	.	.	.	ID=PRO_0000202801;Note=Protein LST7	
+P53237	UniProtKB	Domain	48	212	.	.	.	Note=uDENN FLCN/SMCR8-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01178	
+P53237	UniProtKB	Natural variant	4	4	.	.	.	Note=In strain: SK1. T->I	
+##sequence-region Q06508 1 300
+Q06508	UniProtKB	Chain	1	300	.	.	.	ID=PRO_0000065908;Note=Lysophosphatidic acid:oleoyl-CoA acyltransferase 1	
+Q06508	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06508	UniProtKB	Motif	101	106	.	.	.	Note=HXXXXD motif	
+##sequence-region P43586 1 204
+P43586	UniProtKB	Chain	1	204	.	.	.	ID=PRO_0000202680;Note=60S ribosomal subunit assembly/export protein LOC1	
+P43586	UniProtKB	Coiled coil	120	166	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43586	UniProtKB	Compositional bias	39	199	.	.	.	Note=Lys-rich	
+P43586	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P34234 1 306
+P34234	UniProtKB	Chain	1	306	.	.	.	ID=PRO_0000203137;Note=Protein LOT5	
+##sequence-region Q12405 1 387
+Q12405	UniProtKB	Chain	1	387	.	.	.	ID=PRO_0000270570;Note=Peroxisomal membrane protein LPX1	
+Q12405	UniProtKB	Region	385	387	.	.	.	Note=Peroxisomal targeting signal type 1	
+Q12405	UniProtKB	Beta strand	5	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Beta strand	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Beta strand	32	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Turn	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Beta strand	51	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	65	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Turn	80	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Beta strand	84	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	98	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Turn	104	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	114	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6V	
+Q12405	UniProtKB	Beta strand	136	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	146	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Beta strand	163	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	194	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Beta strand	207	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	211	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Turn	223	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	229	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Beta strand	253	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	259	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	269	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	273	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Beta strand	285	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	300	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Beta strand	311	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	325	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	330	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	360	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U	
+Q12405	UniProtKB	Helix	383	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6V	
+##sequence-region P35688 1 1017
+P35688	UniProtKB	Chain	1	1017	.	.	.	ID=PRO_0000075838;Note=Rho-GTPase-activating protein LRG1	
+P35688	UniProtKB	Domain	28	88	.	.	.	Note=LIM zinc-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125	
+P35688	UniProtKB	Domain	98	148	.	.	.	Note=LIM zinc-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125	
+P35688	UniProtKB	Domain	155	184	.	.	.	Note=LIM zinc-binding 3%3B truncated;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125	
+P35688	UniProtKB	Domain	419	474	.	.	.	Note=LIM zinc-binding 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125	
+P35688	UniProtKB	Domain	730	953	.	.	.	Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172	
+P35688	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P35688	UniProtKB	Modified residue	562	562	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35688	UniProtKB	Sequence conflict	531	531	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35688	UniProtKB	Sequence conflict	766	766	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35688	UniProtKB	Sequence conflict	791	791	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35688	UniProtKB	Sequence conflict	821	821	.	.	.	Note=L->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35688	UniProtKB	Sequence conflict	838	838	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35688	UniProtKB	Sequence conflict	849	849	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35688	UniProtKB	Sequence conflict	895	895	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35688	UniProtKB	Sequence conflict	928	928	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35688	UniProtKB	Sequence conflict	935	935	.	.	.	Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35688	UniProtKB	Sequence conflict	977	1017	.	.	.	Note=INHFISTVMQSKTIDYSECDIKTPVTVKDSTTTVIQGEINK->TILFPPLCKVKQSIIPNVT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47093 1 109
+P47093	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000203088;Note=U6 snRNA-associated Sm-like protein LSm8	
+P47093	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24240276;Dbxref=PMID:24240276	
+P47093	UniProtKB	Helix	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D	
+P47093	UniProtKB	Beta strand	11	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D	
+P47093	UniProtKB	Beta strand	22	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D	
+P47093	UniProtKB	Beta strand	36	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D	
+P47093	UniProtKB	Turn	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D	
+P47093	UniProtKB	Beta strand	48	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D	
+P47093	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D	
+P47093	UniProtKB	Beta strand	61	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D	
+P47093	UniProtKB	Helix	96	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M77	
+##sequence-region P40495 1 371
+P40495	UniProtKB	Transit peptide	1	22	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40495	UniProtKB	Chain	23	371	.	.	.	ID=PRO_0000043097;Note=Homoisocitrate dehydrogenase%2C mitochondrial	
+P40495	UniProtKB	Metal binding	243	243	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40495	UniProtKB	Metal binding	267	267	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40495	UniProtKB	Metal binding	271	271	.	.	.	Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40495	UniProtKB	Binding site	114	114	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40495	UniProtKB	Binding site	124	124	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40495	UniProtKB	Binding site	143	143	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40495	UniProtKB	Binding site	243	243	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40495	UniProtKB	Site	150	150	.	.	.	Note=Critical for catalysis	
+P40495	UniProtKB	Site	206	206	.	.	.	Note=Critical for catalysis	
+P40495	UniProtKB	Modified residue	98	98	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40495	UniProtKB	Mutagenesis	150	150	.	.	.	Note=Strongly reduced enzyme activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19530703;Dbxref=PMID:19530703	
+P40495	UniProtKB	Mutagenesis	206	206	.	.	.	Note=Strongly reduced enzyme activity. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19530703;Dbxref=PMID:19530703	
+##sequence-region P47051 1 409
+P47051	UniProtKB	Chain	1	409	.	.	.	ID=PRO_0000203066;Note=Putative lipoate-protein ligase A	
+P47051	UniProtKB	Domain	146	330	.	.	.	Note=BPL/LPL catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01067	
+P47051	UniProtKB	Nucleotide binding	193	196	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47051	UniProtKB	Binding site	188	188	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47051	UniProtKB	Binding site	249	249	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47051	UniProtKB	Binding site	249	249	.	.	.	Note=Lipoate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04087 1 347
+Q04087	UniProtKB	Chain	1	347	.	.	.	ID=PRO_0000257808;Note=Monopolin complex subunit LRS4	
+Q04087	UniProtKB	Coiled coil	46	118	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04087	UniProtKB	Modified residue	168	168	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04087	UniProtKB	Modified residue	230	230	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P43603 1 459
+P43603	UniProtKB	Chain	1	459	.	.	.	ID=PRO_0000202691;Note=LAS seventeen-binding protein 3	
+P43603	UniProtKB	Domain	400	459	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P43603	UniProtKB	Compositional bias	229	284	.	.	.	Note=Asp-rich	
+P43603	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43603	UniProtKB	Modified residue	298	298	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43603	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P43603	UniProtKB	Modified residue	303	303	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P43603	UniProtKB	Modified residue	393	393	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P43603	UniProtKB	Modified residue	397	397	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43603	UniProtKB	Modified residue	402	402	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P43603	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43603	UniProtKB	Beta strand	404	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT	
+P43603	UniProtKB	Beta strand	426	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT	
+P43603	UniProtKB	Beta strand	438	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT	
+P43603	UniProtKB	Beta strand	447	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT	
+P43603	UniProtKB	Helix	453	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT	
+P43603	UniProtKB	Beta strand	456	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT	
+##sequence-region P47017 1 172
+P47017	UniProtKB	Chain	1	172	.	.	.	ID=PRO_0000125553;Note=Sm-like protein LSm1	
+P47017	UniProtKB	Mutagenesis	105	105	.	.	.	Note=Slightly reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24513854;Dbxref=PMID:24513854	
+P47017	UniProtKB	Helix	42	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M75	
+P47017	UniProtKB	Beta strand	48	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P47017	UniProtKB	Beta strand	63	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P47017	UniProtKB	Beta strand	77	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P47017	UniProtKB	Turn	89	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P47017	UniProtKB	Beta strand	93	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P47017	UniProtKB	Helix	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P47017	UniProtKB	Beta strand	109	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P47017	UniProtKB	Helix	117	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P47017	UniProtKB	Beta strand	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P47017	UniProtKB	Helix	132	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P47017	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+##sequence-region Q12230 1 341
+Q12230	UniProtKB	Chain	1	341	.	.	.	ID=PRO_0000084505;Note=Sphingolipid long chain base-responsive protein LSP1	
+Q12230	UniProtKB	Compositional bias	21	25	.	.	.	Note=Poly-Pro	
+Q12230	UniProtKB	Compositional bias	283	324	.	.	.	Note=Glu-rich	
+Q12230	UniProtKB	Modified residue	233	233	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q12230	UniProtKB	Turn	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT	
+Q12230	UniProtKB	Helix	56	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT	
+Q12230	UniProtKB	Helix	95	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT	
+Q12230	UniProtKB	Helix	165	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT	
+Q12230	UniProtKB	Beta strand	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT	
+Q12230	UniProtKB	Helix	244	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT	
+##sequence-region Q04781 1 1562
+Q04781	UniProtKB	Chain	1	1562	.	.	.	ID=PRO_0000056341;Note=E3 ubiquitin-protein ligase listerin	
+Q04781	UniProtKB	Repeat	41	78	.	.	.	Note=HEAT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	127	164	.	.	.	Note=HEAT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	175	217	.	.	.	Note=HEAT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	262	301	.	.	.	Note=HEAT 4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	304	348	.	.	.	Note=HEAT 5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	495	532	.	.	.	Note=HEAT 6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	555	592	.	.	.	Note=HEAT 7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	813	850	.	.	.	Note=HEAT 8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	908	945	.	.	.	Note=HEAT 9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	997	1037	.	.	.	Note=HEAT 10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	1047	1085	.	.	.	Note=HEAT 11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	1188	1226	.	.	.	Note=HEAT 12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	1263	1298	.	.	.	Note=HEAT 13;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Repeat	1299	1339	.	.	.	Note=HEAT 14;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04781	UniProtKB	Zinc finger	1508	1555	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q04781	UniProtKB	Mutagenesis	1542	1542	.	.	.	Note=Abolishes ability to control levels of proteins with 'non-stop'. W->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20835226;Dbxref=PMID:20835226	
+Q04781	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Beta strand	27	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	36	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	45	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	59	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Turn	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG1	
+Q04781	UniProtKB	Helix	85	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	104	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Turn	122	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	129	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	145	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	163	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	174	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	190	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Turn	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	201	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	229	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	234	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Beta strand	243	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG1	
+Q04781	UniProtKB	Helix	247	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Beta strand	253	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	259	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	276	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	281	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	295	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Turn	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	303	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	310	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Turn	321	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	327	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	335	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	354	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	366	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Turn	373	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	377	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Helix	398	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+Q04781	UniProtKB	Turn	414	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0	
+##sequence-region P22134 1 296
+P22134	UniProtKB	Chain	1	296	.	.	.	ID=PRO_0000194883;Note=DNA-3-methyladenine glycosylase	
+P22134	UniProtKB	Active site	209	209	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22134	UniProtKB	Site	189	189	.	.	.	Note=Determinant for substrate specificity and/or activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22134	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q12176 1 1025
+Q12176	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12176	UniProtKB	Chain	2	1025	.	.	.	ID=PRO_0000173472;Note=Ribosome biogenesis protein MAK21	
+Q12176	UniProtKB	Compositional bias	74	77	.	.	.	Note=Poly-Asp	
+Q12176	UniProtKB	Compositional bias	117	122	.	.	.	Note=Poly-Asp	
+Q12176	UniProtKB	Compositional bias	979	986	.	.	.	Note=Poly-Glu	
+Q12176	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12176	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q12176	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12176	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12176	UniProtKB	Modified residue	275	275	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12176	UniProtKB	Modified residue	708	708	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12176	UniProtKB	Modified residue	710	710	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12176	UniProtKB	Modified residue	874	874	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12176	UniProtKB	Modified residue	878	878	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12176	UniProtKB	Modified residue	977	977	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12176	UniProtKB	Modified residue	978	978	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12176	UniProtKB	Modified residue	1024	1024	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53341 1 584
+P53341	UniProtKB	Chain	1	584	.	.	.	ID=PRO_0000054328;Note=Alpha-glucosidase MAL12	
+P53341	UniProtKB	Active site	214	214	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53341	UniProtKB	Active site	276	276	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53341	UniProtKB	Site	349	349	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12246 1 624
+Q12246	UniProtKB	Chain	1	624	.	.	.	ID=PRO_0000255956;Note=Sphingoid long chain base kinase 4	
+Q12246	UniProtKB	Domain	224	363	.	.	.	Note=DAGKc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q12246	UniProtKB	Nucleotide binding	234	236	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q12246	UniProtKB	Nucleotide binding	324	326	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q12246	UniProtKB	Nucleotide binding	589	591	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q12246	UniProtKB	Region	291	294	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12246	UniProtKB	Active site	293	293	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12246	UniProtKB	Binding site	266	266	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q12246	UniProtKB	Binding site	298	298	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q12246	UniProtKB	Binding site	392	392	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q12246	UniProtKB	Binding site	398	398	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783	
+Q12246	UniProtKB	Modified residue	111	111	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12246	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12246	UniProtKB	Modified residue	154	154	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12246	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12246	UniProtKB	Modified residue	451	451	.	.	.	Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15598647;Dbxref=PMID:17330950,PMID:19779198,PMID:15598647	
+Q12246	UniProtKB	Modified residue	454	454	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12246	UniProtKB	Modified residue	455	455	.	.	.	Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15598647;Dbxref=PMID:17330950,PMID:19779198,PMID:15598647	
+Q12246	UniProtKB	Modified residue	460	460	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12246	UniProtKB	Lipidation	43	43	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227572;Dbxref=PMID:16227572	
+Q12246	UniProtKB	Lipidation	46	46	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227572;Dbxref=PMID:16227572	
+Q12246	UniProtKB	Cross-link	148	148	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q12502 1 818
+Q12502	UniProtKB	Chain	1	818	.	.	.	ID=PRO_0000240388;Note=Protein LDB19	
+Q12502	UniProtKB	Compositional bias	67	124	.	.	.	Note=Ser-rich	
+Q12502	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12502	UniProtKB	Modified residue	384	384	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12502	UniProtKB	Modified residue	619	619	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12502	UniProtKB	Modified residue	808	808	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12502	UniProtKB	Cross-link	486	486	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538	
+##sequence-region Q02783 1 413
+Q02783	UniProtKB	Transit peptide	1	35	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02783	UniProtKB	Chain	36	413	.	.	.	ID=PRO_0000042816;Note=Mitochondrial inner membrane magnesium transporter MFM1	
+Q02783	UniProtKB	Transmembrane	329	349	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02783	UniProtKB	Transmembrane	367	387	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02783	UniProtKB	Motif	353	356	.	.	.	Note=YGMN	
+Q02783	UniProtKB	Glycosylation	202	202	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02783	UniProtKB	Sequence conflict	267	267	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40070 1 187
+P40070	UniProtKB	Chain	1	187	.	.	.	ID=PRO_0000125571;Note=U6 snRNA-associated Sm-like protein LSm4	
+P40070	UniProtKB	Mutagenesis	72	72	.	.	.	Note=Slightly reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854	
+P40070	UniProtKB	Sequence conflict	155	155	.	.	.	Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40070	UniProtKB	Helix	2	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40070	UniProtKB	Turn	9	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M78	
+P40070	UniProtKB	Beta strand	14	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40070	UniProtKB	Beta strand	22	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40070	UniProtKB	Beta strand	38	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40070	UniProtKB	Helix	48	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40070	UniProtKB	Beta strand	64	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40070	UniProtKB	Helix	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40070	UniProtKB	Beta strand	76	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40070	UniProtKB	Helix	83	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D	
+##sequence-region P40089 1 93
+P40089	UniProtKB	Chain	1	93	.	.	.	ID=PRO_0000125574;Note=U6 snRNA-associated Sm-like protein LSm5	
+P40089	UniProtKB	Mutagenesis	74	74	.	.	.	Note=Slightly increases affinity for poly-U RNA ends. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854	
+P40089	UniProtKB	Helix	8	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40089	UniProtKB	Turn	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D	
+P40089	UniProtKB	Beta strand	18	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40089	UniProtKB	Beta strand	43	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40089	UniProtKB	Beta strand	62	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40089	UniProtKB	Beta strand	69	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P40089	UniProtKB	Beta strand	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+##sequence-region P53905 1 115
+P53905	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000125581;Note=U6 snRNA-associated Sm-like protein LSm7	
+P53905	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Slightly reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854	
+P53905	UniProtKB	Helix	30	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P53905	UniProtKB	Beta strand	36	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P53905	UniProtKB	Turn	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7A	
+P53905	UniProtKB	Beta strand	47	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P53905	UniProtKB	Beta strand	61	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P53905	UniProtKB	Beta strand	86	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P53905	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P53905	UniProtKB	Beta strand	99	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+##sequence-region P32487 1 611
+P32487	UniProtKB	Chain	1	611	.	.	.	ID=PRO_0000054156;Note=Lysine-specific permease	
+P32487	UniProtKB	Topological domain	1	115	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	137	141	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	163	185	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	186	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	206	223	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	224	243	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	244	256	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	257	274	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	275	303	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	304	321	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	322	344	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	345	365	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	366	398	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	399	418	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	419	445	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	446	464	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	465	473	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	474	494	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	495	513	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	514	532	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	533	547	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Transmembrane	548	566	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Topological domain	567	611	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32487	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32487	UniProtKB	Modified residue	75	75	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32487	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32487	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P32487	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32487	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32487	UniProtKB	Cross-link	54	54	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32487	UniProtKB	Sequence conflict	90	90	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32487	UniProtKB	Sequence conflict	93	93	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32487	UniProtKB	Sequence conflict	561	561	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40971 1 790
+P40971	UniProtKB	Chain	1	790	.	.	.	ID=PRO_0000114955;Note=Lysine biosynthesis regulatory protein LYS14	
+P40971	UniProtKB	DNA binding	159	186	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P40971	UniProtKB	Sequence conflict	121	121	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40971	UniProtKB	Sequence conflict	760	760	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38828 1 187
+P38828	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38828	UniProtKB	Chain	2	187	.	.	.	ID=PRO_0000202913;Note=Protein LSM12	
+P38828	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P10962 1 306
+P10962	UniProtKB	Chain	1	306	.	.	.	ID=PRO_0000203793;Note=Protein MAK16	
+P10962	UniProtKB	Repeat	213	220	.	.	.	Note=1	
+P10962	UniProtKB	Repeat	222	229	.	.	.	Note=2	
+P10962	UniProtKB	Region	213	229	.	.	.	Note=2 X 8 AA repeats	
+P10962	UniProtKB	Region	251	264	.	.	.	Note=7 X 2 AA repeats of S-[DE]	
+P10962	UniProtKB	Motif	139	144	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10962	UniProtKB	Motif	282	287	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10962	UniProtKB	Compositional bias	195	235	.	.	.	Note=Asp/Glu-rich (acidic)	
+P10962	UniProtKB	Sequence conflict	250	250	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10962	UniProtKB	Sequence conflict	250	250	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P23060 1 363
+P23060	UniProtKB	Chain	1	363	.	.	.	ID=PRO_0000084555;Note=Protein MAK32	
+P23060	UniProtKB	Sequence conflict	15	15	.	.	.	Note=I->II;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23060	UniProtKB	Sequence conflict	82	82	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53048 1 616
+P53048	UniProtKB	Chain	1	616	.	.	.	ID=PRO_0000050425;Note=General alpha-glucoside permease	
+P53048	UniProtKB	Topological domain	1	115	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	137	150	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	151	171	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	172	186	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	208	208	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	230	242	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	264	278	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	279	299	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	300	370	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	371	391	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	392	404	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	405	425	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	426	433	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	434	454	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	455	466	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	467	487	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	488	499	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	500	520	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	521	532	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Transmembrane	533	553	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Topological domain	554	616	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Glycosylation	523	523	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53048	UniProtKB	Sequence conflict	396	398	.	.	.	Note=RAG->KKQV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38157 1 468
+P38157	UniProtKB	Chain	1	468	.	.	.	ID=PRO_0000114957;Note=Maltose fermentation regulatory protein MAL33	
+P38157	UniProtKB	DNA binding	8	34	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P38157	UniProtKB	Motif	41	49	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CW40 1 589
+P0CW40	UniProtKB	Chain	1	589	.	.	.	ID=PRO_0000054332;Note=Oligo-1%2C6-glucosidase IMA3	
+P0CW40	UniProtKB	Active site	215	215	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CW40	UniProtKB	Active site	277	277	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CW40	UniProtKB	Site	352	352	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53051 1 589
+P53051	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15291818;Dbxref=PMID:15291818	
+P53051	UniProtKB	Chain	2	589	.	.	.	ID=PRO_0000054333;Note=Oligo-1%2C6-glucosidase IMA1	
+P53051	UniProtKB	Active site	215	215	.	.	.	Note=Nucleophile	
+P53051	UniProtKB	Active site	277	277	.	.	.	Note=Proton donor	
+P53051	UniProtKB	Site	352	352	.	.	.	Note=Transition state stabilizer	
+P53051	UniProtKB	Mutagenesis	215	215	.	.	.	Note=Abolishes catalytic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15291818;Dbxref=PMID:15291818	
+P53051	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Can also hydrolyze maltose. V->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15291818;Dbxref=PMID:15291818	
+P53051	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Does not alter substrate specificity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15291818;Dbxref=PMID:15291818	
+P53051	UniProtKB	Mutagenesis	218	218	.	.	.	Note=Does not alter substrate specificity. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15291818;Dbxref=PMID:15291818	
+P53051	UniProtKB	Sequence conflict	428	428	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53051	UniProtKB	Helix	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	14	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	31	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	39	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	46	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	55	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Turn	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	75	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Turn	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	87	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	103	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	118	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	160	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Turn	168	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	172	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	190	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	202	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	211	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	242	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	251	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	273	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	283	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	292	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	298	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	304	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	314	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	323	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Turn	332	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	335	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	356	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Turn	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	368	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	382	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	392	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	404	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	410	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	425	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	428	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	442	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Turn	455	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	473	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	481	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	491	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Helix	506	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	513	519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	523	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	535	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	544	546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	559	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Turn	568	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+P53051	UniProtKB	Beta strand	583	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7	
+##sequence-region P40065 1 302
+P40065	UniProtKB	Chain	1	302	.	.	.	ID=PRO_0000202645;Note=Monopolin complex subunit MAM1	
+P40065	UniProtKB	Sequence conflict	202	202	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40065	UniProtKB	Helix	94	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P40065	UniProtKB	Helix	101	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P40065	UniProtKB	Turn	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P40065	UniProtKB	Helix	121	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P40065	UniProtKB	Helix	130	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P40065	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P40065	UniProtKB	Beta strand	141	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P40065	UniProtKB	Helix	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P40065	UniProtKB	Helix	158	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P40065	UniProtKB	Helix	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P40065	UniProtKB	Beta strand	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CZO	
+P40065	UniProtKB	Helix	184	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ	
+P40065	UniProtKB	Helix	231	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KTB	
+P40065	UniProtKB	Helix	234	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KTB	
+P40065	UniProtKB	Helix	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KTB	
+P40065	UniProtKB	Helix	247	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KTB	
+##sequence-region Q01662 1 387
+Q01662	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q01662	UniProtKB	Propeptide	2	10	.	.	.	ID=PRO_0000018596;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1569059;Dbxref=PMID:1569059	
+Q01662	UniProtKB	Chain	11	387	.	.	.	ID=PRO_0000018597;Note=Methionine aminopeptidase 1	
+Q01662	UniProtKB	Region	22	66	.	.	.	Note=Zinc finger-like%3B important for proper ribosome association	
+Q01662	UniProtKB	Metal binding	219	219	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174	
+Q01662	UniProtKB	Metal binding	230	230	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174	
+Q01662	UniProtKB	Metal binding	230	230	.	.	.	Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174	
+Q01662	UniProtKB	Metal binding	294	294	.	.	.	Note=Divalent metal cation 2%3B catalytic%3B via tele nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174	
+Q01662	UniProtKB	Metal binding	327	327	.	.	.	Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174	
+Q01662	UniProtKB	Metal binding	358	358	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174	
+Q01662	UniProtKB	Metal binding	358	358	.	.	.	Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174	
+Q01662	UniProtKB	Binding site	202	202	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174	
+Q01662	UniProtKB	Binding site	301	301	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174	
+Q01662	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q01662	UniProtKB	Mutagenesis	22	22	.	.	.	Note=Changes the ribosome profile distribution of the protein and also increases its occurrence in the cytosolic fraction. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11968008;Dbxref=PMID:11968008	
+Q01662	UniProtKB	Mutagenesis	62	62	.	.	.	Note=Changes the ribosome profile distribution of the protein. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11968008;Dbxref=PMID:11968008	
+Q01662	UniProtKB	Mutagenesis	219	219	.	.	.	Note=Reduces activity 1000-fold. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9367524;Dbxref=PMID:9367524	
+##sequence-region P38174 1 421
+P38174	UniProtKB	Chain	1	421	.	.	.	ID=PRO_0000148988;Note=Methionine aminopeptidase 2	
+P38174	UniProtKB	Compositional bias	41	57	.	.	.	Note=Lys-rich	
+P38174	UniProtKB	Metal binding	194	194	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175	
+P38174	UniProtKB	Metal binding	205	205	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175	
+P38174	UniProtKB	Metal binding	205	205	.	.	.	Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175	
+P38174	UniProtKB	Metal binding	274	274	.	.	.	Note=Divalent metal cation 2%3B catalytic%3B via tele nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175	
+P38174	UniProtKB	Metal binding	307	307	.	.	.	Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175	
+P38174	UniProtKB	Metal binding	402	402	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175	
+P38174	UniProtKB	Metal binding	402	402	.	.	.	Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175	
+P38174	UniProtKB	Binding site	174	174	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175	
+P38174	UniProtKB	Binding site	282	282	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175	
+P38174	UniProtKB	Modified residue	35	35	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38174	UniProtKB	Mutagenesis	174	174	.	.	.	Note=Abolishes catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15547949;Dbxref=PMID:15547949	
+P38174	UniProtKB	Sequence conflict	86	86	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38174	UniProtKB	Sequence conflict	86	86	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q9ZZW7 1 517
+Q9ZZW7	UniProtKB	Chain	1	517	.	.	.	ID=PRO_0000061915;Note=Cytochrome b mRNA maturase bI3	
+Q9ZZW7	UniProtKB	Topological domain	1	31	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZW7	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968	
+Q9ZZW7	UniProtKB	Topological domain	53	84	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZW7	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968	
+Q9ZZW7	UniProtKB	Topological domain	106	115	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZW7	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968	
+Q9ZZW7	UniProtKB	Topological domain	137	145	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZW7	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968	
+Q9ZZW7	UniProtKB	Topological domain	167	184	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZW7	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968	
+Q9ZZW7	UniProtKB	Topological domain	206	224	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZW7	UniProtKB	Transmembrane	225	242	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968	
+Q9ZZW7	UniProtKB	Topological domain	243	517	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZW7	UniProtKB	Region	1	169	.	.	.	Note=Cytochrome b	
+Q9ZZW7	UniProtKB	Region	170	517	.	.	.	Note=Maturase	
+Q9ZZW7	UniProtKB	Natural variant	269	269	.	.	.	Note=In strain: 777-3A. G->V	
+Q9ZZW7	UniProtKB	Natural variant	350	350	.	.	.	Note=In strain: 777-3A. D->N	
+Q9ZZW7	UniProtKB	Natural variant	412	412	.	.	.	Note=In strain: 777-3A. E->K	
+Q9ZZW7	UniProtKB	Natural variant	434	434	.	.	.	Note=In strain: 777-3A. Q->M	
+Q9ZZW7	UniProtKB	Natural variant	437	437	.	.	.	Note=In strain: 777-3A. S->N	
+Q9ZZW7	UniProtKB	Natural variant	451	452	.	.	.	Note=In strain: 777-3A. TQ->NN	
+Q9ZZW7	UniProtKB	Natural variant	456	458	.	.	.	Note=In strain: 777-3A. TDK->MNE	
+Q9ZZW7	UniProtKB	Natural variant	463	463	.	.	.	Note=In strain: 777-3A. R->K	
+Q9ZZW7	UniProtKB	Natural variant	471	471	.	.	.	Note=In strain: 777-3A. G->D	
+Q9ZZW7	UniProtKB	Natural variant	515	515	.	.	.	Note=In strain: 777-3A. P->S	
+Q9ZZW7	UniProtKB	Mutagenesis	151	151	.	.	.	Note=In M2011%3B leads to absence of functional cytochrome b%2C but does not affect splicing. F->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2538624;Dbxref=PMID:2538624	
+Q9ZZW7	UniProtKB	Mutagenesis	407	407	.	.	.	Note=In G5037%3B blocks formation of mature cytochrome b mRNA. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2538624;Dbxref=PMID:2538624	
+Q9ZZW7	UniProtKB	Helix	264	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Beta strand	276	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Beta strand	286	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	300	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Beta strand	314	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Beta strand	327	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	338	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	345	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	359	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	376	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	392	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	401	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Beta strand	413	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Beta strand	423	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Beta strand	427	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	438	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Beta strand	454	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Beta strand	462	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	469	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	489	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+Q9ZZW7	UniProtKB	Helix	505	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5	
+##sequence-region P42951 1 607
+P42951	UniProtKB	Chain	1	607	.	.	.	ID=PRO_0000088850;Note=Phosphatidylinositol 4-kinase LSB6	
+P42951	UniProtKB	Domain	170	507	.	.	.	Note=PI3K/PI4K	
+##sequence-region P38203 1 95
+P38203	UniProtKB	Chain	1	95	.	.	.	ID=PRO_0000125559;Note=U6 snRNA-associated Sm-like protein LSm2	
+P38203	UniProtKB	Mutagenesis	35	35	.	.	.	Note=Strongly reduces affinity for poly-U RNA ends. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24240276;Dbxref=PMID:24240276	
+P38203	UniProtKB	Mutagenesis	37	37	.	.	.	Note=Strongly reduces affinity for poly-U RNA ends. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24240276;Dbxref=PMID:24240276	
+P38203	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Strongly reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854	
+P38203	UniProtKB	Helix	2	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P38203	UniProtKB	Turn	9	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P38203	UniProtKB	Beta strand	13	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P38203	UniProtKB	Turn	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D	
+P38203	UniProtKB	Beta strand	24	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P38203	UniProtKB	Beta strand	38	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P38203	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P38203	UniProtKB	Beta strand	54	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M75	
+P38203	UniProtKB	Beta strand	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P38203	UniProtKB	Helix	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P38203	UniProtKB	Beta strand	67	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P38203	UniProtKB	Helix	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P38203	UniProtKB	Helix	79	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+##sequence-region P34239 1 828
+P34239	UniProtKB	Chain	1	828	.	.	.	ID=PRO_0000203139;Note=Protein LST4	
+P34239	UniProtKB	Domain	114	302	.	.	.	Note=uDENN FNIP1/2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01180	
+P34239	UniProtKB	Domain	310	712	.	.	.	Note=cDENN FNIP1/2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01180	
+P34239	UniProtKB	Domain	718	825	.	.	.	Note=dDENN FNIP1/2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01180	
+P34239	UniProtKB	Compositional bias	437	570	.	.	.	Note=Ser-rich	
+P34239	UniProtKB	Modified residue	401	401	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P41318 1 303
+P41318	UniProtKB	Chain	1	303	.	.	.	ID=PRO_0000051483;Note=Target of rapamycin complex subunit LST8	
+P41318	UniProtKB	Repeat	1	27	.	.	.	Note=WD 1	
+P41318	UniProtKB	Repeat	30	68	.	.	.	Note=WD 2	
+P41318	UniProtKB	Repeat	73	112	.	.	.	Note=WD 3	
+P41318	UniProtKB	Repeat	114	153	.	.	.	Note=WD 4	
+P41318	UniProtKB	Repeat	157	196	.	.	.	Note=WD 5	
+P41318	UniProtKB	Repeat	205	244	.	.	.	Note=WD 6	
+P41318	UniProtKB	Repeat	248	287	.	.	.	Note=WD 7	
+P41318	UniProtKB	Mutagenesis	138	138	.	.	.	Note=In LST8-3%3B abolishes repression of RTG1-RTG3-dependent gene expression. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11742997;Dbxref=PMID:11742997	
+P41318	UniProtKB	Mutagenesis	146	146	.	.	.	Note=In LST8-2%3B abolishes repression of RTG1-RTG3-dependent gene expression. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11742997;Dbxref=PMID:11742997	
+P41318	UniProtKB	Mutagenesis	171	171	.	.	.	Note=In LST8-5%3B abolishes repression of RTG1-RTG3-dependent gene expression. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11742997;Dbxref=PMID:11742997	
+P41318	UniProtKB	Mutagenesis	181	181	.	.	.	Note=In LST8-4%3B abolishes repression of RTG1-RTG3-dependent gene expression. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11742997;Dbxref=PMID:11742997	
+P41318	UniProtKB	Mutagenesis	300	300	.	.	.	Note=In LST8-1%3B abolishes repression of RTG2- and RTG1-RTG3-dependent gene expression. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9409822;Dbxref=PMID:9409822	
+##sequence-region P07866 1 1435
+P07866	UniProtKB	Chain	1	1435	.	.	.	ID=PRO_0000068884;Note=Guanine nucleotide exchange factor LTE1	
+P07866	UniProtKB	Domain	25	157	.	.	.	Note=N-terminal Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00135	
+P07866	UniProtKB	Domain	1194	1434	.	.	.	Note=Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00168	
+P07866	UniProtKB	Modified residue	271	271	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07866	UniProtKB	Modified residue	559	559	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07866	UniProtKB	Modified residue	689	689	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07866	UniProtKB	Modified residue	691	691	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07866	UniProtKB	Modified residue	808	808	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07866	UniProtKB	Modified residue	810	810	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07866	UniProtKB	Modified residue	1028	1028	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P07866	UniProtKB	Modified residue	1109	1109	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07866	UniProtKB	Sequence conflict	998	1009	.	.	.	Note=TNSNISGSVLTM->LIVHIRKCIDN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07866	UniProtKB	Sequence conflict	1161	1163	.	.	.	Note=AAQ->GE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07508 1 261
+Q07508	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q07508	UniProtKB	Chain	2	261	.	.	.	ID=PRO_0000255959;Note=Protein LUC7	
+Q07508	UniProtKB	Coiled coil	123	190	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07508	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P35192 1 417
+P35192	UniProtKB	Chain	1	417	.	.	.	ID=PRO_0000194928;Note=Metal-binding activator 1	
+P35192	UniProtKB	Repeat	264	279	.	.	.	Note=1	
+P35192	UniProtKB	Repeat	322	337	.	.	.	Note=2	
+P35192	UniProtKB	DNA binding	1	40	.	.	.	Note=Copper-fist;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+P35192	UniProtKB	Region	264	337	.	.	.	Note=2 X 16 AA repeat of C-X-C-X(4)-C-X-C-X-X-C-X-X-H	
+P35192	UniProtKB	Metal binding	11	11	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+P35192	UniProtKB	Metal binding	14	14	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+P35192	UniProtKB	Metal binding	23	23	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+P35192	UniProtKB	Metal binding	25	25	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055	
+P35192	UniProtKB	Modified residue	143	143	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P35192	UniProtKB	Mutagenesis	279	279	.	.	.	Note=Gain of function. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8262047;Dbxref=PMID:8262047	
+P35192	UniProtKB	Sequence conflict	198	198	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35192	UniProtKB	Sequence conflict	380	380	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06436 1 670
+Q06436	UniProtKB	Chain	1	670	.	.	.	ID=PRO_0000257809;Note=RING-finger protein MAG2	
+Q06436	UniProtKB	Zinc finger	195	250	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+##sequence-region P0CW41 1 589
+P0CW41	UniProtKB	Chain	1	589	.	.	.	ID=PRO_0000408197;Note=Oligo-1%2C6-glucosidase IMA4	
+P0CW41	UniProtKB	Active site	215	215	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CW41	UniProtKB	Active site	277	277	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CW41	UniProtKB	Site	352	352	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P30952 1 554
+P30952	UniProtKB	Chain	1	554	.	.	.	ID=PRO_0000166864;Note=Malate synthase 1%2C glyoxysomal	
+P30952	UniProtKB	Motif	552	554	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30952	UniProtKB	Active site	177	177	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30952	UniProtKB	Active site	457	457	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30952	UniProtKB	Natural variant	118	118	.	.	.	Note=In strain: Awamori-1%2C AKU-4011%2C K1%2C K5%2C NRIC 23%2C NRIC 1413 and NRIC 1685. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16103919;Dbxref=PMID:16103919	
+P30952	UniProtKB	Natural variant	199	199	.	.	.	Note=In strain: Pasteur Red. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16103919;Dbxref=PMID:16103919	
+P30952	UniProtKB	Natural variant	217	217	.	.	.	Note=In strain: YJM326. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P30952	UniProtKB	Natural variant	253	253	.	.	.	Note=In strain: Levuline ALS%2C Lalvin CY-3079%2C Cote des Blancs%2C I14%2C M1%2C M11%2C M12%2C M13%2C M15%2C M2%2C M20%2C M21%2C M22%2C M24%2C M29%2C M3%2C M30%2C M31%2C M32%2C M33%2C M34%2C M4%2C M5%2C M6%2C M7%2C M8%2C M9%2C NRRL Y-1438%2C NRRL YB-1952%2C NRRL Y-2411%2C Pasteur Red%2C UCD 51%2C UCD 2120%2C UCD 175%2C UCD 529%2C UCD 765%2C UCD 781%2C UCD 820%2C UCD 762%2C YJM269%2C YJM270%2C YJM308%2C YJM326%2C YJM434 and YJM1129. T->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16103919,ECO:0000269|PubMed:18780730;Dbxref=PMID:16103919,PMID:18780730	
+P30952	UniProtKB	Natural variant	310	310	.	.	.	Note=In strain: SK1%2C V1-09%2C YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326%2C YJM339%2C YJM627 and YJM1129. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P30952	UniProtKB	Natural variant	541	541	.	.	.	Note=In strain: YJM269 and YJM270. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+##sequence-region P21826 1 554
+P21826	UniProtKB	Chain	1	554	.	.	.	ID=PRO_0000166865;Note=Malate synthase 2%2C glyoxysomal	
+P21826	UniProtKB	Motif	552	554	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21826	UniProtKB	Active site	177	177	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21826	UniProtKB	Active site	457	457	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21826	UniProtKB	Sequence conflict	115	115	.	.	.	Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21826	UniProtKB	Sequence conflict	115	115	.	.	.	Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21826	UniProtKB	Sequence conflict	166	166	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21826	UniProtKB	Sequence conflict	166	166	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21826	UniProtKB	Sequence conflict	302	302	.	.	.	Note=P->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21826	UniProtKB	Sequence conflict	302	302	.	.	.	Note=P->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P50113 1 272
+P50113	UniProtKB	Chain	1	272	.	.	.	ID=PRO_0000175742;Note=L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase	
+##sequence-region P47074 1 515
+P47074	UniProtKB	Chain	1	515	.	.	.	ID=PRO_0000084549;Note=Spindle assembly checkpoint component MAD3	
+P47074	UniProtKB	Domain	67	228	.	.	.	Note=BUB1 N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00822	
+P47074	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47074	UniProtKB	Mutagenesis	156	159	.	.	.	Note=Abolishes interaction with CDC20. Benomyl-sensitive phenotype. GIGS->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10704439;Dbxref=PMID:10704439	
+P47074	UniProtKB	Mutagenesis	382	382	.	.	.	Note=Abolishes interaction with BUB3. Benomyl-sensitive phenotype. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10704439;Dbxref=PMID:10704439	
+P47074	UniProtKB	Beta strand	356	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3T	
+P47074	UniProtKB	Helix	362	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3T	
+P47074	UniProtKB	Helix	381	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3T	
+P47074	UniProtKB	Turn	388	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3T	
+##sequence-region P41910 1 395
+P41910	UniProtKB	Chain	1	395	.	.	.	ID=PRO_0000213972;Note=Repressor of RNA polymerase III transcription MAF1	
+P41910	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41910	UniProtKB	Modified residue	209	209	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P41910	UniProtKB	Modified residue	210	210	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P41910	UniProtKB	Modified residue	347	347	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P39534 1 108
+P39534	UniProtKB	Chain	1	108	.	.	.	ID=PRO_0000203017;Note=Uncharacterized protein MBB1	
+##sequence-region Q07376 1 486
+Q07376	UniProtKB	Chain	1	486	.	.	.	ID=PRO_0000084877;Note=Probable transporter MCH1	
+Q07376	UniProtKB	Topological domain	1	29	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	30	50	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	51	67	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	89	93	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	115	133	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	134	154	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	155	163	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	185	212	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	213	233	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	234	279	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	280	300	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	301	320	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	321	343	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	344	347	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	348	368	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	369	385	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	386	406	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	407	413	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	414	434	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	435	456	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Transmembrane	457	477	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Topological domain	478	486	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Modified residue	255	255	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q07376	UniProtKB	Glycosylation	60	60	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Glycosylation	131	131	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07376	UniProtKB	Glycosylation	194	194	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36032 1 473
+P36032	UniProtKB	Chain	1	473	.	.	.	ID=PRO_0000211403;Note=Probable transporter MCH2	
+P36032	UniProtKB	Topological domain	1	37	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	59	83	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	84	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	106	111	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	112	135	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	136	141	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	142	163	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	164	169	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	170	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	187	200	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	201	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	221	243	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	244	268	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	269	286	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	287	304	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	305	312	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	313	332	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	333	342	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	343	362	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	363	370	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	371	394	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	395	408	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Transmembrane	409	433	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Topological domain	434	473	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Glycosylation	72	72	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36032	UniProtKB	Sequence conflict	342	342	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36032	UniProtKB	Sequence conflict	342	342	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08777 1 521
+Q08777	UniProtKB	Chain	1	521	.	.	.	ID=PRO_0000257810;Note=Riboflavin transporter MCH5	
+Q08777	UniProtKB	Topological domain	1	103	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	125	143	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	144	164	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	165	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	194	200	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	201	221	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	222	233	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	234	254	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	255	269	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	270	290	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	291	325	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	326	346	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	347	367	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	368	388	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	389	396	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	397	417	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	418	422	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	423	443	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	444	461	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	462	482	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	483	487	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Transmembrane	488	508	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Topological domain	509	521	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Glycosylation	125	125	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Glycosylation	194	194	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Glycosylation	419	419	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08777	UniProtKB	Sequence conflict	495	495	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08777	UniProtKB	Sequence conflict	495	495	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12262 1 181
+Q12262	UniProtKB	Chain	1	181	.	.	.	ID=PRO_0000096281;Note=Central kinetochore subunit MCM16	
+Q12262	UniProtKB	Coiled coil	112	171	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06675 1 368
+Q06675	UniProtKB	Chain	1	368	.	.	.	ID=PRO_0000096282;Note=Central kinetochore subunit MCM21	
+Q06675	UniProtKB	Coiled coil	1	43	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06675	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P11746 1 286
+P11746	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P11746	UniProtKB	Chain	2	286	.	.	.	ID=PRO_0000199439;Note=Pheromone receptor transcription factor	
+P11746	UniProtKB	Domain	18	72	.	.	.	Note=MADS-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00251	
+P11746	UniProtKB	Compositional bias	98	120	.	.	.	Note=Asp/Glu-rich (acidic)	
+P11746	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P11746	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P11746	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P11746	UniProtKB	Sequence conflict	9	9	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11746	UniProtKB	Sequence conflict	37	37	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11746	UniProtKB	Sequence conflict	156	157	.	.	.	Note=GA->AR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11746	UniProtKB	Sequence conflict	158	286	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11746	UniProtKB	Helix	29	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM	
+P11746	UniProtKB	Beta strand	57	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM	
+P11746	UniProtKB	Beta strand	69	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM	
+P11746	UniProtKB	Turn	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM	
+P11746	UniProtKB	Helix	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM	
+P11746	UniProtKB	Helix	84	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM	
+##sequence-region P17505 1 334
+P17505	UniProtKB	Transit peptide	1	17	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:3072021,ECO:0000269|PubMed:3552052;Dbxref=PMID:3072021,PMID:3552052	
+P17505	UniProtKB	Chain	18	334	.	.	.	ID=PRO_0000018633;Note=Malate dehydrogenase%2C mitochondrial	
+P17505	UniProtKB	Nucleotide binding	24	30	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17505	UniProtKB	Nucleotide binding	135	137	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17505	UniProtKB	Active site	195	195	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17505	UniProtKB	Binding site	50	50	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17505	UniProtKB	Binding site	99	99	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P17505	UniProtKB	Binding site	105	105	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P17505	UniProtKB	Binding site	112	112	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17505	UniProtKB	Binding site	137	137	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P17505	UniProtKB	Binding site	171	171	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P17505	UniProtKB	Binding site	245	245	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P17505	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P17505	UniProtKB	Modified residue	199	199	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P17505	UniProtKB	Sequence conflict	68	68	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17505	UniProtKB	Sequence conflict	306	306	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07923 1 191
+Q07923	UniProtKB	Chain	1	191	.	.	.	ID=PRO_0000234661;Note=NAD(P)H-dependent FMN reductase LOT6	
+Q07923	UniProtKB	Region	94	97	.	.	.	Note=FMN binding	
+Q07923	UniProtKB	Binding site	11	11	.	.	.	Note=FMN	
+Q07923	UniProtKB	Binding site	124	124	.	.	.	Note=FMN	
+Q07923	UniProtKB	Beta strand	2	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Helix	16	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Turn	31	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Beta strand	39	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Helix	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Helix	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Helix	73	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Beta strand	86	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Helix	101	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Turn	112	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Beta strand	118	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Turn	126	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Helix	130	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Beta strand	146	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Turn	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Helix	168	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+Q07923	UniProtKB	Helix	174	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I	
+##sequence-region P25369 1 354
+P25369	UniProtKB	Chain	1	354	.	.	.	ID=PRO_0000084502;Note=LAS seventeen-binding protein 5	
+P25369	UniProtKB	Domain	15	161	.	.	.	Note=VHS	
+##sequence-region P53145 1 640
+P53145	UniProtKB	Chain	1	640	.	.	.	ID=PRO_0000122454;Note=Large subunit GTPase 1	
+P53145	UniProtKB	Domain	188	394	.	.	.	Note=CP-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01058	
+P53145	UniProtKB	Nucleotide binding	236	239	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53145	UniProtKB	Nucleotide binding	343	350	.	.	.	Note=GTP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53145	UniProtKB	Nucleotide binding	387	390	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53145	UniProtKB	Modified residue	103	103	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53145	UniProtKB	Mutagenesis	204	204	.	.	.	Note=Impairs the nuclear export of 60S ribosomal subunit in cytoplasm. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15660131;Dbxref=PMID:15660131	
+P53145	UniProtKB	Mutagenesis	349	349	.	.	.	Note=Dominant negative mutant%3B prevents the nuclear export of 60S ribosomal subunit in cytoplasm. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15660131;Dbxref=PMID:15660131	
+##sequence-region P34078 1 463
+P34078	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P34078	UniProtKB	Chain	2	463	.	.	.	ID=PRO_0000084522;Note=Protein LTV1	
+P34078	UniProtKB	Coiled coil	355	462	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34078	UniProtKB	Motif	168	179	.	.	.	Note=Nuclear export signal	
+P34078	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P34078	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34078	UniProtKB	Modified residue	293	293	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34078	UniProtKB	Modified residue	299	299	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34078	UniProtKB	Modified residue	303	303	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P40957 1 749
+P40957	UniProtKB	Chain	1	749	.	.	.	ID=PRO_0000213798;Note=Spindle assembly checkpoint component MAD1	
+P40957	UniProtKB	Coiled coil	57	324	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40957	UniProtKB	Coiled coil	390	656	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40957	UniProtKB	Compositional bias	323	329	.	.	.	Note=Poly-Asp	
+P40957	UniProtKB	Compositional bias	330	347	.	.	.	Note=Poly-Asn	
+P40957	UniProtKB	Compositional bias	355	363	.	.	.	Note=Poly-Asn	
+P40957	UniProtKB	Compositional bias	601	604	.	.	.	Note=Poly-Leu	
+P40957	UniProtKB	Modified residue	502	502	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40957	UniProtKB	Mutagenesis	653	655	.	.	.	Note=Abolishes interaction with BUB1 and BUB3 and spindle checkpoint function. RLK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10837255;Dbxref=PMID:10837255	
+##sequence-region P40958 1 196
+P40958	UniProtKB	Chain	1	196	.	.	.	ID=PRO_0000126115;Note=Mitotic spindle checkpoint component MAD2	
+P40958	UniProtKB	Domain	8	192	.	.	.	Note=HORMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00109	
+##sequence-region P20484 1 414
+P20484	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P20484	UniProtKB	Chain	2	414	.	.	.	ID=PRO_0000051079;Note=Protein MAK11	
+P20484	UniProtKB	Repeat	50	78	.	.	.	Note=WD 1	
+P20484	UniProtKB	Repeat	90	135	.	.	.	Note=WD 2	
+P20484	UniProtKB	Repeat	147	177	.	.	.	Note=WD 3	
+P20484	UniProtKB	Repeat	189	221	.	.	.	Note=WD 4	
+P20484	UniProtKB	Repeat	238	267	.	.	.	Note=WD 5	
+P20484	UniProtKB	Repeat	298	330	.	.	.	Note=WD 6	
+P20484	UniProtKB	Compositional bias	386	408	.	.	.	Note=Lys-rich (basic)	
+P20484	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P20484	UniProtKB	Modified residue	376	376	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P20484	UniProtKB	Modified residue	380	380	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P20484	UniProtKB	Modified residue	382	382	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38112 1 773
+P38112	UniProtKB	Chain	1	773	.	.	.	ID=PRO_0000055048;Note=ATP-dependent RNA helicase MAK5	
+P38112	UniProtKB	Domain	202	399	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P38112	UniProtKB	Domain	452	615	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P38112	UniProtKB	Nucleotide binding	215	222	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P38112	UniProtKB	Motif	171	199	.	.	.	Note=Q motif	
+P38112	UniProtKB	Motif	333	336	.	.	.	Note=DEAD box	
+P38112	UniProtKB	Modified residue	135	135	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38112	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38112	UniProtKB	Modified residue	678	678	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38112	UniProtKB	Mutagenesis	218	218	.	.	.	Note=Delays the appearance and decreases the level of 25S rRNA. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:13680366;Dbxref=PMID:13680366	
+##sequence-region P57743 1 89
+P57743	UniProtKB	Chain	1	89	.	.	.	ID=PRO_0000125563;Note=U6 snRNA-associated Sm-like protein LSm3	
+P57743	UniProtKB	Mutagenesis	36	36	.	.	.	Note=Strongly reduces affinity for poly-U RNA ends. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24240276;Dbxref=PMID:24240276	
+P57743	UniProtKB	Mutagenesis	38	38	.	.	.	Note=Strongly reduces affinity for poly-U RNA ends. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24240276;Dbxref=PMID:24240276	
+P57743	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Strongly reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854	
+P57743	UniProtKB	Helix	4	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P57743	UniProtKB	Turn	10	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P57743	UniProtKB	Beta strand	14	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P57743	UniProtKB	Turn	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P57743	UniProtKB	Beta strand	24	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P57743	UniProtKB	Beta strand	39	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P57743	UniProtKB	Beta strand	55	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P57743	UniProtKB	Helix	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+P57743	UniProtKB	Beta strand	73	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+##sequence-region Q06406 1 86
+Q06406	UniProtKB	Chain	1	86	.	.	.	ID=PRO_0000125578;Note=U6 snRNA-associated Sm-like protein LSm6	
+Q06406	UniProtKB	Mutagenesis	74	74	.	.	.	Note=Reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854	
+Q06406	UniProtKB	Helix	11	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+Q06406	UniProtKB	Turn	18	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+Q06406	UniProtKB	Beta strand	22	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+Q06406	UniProtKB	Beta strand	31	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+Q06406	UniProtKB	Beta strand	47	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+Q06406	UniProtKB	Turn	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M75	
+Q06406	UniProtKB	Beta strand	65	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7A	
+Q06406	UniProtKB	Beta strand	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+Q06406	UniProtKB	Helix	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+Q06406	UniProtKB	Beta strand	78	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92	
+##sequence-region P36007 1 326
+P36007	UniProtKB	Chain	1	326	.	.	.	ID=PRO_0000185589;Note=L-threo-3-hydroxyaspartate ammonia-lyase	
+P36007	UniProtKB	Region	179	183	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04968	
+P36007	UniProtKB	Binding site	80	80	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04968	
+P36007	UniProtKB	Binding site	304	304	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04968	
+P36007	UniProtKB	Modified residue	53	53	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04968	
+##sequence-region P38156 1 614
+P38156	UniProtKB	Chain	1	614	.	.	.	ID=PRO_0000050422;Note=Maltose permease MAL31	
+P38156	UniProtKB	Topological domain	1	108	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	130	144	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	166	180	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	181	201	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	202	202	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	203	223	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	224	236	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	237	257	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	258	272	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	273	293	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	294	364	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	365	385	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	386	398	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	399	419	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	420	427	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	428	448	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	449	460	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	461	481	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	482	493	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	494	514	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	515	526	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Transmembrane	527	547	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38156	UniProtKB	Topological domain	548	614	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P22855 1 1083
+P22855	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P22855	UniProtKB	Chain	2	1083	.	.	.	ID=PRO_0000206910;Note=Alpha-mannosidase	
+P22855	UniProtKB	Active site	411	411	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22855	UniProtKB	Metal binding	298	298	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22855	UniProtKB	Metal binding	300	300	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22855	UniProtKB	Metal binding	411	411	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22855	UniProtKB	Metal binding	626	626	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22855	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P22855	UniProtKB	Sequence conflict	786	786	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22855	UniProtKB	Sequence conflict	798	798	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q92328 1 271
+Q92328	UniProtKB	Chain	1	271	.	.	.	ID=PRO_0000096329;Note=Mitochondrial distribution and morphology protein 12	
+Q92328	UniProtKB	Cross-link	49	49	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q92328	UniProtKB	Sequence conflict	91	91	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q92328	UniProtKB	Sequence conflict	269	269	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q92328	UniProtKB	Beta strand	1	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Helix	8	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Helix	16	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Beta strand	37	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Beta strand	49	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Helix	64	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Beta strand	119	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Beta strand	132	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Beta strand	143	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Beta strand	149	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Beta strand	174	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Helix	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Helix	200	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Helix	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Beta strand	213	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Helix	225	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Helix	231	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+Q92328	UniProtKB	Beta strand	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD	
+##sequence-region P38295 1 451
+P38295	UniProtKB	Chain	1	451	.	.	.	ID=PRO_0000212454;Note=Medium-chain fatty acid ethyl ester synthase/esterase 2	
+P38295	UniProtKB	Domain	166	430	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38295	UniProtKB	Active site	247	247	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38295	UniProtKB	Active site	395	395	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38295	UniProtKB	Active site	423	423	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38295	UniProtKB	Cross-link	114	114	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P47167 1 239
+P47167	UniProtKB	Chain	1	239	.	.	.	ID=PRO_0000096283;Note=Central kinetochore subunit MCM22	
+##sequence-region P29469 1 868
+P29469	UniProtKB	Chain	1	868	.	.	.	ID=PRO_0000194091;Note=DNA replication licensing factor MCM2	
+P29469	UniProtKB	Domain	493	700	.	.	.	Note=MCM	
+P29469	UniProtKB	Zinc finger	341	367	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29469	UniProtKB	Nucleotide binding	543	550	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29469	UniProtKB	Motif	675	678	.	.	.	Note=Arginine finger	
+P29469	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P29469	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P29469	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P29469	UniProtKB	Modified residue	164	164	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P29469	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P29469	UniProtKB	Natural variant	392	392	.	.	.	Note=In allele MCM2-1. E->K	
+P29469	UniProtKB	Mutagenesis	364	364	.	.	.	Note=Loss of activity. C->Y%2CF%2CS%2CH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044961;Dbxref=PMID:2044961	
+P29469	UniProtKB	Mutagenesis	367	367	.	.	.	Note=Loss of activity. C->Y%2CF%2CS%2CH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044961;Dbxref=PMID:2044961	
+P29469	UniProtKB	Mutagenesis	549	549	.	.	.	Note=Reduces MCM2-7 complex helicase activity. Abolishes MCM2-7 complex helicase activity%3B when associated with MCM5 A-422. Reduces MCM2-7 complex helicase activity%3B when associated with MCM3 A-415. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510	
+P29469	UniProtKB	Mutagenesis	676	676	.	.	.	Note=Loss of MCM2-7 complex helicase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510	
+P29469	UniProtKB	Sequence conflict	164	164	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29469	UniProtKB	Sequence conflict	172	173	.	.	.	Note=MD->IH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29469	UniProtKB	Sequence conflict	529	529	.	.	.	Note=G->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29469	UniProtKB	Sequence conflict	578	578	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29469	UniProtKB	Sequence conflict	583	583	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29469	UniProtKB	Sequence conflict	712	712	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29469	UniProtKB	Sequence conflict	733	747	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29469	UniProtKB	Sequence conflict	859	868	.	.	.	Note=RSFAIYTLGH->SLSQFIPWVTKTLLFLRISGYEDKKFSVSIHVLAILFSIYKFPLFFV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P30665 1 933
+P30665	UniProtKB	Chain	1	933	.	.	.	ID=PRO_0000194105;Note=DNA replication licensing factor MCM4	
+P30665	UniProtKB	Domain	518	725	.	.	.	Note=MCM	
+P30665	UniProtKB	Nucleotide binding	568	575	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P30665	UniProtKB	Motif	700	703	.	.	.	Note=Arginine finger	
+P30665	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P30665	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P30665	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P30665	UniProtKB	Mutagenesis	574	574	.	.	.	Note=Loss of MCM2-7 complex helicase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510	
+##sequence-region P53091 1 1017
+P53091	UniProtKB	Chain	1	1017	.	.	.	ID=PRO_0000194117;Note=DNA replication licensing factor MCM6	
+P53091	UniProtKB	Domain	525	732	.	.	.	Note=MCM	
+P53091	UniProtKB	Nucleotide binding	575	582	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53091	UniProtKB	Motif	707	710	.	.	.	Note=Arginine finger	
+P53091	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53091	UniProtKB	Modified residue	249	249	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53091	UniProtKB	Modified residue	372	372	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53091	UniProtKB	Modified residue	766	766	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53091	UniProtKB	Mutagenesis	581	581	.	.	.	Note=Loss of MCM2-7 complex helicase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510	
+P53091	UniProtKB	Sequence conflict	179	179	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38132 1 845
+P38132	UniProtKB	Chain	1	845	.	.	.	ID=PRO_0000194124;Note=DNA replication licensing factor MCM7	
+P38132	UniProtKB	Domain	410	617	.	.	.	Note=MCM	
+P38132	UniProtKB	Nucleotide binding	460	467	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38132	UniProtKB	Motif	592	595	.	.	.	Note=Arginine finger	
+P38132	UniProtKB	Modified residue	811	811	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P38132	UniProtKB	Modified residue	819	819	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38132	UniProtKB	Modified residue	838	838	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38132	UniProtKB	Mutagenesis	466	466	.	.	.	Note=Loss of MCM2-7 complex helicase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510	
+P38132	UniProtKB	Sequence conflict	552	552	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38132	UniProtKB	Sequence conflict	552	552	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38132	UniProtKB	Sequence conflict	556	558	.	.	.	Note=TLN->NPG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38132	UniProtKB	Sequence conflict	556	558	.	.	.	Note=TLN->NPG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38132	UniProtKB	Sequence conflict	574	574	.	.	.	Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38132	UniProtKB	Sequence conflict	574	574	.	.	.	Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32419 1 343
+P32419	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1447211;Dbxref=PMID:1447211	
+P32419	UniProtKB	Chain	2	343	.	.	.	ID=PRO_0000113342;Note=Malate dehydrogenase%2C peroxisomal	
+P32419	UniProtKB	Nucleotide binding	8	14	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32419	UniProtKB	Nucleotide binding	116	118	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32419	UniProtKB	Active site	187	187	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32419	UniProtKB	Binding site	34	34	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32419	UniProtKB	Binding site	80	80	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P32419	UniProtKB	Binding site	86	86	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P32419	UniProtKB	Binding site	93	93	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32419	UniProtKB	Binding site	118	118	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P32419	UniProtKB	Binding site	152	152	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P32419	UniProtKB	Binding site	237	237	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32419	UniProtKB	Sequence conflict	240	240	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05930 1 598
+Q05930	UniProtKB	Chain	1	598	.	.	.	ID=PRO_0000119969;Note=Mitochondrial distribution and morphology protein 30	
+Q05930	UniProtKB	Domain	13	59	.	.	.	Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080	
+##sequence-region Q12285 1 212
+Q12285	UniProtKB	Chain	1	212	.	.	.	ID=PRO_0000235917;Note=Ubiquitin-like protein MDY2	
+Q12285	UniProtKB	Domain	74	152	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+Q12285	UniProtKB	Helix	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LKU	
+Q12285	UniProtKB	Helix	8	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12285	UniProtKB	Helix	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV	
+Q12285	UniProtKB	Beta strand	74	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20	
+Q12285	UniProtKB	Beta strand	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20	
+Q12285	UniProtKB	Beta strand	86	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20	
+Q12285	UniProtKB	Helix	98	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20	
+Q12285	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20	
+Q12285	UniProtKB	Beta strand	117	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20	
+Q12285	UniProtKB	Beta strand	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20	
+Q12285	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20	
+Q12285	UniProtKB	Beta strand	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM	
+Q12285	UniProtKB	Beta strand	143	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20	
+Q12285	UniProtKB	Helix	179	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VEJ	
+Q12285	UniProtKB	Turn	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VEJ	
+Q12285	UniProtKB	Helix	194	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VEJ	
+##sequence-region P32259 1 974
+P32259	UniProtKB	Chain	1	974	.	.	.	ID=PRO_0000096364;Note=Mediator of RNA polymerase II transcription subunit 16	
+P32259	UniProtKB	Motif	889	893	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32259	UniProtKB	Compositional bias	63	81	.	.	.	Note=Ser/Thr-rich	
+##sequence-region Q08278 1 222
+Q08278	UniProtKB	Chain	1	222	.	.	.	ID=PRO_0000096393;Note=Mediator of RNA polymerase II transcription subunit 7	
+Q08278	UniProtKB	Helix	18	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+Q08278	UniProtKB	Helix	25	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+Q08278	UniProtKB	Helix	61	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+Q08278	UniProtKB	Helix	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+Q08278	UniProtKB	Helix	112	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH	
+Q08278	UniProtKB	Beta strand	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH	
+Q08278	UniProtKB	Helix	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH	
+Q08278	UniProtKB	Helix	144	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH	
+Q08278	UniProtKB	Helix	166	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH	
+##sequence-region P38304 1 223
+P38304	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9918841;Dbxref=PMID:9918841	
+P38304	UniProtKB	Chain	2	223	.	.	.	ID=PRO_0000096397;Note=Mediator of RNA polymerase II transcription subunit 8	
+P38304	UniProtKB	Region	2	138	.	.	.	Note=Interaction with TBP1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16964259;Dbxref=PMID:16964259	
+P38304	UniProtKB	Coiled coil	33	59	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38304	UniProtKB	Helix	198	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZS	
+##sequence-region P24719 1 497
+P24719	UniProtKB	Chain	1	497	.	.	.	ID=PRO_0000086321;Note=Meiosis-specific serine/threonine-protein kinase MEK1	
+P24719	UniProtKB	Domain	47	102	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+P24719	UniProtKB	Domain	162	444	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P24719	UniProtKB	Nucleotide binding	168	176	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P24719	UniProtKB	Active site	290	290	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P24719	UniProtKB	Binding site	199	199	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region Q12198 1 575
+Q12198	UniProtKB	Chain	1	575	.	.	.	ID=PRO_0000114782;Note=Putative cystathionine gamma-synthase YLL058W	
+Q12198	UniProtKB	Modified residue	376	376	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q99257 1 599
+Q99257	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q99257	UniProtKB	Chain	2	599	.	.	.	ID=PRO_0000220542;Note=mRNA export factor MEX67	
+Q99257	UniProtKB	Repeat	163	184	.	.	.	Note=LRR 1	
+Q99257	UniProtKB	Repeat	189	210	.	.	.	Note=LRR 2	
+Q99257	UniProtKB	Domain	224	262	.	.	.	Note=LRRCT	
+Q99257	UniProtKB	Domain	280	467	.	.	.	Note=NTF2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00137	
+Q99257	UniProtKB	Domain	546	599	.	.	.	Note=TAP-C;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00611	
+Q99257	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q99257	UniProtKB	Mutagenesis	400	400	.	.	.	Note=Impairs association with the nuclear pores and interaction with MTR2. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10952996;Dbxref=PMID:10952996	
+Q99257	UniProtKB	Beta strand	24	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	35	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Beta strand	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Beta strand	59	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	67	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Beta strand	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Beta strand	87	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	102	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Turn	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Beta strand	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	131	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Beta strand	140	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	148	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Beta strand	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	177	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Beta strand	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	205	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Beta strand	218	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	225	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	232	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	254	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Beta strand	269	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	279	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Helix	296	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Beta strand	303	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Turn	332	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Turn	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	347	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+Q99257	UniProtKB	Helix	357	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Beta strand	371	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Turn	375	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Helix	379	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Beta strand	383	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Helix	390	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Beta strand	394	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Beta strand	441	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Beta strand	457	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+Q99257	UniProtKB	Helix	546	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7	
+Q99257	UniProtKB	Helix	563	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7	
+Q99257	UniProtKB	Turn	573	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7	
+Q99257	UniProtKB	Helix	578	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7	
+Q99257	UniProtKB	Turn	588	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7	
+Q99257	UniProtKB	Helix	593	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7	
+##sequence-region P34166 1 38
+P34166	UniProtKB	Propeptide	1	23	.	.	.	ID=PRO_0000021693;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3542988;Dbxref=PMID:3542988	
+P34166	UniProtKB	Peptide	24	35	.	.	.	ID=PRO_0000021694;Note=Mating hormone A-factor 2	
+P34166	UniProtKB	Propeptide	36	38	.	.	.	ID=PRO_0000021695;Note=Removed in mature form	
+P34166	UniProtKB	Modified residue	35	35	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3056940;Dbxref=PMID:3056940	
+P34166	UniProtKB	Lipidation	35	35	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3056940;Dbxref=PMID:3056940	
+##sequence-region P40578 1 1113
+P40578	UniProtKB	Chain	1	1113	.	.	.	ID=PRO_0000067074;Note=Protein MGA2	
+P40578	UniProtKB	Transmembrane	1037	1054	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40578	UniProtKB	Domain	530	610	.	.	.	Note=IPT/TIG	
+P40578	UniProtKB	Repeat	719	748	.	.	.	Note=ANK 1	
+P40578	UniProtKB	Repeat	752	781	.	.	.	Note=ANK 2	
+P40578	UniProtKB	Modified residue	255	255	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40578	UniProtKB	Modified residue	467	467	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+##sequence-region P43638 1 1398
+P43638	UniProtKB	Chain	1	1398	.	.	.	ID=PRO_0000072754;Note=MAP-homologous protein 1	
+P43638	UniProtKB	Region	1227	1258	.	.	.	Note=Tau/MAP repeat-like;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8947554;Dbxref=PMID:8947554	
+P43638	UniProtKB	Compositional bias	66	69	.	.	.	Note=Poly-Ser	
+P43638	UniProtKB	Compositional bias	128	137	.	.	.	Note=Poly-His	
+P43638	UniProtKB	Compositional bias	396	400	.	.	.	Note=Poly-Asn	
+P43638	UniProtKB	Compositional bias	423	426	.	.	.	Note=Poly-Ser	
+P43638	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P43638	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43638	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P43638	UniProtKB	Modified residue	309	309	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P43638	UniProtKB	Modified residue	311	311	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P43638	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43638	UniProtKB	Modified residue	357	357	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43638	UniProtKB	Modified residue	577	577	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P43638	UniProtKB	Cross-link	221	221	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P43638	UniProtKB	Sequence conflict	108	108	.	.	.	Note=R->RV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43638	UniProtKB	Sequence conflict	112	184	.	.	.	Note=KSVVETNLSNVEADSGHHHHHRHHHHTEDAPAPKKVGFFKSLFGHRKKDQEQQEKERERKERSPSPTHVDRGA->QWWRLTCLTLRLTPDIITTTATTITRKMLLHLRRSDSLRVCLAIGRRIRNNRRRNEKGKSAHPLRLTWTVAR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43638	UniProtKB	Sequence conflict	331	331	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43638	UniProtKB	Sequence conflict	419	419	.	.	.	Note=T->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43638	UniProtKB	Sequence conflict	594	595	.	.	.	Note=ID->MH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43638	UniProtKB	Sequence conflict	619	619	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43638	UniProtKB	Sequence conflict	659	660	.	.	.	Note=KQ->NE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43638	UniProtKB	Sequence conflict	1175	1176	.	.	.	Note=LL->FI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43638	UniProtKB	Sequence conflict	1309	1320	.	.	.	Note=KQGNQEETAFRT->NRETKKRPRSEP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43638	UniProtKB	Sequence conflict	1339	1339	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43638	UniProtKB	Sequence conflict	1356	1356	.	.	.	Note=A->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12525 1 324
+Q12525	UniProtKB	Chain	1	324	.	.	.	ID=PRO_0000114618;Note=Homocysteine S-methyltransferase 1	
+Q12525	UniProtKB	Domain	6	320	.	.	.	Note=Hcy-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333	
+Q12525	UniProtKB	Metal binding	238	238	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333	
+Q12525	UniProtKB	Metal binding	305	305	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333	
+Q12525	UniProtKB	Metal binding	306	306	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333	
+##sequence-region P38880 1 579
+P38880	UniProtKB	Transit peptide	1	47	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38880	UniProtKB	Chain	48	579	.	.	.	ID=PRO_0000021664;Note=Mitochondrial distribution and morphology protein 31	
+P38880	UniProtKB	Topological domain	48	114	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38880	UniProtKB	Transmembrane	115	135	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38880	UniProtKB	Topological domain	136	558	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38880	UniProtKB	Transmembrane	559	578	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38880	UniProtKB	Topological domain	579	579	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53083 1 459
+P53083	UniProtKB	Chain	1	459	.	.	.	ID=PRO_0000096331;Note=Mitochondrial distribution and morphology protein 34	
+##sequence-region Q12019 1 4910
+Q12019	UniProtKB	Chain	1	4910	.	.	.	ID=PRO_0000096337;Note=Midasin	
+Q12019	UniProtKB	Domain	4704	4899	.	.	.	Note=VWFA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00219	
+Q12019	UniProtKB	Nucleotide binding	315	322	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12019	UniProtKB	Nucleotide binding	653	660	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12019	UniProtKB	Nucleotide binding	1083	1090	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12019	UniProtKB	Nucleotide binding	1368	1375	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12019	UniProtKB	Nucleotide binding	1747	1754	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12019	UniProtKB	Nucleotide binding	2054	2061	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12019	UniProtKB	Compositional bias	768	771	.	.	.	Note=Poly-Lys	
+Q12019	UniProtKB	Compositional bias	2904	2907	.	.	.	Note=Poly-Leu	
+Q12019	UniProtKB	Compositional bias	4136	4139	.	.	.	Note=Poly-Glu	
+Q12019	UniProtKB	Modified residue	1026	1026	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12019	UniProtKB	Modified residue	2971	2971	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12019	UniProtKB	Modified residue	4353	4353	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12019	UniProtKB	Modified residue	4388	4388	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12019	UniProtKB	Modified residue	4555	4555	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q06213 1 157
+Q06213	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000096357;Note=Mediator of RNA polymerase II transcription subunit 10	
+##sequence-region P32585 1 307
+P32585	UniProtKB	Chain	1	307	.	.	.	ID=PRO_0000096368;Note=Mediator of RNA polymerase II transcription subunit 18	
+P32585	UniProtKB	Mutagenesis	22	22	.	.	.	Note=In SRB5-1%3B suppresses the phenotypic defects of an RNA polymerase II CTD truncation. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8324825;Dbxref=PMID:8324825	
+P32585	UniProtKB	Sequence conflict	225	225	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32585	UniProtKB	Beta strand	3	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Helix	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Helix	16	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Beta strand	32	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Helix	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Beta strand	64	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Helix	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Helix	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZS	
+P32585	UniProtKB	Turn	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZS	
+P32585	UniProtKB	Helix	87	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Beta strand	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Beta strand	164	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Helix	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Beta strand	180	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Helix	200	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Beta strand	209	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Helix	225	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Beta strand	229	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Beta strand	242	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Turn	246	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Beta strand	250	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Helix	265	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Turn	282	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Helix	293	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P32585	UniProtKB	Helix	299	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+##sequence-region P25046 1 220
+P25046	UniProtKB	Chain	1	220	.	.	.	ID=PRO_0000096370;Note=Mediator of RNA polymerase II transcription subunit 19	
+P25046	UniProtKB	Sequence conflict	18	18	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P34162 1 210
+P34162	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000096374;Note=Mediator of RNA polymerase II transcription subunit 20	
+P34162	UniProtKB	Compositional bias	1	210	.	.	.	Note=Ser/Thr/Tyr-rich	
+P34162	UniProtKB	Mutagenesis	14	14	.	.	.	Note=In SRB2-1%3B suppresses the phenotypic defects of an RNA polymerase II CTD truncation. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1591782;Dbxref=PMID:1591782	
+P34162	UniProtKB	Beta strand	4	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Helix	16	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Helix	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Beta strand	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZS	
+P34162	UniProtKB	Beta strand	35	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZS	
+P34162	UniProtKB	Beta strand	56	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Beta strand	76	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Helix	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Helix	104	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Turn	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Beta strand	116	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Beta strand	135	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Beta strand	147	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Helix	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Helix	163	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Beta strand	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+P34162	UniProtKB	Helix	196	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM	
+##sequence-region P40469 1 1032
+P40469	UniProtKB	Chain	1	1032	.	.	.	ID=PRO_0000096445;Note=DNA repair/transcription protein MET18/MMS19	
+P40469	UniProtKB	Repeat	40	77	.	.	.	Note=HEAT 1	
+P40469	UniProtKB	Repeat	121	160	.	.	.	Note=HEAT 2	
+P40469	UniProtKB	Repeat	256	293	.	.	.	Note=HEAT 3	
+P40469	UniProtKB	Repeat	463	500	.	.	.	Note=HEAT 4	
+P40469	UniProtKB	Repeat	504	542	.	.	.	Note=HEAT 5	
+P40469	UniProtKB	Repeat	550	587	.	.	.	Note=HEAT 6	
+P40469	UniProtKB	Repeat	614	651	.	.	.	Note=HEAT 7	
+P40469	UniProtKB	Repeat	759	796	.	.	.	Note=HEAT 8	
+P40469	UniProtKB	Repeat	808	850	.	.	.	Note=HEAT 9	
+P40469	UniProtKB	Repeat	863	901	.	.	.	Note=HEAT 10	
+P40469	UniProtKB	Repeat	906	943	.	.	.	Note=HEAT 11	
+P40469	UniProtKB	Repeat	947	987	.	.	.	Note=HEAT 12	
+P40469	UniProtKB	Repeat	992	1029	.	.	.	Note=HEAT 13	
+P40469	UniProtKB	Compositional bias	628	635	.	.	.	Note=Poly-Asn	
+P40469	UniProtKB	Natural variant	111	112	.	.	.	Note=In strain: SK1. AL->SF	
+P40469	UniProtKB	Natural variant	329	329	.	.	.	Note=In strain: SK1. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40469	UniProtKB	Natural variant	335	335	.	.	.	Note=In strain: SK1. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40469	UniProtKB	Natural variant	444	444	.	.	.	Note=In strain: SK1. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40469	UniProtKB	Natural variant	697	697	.	.	.	Note=In strain: SK1. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40469	UniProtKB	Natural variant	814	814	.	.	.	Note=In strain: SK1. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40469	UniProtKB	Natural variant	816	816	.	.	.	Note=In strain: SK1. K->M	
+P40469	UniProtKB	Natural variant	930	930	.	.	.	Note=In strain: SK1. A->T	
+P40469	UniProtKB	Natural variant	963	963	.	.	.	Note=In strain: SK1. H->Q	
+P40469	UniProtKB	Natural variant	969	969	.	.	.	Note=In strain: SK1. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40469	UniProtKB	Sequence conflict	230	230	.	.	.	Note=P->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40469	UniProtKB	Sequence conflict	329	329	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40469	UniProtKB	Sequence conflict	335	335	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40469	UniProtKB	Sequence conflict	361	361	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32179 1 357
+P32179	UniProtKB	Chain	1	357	.	.	.	ID=PRO_0000142537;Note=3'(2')%2C5'-bisphosphate nucleotidase	
+P32179	UniProtKB	Region	144	147	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32179	UniProtKB	Metal binding	72	72	.	.	.	Note=Magnesium 1	
+P32179	UniProtKB	Metal binding	142	142	.	.	.	Note=Magnesium 1	
+P32179	UniProtKB	Metal binding	142	142	.	.	.	Note=Magnesium 2	
+P32179	UniProtKB	Metal binding	144	144	.	.	.	Note=Magnesium 1%3B via carbonyl oxygen	
+P32179	UniProtKB	Metal binding	145	145	.	.	.	Note=Magnesium 2	
+P32179	UniProtKB	Metal binding	294	294	.	.	.	Note=Magnesium 2	
+P32179	UniProtKB	Binding site	72	72	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32179	UniProtKB	Binding site	294	294	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32179	UniProtKB	Natural variant	40	40	.	.	.	Note=In strain: Montrache. N->S	
+P32179	UniProtKB	Natural variant	61	61	.	.	.	Note=In strain: Montrache. K->M	
+P32179	UniProtKB	Natural variant	63	63	.	.	.	Note=In strain: Montrache. N->S	
+P32179	UniProtKB	Natural variant	308	308	.	.	.	Note=In strain: Montrache. I->V	
+P32179	UniProtKB	Helix	4	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Turn	31	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Helix	47	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Helix	80	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Helix	118	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	134	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Helix	147	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	157	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	167	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Helix	180	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Turn	189	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	196	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Turn	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K9Z	
+P32179	UniProtKB	Beta strand	206	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Turn	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	218	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K9Z	
+P32179	UniProtKB	Helix	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	232	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Turn	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Helix	244	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	258	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Helix	266	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	277	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Helix	292	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Helix	296	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	308	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	322	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	327	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Beta strand	331	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+P32179	UniProtKB	Helix	338	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1	
+##sequence-region P34165 1 36
+P34165	UniProtKB	Propeptide	1	21	.	.	.	ID=PRO_0000021690;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3542988;Dbxref=PMID:3542988	
+P34165	UniProtKB	Peptide	22	33	.	.	.	ID=PRO_0000021691;Note=Mating hormone A-factor 1	
+P34165	UniProtKB	Propeptide	34	36	.	.	.	ID=PRO_0000021692;Note=Removed in mature form	
+P34165	UniProtKB	Modified residue	33	33	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3056940;Dbxref=PMID:3056940	
+P34165	UniProtKB	Lipidation	33	33	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3056940;Dbxref=PMID:3056940	
+##sequence-region P32435 1 120
+P32435	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32435	UniProtKB	Propeptide	22	86	.	.	.	ID=PRO_0000419677	
+P32435	UniProtKB	Peptide	87	99	.	.	.	ID=PRO_0000021702;Note=Mating factor alpha-like	
+P32435	UniProtKB	Propeptide	102	107	.	.	.	ID=PRO_0000419678	
+P32435	UniProtKB	Peptide	108	120	.	.	.	ID=PRO_0000021703;Note=Mating factor alpha	
+##sequence-region P40002 1 666
+P40002	UniProtKB	Chain	1	666	.	.	.	ID=PRO_0000202617;Note=Transcriptional regulator MIT1	
+P40002	UniProtKB	Compositional bias	334	382	.	.	.	Note=Asn-rich	
+P40002	UniProtKB	Modified residue	152	152	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38286 1 347
+P38286	UniProtKB	Chain	1	347	.	.	.	ID=PRO_0000054868;Note=Very-long-chain 3-oxoacyl-CoA reductase	
+P38286	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03107	
+P38286	UniProtKB	Active site	223	223	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03107	
+P38286	UniProtKB	Binding site	210	210	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03107	
+##sequence-region P32490 1 508
+P32490	UniProtKB	Chain	1	508	.	.	.	ID=PRO_0000086332;Note=MAP kinase kinase MKK1/SSP32	
+P32490	UniProtKB	Domain	221	488	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32490	UniProtKB	Nucleotide binding	227	235	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32490	UniProtKB	Active site	349	349	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P32490	UniProtKB	Binding site	250	250	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32490	UniProtKB	Modified residue	192	192	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53141 1 149
+P53141	UniProtKB	Chain	1	149	.	.	.	ID=PRO_0000198765;Note=Myosin light chain 1	
+P53141	UniProtKB	Domain	2	37	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53141	UniProtKB	Domain	81	116	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53141	UniProtKB	Domain	117	149	.	.	.	Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53141	UniProtKB	Calcium binding	15	26	.	.	.	Note=1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53141	UniProtKB	Calcium binding	94	105	.	.	.	Note=2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53141	UniProtKB	Calcium binding	121	132	.	.	.	Note=3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53141	UniProtKB	Cross-link	116	116	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P53141	UniProtKB	Mutagenesis	93	93	.	.	.	Note=In MLC1-1%3B causes a defect in septum formation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12456647;Dbxref=PMID:12456647	
+P53141	UniProtKB	Mutagenesis	114	114	.	.	.	Note=In MLC1-11%3B abolishes interaction with MYO2 and IQG1 and reduces interaction with MYO1. Leads to mislocalization of IQG1 and a severe defect in cytokinesis. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15210731;Dbxref=PMID:15210731	
+P53141	UniProtKB	Mutagenesis	135	135	.	.	.	Note=In MLC1-93%3B reduces interaction with MYO1%2C but does not cause any defect in cytokinesis. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15210731;Dbxref=PMID:15210731	
+P53141	UniProtKB	Mutagenesis	142	142	.	.	.	Note=In MLC1-5%3B causes a defect in septum formation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12456647;Dbxref=PMID:12456647	
+P53141	UniProtKB	Helix	11	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Beta strand	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Helix	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Helix	27	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Helix	40	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Helix	51	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N2D	
+P53141	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Helix	61	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Helix	72	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Helix	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Helix	84	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Beta strand	95	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Helix	103	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Beta strand	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N2D	
+P53141	UniProtKB	Helix	119	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Beta strand	135	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P53141	UniProtKB	Helix	139	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+##sequence-region Q12083 1 715
+Q12083	UniProtKB	Chain	1	715	.	.	.	ID=PRO_0000245570;Note=DNA mismatch repair protein MLH3	
+##sequence-region P38998 1 373
+P38998	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:418069,ECO:0000269|Ref.4;Dbxref=PMID:418069	
+P38998	UniProtKB	Chain	2	373	.	.	.	ID=PRO_0000199016;Note=Saccharopine dehydrogenase [NAD(+)%2C L-lysine-forming]	
+P38998	UniProtKB	Active site	205	205	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:378997;Dbxref=PMID:378997	
+P38998	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4	
+P38998	UniProtKB	Sequence conflict	209	209	.	.	.	Note=A->AL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38998	UniProtKB	Sequence conflict	309	309	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38998	UniProtKB	Beta strand	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	23	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	35	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRL	
+P38998	UniProtKB	Helix	48	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	63	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	71	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	104	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UHA	
+P38998	UniProtKB	Helix	136	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	172	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Turn	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	196	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	204	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	223	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	228	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	239	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	243	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	274	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	308	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Beta strand	313	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	326	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Turn	345	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	351	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ	
+P38998	UniProtKB	Helix	370	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRL	
+##sequence-region P07702 1 1392
+P07702	UniProtKB	Chain	1	1392	.	.	.	ID=PRO_0000193153;Note=L-2-aminoadipate reductase	
+P07702	UniProtKB	Domain	843	920	.	.	.	Note=Carrier;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258	
+P07702	UniProtKB	Modified residue	880	880	.	.	.	Note=O-(pantetheine 4'-phosphoryl)serine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00258,ECO:0000269|PubMed:10320345;Dbxref=PMID:10320345	
+P07702	UniProtKB	Cross-link	541	541	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P07702	UniProtKB	Cross-link	1276	1276	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P49367 1 693
+P49367	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49367	UniProtKB	Chain	21	693	.	.	.	ID=PRO_0000000551;Note=Homoaconitase%2C mitochondrial	
+P49367	UniProtKB	Metal binding	340	340	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49367	UniProtKB	Metal binding	407	407	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49367	UniProtKB	Metal binding	410	410	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49367	UniProtKB	Sequence conflict	581	581	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38999 1 446
+P38999	UniProtKB	Chain	1	446	.	.	.	ID=PRO_0000212839;Note=Saccharopine dehydrogenase [NADP(+)%2C L-glutamate-forming]	
+P38999	UniProtKB	Sequence conflict	393	393	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38999	UniProtKB	Beta strand	3	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	14	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	27	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	36	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Turn	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	58	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	80	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	102	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Turn	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	128	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	146	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	176	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	186	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	193	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Turn	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	202	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	217	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	228	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	238	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	250	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Turn	260	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	269	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	277	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	292	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	308	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Turn	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	335	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	355	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	372	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	390	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	414	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Helix	422	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+P38999	UniProtKB	Beta strand	441	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ	
+##sequence-region O14467 1 151
+O14467	UniProtKB	Chain	1	151	.	.	.	ID=PRO_0000149814;Note=Multiprotein-bridging factor 1	
+O14467	UniProtKB	Domain	85	139	.	.	.	Note=HTH cro/C1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00257	
+O14467	UniProtKB	DNA binding	96	115	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00257	
+O14467	UniProtKB	Region	41	119	.	.	.	Note=Essential for TBP-binding	
+O14467	UniProtKB	Modified residue	143	143	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+O14467	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Reduces interaction to TBP. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9710580;Dbxref=PMID:9710580	
+##sequence-region Q08601 1 432
+Q08601	UniProtKB	Region	29	131	.	.	.	Note=Prion domain (PrD)	
+Q08601	UniProtKB	Active site	220	220	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08601	UniProtKB	Active site	276	276	.	.	.	.	
+Q08601	UniProtKB	Mutagenesis	276	276	.	.	.	Note=Blocks the processing and reduces caspase activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983181;Dbxref=PMID:11983181	
+Q08601	UniProtKB	Turn	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6O	
+Q08601	UniProtKB	Beta strand	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6O	
+Q08601	UniProtKB	Beta strand	136	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Helix	155	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Helix	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Beta strand	177	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Helix	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Helix	193	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Beta strand	212	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Beta strand	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Beta strand	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Helix	244	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Helix	252	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Turn	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Beta strand	268	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Beta strand	275	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Turn	279	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Beta strand	285	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Beta strand	292	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Beta strand	354	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Helix	380	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Helix	397	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Turn	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+Q08601	UniProtKB	Beta strand	415	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P	
+##sequence-region Q12106 1 302
+Q12106	UniProtKB	Chain	1	302	.	.	.	ID=PRO_0000245281;Note=MDM10-complementing protein 1	
+Q12106	UniProtKB	Topological domain	1	61	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023	
+Q12106	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12106	UniProtKB	Topological domain	83	100	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023	
+Q12106	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12106	UniProtKB	Topological domain	122	173	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023	
+Q12106	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12106	UniProtKB	Topological domain	195	219	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023	
+Q12106	UniProtKB	Transmembrane	220	240	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12106	UniProtKB	Topological domain	241	258	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023	
+Q12106	UniProtKB	Transmembrane	259	276	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12106	UniProtKB	Topological domain	277	302	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23781023;Dbxref=PMID:23781023	
+##sequence-region P35191 1 511
+P35191	UniProtKB	Transit peptide	1	55	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35191	UniProtKB	Chain	56	511	.	.	.	ID=PRO_0000007268;Note=DnaJ homolog 1%2C mitochondrial	
+P35191	UniProtKB	Domain	59	127	.	.	.	Note=J	
+P35191	UniProtKB	Repeat	230	237	.	.	.	Note=CXXCXGXG motif	
+P35191	UniProtKB	Repeat	247	254	.	.	.	Note=CXXCXGXG motif	
+P35191	UniProtKB	Repeat	269	276	.	.	.	Note=CXXCXGXG motif	
+P35191	UniProtKB	Repeat	285	292	.	.	.	Note=CXXCXGXG motif	
+P35191	UniProtKB	Zinc finger	217	297	.	.	.	Note=CR-type	
+P35191	UniProtKB	Compositional bias	130	186	.	.	.	Note=Gly-rich	
+##sequence-region P19659 1 1081
+P19659	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P19659	UniProtKB	Chain	2	1081	.	.	.	ID=PRO_0000096363;Note=Mediator of RNA polymerase II transcription subunit 15	
+P19659	UniProtKB	Repeat	422	423	.	.	.	Note=1	
+P19659	UniProtKB	Repeat	424	425	.	.	.	Note=2	
+P19659	UniProtKB	Repeat	426	427	.	.	.	Note=3	
+P19659	UniProtKB	Repeat	428	429	.	.	.	Note=4	
+P19659	UniProtKB	Repeat	430	431	.	.	.	Note=5	
+P19659	UniProtKB	Repeat	432	433	.	.	.	Note=6	
+P19659	UniProtKB	Repeat	434	435	.	.	.	Note=7	
+P19659	UniProtKB	Repeat	436	437	.	.	.	Note=8	
+P19659	UniProtKB	Repeat	438	439	.	.	.	Note=9	
+P19659	UniProtKB	Repeat	440	441	.	.	.	Note=10	
+P19659	UniProtKB	Repeat	442	443	.	.	.	Note=11	
+P19659	UniProtKB	Repeat	444	445	.	.	.	Note=12%3B approximate	
+P19659	UniProtKB	Repeat	446	447	.	.	.	Note=13%3B approximate	
+P19659	UniProtKB	Repeat	448	449	.	.	.	Note=14	
+P19659	UniProtKB	Repeat	450	451	.	.	.	Note=15	
+P19659	UniProtKB	Repeat	452	453	.	.	.	Note=16	
+P19659	UniProtKB	Repeat	454	455	.	.	.	Note=17	
+P19659	UniProtKB	Repeat	456	457	.	.	.	Note=18	
+P19659	UniProtKB	Repeat	458	459	.	.	.	Note=19	
+P19659	UniProtKB	Repeat	460	461	.	.	.	Note=20	
+P19659	UniProtKB	Repeat	462	463	.	.	.	Note=21	
+P19659	UniProtKB	Repeat	464	465	.	.	.	Note=22	
+P19659	UniProtKB	Repeat	466	467	.	.	.	Note=23	
+P19659	UniProtKB	Repeat	468	469	.	.	.	Note=24	
+P19659	UniProtKB	Repeat	470	471	.	.	.	Note=25	
+P19659	UniProtKB	Repeat	472	473	.	.	.	Note=26	
+P19659	UniProtKB	Repeat	474	475	.	.	.	Note=27	
+P19659	UniProtKB	Repeat	476	477	.	.	.	Note=28	
+P19659	UniProtKB	Repeat	478	479	.	.	.	Note=29	
+P19659	UniProtKB	Repeat	480	481	.	.	.	Note=30	
+P19659	UniProtKB	Region	422	481	.	.	.	Note=30 X 2 AA approximate tandem repeats of Q-A	
+P19659	UniProtKB	Compositional bias	147	158	.	.	.	Note=Poly-Gln	
+P19659	UniProtKB	Compositional bias	674	696	.	.	.	Note=Poly-Gln	
+P19659	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P19659	UniProtKB	Modified residue	335	335	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P19659	UniProtKB	Modified residue	736	736	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P19659	UniProtKB	Modified residue	752	752	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P19659	UniProtKB	Modified residue	783	783	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P19659	UniProtKB	Modified residue	785	785	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19659	UniProtKB	Modified residue	789	789	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19659	UniProtKB	Modified residue	793	793	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P19659	UniProtKB	Modified residue	831	831	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19659	UniProtKB	Modified residue	1003	1003	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P19659	UniProtKB	Modified residue	1008	1008	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P19659	UniProtKB	Modified residue	1018	1018	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P19659	UniProtKB	Modified residue	1034	1034	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P19659	UniProtKB	Sequence conflict	171	171	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19659	UniProtKB	Sequence conflict	302	302	.	.	.	Note=P->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19659	UniProtKB	Sequence conflict	499	499	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19659	UniProtKB	Sequence conflict	751	751	.	.	.	Note=P->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19659	UniProtKB	Beta strand	8	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0N	
+P19659	UniProtKB	Helix	14	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0N	
+P19659	UniProtKB	Helix	41	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0N	
+P19659	UniProtKB	Helix	63	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0N	
+P19659	UniProtKB	Helix	164	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB	
+P19659	UniProtKB	Helix	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB	
+P19659	UniProtKB	Helix	180	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB	
+P19659	UniProtKB	Helix	196	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB	
+P19659	UniProtKB	Helix	201	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB	
+P19659	UniProtKB	Helix	210	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB	
+##sequence-region P47822 1 140
+P47822	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000096377;Note=Mediator of RNA polymerase II transcription subunit 21	
+P47822	UniProtKB	Coiled coil	85	125	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47822	UniProtKB	Mutagenesis	21	21	.	.	.	Note=In SRB7-1%3B suppresses the phenotypic defects of an RNA polymerase II CTD truncation. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7774808;Dbxref=PMID:7774808	
+P47822	UniProtKB	Helix	3	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH	
+P47822	UniProtKB	Helix	31	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKE	
+P47822	UniProtKB	Helix	52	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH	
+P47822	UniProtKB	Turn	81	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH	
+P47822	UniProtKB	Helix	87	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH	
+##sequence-region Q02205 1 184
+Q02205	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02205	UniProtKB	Chain	2	184	.	.	.	ID=PRO_0000203193;Note=Protein MEH1	
+Q02205	UniProtKB	Coiled coil	30	71	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02205	UniProtKB	Modified residue	146	146	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q02205	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q02205	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16732272;Dbxref=PMID:16732272	
+Q02205	UniProtKB	Lipidation	7	7	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+Q02205	UniProtKB	Lipidation	8	8	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+Q02205	UniProtKB	Beta strand	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM	
+Q02205	UniProtKB	Helix	154	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM	
+Q02205	UniProtKB	Beta strand	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM	
+##sequence-region P33441 1 392
+P33441	UniProtKB	Chain	1	392	.	.	.	ID=PRO_0000096463;Note=THO complex subunit MFT1	
+P33441	UniProtKB	Modified residue	266	266	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P25573 1 417
+P25573	UniProtKB	Chain	1	417	.	.	.	ID=PRO_0000202546;Note=Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR1	
+P25573	UniProtKB	Topological domain	1	56	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16267274;Dbxref=PMID:16267274	
+P25573	UniProtKB	Transmembrane	57	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25573	UniProtKB	Topological domain	74	151	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16267274;Dbxref=PMID:16267274	
+P25573	UniProtKB	Transmembrane	152	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25573	UniProtKB	Topological domain	170	417	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16267274;Dbxref=PMID:16267274	
+##sequence-region Q96VH5 1 97
+Q96VH5	UniProtKB	Chain	1	97	.	.	.	ID=PRO_0000221640;Note=MICOS complex subunit MIC10	
+Q96VH5	UniProtKB	Topological domain	1	35	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q96VH5	UniProtKB	Transmembrane	36	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q96VH5	UniProtKB	Topological domain	59	97	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P50087 1 233
+P50087	UniProtKB	Chain	1	233	.	.	.	ID=PRO_0000202852;Note=MICOS subunit MIC26	
+P50087	UniProtKB	Topological domain	1	119	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50087	UniProtKB	Transmembrane	120	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50087	UniProtKB	Topological domain	138	141	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50087	UniProtKB	Transmembrane	142	164	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50087	UniProtKB	Topological domain	165	233	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P35201 1 549
+P35201	UniProtKB	Chain	1	549	.	.	.	ID=PRO_0000096486;Note=Protein MIF2	
+P35201	UniProtKB	DNA binding	356	364	.	.	.	Note=A.T hook	
+P35201	UniProtKB	Compositional bias	178	263	.	.	.	Note=Asp/Glu-rich (acidic)	
+P35201	UniProtKB	Modified residue	325	325	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P35201	UniProtKB	Turn	447	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV	
+P35201	UniProtKB	Beta strand	453	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV	
+P35201	UniProtKB	Helix	463	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV	
+P35201	UniProtKB	Beta strand	467	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV	
+P35201	UniProtKB	Beta strand	473	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV	
+P35201	UniProtKB	Beta strand	492	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV	
+P35201	UniProtKB	Beta strand	501	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV	
+P35201	UniProtKB	Beta strand	509	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV	
+P35201	UniProtKB	Beta strand	516	518	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV	
+P35201	UniProtKB	Beta strand	520	528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV	
+##sequence-region P27705 1 504
+P27705	UniProtKB	Chain	1	504	.	.	.	ID=PRO_0000046881;Note=Regulatory protein MIG1	
+P27705	UniProtKB	Zinc finger	38	60	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P27705	UniProtKB	Zinc finger	66	90	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P27705	UniProtKB	Compositional bias	253	260	.	.	.	Note=Gln-rich	
+P27705	UniProtKB	Compositional bias	411	444	.	.	.	Note=Asn/Gln-rich	
+P27705	UniProtKB	Modified residue	278	278	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27705	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P27705	UniProtKB	Modified residue	310	310	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27705	UniProtKB	Modified residue	311	311	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27705	UniProtKB	Modified residue	314	314	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27705	UniProtKB	Modified residue	377	377	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q06820 1 579
+Q06820	UniProtKB	Chain	1	579	.	.	.	ID=PRO_0000096332;Note=Mitochondrial distribution and morphology protein 36	
+Q06820	UniProtKB	Compositional bias	143	147	.	.	.	Note=Poly-Asp	
+Q06820	UniProtKB	Modified residue	42	42	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q08179 1 573
+Q08179	UniProtKB	Transit peptide	1	56	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08179	UniProtKB	Chain	57	573	.	.	.	ID=PRO_0000017697;Note=Mitochondrial distribution and morphology protein 38	
+Q08179	UniProtKB	Topological domain	57	138	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08179	UniProtKB	Transmembrane	139	159	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08179	UniProtKB	Topological domain	160	573	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08179	UniProtKB	Domain	182	404	.	.	.	Note=Letm1 RBD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01094	
+Q08179	UniProtKB	Coiled coil	408	440	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08179	UniProtKB	Coiled coil	503	541	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08179	UniProtKB	Compositional bias	423	552	.	.	.	Note=Glu-rich	
+Q08179	UniProtKB	Helix	183	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	212	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Beta strand	234	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	238	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	250	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	259	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	277	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	308	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	327	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	348	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	356	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Beta strand	359	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Beta strand	368	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	373	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Beta strand	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Helix	383	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+Q08179	UniProtKB	Turn	405	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ	
+##sequence-region Q02574 1 474
+Q02574	UniProtKB	Chain	1	474	.	.	.	ID=PRO_0000096344;Note=DNA damage checkpoint control protein MEC3	
+Q02574	UniProtKB	Modified residue	452	452	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02574	UniProtKB	Sequence conflict	120	120	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02574	UniProtKB	Sequence conflict	176	176	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02574	UniProtKB	Sequence conflict	454	454	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12321 1 566
+Q12321	UniProtKB	Chain	1	566	.	.	.	ID=PRO_0000096372;Note=Mediator of RNA polymerase II transcription subunit 1	
+Q12321	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12321	UniProtKB	Modified residue	423	423	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32570 1 121
+P32570	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32570	UniProtKB	Chain	2	121	.	.	.	ID=PRO_0000096379;Note=Mediator of RNA polymerase II transcription subunit 22	
+P32570	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32570	UniProtKB	Mutagenesis	86	86	.	.	.	Note=In SRB6-1%3B suppresses the phenotypic defects of an RNA polymerase II CTD truncation. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8324825;Dbxref=PMID:8324825	
+P32570	UniProtKB	Helix	4	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84	
+P32570	UniProtKB	Helix	42	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84	
+P32570	UniProtKB	Helix	50	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84	
+P32570	UniProtKB	Helix	101	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+##sequence-region Q12041 1 191
+Q12041	UniProtKB	Chain	1	191	.	.	.	ID=PRO_0000046809;Note=Transcriptional regulator MET32	
+Q12041	UniProtKB	Zinc finger	98	120	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q12041	UniProtKB	Zinc finger	126	150	.	.	.	Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+##sequence-region P43623 1 340
+P43623	UniProtKB	Chain	1	340	.	.	.	ID=PRO_0000114774;Note=Putative cystathionine beta-lyase	
+P43623	UniProtKB	Modified residue	208	208	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04533 1 649
+Q04533	UniProtKB	Chain	1	649	.	.	.	ID=PRO_0000114783;Note=Putative cystathionine gamma-synthase YML082W	
+Q04533	UniProtKB	Modified residue	287	287	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04533	UniProtKB	Modified residue	451	451	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P01149 1 165
+P01149	UniProtKB	Signal peptide	1	19	.	.	.	Note=Or 20;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:340452,ECO:0000305|Ref.7;Dbxref=PMID:340452	
+P01149	UniProtKB	Propeptide	20	89	.	.	.	ID=PRO_0000419673	
+P01149	UniProtKB	Peptide	90	102	.	.	.	ID=PRO_0000021697;Note=Mating factor alpha	
+P01149	UniProtKB	Propeptide	105	110	.	.	.	ID=PRO_0000419674	
+P01149	UniProtKB	Peptide	111	123	.	.	.	ID=PRO_0000021698;Note=Mating factor alpha	
+P01149	UniProtKB	Propeptide	126	131	.	.	.	ID=PRO_0000419675	
+P01149	UniProtKB	Peptide	132	144	.	.	.	ID=PRO_0000021699;Note=Mating factor alpha	
+P01149	UniProtKB	Propeptide	147	152	.	.	.	ID=PRO_0000419676	
+P01149	UniProtKB	Peptide	153	165	.	.	.	ID=PRO_0000021700;Note=Mating factor alpha	
+P01149	UniProtKB	Natural variant	165	165	.	.	.	Note=In strain: Italicus / IFO 0253. Y->YKREADAEAWHWLQLKPGQPMY	
+P01149	UniProtKB	Sequence conflict	42	42	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P01149	UniProtKB	Sequence conflict	107	107	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53050 1 456
+P53050	UniProtKB	Chain	1	456	.	.	.	ID=PRO_0000124593;Note=Protein MGA1	
+P53050	UniProtKB	DNA binding	3	118	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53050	UniProtKB	Compositional bias	182	185	.	.	.	Note=Poly-Gln	
+P53050	UniProtKB	Compositional bias	283	290	.	.	.	Note=Poly-Gln	
+##sequence-region P40081 1 178
+P40081	UniProtKB	Chain	1	178	.	.	.	ID=PRO_0000202650;Note=Putative magnesium-dependent phosphatase YER134C	
+P40081	UniProtKB	Active site	11	11	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40081	UniProtKB	Active site	13	13	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40081	UniProtKB	Metal binding	11	11	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40081	UniProtKB	Metal binding	13	13	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40081	UniProtKB	Metal binding	141	141	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40081	UniProtKB	Binding site	12	12	.	.	.	Note=Phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40081	UniProtKB	Binding site	13	13	.	.	.	Note=Phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40081	UniProtKB	Binding site	74	74	.	.	.	Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40081	UniProtKB	Binding site	75	75	.	.	.	Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40081	UniProtKB	Binding site	75	75	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q06630 1 226
+Q06630	UniProtKB	Chain	1	226	.	.	.	ID=PRO_0000255967;Note=Mitochondrial homologous recombination protein 1	
+Q06630	UniProtKB	Mutagenesis	172	172	.	.	.	Note=In MHR1-1%3B causes a defect in the partitioning of nascent mtDNA into buds and delays generation of homoplasmic cells. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12198175,ECO:0000269|PubMed:14565971;Dbxref=PMID:12198175,PMID:14565971	
+##sequence-region P43594 1 170
+P43594	UniProtKB	Chain	1	170	.	.	.	ID=PRO_0000202684;Note=MICOS complex subunit MIC19	
+##sequence-region P36027 1 376
+P36027	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36027	UniProtKB	Chain	26	376	.	.	.	ID=PRO_0000096485;Note=Cell wall integrity sensor MID2	
+P36027	UniProtKB	Topological domain	26	224	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36027	UniProtKB	Transmembrane	225	245	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36027	UniProtKB	Topological domain	246	376	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36027	UniProtKB	Compositional bias	31	219	.	.	.	Note=Ser-rich	
+P36027	UniProtKB	Modified residue	260	260	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36027	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36027	UniProtKB	Modified residue	329	329	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36027	UniProtKB	Modified residue	355	355	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36027	UniProtKB	Glycosylation	35	35	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36027	UniProtKB	Glycosylation	211	211	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36027	UniProtKB	Sequence conflict	303	304	.	.	.	Note=GG->VV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38760 1 659
+P38760	UniProtKB	Chain	1	659	.	.	.	ID=PRO_0000082032;Note=RNA-binding protein MIP6	
+P38760	UniProtKB	Domain	111	189	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P38760	UniProtKB	Domain	199	267	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P38760	UniProtKB	Domain	313	389	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P38760	UniProtKB	Beta strand	314	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78	
+P38760	UniProtKB	Helix	326	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78	
+P38760	UniProtKB	Turn	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78	
+P38760	UniProtKB	Beta strand	339	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78	
+P38760	UniProtKB	Beta strand	354	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78	
+P38760	UniProtKB	Helix	362	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78	
+P38760	UniProtKB	Beta strand	375	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78	
+P38760	UniProtKB	Beta strand	380	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78	
+##sequence-region Q02455 1 1875
+Q02455	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q02455	UniProtKB	Chain	2	1875	.	.	.	ID=PRO_0000096501;Note=Protein MLP1	
+Q02455	UniProtKB	Coiled coil	69	487	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02455	UniProtKB	Coiled coil	531	1678	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02455	UniProtKB	Coiled coil	1834	1866	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02455	UniProtKB	Motif	1496	1565	.	.	.	Note=Required for nuclear localization	
+Q02455	UniProtKB	Compositional bias	1804	1865	.	.	.	Note=Glu-rich	
+Q02455	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q02455	UniProtKB	Modified residue	337	337	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q02455	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02455	UniProtKB	Modified residue	1670	1670	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02455	UniProtKB	Modified residue	1710	1710	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q02455	UniProtKB	Modified residue	1733	1733	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02455	UniProtKB	Modified residue	1803	1803	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02455	UniProtKB	Sequence conflict	301	301	.	.	.	Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38300 1 278
+P38300	UniProtKB	Transit peptide	1	33	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38300	UniProtKB	Chain	34	278	.	.	.	ID=PRO_0000021656;Note=Inner membrane mitoribosome receptor MBA1%2C mitochondrial	
+##sequence-region P32354 1 571
+P32354	UniProtKB	Chain	1	571	.	.	.	ID=PRO_0000079949;Note=Minichromosome maintenance protein 10	
+P32354	UniProtKB	Region	309	335	.	.	.	Note=Zinc finger-like	
+P32354	UniProtKB	Region	435	512	.	.	.	Note=Sufficient for nuclear localization	
+P32354	UniProtKB	Region	453	553	.	.	.	Note=Sufficient for nuclear localization	
+P32354	UniProtKB	Motif	435	451	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32354	UniProtKB	Motif	512	527	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32354	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32354	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32354	UniProtKB	Modified residue	453	453	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32354	UniProtKB	Modified residue	454	454	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32354	UniProtKB	Mutagenesis	245	245	.	.	.	Note=Inhibits interaction with POL30/PCNA and abolishes cell proliferation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16782870;Dbxref=PMID:16782870	
+P32354	UniProtKB	Mutagenesis	261	261	.	.	.	Note=Temperature sensitive%3B loss of CDC17 stabilization. G->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16675460;Dbxref=PMID:16675460	
+P32354	UniProtKB	Mutagenesis	268	268	.	.	.	Note=Temperature sensitive%3B loss of CDC17 stabilization. N->D%2CI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16675460;Dbxref=PMID:16675460	
+P32354	UniProtKB	Mutagenesis	269	269	.	.	.	Note=In mcm10-1%3B diminishes interaction with MCM7. P->L	
+P32354	UniProtKB	Mutagenesis	320	320	.	.	.	Note=In mcm10-43%3B abolishes self-association and diminishes interaction with MCM7. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12844493;Dbxref=PMID:12844493	
+P32354	UniProtKB	Mutagenesis	332	332	.	.	.	Note=Abolishes self-association%3B when associated with L-335. C->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12844493;Dbxref=PMID:12844493	
+P32354	UniProtKB	Mutagenesis	335	335	.	.	.	Note=Abolishes self-association%3B when associated with G-332. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12844493;Dbxref=PMID:12844493	
+P32354	UniProtKB	Mutagenesis	449	451	.	.	.	Note=No effect on nuclear localization. RRR->GGG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:13680157;Dbxref=PMID:13680157	
+P32354	UniProtKB	Sequence conflict	38	38	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32354	UniProtKB	Sequence conflict	458	458	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32354	UniProtKB	Sequence conflict	492	571	.	.	.	Note=ISQVLKSSVSGSEPKNNLLGKKKTVINDLLHYKKEKVILAPSKNEWFKKRSHREEVWQKHFGSKETKETSDGSASDLEII->NFPKYSSLLYQGANLRTTYSVKKKLL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P22133 1 377
+P22133	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1986231,ECO:0000269|PubMed:3552052;Dbxref=PMID:1986231,PMID:3552052	
+P22133	UniProtKB	Chain	2	377	.	.	.	ID=PRO_0000113338;Note=Malate dehydrogenase%2C cytoplasmic	
+P22133	UniProtKB	Nucleotide binding	20	26	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22133	UniProtKB	Nucleotide binding	144	146	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22133	UniProtKB	Active site	215	215	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22133	UniProtKB	Binding site	57	57	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22133	UniProtKB	Binding site	106	106	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P22133	UniProtKB	Binding site	112	112	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P22133	UniProtKB	Binding site	119	119	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22133	UniProtKB	Binding site	146	146	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P22133	UniProtKB	Binding site	185	185	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004	
+P22133	UniProtKB	Binding site	266	266	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22133	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region O60200 1 86
+O60200	UniProtKB	Chain	1	86	.	.	.	ID=PRO_0000220526;Note=Mitochondrial distribution and morphology protein 35	
+O60200	UniProtKB	Domain	10	60	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+O60200	UniProtKB	Motif	13	23	.	.	.	Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+O60200	UniProtKB	Motif	42	52	.	.	.	Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+O60200	UniProtKB	Disulfide bond	13	52	.	.	.	Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4XHR,ECO:0000244|PDB:4XIZ,ECO:0000244|PDB:4YTV,ECO:0000244|PDB:4YTW,ECO:0000244|PDB:4YTX,ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000269|PubMed:26071601,ECO:0000269|PubMed:26235513;Dbxref=PMID:26071601,PMID:26235513	
+O60200	UniProtKB	Disulfide bond	23	42	.	.	.	Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4XHR,ECO:0000244|PDB:4XIZ,ECO:0000244|PDB:4YTV,ECO:0000244|PDB:4YTW,ECO:0000244|PDB:4YTX,ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000269|PubMed:26071601,ECO:0000269|PubMed:26235513;Dbxref=PMID:26071601,PMID:26235513	
+O60200	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Impairs interaction with UPS1 and UPS2%3B when associated with A-27 and A-28. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513	
+O60200	UniProtKB	Mutagenesis	27	27	.	.	.	Note=Impairs interaction with UPS1 and UPS2%3B when associated with A-24 and A-28. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513	
+O60200	UniProtKB	Mutagenesis	28	28	.	.	.	Note=Impairs interaction with UPS1 and UPS2%3B when associated with A-24 and A-27. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513	
+O60200	UniProtKB	Mutagenesis	32	32	.	.	.	Note=Impairs interaction with UPS1 and UPS2. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513	
+O60200	UniProtKB	Helix	4	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTV	
+O60200	UniProtKB	Helix	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+O60200	UniProtKB	Helix	14	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+O60200	UniProtKB	Turn	31	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+O60200	UniProtKB	Helix	43	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+O60200	UniProtKB	Helix	63	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW	
+##sequence-region P53094 1 1487
+P53094	UniProtKB	Chain	1	1487	.	.	.	ID=PRO_0000119137;Note=Negative regulator of sporulation MDS3	
+P53094	UniProtKB	Repeat	171	226	.	.	.	Note=Kelch 1	
+P53094	UniProtKB	Repeat	234	287	.	.	.	Note=Kelch 2	
+P53094	UniProtKB	Repeat	371	419	.	.	.	Note=Kelch 3	
+P53094	UniProtKB	Modified residue	472	472	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53094	UniProtKB	Modified residue	475	475	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53094	UniProtKB	Modified residue	621	621	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53094	UniProtKB	Modified residue	639	639	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P53094	UniProtKB	Modified residue	693	693	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53094	UniProtKB	Modified residue	698	698	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53094	UniProtKB	Modified residue	744	744	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53094	UniProtKB	Modified residue	747	747	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53094	UniProtKB	Modified residue	756	756	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53094	UniProtKB	Modified residue	757	757	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53094	UniProtKB	Modified residue	781	781	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53094	UniProtKB	Modified residue	785	785	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53094	UniProtKB	Modified residue	787	787	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53094	UniProtKB	Modified residue	900	900	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53094	UniProtKB	Modified residue	904	904	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53094	UniProtKB	Modified residue	930	930	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53094	UniProtKB	Modified residue	1187	1187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53094	UniProtKB	Sequence conflict	262	264	.	.	.	Note=QSE->HPK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53094	UniProtKB	Sequence conflict	262	264	.	.	.	Note=QSE->HPK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53094	UniProtKB	Sequence conflict	403	403	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53094	UniProtKB	Sequence conflict	403	403	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47025 1 714
+P47025	UniProtKB	Chain	1	714	.	.	.	ID=PRO_0000051477;Note=Mitochondrial division protein 1	
+P47025	UniProtKB	Repeat	396	436	.	.	.	Note=WD 1	
+P47025	UniProtKB	Repeat	439	478	.	.	.	Note=WD 2	
+P47025	UniProtKB	Repeat	500	539	.	.	.	Note=WD 3	
+P47025	UniProtKB	Repeat	561	603	.	.	.	Note=WD 4	
+P47025	UniProtKB	Repeat	604	642	.	.	.	Note=WD 5	
+P47025	UniProtKB	Repeat	644	681	.	.	.	Note=WD 6	
+P47025	UniProtKB	Repeat	685	714	.	.	.	Note=WD 7	
+P47025	UniProtKB	Coiled coil	240	298	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47025	UniProtKB	Modified residue	376	376	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47025	UniProtKB	Mutagenesis	148	148	.	.	.	Note=Abolishes interaction with FIS1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16272155;Dbxref=PMID:16272155	
+P47025	UniProtKB	Mutagenesis	250	250	.	.	.	Note=Suppresses the mitochondrial fission defect of a FIS1-3 mutant by affecting interaction with FIS1. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16247028;Dbxref=PMID:16247028	
+P47025	UniProtKB	Mutagenesis	400	400	.	.	.	Note=No interaction with FIS1%3B slight decrease in interaction with DNM1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14517324;Dbxref=PMID:14517324	
+P47025	UniProtKB	Mutagenesis	440	440	.	.	.	Note=Abolishes interaction with DNM1. H->E%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16272155;Dbxref=PMID:16272155	
+P47025	UniProtKB	Mutagenesis	461	461	.	.	.	Note=Slight decrease in interaction with FIS1%3B 20-fold decrease in interaction with DNM1%3B even distribution along mitochondria not punctate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14517324;Dbxref=PMID:14517324	
+P47025	UniProtKB	Mutagenesis	544	544	.	.	.	Note=Results in mitrochondrial division defect%2C but has no effect on the interaction with DNM1. N->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16272155;Dbxref=PMID:16272155	
+P47025	UniProtKB	Mutagenesis	605	605	.	.	.	Note=Abolishes interaction with DNM1. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16272155;Dbxref=PMID:16272155	
+P47025	UniProtKB	Mutagenesis	664	664	.	.	.	Note=Slight decrease in interaction with DNM1. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14517324;Dbxref=PMID:14517324	
+P47025	UniProtKB	Mutagenesis	689	689	.	.	.	Note=Slight decrease in interaction with DNM1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14517324;Dbxref=PMID:14517324	
+P47025	UniProtKB	Helix	148	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PQN	
+P47025	UniProtKB	Helix	231	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XU6	
+##sequence-region P19263 1 1082
+P19263	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P19263	UniProtKB	Chain	2	1082	.	.	.	ID=PRO_0000096362;Note=Mediator of RNA polymerase II transcription subunit 14	
+P19263	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P19263	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956	
+P19263	UniProtKB	Modified residue	1036	1036	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P19263	UniProtKB	Sequence conflict	46	46	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19263	UniProtKB	Sequence conflict	51	51	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19263	UniProtKB	Sequence conflict	56	56	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19263	UniProtKB	Sequence conflict	285	285	.	.	.	Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19263	UniProtKB	Sequence conflict	746	746	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P29467 1 408
+P29467	UniProtKB	Chain	1	408	.	.	.	ID=PRO_0000096402;Note=Meiosis-specific protein MEI4	
+P29467	UniProtKB	Sequence conflict	329	329	.	.	.	Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39692 1 1035
+P39692	UniProtKB	Chain	1	1035	.	.	.	ID=PRO_0000199947;Note=Sulfite reductase [NADPH] flavoprotein component	
+P39692	UniProtKB	Domain	648	879	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+P39692	UniProtKB	Nucleotide binding	684	695	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39692	UniProtKB	Nucleotide binding	814	824	.	.	.	Note=FAD (flavin part);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39692	UniProtKB	Sequence conflict	172	172	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39692	UniProtKB	Sequence conflict	420	420	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39692	UniProtKB	Sequence conflict	977	977	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39014 1 640
+P39014	UniProtKB	Chain	1	640	.	.	.	ID=PRO_0000051087;Note=F-box protein MET30	
+P39014	UniProtKB	Domain	181	227	.	.	.	Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080	
+P39014	UniProtKB	Repeat	300	328	.	.	.	Note=WD 1	
+P39014	UniProtKB	Repeat	340	368	.	.	.	Note=WD 2	
+P39014	UniProtKB	Repeat	380	408	.	.	.	Note=WD 3	
+P39014	UniProtKB	Repeat	419	449	.	.	.	Note=WD 4	
+P39014	UniProtKB	Repeat	461	499	.	.	.	Note=WD 5	
+P39014	UniProtKB	Repeat	509	538	.	.	.	Note=WD 6	
+P39014	UniProtKB	Repeat	550	578	.	.	.	Note=WD 7	
+P39014	UniProtKB	Repeat	607	635	.	.	.	Note=WD 8	
+P39014	UniProtKB	Region	1	299	.	.	.	Note=Necessary to mediate nuclear localization	
+P39014	UniProtKB	Region	180	277	.	.	.	Note=Important for mediating homomultimerization	
+P39014	UniProtKB	Region	180	225	.	.	.	Note=Interaction with SKP1/CBF3D	
+P39014	UniProtKB	Region	277	640	.	.	.	Note=Interaction with MET4	
+P39014	UniProtKB	Modified residue	67	67	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39014	UniProtKB	Mutagenesis	187	187	.	.	.	Note=Strongly reduces nuclear localization%3B inhibits interaction with SKP1/CBF3D. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14660673;Dbxref=PMID:14660673	
+P39014	UniProtKB	Mutagenesis	190	190	.	.	.	Note=Strongly reduces nuclear localization%3B inhibits interaction with SKP1/CBF3D. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14660673;Dbxref=PMID:14660673	
+P39014	UniProtKB	Mutagenesis	386	386	.	.	.	Note=Inactivates MET30 and prevents MET4 interaction%3B when associated with A-425 and A-467. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15883825;Dbxref=PMID:15883825	
+P39014	UniProtKB	Mutagenesis	425	425	.	.	.	Note=Inactivates MET30 and prevents MET4 interaction%3B when associated with D-530 or D-386 and A-467. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15883825;Dbxref=PMID:15883825	
+P39014	UniProtKB	Mutagenesis	467	467	.	.	.	Note=Inactivates MET30 and prevents MET4 interaction%3B when associated with D-386 and A-425. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15883825;Dbxref=PMID:15883825	
+P39014	UniProtKB	Mutagenesis	530	530	.	.	.	Note=Inactivates MET30 and prevents MET4 interaction%3B when associated with A-425. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15883825;Dbxref=PMID:15883825	
+P39014	UniProtKB	Sequence conflict	61	61	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P08536 1 511
+P08536	UniProtKB	Chain	1	511	.	.	.	ID=PRO_0000105954;Note=Sulfate adenylyltransferase	
+P08536	UniProtKB	Nucleotide binding	194	198	.	.	.	Note=ATP	
+P08536	UniProtKB	Nucleotide binding	289	293	.	.	.	Note=ATP	
+P08536	UniProtKB	Region	1	167	.	.	.	Note=N-terminal	
+P08536	UniProtKB	Region	168	393	.	.	.	Note=Catalytic	
+P08536	UniProtKB	Region	394	511	.	.	.	Note=Required for oligomerization%3B adenylyl-sulfate kinase-like	
+P08536	UniProtKB	Active site	196	196	.	.	.	.	
+P08536	UniProtKB	Active site	197	197	.	.	.	.	
+P08536	UniProtKB	Active site	198	198	.	.	.	.	
+P08536	UniProtKB	Binding site	204	204	.	.	.	Note=Substrate	
+P08536	UniProtKB	Binding site	331	331	.	.	.	Note=ATP%3B via amide nitrogen	
+P08536	UniProtKB	Binding site	355	355	.	.	.	Note=Substrate	
+P08536	UniProtKB	Binding site	356	356	.	.	.	Note=Substrate%3B via carbonyl oxygen	
+P08536	UniProtKB	Site	201	201	.	.	.	Note=Transition state stabilizer	
+P08536	UniProtKB	Site	204	204	.	.	.	Note=Transition state stabilizer	
+P08536	UniProtKB	Site	328	328	.	.	.	Note=Induces change in substrate recognition on ATP binding	
+P08536	UniProtKB	Sequence conflict	221	221	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08536	UniProtKB	Helix	12	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	20	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	32	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	39	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Turn	51	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	62	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	90	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	101	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Turn	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	110	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	125	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	140	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	151	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Turn	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+P08536	UniProtKB	Helix	176	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	191	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	202	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	235	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	267	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	284	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Turn	290	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	309	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	324	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	331	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	335	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	339	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Turn	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Beta strand	348	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	358	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Turn	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	378	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X	
+P08536	UniProtKB	Helix	391	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+P08536	UniProtKB	Beta strand	396	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+P08536	UniProtKB	Helix	408	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+P08536	UniProtKB	Beta strand	428	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+P08536	UniProtKB	Helix	437	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+P08536	UniProtKB	Helix	443	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+P08536	UniProtKB	Beta strand	452	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+P08536	UniProtKB	Helix	461	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+P08536	UniProtKB	Beta strand	472	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+P08536	UniProtKB	Beta strand	482	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+P08536	UniProtKB	Helix	492	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F	
+##sequence-region P47164 1 639
+P47164	UniProtKB	Chain	1	639	.	.	.	ID=PRO_0000114781;Note=Cystathionine gamma-synthase	
+P47164	UniProtKB	Modified residue	443	443	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P19358 1 384
+P19358	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P19358	UniProtKB	Chain	2	384	.	.	.	ID=PRO_0000174452;Note=S-adenosylmethionine synthase 2	
+P19358	UniProtKB	Nucleotide binding	168	170	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266	
+P19358	UniProtKB	Nucleotide binding	236	239	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266	
+P19358	UniProtKB	Nucleotide binding	253	254	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P19358	UniProtKB	Metal binding	12	12	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13444	
+P19358	UniProtKB	Metal binding	46	46	.	.	.	Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P19358	UniProtKB	Binding site	18	18	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266	
+P19358	UniProtKB	Binding site	59	59	.	.	.	Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P19358	UniProtKB	Binding site	102	102	.	.	.	Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P19358	UniProtKB	Binding site	247	247	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266	
+P19358	UniProtKB	Binding site	247	247	.	.	.	Note=Methionine%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P19358	UniProtKB	Binding site	270	270	.	.	.	Note=ATP%3B via amide nitrogen%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P19358	UniProtKB	Binding site	274	274	.	.	.	Note=ATP%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P19358	UniProtKB	Binding site	278	278	.	.	.	Note=ATP%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13444	
+P19358	UniProtKB	Binding site	278	278	.	.	.	Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817	
+P19358	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P19358	UniProtKB	Sequence conflict	130	130	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02889 1 113
+Q02889	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000252278;Note=Protein MGR2	
+Q02889	UniProtKB	Topological domain	1	22	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02889	UniProtKB	Transmembrane	23	43	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02889	UniProtKB	Topological domain	44	56	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02889	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02889	UniProtKB	Topological domain	78	113	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E835 1 90
+Q3E835	UniProtKB	Chain	1	90	.	.	.	ID=PRO_0000235928;Note=MHF histone-fold complex subunit 1	
+Q3E835	UniProtKB	Mutagenesis	55	55	.	.	.	Note=Disrupts the heterotetrameric state and becomes hypersensitive to MMS%3B when associated with A-62. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22325783;Dbxref=PMID:22325783	
+Q3E835	UniProtKB	Mutagenesis	62	62	.	.	.	Note=Disrupts the heterotetrameric state and becomes hypersensitive to MMS%3B when associated with A-55 or 78-AA-79. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22325783;Dbxref=PMID:22325783	
+Q3E835	UniProtKB	Mutagenesis	78	79	.	.	.	Note=Disrupts the heterotetrameric state and becomes hypersensitive to MMS%3B when associated with A-62. RK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22325783;Dbxref=PMID:22325783	
+Q3E835	UniProtKB	Helix	3	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R	
+Q3E835	UniProtKB	Helix	35	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R	
+Q3E835	UniProtKB	Beta strand	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R	
+Q3E835	UniProtKB	Helix	70	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R	
+Q3E835	UniProtKB	Turn	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R	
+Q3E835	UniProtKB	Helix	81	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R	
+##sequence-region P36051 1 919
+P36051	UniProtKB	Chain	1	919	.	.	.	ID=PRO_0000211412;Note=GPI ethanolamine phosphate transferase 1	
+P36051	UniProtKB	Topological domain	1	9	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	31	457	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	458	478	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	479	488	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	489	509	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	510	512	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	513	533	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	534	553	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	554	574	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	575	576	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	577	597	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	598	598	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	599	619	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	620	626	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	627	647	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	648	655	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	656	676	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	677	687	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	688	708	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	709	720	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	721	741	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	742	776	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	777	797	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	798	807	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	808	828	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	829	848	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	849	869	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	870	885	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Transmembrane	886	906	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Topological domain	907	919	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Glycosylation	90	90	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Glycosylation	138	138	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Glycosylation	198	198	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Glycosylation	202	202	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Glycosylation	286	286	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Glycosylation	312	312	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36051	UniProtKB	Mutagenesis	227	227	.	.	.	Note=In mcd4-174%3B defective in endoplasmic reticulum-to-Golgi transport of GPI-anchored proteins. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10069808;Dbxref=PMID:10069808	
+P36051	UniProtKB	Mutagenesis	302	302	.	.	.	Note=Induces auxotrophy for ethanolamine. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11470244;Dbxref=PMID:11470244	
+P36051	UniProtKB	Mutagenesis	916	917	.	.	.	Note=No effect on subcellular location. KK->SS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10069808;Dbxref=PMID:10069808	
+##sequence-region P21965 1 375
+P21965	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P21965	UniProtKB	Chain	2	375	.	.	.	ID=PRO_0000086317;Note=Protein kinase MCK1	
+P21965	UniProtKB	Domain	35	327	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P21965	UniProtKB	Nucleotide binding	41	49	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P21965	UniProtKB	Active site	164	164	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P21965	UniProtKB	Binding site	68	68	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P21965	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P21965	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P21965	UniProtKB	Modified residue	199	199	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P21965	UniProtKB	Modified residue	202	202	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P24279 1 971
+P24279	UniProtKB	Chain	1	971	.	.	.	ID=PRO_0000194099;Note=DNA replication licensing factor MCM3	
+P24279	UniProtKB	Domain	359	566	.	.	.	Note=MCM	
+P24279	UniProtKB	Nucleotide binding	409	416	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24279	UniProtKB	Motif	541	544	.	.	.	Note=Arginine finger	
+P24279	UniProtKB	Modified residue	761	761	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P24279	UniProtKB	Modified residue	777	777	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P24279	UniProtKB	Modified residue	781	781	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P24279	UniProtKB	Modified residue	868	868	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P24279	UniProtKB	Mutagenesis	415	415	.	.	.	Note=No effect on MCM2-7 complex helicase activity. Loss of MCM2-7 complex helicase activity%3B when associated with MCM5 A-422. Reduces MCM2-7 complex helicase activity%3B when associated with MCM2 A-549. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510	
+##sequence-region Q12171 1 622
+Q12171	UniProtKB	Transit peptide	1	70	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12171	UniProtKB	Chain	71	622	.	.	.	ID=PRO_0000021665;Note=Mitochondrial distribution and morphology protein 32	
+Q12171	UniProtKB	Topological domain	71	123	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12171	UniProtKB	Transmembrane	124	144	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12171	UniProtKB	Topological domain	145	601	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12171	UniProtKB	Transmembrane	602	622	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q99278 1 115
+Q99278	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000096358;Note=Mediator of RNA polymerase II transcription subunit 11	
+Q99278	UniProtKB	Coiled coil	56	107	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99278	UniProtKB	Mutagenesis	17	17	.	.	.	Note=Results in a decrease of TFIIK and RNA polymerase II occupancies at active promoters%3B when associated with K-24. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21498544;Dbxref=PMID:21498544	
+Q99278	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Results in a decrease of TFIIK and RNA polymerase II occupancies at active promoters%3B when associated with K-17. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21498544;Dbxref=PMID:21498544	
+Q99278	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Impairs interaction with RAD3%2C reducing the interaction of TFIIH with the head module and consequently resulting in a reduction of RNA polymerase II CTD 'Ser-5' phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18691966;Dbxref=PMID:18691966	
+Q99278	UniProtKB	Mutagenesis	66	66	.	.	.	Note=Impairs interaction with SRB4/MED17%2C SRB6/MED22 and RAD3. L->P	
+Q99278	UniProtKB	Mutagenesis	92	92	.	.	.	Note=Impairs interaction with SRB4/MED17. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18691966;Dbxref=PMID:18691966	
+Q99278	UniProtKB	Helix	5	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84	
+Q99278	UniProtKB	Helix	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84	
+Q99278	UniProtKB	Helix	45	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84	
+Q99278	UniProtKB	Turn	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84	
+Q99278	UniProtKB	Helix	94	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+##sequence-region Q12343 1 284
+Q12343	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12343	UniProtKB	Chain	2	284	.	.	.	ID=PRO_0000096386;Note=Mediator of RNA polymerase II transcription subunit 4	
+Q12343	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12343	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphothreonine%3B by KIN28;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15126497;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198,PMID:15126497	
+Q12343	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+##sequence-region P33308 1 149
+P33308	UniProtKB	Chain	1	149	.	.	.	ID=PRO_0000076529;Note=Mediator of RNA polymerase II transcription subunit 9	
+P33308	UniProtKB	Motif	77	99	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33308	UniProtKB	Motif	136	149	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P08465 1 486
+P08465	UniProtKB	Chain	1	486	.	.	.	ID=PRO_0000155758;Note=Homoserine O-acetyltransferase	
+P08465	UniProtKB	Domain	66	436	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08465	UniProtKB	Active site	162	162	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P45131	
+P08465	UniProtKB	Active site	401	401	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P45131	
+P08465	UniProtKB	Active site	430	430	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P45131	
+P08465	UniProtKB	Sequence conflict	429	486	.	.	.	Note=GHDAFLLEFKLINKLIVQFLKTNCKAITDAAPRAWGGDVGNDETKTSVFGEAEEVTNW->ATMPSYWSLS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08465	UniProtKB	Sequence conflict	429	486	.	.	.	Note=GHDAFLLEFKLINKLIVQFLKTNCKAITDAAPRAWGGDVGNDETKTSVFGEAEEVTNW->ATMPSYWSLS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53338 1 473
+P53338	UniProtKB	Chain	1	473	.	.	.	ID=PRO_0000114956;Note=Maltose fermentation regulatory protein MAL13	
+P53338	UniProtKB	DNA binding	13	39	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P53338	UniProtKB	Motif	46	54	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38158 1 584
+P38158	UniProtKB	Chain	1	584	.	.	.	ID=PRO_0000054329;Note=Alpha-glucosidase MAL32	
+P38158	UniProtKB	Active site	214	214	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38158	UniProtKB	Active site	276	276	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38158	UniProtKB	Site	349	349	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P40513 1 266
+P40513	UniProtKB	Transit peptide	1	47	.	.	.	Note=Mitochondrion	
+P40513	UniProtKB	Chain	48	266	.	.	.	ID=PRO_0000018589;Note=Mitochondrial acidic protein MAM33	
+P40513	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40513	UniProtKB	Sequence conflict	129	129	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40513	UniProtKB	Helix	50	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Helix	74	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Beta strand	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Beta strand	95	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Beta strand	108	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Helix	115	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Beta strand	151	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Beta strand	166	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Turn	175	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Beta strand	179	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Helix	191	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Helix	199	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Helix	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Helix	219	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+P40513	UniProtKB	Helix	236	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0	
+##sequence-region Q12296 1 706
+Q12296	UniProtKB	Chain	1	706	.	.	.	ID=PRO_0000255960;Note=Protein MAM3	
+Q12296	UniProtKB	Topological domain	1	16	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12296	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12296	UniProtKB	Topological domain	38	65	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12296	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12296	UniProtKB	Topological domain	87	120	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12296	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12296	UniProtKB	Topological domain	142	145	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12296	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12296	UniProtKB	Topological domain	167	177	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12296	UniProtKB	Transmembrane	178	198	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12296	UniProtKB	Topological domain	199	706	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12296	UniProtKB	Domain	65	233	.	.	.	Note=DUF21	
+Q12296	UniProtKB	Domain	259	320	.	.	.	Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+Q12296	UniProtKB	Domain	321	386	.	.	.	Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+Q12296	UniProtKB	Modified residue	439	439	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12296	UniProtKB	Modified residue	447	447	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12296	UniProtKB	Modified residue	527	527	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q12296	UniProtKB	Modified residue	603	603	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12296	UniProtKB	Modified residue	604	604	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12296	UniProtKB	Modified residue	607	607	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12296	UniProtKB	Modified residue	614	614	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P03879 1 638
+P03879	UniProtKB	Region	1	253	.	.	.	Note=COB exons 1 to 4 encoded	
+P03879	UniProtKB	Region	253	638	.	.	.	Note=COB intron 4 encoded	
+P03879	UniProtKB	Sequence conflict	370	370	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03879	UniProtKB	Sequence conflict	390	390	.	.	.	Note=T->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03879	UniProtKB	Sequence conflict	433	433	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03879	UniProtKB	Sequence conflict	459	459	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03879	UniProtKB	Sequence conflict	465	465	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03879	UniProtKB	Sequence conflict	586	586	.	.	.	Note=T->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39678 1 833
+P39678	UniProtKB	Chain	1	833	.	.	.	ID=PRO_0000067062;Note=Transcription factor MBP1	
+P39678	UniProtKB	Domain	5	111	.	.	.	Note=HTH APSES-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630	
+P39678	UniProtKB	Repeat	394	423	.	.	.	Note=ANK 1	
+P39678	UniProtKB	Repeat	512	541	.	.	.	Note=ANK 2	
+P39678	UniProtKB	DNA binding	36	57	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630	
+P39678	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39678	UniProtKB	Modified residue	325	325	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39678	UniProtKB	Modified residue	326	326	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39678	UniProtKB	Modified residue	330	330	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39678	UniProtKB	Modified residue	827	827	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39678	UniProtKB	Beta strand	5	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8	
+P39678	UniProtKB	Beta strand	13	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8	
+P39678	UniProtKB	Beta strand	24	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8	
+P39678	UniProtKB	Turn	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8	
+P39678	UniProtKB	Beta strand	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1L3G	
+P39678	UniProtKB	Helix	36	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8	
+P39678	UniProtKB	Helix	47	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8	
+P39678	UniProtKB	Turn	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8	
+P39678	UniProtKB	Beta strand	64	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8	
+P39678	UniProtKB	Turn	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MB1	
+P39678	UniProtKB	Beta strand	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8	
+P39678	UniProtKB	Helix	80	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8	
+P39678	UniProtKB	Helix	93	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8	
+##sequence-region P23493 1 339
+P23493	UniProtKB	Chain	1	339	.	.	.	ID=PRO_0000096271;Note=Mitochondrial biogenesis regulation protein 1	
+P23493	UniProtKB	Modified residue	159	159	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23493	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23493	UniProtKB	Modified residue	224	224	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23493	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23493	UniProtKB	Sequence conflict	88	88	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23493	UniProtKB	Sequence conflict	168	168	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23493	UniProtKB	Sequence conflict	206	206	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23493	UniProtKB	Sequence conflict	245	245	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q01159 1 459
+Q01159	UniProtKB	Chain	1	459	.	.	.	ID=PRO_0000210106;Note=mRNA-capping enzyme subunit alpha	
+Q01159	UniProtKB	Active site	70	70	.	.	.	Note=N6-GMP-lysine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8022828;Dbxref=PMID:8022828	
+Q01159	UniProtKB	Mutagenesis	57	57	.	.	.	Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	58	58	.	.	.	Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	59	59	.	.	.	Note=No effect. K->A%2CT%2CS%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8022828;Dbxref=PMID:8022828	
+Q01159	UniProtKB	Mutagenesis	66	66	.	.	.	Note=Temperature-sensitive. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	70	70	.	.	.	Note=Lethal. K->A%2CR%2CM%2CI%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8022828;Dbxref=PMID:8022828	
+Q01159	UniProtKB	Mutagenesis	71	71	.	.	.	Note=No effect. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	72	72	.	.	.	Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Lethal. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Temperature-sensitive. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	96	96	.	.	.	Note=Temperature-sensitive. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Temperature-sensitive. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	107	109	.	.	.	Note=Reduced growth at 25 degrees and lethal at 37 degrees. RFP->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	114	114	.	.	.	Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	115	115	.	.	.	Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	116	116	.	.	.	Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	117	117	.	.	.	Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	118	118	.	.	.	Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	129	129	.	.	.	Note=No effect. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Lethal. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Temperature-sensitive. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	132	132	.	.	.	Note=Lethal. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	134	134	.	.	.	Note=No effect. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	218	218	.	.	.	Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	219	219	.	.	.	Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Lethal. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	226	226	.	.	.	Note=Lethal. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	241	241	.	.	.	Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	242	242	.	.	.	Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	249	249	.	.	.	Note=Lethal. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	253	253	.	.	.	Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	254	254	.	.	.	Note=No effect. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	255	255	.	.	.	Note=Temperature-sensitive. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	257	257	.	.	.	Note=Lethal. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	274	274	.	.	.	Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	275	275	.	.	.	Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	276	276	.	.	.	Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	395	395	.	.	.	Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Mutagenesis	396	396	.	.	.	Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582	
+Q01159	UniProtKB	Sequence conflict	45	45	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01159	UniProtKB	Sequence conflict	300	300	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01159	UniProtKB	Helix	21	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	53	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	65	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	73	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Turn	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	89	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	100	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	126	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Turn	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	144	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	166	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	178	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	197	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	210	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	224	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	238	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Turn	251	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	257	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	291	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	300	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Turn	313	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	317	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Turn	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	324	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Turn	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	337	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	350	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Turn	358	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	365	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Beta strand	372	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	378	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	395	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	399	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+Q01159	UniProtKB	Helix	402	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH	
+##sequence-region P32783 1 436
+P32783	UniProtKB	Chain	1	436	.	.	.	ID=PRO_0000210134;Note=mRNA cap guanine-N7 methyltransferase	
+P32783	UniProtKB	Domain	101	430	.	.	.	Note=mRNA cap 0 methyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895	
+P32783	UniProtKB	Region	150	151	.	.	.	Note=mRNA cap binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895	
+P32783	UniProtKB	Binding site	154	154	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895	
+P32783	UniProtKB	Binding site	172	172	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895	
+P32783	UniProtKB	Binding site	194	194	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895	
+P32783	UniProtKB	Binding site	223	223	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43148	
+P32783	UniProtKB	Binding site	249	249	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43148	
+P32783	UniProtKB	Binding site	253	253	.	.	.	Note=mRNA cap;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895	
+P32783	UniProtKB	Binding site	254	254	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43148	
+P32783	UniProtKB	Binding site	347	347	.	.	.	Note=mRNA cap;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895	
+P32783	UniProtKB	Binding site	416	416	.	.	.	Note=mRNA cap;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895	
+P32783	UniProtKB	Site	175	175	.	.	.	Note=mRNA cap binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895	
+P32783	UniProtKB	Site	181	181	.	.	.	Note=mRNA cap binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895	
+P32783	UniProtKB	Site	206	206	.	.	.	Note=mRNA cap binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895	
+P32783	UniProtKB	Mutagenesis	168	168	.	.	.	Note=Still viable%3B normal growth. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	170	170	.	.	.	Note=Non-viable%3B reduced enzyme activity to 8%25 of wild-type. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431	
+P32783	UniProtKB	Mutagenesis	170	170	.	.	.	Note=Still viable%3B increase in activity. E->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431	
+P32783	UniProtKB	Mutagenesis	170	170	.	.	.	Note=Non-viable%3B reduced enzyme activity to 8%25 of wild-type. E->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431	
+P32783	UniProtKB	Mutagenesis	172	172	.	.	.	Note=Still viable%3B normal growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	174	174	.	.	.	Note=Non viable%3B no growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073	
+P32783	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Still viable%3B normal growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	178	178	.	.	.	Note=Microcolony formation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073	
+P32783	UniProtKB	Mutagenesis	181	181	.	.	.	Note=Still viable%3B normal growth. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	182	182	.	.	.	Note=Still viable%3B normal growth. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	194	194	.	.	.	Note=Lethal%3B no enzyme activity. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431	
+P32783	UniProtKB	Mutagenesis	194	194	.	.	.	Note=Still viable%3B activity near to wild-type. D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431	
+P32783	UniProtKB	Mutagenesis	194	194	.	.	.	Note=Lethal%3B no enzyme activity. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431	
+P32783	UniProtKB	Mutagenesis	206	206	.	.	.	Note=Lethal. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431	
+P32783	UniProtKB	Mutagenesis	206	206	.	.	.	Note=Still viable%3B little change in enzyme activity. R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431	
+P32783	UniProtKB	Mutagenesis	253	253	.	.	.	Note=Still viable%3B normal growth. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073	
+P32783	UniProtKB	Mutagenesis	254	254	.	.	.	Note=Non viable%3B no growth. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8552073,ECO:0000269|PubMed:9169431;Dbxref=PMID:8552073,PMID:9169431	
+P32783	UniProtKB	Mutagenesis	254	254	.	.	.	Note=Still viable%3B slow growth%3B near to wild-type enzyme activity. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8552073,ECO:0000269|PubMed:9169431;Dbxref=PMID:8552073,PMID:9169431	
+P32783	UniProtKB	Mutagenesis	254	254	.	.	.	Note=Lethal%3B Enzyme activity 10%25 of wild-type. Y->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8552073,ECO:0000269|PubMed:9169431;Dbxref=PMID:8552073,PMID:9169431	
+P32783	UniProtKB	Mutagenesis	276	276	.	.	.	Note=Still viable%3B normal growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	277	277	.	.	.	Note=Still viable%3B normal growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	282	282	.	.	.	Note=Still viable%3B normal growth. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073	
+P32783	UniProtKB	Mutagenesis	287	287	.	.	.	Note=Still viable%3B normal growth. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073	
+P32783	UniProtKB	Mutagenesis	347	347	.	.	.	Note=Still viable%3B normal growth. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	348	348	.	.	.	Note=Still viable%3B normal growth. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	349	349	.	.	.	Note=Still viable%3B normal growth. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	350	350	.	.	.	Note=Still viable%3B normal growth. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	361	361	.	.	.	Note=Still viable%3B normal growth. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073	
+P32783	UniProtKB	Mutagenesis	362	362	.	.	.	Note=Still viable%3B normal growth. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073	
+P32783	UniProtKB	Mutagenesis	363	363	.	.	.	Note=Still viable%3B normal growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	366	366	.	.	.	Note=Still viable%3B normal growth. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	367	367	.	.	.	Note=Still viable%3B normal growth. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Mutagenesis	372	372	.	.	.	Note=Still viable%3B normal growth. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431	
+P32783	UniProtKB	Sequence conflict	126	126	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02891 1 456
+Q02891	UniProtKB	Chain	1	456	.	.	.	ID=PRO_0000212456;Note=Medium-chain fatty acid ethyl ester synthase/esterase 1	
+Q02891	UniProtKB	Domain	168	434	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02891	UniProtKB	Active site	251	251	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02891	UniProtKB	Active site	399	399	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02891	UniProtKB	Active site	428	428	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P42834 1 146
+P42834	UniProtKB	Chain	1	146	.	.	.	ID=PRO_0000071094;Note=Mitochondrial DnaJ homolog 2	
+P42834	UniProtKB	Domain	85	146	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+##sequence-region P33310 1 695
+P33310	UniProtKB	Transit peptide	1	100	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33310	UniProtKB	Chain	101	695	.	.	.	ID=PRO_0000045330;Note=ATP-dependent permease MDL1%2C mitochondrial	
+P33310	UniProtKB	Transmembrane	103	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P33310	UniProtKB	Transmembrane	156	176	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P33310	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P33310	UniProtKB	Transmembrane	337	357	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P33310	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P33310	UniProtKB	Domain	103	398	.	.	.	Note=ABC transmembrane type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P33310	UniProtKB	Domain	432	673	.	.	.	Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P33310	UniProtKB	Nucleotide binding	467	474	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P33310	UniProtKB	Mutagenesis	467	467	.	.	.	Note=Decreased release of long peptides from mitochondria. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11251115;Dbxref=PMID:11251115	
+P33310	UniProtKB	Mutagenesis	575	575	.	.	.	Note=Decreased release of long peptides from mitochondria. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11251115;Dbxref=PMID:11251115	
+P33310	UniProtKB	Mutagenesis	598	598	.	.	.	Note=Decreased release of long peptides from mitochondria. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11251115;Dbxref=PMID:11251115	
+P33310	UniProtKB	Sequence conflict	22	22	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33310	UniProtKB	Sequence conflict	150	150	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33310	UniProtKB	Sequence conflict	267	268	.	.	.	Note=GA->WP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33310	UniProtKB	Sequence conflict	313	314	.	.	.	Note=NE->KQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33311 1 773
+P33311	UniProtKB	Transit peptide	1	90	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33311	UniProtKB	Chain	91	773	.	.	.	ID=PRO_0000045331;Note=ATP-dependent permease MDL2%2C mitochondrial	
+P33311	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P33311	UniProtKB	Transmembrane	170	192	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P33311	UniProtKB	Transmembrane	257	277	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P33311	UniProtKB	Domain	119	413	.	.	.	Note=ABC transmembrane type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P33311	UniProtKB	Domain	493	733	.	.	.	Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P33311	UniProtKB	Nucleotide binding	481	488	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P33311	UniProtKB	Sequence conflict	56	56	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33311	UniProtKB	Sequence conflict	265	265	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33311	UniProtKB	Sequence conflict	752	752	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32489 1 222
+P32489	UniProtKB	Chain	1	222	.	.	.	ID=PRO_0000096403;Note=Meiosis protein 5	
+P32489	UniProtKB	Sequence conflict	155	156	.	.	.	Note=SD->VT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32489	UniProtKB	Sequence conflict	160	162	.	.	.	Note=QLS->RTFR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32489	UniProtKB	Sequence conflict	168	168	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32489	UniProtKB	Sequence conflict	217	217	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P29496 1 775
+P29496	UniProtKB	Chain	1	775	.	.	.	ID=PRO_0000194111;Note=Minichromosome maintenance protein 5	
+P29496	UniProtKB	Domain	366	573	.	.	.	Note=MCM	
+P29496	UniProtKB	Nucleotide binding	416	423	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P29496	UniProtKB	Motif	548	551	.	.	.	Note=Arginine finger	
+P29496	UniProtKB	Compositional bias	351	356	.	.	.	Note=Poly-Glu	
+P29496	UniProtKB	Mutagenesis	422	422	.	.	.	Note=Loss of MCM2-7 complex helicase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510	
+##sequence-region Q06567 1 569
+Q06567	UniProtKB	Transit peptide	1	18	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06567	UniProtKB	Chain	19	569	.	.	.	ID=PRO_0000200737;Note=ABC1 family protein MCP2	
+Q06567	UniProtKB	Topological domain	19	34	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023	
+Q06567	UniProtKB	Transmembrane	35	51	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06567	UniProtKB	Topological domain	52	569	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23781023;Dbxref=PMID:23781023	
+##sequence-region P36060 1 302
+P36060	UniProtKB	Chain	1	302	.	.	.	ID=PRO_0000019404;Note=NADH-cytochrome b5 reductase p34 form	
+P36060	UniProtKB	Propeptide	1	41	.	.	.	ID=PRO_0000019405;Note=Removed in p32 form;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8001120,ECO:0000269|PubMed:9866716;Dbxref=PMID:8001120,PMID:9866716	
+P36060	UniProtKB	Chain	42	302	.	.	.	ID=PRO_0000019406;Note=NADH-cytochrome b5 reductase p32 form	
+P36060	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36060	UniProtKB	Domain	51	155	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+P36060	UniProtKB	Nucleotide binding	158	193	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36060	UniProtKB	Site	41	42	.	.	.	Note=Cleavage%3B by IMP1	
+P36060	UniProtKB	Modified residue	278	278	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P36060	UniProtKB	Mutagenesis	23	24	.	.	.	Note=Prevents insertion into the outer membrane and increases the efficiency of import into the intermembrane space. AA->QQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9199337;Dbxref=PMID:9199337	
+P36060	UniProtKB	Sequence conflict	2	2	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36060	UniProtKB	Sequence conflict	101	101	.	.	.	Note=N->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53885 1 366
+P53885	UniProtKB	Chain	1	366	.	.	.	ID=PRO_0000096326;Note=Signal transduction protein MDG1	
+P53885	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53885	UniProtKB	Modified residue	216	216	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53885	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53885	UniProtKB	Cross-link	314	314	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P32569 1 687
+P32569	UniProtKB	Chain	1	687	.	.	.	ID=PRO_0000096366;Note=Mediator of RNA polymerase II transcription subunit 17	
+P32569	UniProtKB	Mutagenesis	353	353	.	.	.	Note=In SRB4-1%3B suppresses the phenotypic defects of an RNA polymerase II CTD truncation. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8324825;Dbxref=PMID:8324825	
+P32569	UniProtKB	Sequence conflict	430	431	.	.	.	Note=QL->PI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32569	UniProtKB	Sequence conflict	647	647	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32569	UniProtKB	Beta strand	388	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Beta strand	403	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Helix	425	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Helix	450	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Beta strand	457	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Beta strand	464	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Beta strand	470	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Helix	498	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Turn	525	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Helix	535	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Helix	542	565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Turn	566	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Beta strand	574	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Helix	597	604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Helix	607	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Beta strand	614	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Beta strand	630	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Beta strand	640	642	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Beta strand	644	650	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Turn	654	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Beta strand	660	665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+P32569	UniProtKB	Helix	667	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62	
+##sequence-region Q12124 1 431
+Q12124	UniProtKB	Chain	1	431	.	.	.	ID=PRO_0000096381;Note=Mediator of RNA polymerase II transcription subunit 2	
+Q12124	UniProtKB	Compositional bias	107	142	.	.	.	Note=Glu-rich	
+Q12124	UniProtKB	Compositional bias	264	412	.	.	.	Note=Asn-rich	
+Q12124	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12124	UniProtKB	Modified residue	208	208	.	.	.	Note=Phosphoserine%3B by CDK8;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14988503,ECO:0000269|PubMed:16109375;Dbxref=PMID:14988503,PMID:16109375	
+Q12124	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Reduces expression of several genes from the endogenous 2-micron plasmid and augments expression of numerous iron-response genes. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14988503,ECO:0000269|PubMed:16109375;Dbxref=PMID:14988503,PMID:16109375	
+##sequence-region P38633 1 127
+P38633	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000212534;Note=Mediator of RNA polymerase II transcription subunit 31	
+P38633	UniProtKB	Helix	22	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+P38633	UniProtKB	Helix	36	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+P38633	UniProtKB	Helix	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+P38633	UniProtKB	Helix	53	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+P38633	UniProtKB	Helix	61	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+P38633	UniProtKB	Helix	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+P38633	UniProtKB	Helix	77	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+P38633	UniProtKB	Beta strand	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+P38633	UniProtKB	Helix	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI	
+##sequence-region P40260 1 492
+P40260	UniProtKB	Chain	1	492	.	.	.	ID=PRO_0000139754;Note=Ammonium transporter MEP1	
+P40260	UniProtKB	Topological domain	1	18	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Transmembrane	19	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Topological domain	40	49	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Topological domain	71	109	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Topological domain	131	140	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Topological domain	162	174	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Topological domain	196	210	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Transmembrane	211	231	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Topological domain	232	240	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Topological domain	262	268	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Transmembrane	269	289	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Topological domain	290	290	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Transmembrane	291	311	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Topological domain	312	331	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Transmembrane	332	352	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Topological domain	353	373	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Transmembrane	374	394	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Topological domain	395	492	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40260	UniProtKB	Modified residue	442	442	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40260	UniProtKB	Modified residue	445	445	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P16523 1 270
+P16523	UniProtKB	Chain	1	270	.	.	.	ID=PRO_0000050120;Note=Meiotic recombination 1 protein	
+P16523	UniProtKB	Domain	191	225	.	.	.	Note=KH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+##sequence-region P32389 1 672
+P32389	UniProtKB	Chain	1	672	.	.	.	ID=PRO_0000076519;Note=Transcriptional activator of sulfur metabolism MET4	
+P32389	UniProtKB	Domain	586	649	.	.	.	Note=bZIP	
+P32389	UniProtKB	Region	95	144	.	.	.	Note=Transcriptional activation	
+P32389	UniProtKB	Region	188	235	.	.	.	Note=Inhibitory region%3B AdoMet responsiveness%3B required for interaction with MET30	
+P32389	UniProtKB	Region	312	375	.	.	.	Note=Auxiliary%3B required for high transcriptional activity under nonrepressive growth conditions	
+P32389	UniProtKB	Region	375	403	.	.	.	Note=Required for interaction with MET31 and MET32	
+P32389	UniProtKB	Region	601	612	.	.	.	Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32389	UniProtKB	Region	614	642	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32389	UniProtKB	Coiled coil	609	648	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32389	UniProtKB	Compositional bias	53	57	.	.	.	Note=Poly-Ser	
+P32389	UniProtKB	Compositional bias	106	242	.	.	.	Note=Asn-rich	
+P32389	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32389	UniProtKB	Modified residue	564	564	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32389	UniProtKB	Sequence conflict	441	442	.	.	.	Note=RG->AA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32389	UniProtKB	Sequence conflict	441	442	.	.	.	Note=RG->AA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P15807 1 274
+P15807	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000096446;Note=Siroheme biosynthesis protein MET8	
+P15807	UniProtKB	Nucleotide binding	23	24	.	.	.	Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703	
+P15807	UniProtKB	Nucleotide binding	43	45	.	.	.	Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703	
+P15807	UniProtKB	Active site	141	141	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15807	UniProtKB	Binding site	93	93	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703	
+P15807	UniProtKB	Mutagenesis	22	22	.	.	.	Note=Loss of dehydrogenase activity. No effect on chelatase activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703	
+P15807	UniProtKB	Mutagenesis	141	141	.	.	.	Note=Loss of chelatase and dehydrogenase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703	
+P15807	UniProtKB	Mutagenesis	237	237	.	.	.	Note=No effect on dehydrogenase or chelatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703	
+P15807	UniProtKB	Sequence conflict	15	15	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15807	UniProtKB	Sequence conflict	33	33	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15807	UniProtKB	Sequence conflict	61	61	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15807	UniProtKB	Sequence conflict	102	102	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15807	UniProtKB	Beta strand	5	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Beta strand	15	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	23	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Beta strand	38	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	50	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Turn	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Beta strand	86	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Beta strand	107	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	117	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Beta strand	135	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Beta strand	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Beta strand	152	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Turn	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Beta strand	160	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	171	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	193	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	217	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	241	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Turn	253	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+P15807	UniProtKB	Helix	264	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ	
+##sequence-region P36013 1 669
+P36013	UniProtKB	Active site	187	187	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36013	UniProtKB	Active site	259	259	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36013	UniProtKB	Metal binding	330	330	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36013	UniProtKB	Metal binding	331	331	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36013	UniProtKB	Metal binding	354	354	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36013	UniProtKB	Binding site	354	354	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36013	UniProtKB	Binding site	499	499	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36013	UniProtKB	Site	354	354	.	.	.	Note=Important for activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P03873 1 423
+P03873	UniProtKB	Chain	1	423	.	.	.	ID=PRO_0000061914;Note=Cytochrome b mRNA maturase bI2	
+P03873	UniProtKB	Topological domain	1	31	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P03873	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968	
+P03873	UniProtKB	Topological domain	53	84	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P03873	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968	
+P03873	UniProtKB	Topological domain	106	115	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P03873	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968	
+P03873	UniProtKB	Topological domain	137	153	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P03873	UniProtKB	Transmembrane	154	174	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968	
+P03873	UniProtKB	Topological domain	175	423	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P03873	UniProtKB	Region	1	143	.	.	.	Note=Cytochrome b	
+P03873	UniProtKB	Region	144	423	.	.	.	Note=Maturase	
+P03873	UniProtKB	Natural variant	122	122	.	.	.	Note=In strain: 777-3A. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7004642;Dbxref=PMID:7004642	
+P03873	UniProtKB	Natural variant	221	221	.	.	.	Note=In strain: Capensis / YB4237. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8670880;Dbxref=PMID:8670880	
+P03873	UniProtKB	Natural variant	315	315	.	.	.	Note=In strain: Capensis / YB4237. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8670880;Dbxref=PMID:8670880	
+P03873	UniProtKB	Natural variant	324	324	.	.	.	Note=In strain: 777-3A. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7004642;Dbxref=PMID:7004642	
+P03873	UniProtKB	Natural variant	355	355	.	.	.	Note=In strain: Capensis / YB4237. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8670880;Dbxref=PMID:8670880	
+P03873	UniProtKB	Natural variant	382	382	.	.	.	Note=In strain: Capensis / YB4237. T->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8670880;Dbxref=PMID:8670880	
+P03873	UniProtKB	Mutagenesis	228	228	.	.	.	Note=In M1282 / M4111%3B abolishes maturase and endonuclease activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843	
+P03873	UniProtKB	Mutagenesis	233	233	.	.	.	Note=Abolishes endonuclease activity. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843	
+P03873	UniProtKB	Mutagenesis	235	235	.	.	.	Note=In M4962%3B abolishes maturase and endonuclease activity. H->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843	
+P03873	UniProtKB	Mutagenesis	339	339	.	.	.	Note=Abolishes maturase and endonuclease activity. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843	
+P03873	UniProtKB	Mutagenesis	343	343	.	.	.	Note=Abolishes endonuclease activity. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843	
+P03873	UniProtKB	Mutagenesis	344	344	.	.	.	Note=Abolishes endonuclease activity. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843	
+P03873	UniProtKB	Mutagenesis	364	364	.	.	.	Note=Abolishes endonuclease activity. In box3-2 / G1909%3B abolishes maturase and endonuclease activity%3B when associated with N-393. V->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7004642,ECO:0000269|PubMed:8670880;Dbxref=PMID:7004642,PMID:8670880	
+P03873	UniProtKB	Mutagenesis	379	379	.	.	.	Note=In W404-3%3B abolishes maturase and endonuclease activity%3B when associated with M-395. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843	
+P03873	UniProtKB	Mutagenesis	393	393	.	.	.	Note=Abolishes endonuclease activity. In box3-2 / G1909%3B abolishes maturase and endonuclease activity%3B when associated with F-364. I->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7004642,ECO:0000269|PubMed:8670880;Dbxref=PMID:7004642,PMID:8670880	
+P03873	UniProtKB	Mutagenesis	395	395	.	.	.	Note=In W404-4%3B abolishes maturase and endonuclease activity%3B when associated with Y-379. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843	
+##sequence-region Q08268 1 501
+Q08268	UniProtKB	Chain	1	501	.	.	.	ID=PRO_0000211404;Note=Probable transporter MCH4	
+Q08268	UniProtKB	Topological domain	1	97	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	98	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	121	134	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	135	157	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	158	163	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	164	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	184	187	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	188	210	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	211	222	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	223	245	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	246	254	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	255	274	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	275	310	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	311	333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	334	342	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	343	365	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	366	371	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	372	394	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	395	403	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	404	426	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	427	438	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	439	461	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	462	470	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Transmembrane	471	493	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Topological domain	494	501	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Glycosylation	131	131	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08268	UniProtKB	Cross-link	54	54	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P18409 1 493
+P18409	UniProtKB	Chain	1	493	.	.	.	ID=PRO_0000096327;Note=Mitochondrial distribution and morphology protein 10	
+P18409	UniProtKB	Sequence conflict	272	272	.	.	.	Note=N->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18409	UniProtKB	Sequence conflict	272	272	.	.	.	Note=N->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18409	UniProtKB	Sequence conflict	272	272	.	.	.	Note=N->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q01846 1 1127
+Q01846	UniProtKB	Chain	1	1127	.	.	.	ID=PRO_0000096330;Note=Structural protein MDM1	
+Q01846	UniProtKB	Domain	85	273	.	.	.	Note=PXA;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147,ECO:0000255|PROSITE-ProRule:PRU00553	
+Q01846	UniProtKB	Domain	782	905	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
+Q01846	UniProtKB	Coiled coil	705	762	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01846	UniProtKB	Modified residue	670	670	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q01846	UniProtKB	Modified residue	673	673	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q01846	UniProtKB	Modified residue	692	692	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q01846	UniProtKB	Sequence conflict	635	635	.	.	.	Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01846	UniProtKB	Sequence conflict	772	772	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01846	UniProtKB	Sequence conflict	899	899	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01846	UniProtKB	Sequence conflict	1063	1063	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01846	UniProtKB	Sequence conflict	1081	1081	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01846	UniProtKB	Sequence conflict	1096	1096	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40356 1 397
+P40356	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000096382;Note=Mediator of RNA polymerase II transcription subunit 3	
+P40356	UniProtKB	Compositional bias	347	362	.	.	.	Note=Gln-rich	
+P40356	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40356	UniProtKB	Sequence conflict	158	158	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53114 1 1132
+P53114	UniProtKB	Chain	1	1132	.	.	.	ID=PRO_0000096387;Note=Mediator of RNA polymerase II transcription subunit 5	
+##sequence-region P38782 1 295
+P38782	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000096391;Note=Mediator of RNA polymerase II transcription subunit 6	
+P38782	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P41948 1 499
+P41948	UniProtKB	Chain	1	499	.	.	.	ID=PRO_0000139755;Note=Ammonium transporter MEP2	
+P41948	UniProtKB	Topological domain	1	31	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Topological domain	53	62	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Topological domain	84	122	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Topological domain	144	152	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Topological domain	174	187	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Topological domain	209	230	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Transmembrane	231	251	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Topological domain	252	257	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Transmembrane	258	278	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Topological domain	279	300	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Transmembrane	301	321	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Topological domain	322	346	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Transmembrane	347	367	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Topological domain	368	393	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Transmembrane	394	414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Topological domain	415	499	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41948	UniProtKB	Glycosylation	4	4	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069679;Dbxref=PMID:11069679	
+P41948	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Molecular weight equal to non-glycosylated form. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069679;Dbxref=PMID:11069679	
+P41948	UniProtKB	Mutagenesis	252	252	.	.	.	Note=Molecular weight similar to wild-type glycosylated form. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069679;Dbxref=PMID:11069679	
+P41948	UniProtKB	Mutagenesis	368	368	.	.	.	Note=Molecular weight similar to wild-type glycosylated form. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069679;Dbxref=PMID:11069679	
+P41948	UniProtKB	Mutagenesis	483	483	.	.	.	Note=Molecular weight similar to wild-type glycosylated form. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069679;Dbxref=PMID:11069679	
+P41948	UniProtKB	Helix	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	29	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	45	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	65	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	84	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Beta strand	91	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Beta strand	111	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	122	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	150	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	165	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Turn	178	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Turn	190	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	194	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	228	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	248	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Beta strand	251	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	255	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	291	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Turn	303	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	314	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	333	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	342	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	365	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	369	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	382	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	389	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Turn	419	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Turn	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Helix	436	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+P41948	UniProtKB	Beta strand	441	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX	
+##sequence-region P53390 1 489
+P53390	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000139756;Note=Ammonium transporter MEP3	
+P53390	UniProtKB	Topological domain	1	17	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Transmembrane	18	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Topological domain	39	48	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Topological domain	70	108	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Topological domain	130	139	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Topological domain	161	173	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Topological domain	195	209	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Transmembrane	210	230	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Topological domain	231	239	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Transmembrane	240	260	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Topological domain	261	267	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Transmembrane	268	288	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Topological domain	289	289	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Transmembrane	290	310	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Topological domain	311	330	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Transmembrane	331	351	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Topological domain	352	372	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Topological domain	394	489	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53390	UniProtKB	Sequence conflict	7	7	.	.	.	Note=H->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32559 1 526
+P32559	UniProtKB	Transit peptide	1	19	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32559	UniProtKB	Chain	20	526	.	.	.	ID=PRO_0000035781;Note=tRNA modification GTPase MSS1%2C mitochondrial	
+P32559	UniProtKB	Domain	274	444	.	.	.	Note=TrmE-type G	
+P32559	UniProtKB	Nucleotide binding	281	288	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32559	UniProtKB	Nucleotide binding	328	332	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32559	UniProtKB	Nucleotide binding	394	397	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32559	UniProtKB	Sequence conflict	53	53	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CY06 1 175
+P0CY06	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000096610;Note=Mating-type protein ALPHA1	
+P0CY06	UniProtKB	DNA binding	88	144	.	.	.	Note=Alpha box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00655	
+##sequence-region P38849 1 526
+P38849	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Chain	21	526	.	.	.	ID=PRO_0000202926;Note=Maintenance of telomere capping protein 6	
+P38849	UniProtKB	Topological domain	21	477	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Transmembrane	478	498	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Topological domain	499	526	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	32	32	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	60	60	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	80	80	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	89	89	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	156	156	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	171	171	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	175	175	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	202	202	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	240	240	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	259	259	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	311	311	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	362	362	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38849	UniProtKB	Glycosylation	433	433	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX81 1 61
+P0CX81	UniProtKB	Propeptide	1	8	.	.	.	ID=PRO_0000410444	
+P0CX81	UniProtKB	Chain	9	61	.	.	.	ID=PRO_0000410445;Note=Copper metallothionein 1-2	
+P0CX81	UniProtKB	Metal binding	15	15	.	.	.	Note=Copper 1	
+P0CX81	UniProtKB	Metal binding	15	15	.	.	.	Note=Copper 2	
+P0CX81	UniProtKB	Metal binding	17	17	.	.	.	Note=Copper 1	
+P0CX81	UniProtKB	Metal binding	17	17	.	.	.	Note=Copper 3	
+P0CX81	UniProtKB	Metal binding	19	19	.	.	.	Note=Copper 4	
+P0CX81	UniProtKB	Metal binding	19	19	.	.	.	Note=Copper 5	
+P0CX81	UniProtKB	Metal binding	22	22	.	.	.	Note=Copper 3	
+P0CX81	UniProtKB	Metal binding	22	22	.	.	.	Note=Copper 4	
+P0CX81	UniProtKB	Metal binding	22	22	.	.	.	Note=Copper 6	
+P0CX81	UniProtKB	Metal binding	28	28	.	.	.	Note=Copper 2	
+P0CX81	UniProtKB	Metal binding	28	28	.	.	.	Note=Copper 6	
+P0CX81	UniProtKB	Metal binding	32	32	.	.	.	Note=Copper 1	
+P0CX81	UniProtKB	Metal binding	32	32	.	.	.	Note=Copper 7	
+P0CX81	UniProtKB	Metal binding	34	34	.	.	.	Note=Copper 3	
+P0CX81	UniProtKB	Metal binding	34	34	.	.	.	Note=Copper 7	
+P0CX81	UniProtKB	Metal binding	34	34	.	.	.	Note=Copper 8	
+P0CX81	UniProtKB	Metal binding	38	38	.	.	.	Note=Copper 5	
+P0CX81	UniProtKB	Metal binding	38	38	.	.	.	Note=Copper 8	
+P0CX81	UniProtKB	Metal binding	44	44	.	.	.	Note=Copper 4	
+P0CX81	UniProtKB	Metal binding	44	44	.	.	.	Note=Copper 8	
+P0CX81	UniProtKB	Metal binding	46	46	.	.	.	Note=Copper 6	
+P0CX81	UniProtKB	Metal binding	46	46	.	.	.	Note=Copper 7	
+P0CX81	UniProtKB	Cross-link	30	30	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q02046 1 320
+Q02046	UniProtKB	Chain	1	320	.	.	.	ID=PRO_0000199319;Note=Methylenetetrahydrofolate dehydrogenase [NAD(+)]	
+Q02046	UniProtKB	Nucleotide binding	185	186	.	.	.	Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10933503;Dbxref=PMID:10933503	
+Q02046	UniProtKB	Nucleotide binding	208	209	.	.	.	Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10933503;Dbxref=PMID:10933503	
+Q02046	UniProtKB	Nucleotide binding	274	276	.	.	.	Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10933503;Dbxref=PMID:10933503	
+Q02046	UniProtKB	Active site	150	150	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q02046	UniProtKB	Helix	10	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Turn	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	38	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Helix	48	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	67	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Helix	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Helix	79	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	94	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	101	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Helix	105	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Turn	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Turn	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EE9	
+Q02046	UniProtKB	Helix	125	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	137	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Helix	150	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Turn	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	179	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Turn	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Helix	190	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	203	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	209	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	227	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Helix	236	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	247	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Turn	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	269	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	275	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Helix	282	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Beta strand	288	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+Q02046	UniProtKB	Helix	296	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ	
+##sequence-region Q03151 1 367
+Q03151	UniProtKB	Domain	36	228	.	.	.	Note=CP-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01058	
+Q03151	UniProtKB	Nucleotide binding	89	92	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03151	UniProtKB	Nucleotide binding	160	165	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03151	UniProtKB	Binding site	224	224	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P47095 1 244
+P47095	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000162938;Note=Methylthioribulose-1-phosphate dehydratase	
+P47095	UniProtKB	Active site	130	130	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03116	
+P47095	UniProtKB	Metal binding	107	107	.	.	.	Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03116	
+P47095	UniProtKB	Metal binding	109	109	.	.	.	Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03116	
+P47095	UniProtKB	Metal binding	192	192	.	.	.	Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03116	
+P47095	UniProtKB	Binding site	89	89	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03116	
+##sequence-region Q04149 1 632
+Q04149	UniProtKB	Chain	1	632	.	.	.	ID=PRO_0000198861;Note=Crossover junction endonuclease MUS81	
+Q04149	UniProtKB	Domain	351	448	.	.	.	Note=ERCC4	
+Q04149	UniProtKB	Region	527	632	.	.	.	Note=Interaction with MMS4	
+Q04149	UniProtKB	Active site	415	415	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q04149	UniProtKB	Mutagenesis	414	415	.	.	.	Note=In allele MUS81-DD%3B abrogates endonuclease activity. DD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12750322;Dbxref=PMID:12750322	
+##sequence-region P40959 1 511
+P40959	UniProtKB	Chain	1	511	.	.	.	ID=PRO_0000213802;Note=Sorting nexin MVP1	
+P40959	UniProtKB	Domain	128	247	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
+P40959	UniProtKB	Binding site	172	172	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40959	UniProtKB	Binding site	174	174	.	.	.	Note=Phosphatidylinositol 3-phosphate%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40959	UniProtKB	Binding site	198	198	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40959	UniProtKB	Binding site	213	213	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40959	UniProtKB	Sequence conflict	85	85	.	.	.	Note=Q->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36006 1 1272
+P36006	UniProtKB	Chain	1	1272	.	.	.	ID=PRO_0000123490;Note=Myosin-3	
+P36006	UniProtKB	Domain	36	715	.	.	.	Note=Myosin motor	
+P36006	UniProtKB	Domain	719	739	.	.	.	Note=IQ 1	
+P36006	UniProtKB	Domain	740	765	.	.	.	Note=IQ 2	
+P36006	UniProtKB	Domain	771	961	.	.	.	Note=TH1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01093	
+P36006	UniProtKB	Domain	1120	1182	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P36006	UniProtKB	Nucleotide binding	129	136	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36006	UniProtKB	Region	404	486	.	.	.	Note=Actin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36006	UniProtKB	Compositional bias	1003	1123	.	.	.	Note=Ala/Pro-rich	
+P36006	UniProtKB	Compositional bias	1109	1116	.	.	.	Note=Poly-Pro	
+P36006	UniProtKB	Compositional bias	1259	1271	.	.	.	Note=Asp-rich (acidic)	
+P36006	UniProtKB	Modified residue	357	357	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:9388196;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:9388196	
+P36006	UniProtKB	Mutagenesis	132	132	.	.	.	Note=Loss of function. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10648569;Dbxref=PMID:10648569	
+P36006	UniProtKB	Mutagenesis	357	357	.	.	.	Note=Loss of function. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10648569,ECO:0000269|PubMed:9388196;Dbxref=PMID:10648569,PMID:9388196	
+P36006	UniProtKB	Mutagenesis	357	357	.	.	.	Note=Has a constitutive higher activity in actin assembly. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10648569,ECO:0000269|PubMed:9388196;Dbxref=PMID:10648569,PMID:9388196	
+P36006	UniProtKB	Mutagenesis	1158	1158	.	.	.	Note=Abolishes interaction with LAS17 and causes severe mislocalization of the protein. W->S	
+P36006	UniProtKB	Mutagenesis	1272	1272	.	.	.	Note=Abolishes interaction with ARC40. Missing	
+P36006	UniProtKB	Sequence conflict	95	95	.	.	.	Note=G->RK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36006	UniProtKB	Sequence conflict	168	169	.	.	.	Note=NP->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36006	UniProtKB	Sequence conflict	263	270	.	.	.	Note=TADTIDDV->SADQLMR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36006	UniProtKB	Sequence conflict	917	918	.	.	.	Note=VG->RLV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36006	UniProtKB	Sequence conflict	1021	1021	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36006	UniProtKB	Beta strand	1123	1129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW	
+P36006	UniProtKB	Beta strand	1137	1139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BTT	
+P36006	UniProtKB	Beta strand	1147	1153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW	
+P36006	UniProtKB	Beta strand	1157	1163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW	
+P36006	UniProtKB	Beta strand	1169	1173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW	
+P36006	UniProtKB	Helix	1174	1176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW	
+P36006	UniProtKB	Beta strand	1177	1179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW	
+##sequence-region P47018 1 478
+P47018	UniProtKB	Chain	1	478	.	.	.	ID=PRO_0000203040;Note=Maintenance of telomere capping protein 1	
+P47018	UniProtKB	Compositional bias	124	141	.	.	.	Note=Poly-Glu	
+P47018	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47018	UniProtKB	Modified residue	436	436	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P53077 1 123
+P53077	UniProtKB	Transit peptide	1	37	.	.	.	Note=Mitochondrion	
+P53077	UniProtKB	Chain	38	123	.	.	.	ID=PRO_0000202714;Note=Maintenance of telomere capping protein 3%2C mitochondrial	
+##sequence-region P53320 1 366
+P53320	UniProtKB	Chain	1	366	.	.	.	ID=PRO_0000090697;Note=Mitochondrial carrier protein MTM1	
+P53320	UniProtKB	Transmembrane	17	36	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53320	UniProtKB	Transmembrane	126	146	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53320	UniProtKB	Transmembrane	162	182	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53320	UniProtKB	Transmembrane	229	249	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53320	UniProtKB	Transmembrane	268	286	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53320	UniProtKB	Transmembrane	331	352	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53320	UniProtKB	Repeat	14	149	.	.	.	Note=Solcar 1	
+P53320	UniProtKB	Repeat	156	250	.	.	.	Note=Solcar 2	
+P53320	UniProtKB	Repeat	266	359	.	.	.	Note=Solcar 3	
+##sequence-region P32377 1 396
+P32377	UniProtKB	Chain	1	396	.	.	.	ID=PRO_0000087015;Note=Diphosphomevalonate decarboxylase	
+P32377	UniProtKB	Sequence conflict	160	160	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32377	UniProtKB	Beta strand	4	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	13	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Turn	25	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	29	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	34	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Turn	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	46	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Turn	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	67	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	75	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	104	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	120	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	142	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	154	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	161	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	179	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	192	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	208	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	221	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	229	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	246	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	276	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	297	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	307	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	313	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	316	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Turn	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	339	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Helix	363	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	367	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+P32377	UniProtKB	Beta strand	389	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4	
+##sequence-region P23059 1 88
+P23059	UniProtKB	Chain	1	88	.	.	.	ID=PRO_0000084554;Note=N-alpha-acetyltransferase 38%2C NatC auxiliary subunit	
+##sequence-region P32505 1 525
+P32505	UniProtKB	Chain	1	525	.	.	.	ID=PRO_0000096687;Note=Nuclear polyadenylated RNA-binding protein NAB2	
+P32505	UniProtKB	Repeat	121	124	.	.	.	Note=1	
+P32505	UniProtKB	Repeat	125	128	.	.	.	Note=2	
+P32505	UniProtKB	Repeat	129	132	.	.	.	Note=3	
+P32505	UniProtKB	Repeat	133	136	.	.	.	Note=4	
+P32505	UniProtKB	Repeat	137	140	.	.	.	Note=5	
+P32505	UniProtKB	Repeat	141	144	.	.	.	Note=6	
+P32505	UniProtKB	Repeat	145	148	.	.	.	Note=7	
+P32505	UniProtKB	Repeat	149	152	.	.	.	Note=8	
+P32505	UniProtKB	Repeat	153	156	.	.	.	Note=9	
+P32505	UniProtKB	Repeat	157	160	.	.	.	Note=10%3B approximate	
+P32505	UniProtKB	Zinc finger	262	278	.	.	.	Note=C3H1-type 1	
+P32505	UniProtKB	Zinc finger	283	300	.	.	.	Note=C3H1-type 2	
+P32505	UniProtKB	Zinc finger	340	355	.	.	.	Note=C3H1-type 3	
+P32505	UniProtKB	Zinc finger	371	386	.	.	.	Note=C3H1-type 4	
+P32505	UniProtKB	Zinc finger	415	430	.	.	.	Note=C3H1-type 5	
+P32505	UniProtKB	Zinc finger	437	452	.	.	.	Note=C3H1-type 6	
+P32505	UniProtKB	Zinc finger	458	473	.	.	.	Note=C3H1-type 7	
+P32505	UniProtKB	Region	121	156	.	.	.	Note=10 X 4 AA tandem repeats of Q-Q-Q-P	
+P32505	UniProtKB	Region	209	228	.	.	.	Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32505	UniProtKB	Compositional bias	97	172	.	.	.	Note=Gln-rich	
+P32505	UniProtKB	Compositional bias	106	116	.	.	.	Note=Poly-Gln	
+P32505	UniProtKB	Natural variant	130	157	.	.	.	Note=In YJA512. Missing	
+P32505	UniProtKB	Helix	7	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V75	
+P32505	UniProtKB	Helix	28	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V75	
+P32505	UniProtKB	Helix	45	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V75	
+P32505	UniProtKB	Helix	61	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V75	
+P32505	UniProtKB	Helix	84	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V75	
+P32505	UniProtKB	Turn	269	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1	
+P32505	UniProtKB	Turn	293	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1	
+P32505	UniProtKB	Beta strand	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1	
+P32505	UniProtKB	Beta strand	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1	
+P32505	UniProtKB	Helix	305	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1	
+P32505	UniProtKB	Beta strand	328	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1	
+P32505	UniProtKB	Helix	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ2	
+P32505	UniProtKB	Beta strand	353	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ2	
+P32505	UniProtKB	Helix	374	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ2	
+P32505	UniProtKB	Beta strand	384	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ2	
+P32505	UniProtKB	Helix	390	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ2	
+P32505	UniProtKB	Beta strand	412	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L	
+P32505	UniProtKB	Helix	418	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L	
+P32505	UniProtKB	Beta strand	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LHN	
+P32505	UniProtKB	Beta strand	433	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L	
+P32505	UniProtKB	Helix	440	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L	
+P32505	UniProtKB	Beta strand	455	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L	
+P32505	UniProtKB	Helix	461	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L	
+P32505	UniProtKB	Beta strand	470	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LHN	
+##sequence-region P40314 1 149
+P40314	UniProtKB	Chain	1	149	.	.	.	ID=PRO_0000213551;Note=Nascent polypeptide-associated complex subunit beta-2	
+P40314	UniProtKB	Domain	38	103	.	.	.	Note=NAC-A/B;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00507	
+##sequence-region P43619 1 295
+P43619	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000155956;Note=Nicotinate-nucleotide pyrophosphorylase [carboxylating]	
+P43619	UniProtKB	Region	142	144	.	.	.	Note=Substrate binding	
+P43619	UniProtKB	Region	256	258	.	.	.	Note=Substrate binding	
+P43619	UniProtKB	Binding site	107	107	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18321072;Dbxref=PMID:18321072	
+P43619	UniProtKB	Binding site	166	166	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18321072;Dbxref=PMID:18321072	
+P43619	UniProtKB	Binding site	176	176	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18321072;Dbxref=PMID:18321072	
+P43619	UniProtKB	Binding site	206	206	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P43619	UniProtKB	Binding site	227	227	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18321072;Dbxref=PMID:18321072	
+P43619	UniProtKB	Helix	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Helix	13	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Helix	31	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	40	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Helix	56	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	69	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Helix	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	85	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	90	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Helix	99	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	137	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Turn	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2V	
+P43619	UniProtKB	Helix	150	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Turn	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	172	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Helix	177	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Helix	186	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2O	
+P43619	UniProtKB	Beta strand	203	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Helix	211	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	222	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	252	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Beta strand	273	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Helix	278	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+P43619	UniProtKB	Turn	281	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2V	
+P43619	UniProtKB	Beta strand	289	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E	
+##sequence-region Q03455 1 724
+Q03455	UniProtKB	Chain	1	724	.	.	.	ID=PRO_0000206115;Note=Probable zinc transporter MSC2	
+Q03455	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	28	58	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	80	90	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	112	134	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	135	155	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	156	174	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	196	219	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	220	240	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	241	244	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	245	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	266	298	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	299	319	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	320	386	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	387	407	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	408	417	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	418	438	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	439	453	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	454	474	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	475	491	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	492	512	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	513	528	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	529	549	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	550	563	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Transmembrane	564	584	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Topological domain	585	724	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03455	UniProtKB	Compositional bias	369	379	.	.	.	Note=His-rich	
+Q03455	UniProtKB	Compositional bias	643	661	.	.	.	Note=His-rich	
+##sequence-region P25847 1 964
+P25847	UniProtKB	Chain	1	964	.	.	.	ID=PRO_0000115191;Note=DNA mismatch repair protein MSH2	
+P25847	UniProtKB	Nucleotide binding	688	695	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25847	UniProtKB	Region	851	964	.	.	.	Note=Interaction with MSH6	
+P25847	UniProtKB	Mutagenesis	42	42	.	.	.	Note=Moderately reduced activity in a mismatch repair assay. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390	
+P25847	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Defective in a mismatch repair assay. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390	
+P25847	UniProtKB	Mutagenesis	317	317	.	.	.	Note=Partially defective in a mismatch repair assay. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10469597,ECO:0000269|PubMed:11555625;Dbxref=PMID:10469597,PMID:11555625	
+P25847	UniProtKB	Mutagenesis	402	402	.	.	.	Note=Partially defective in a mismatch repair assay. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10469597;Dbxref=PMID:10469597	
+P25847	UniProtKB	Mutagenesis	430	430	.	.	.	Note=Partially defective in a mismatch repair assay. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10469597;Dbxref=PMID:10469597	
+P25847	UniProtKB	Mutagenesis	518	518	.	.	.	Note=Defective in MMR%2C but not in NHTR. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644	
+P25847	UniProtKB	Mutagenesis	524	524	.	.	.	Note=Partially defective in a mismatch repair assay. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10469597;Dbxref=PMID:10469597	
+P25847	UniProtKB	Mutagenesis	542	542	.	.	.	Note=Defective in a mismatch repair assay. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10469597;Dbxref=PMID:10469597	
+P25847	UniProtKB	Mutagenesis	561	561	.	.	.	Note=Causes strong defects in MutS alpha mismatch binding. Defective in MMR%2C but not in NHTR. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12875840;Dbxref=PMID:12875840	
+P25847	UniProtKB	Mutagenesis	564	564	.	.	.	Note=Causes strong defects in MutS alpha mismatch binding. Defective in MMR%2C but not in NHTR. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12875840;Dbxref=PMID:12875840	
+P25847	UniProtKB	Mutagenesis	566	566	.	.	.	Note=Defective in MMR%2C but not in NHTR. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12875840;Dbxref=PMID:12875840	
+P25847	UniProtKB	Mutagenesis	574	574	.	.	.	Note=Defective in MMR and in NHTR. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644	
+P25847	UniProtKB	Mutagenesis	584	584	.	.	.	Note=Defective in MMR and in NHTR. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644	
+P25847	UniProtKB	Mutagenesis	640	640	.	.	.	Note=Defective in a mismatch repair assay. P->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10469597,ECO:0000269|PubMed:11555625;Dbxref=PMID:10469597,PMID:11555625	
+P25847	UniProtKB	Mutagenesis	656	656	.	.	.	Note=Causes defects in ATP-dependent dissociation of MutS alpha from mismatch DNA and in interactions between MutS alpha and MutL alpha. Defective in MMR%2C but not in NHTR. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12875840;Dbxref=PMID:12875840	
+P25847	UniProtKB	Mutagenesis	658	658	.	.	.	Note=Fully functional in a mismatch repair assay. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625	
+P25847	UniProtKB	Mutagenesis	688	688	.	.	.	Note=Moderately reduced activity in a mismatch repair assay. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10077621;Dbxref=PMID:10077621	
+P25847	UniProtKB	Mutagenesis	693	693	.	.	.	Note=Has a dominant negative mutator effect. G->A%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10077621,ECO:0000269|PubMed:9819445;Dbxref=PMID:10077621,PMID:9819445	
+P25847	UniProtKB	Mutagenesis	693	693	.	.	.	Note=Has no defect in mismatch DNA binding%2C but lacks ATP-induced conformational change. Defective in MMR and in NHTR. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10077621,ECO:0000269|PubMed:9819445;Dbxref=PMID:10077621,PMID:9819445	
+P25847	UniProtKB	Mutagenesis	694	694	.	.	.	Note=Impairs ATP binding%3B reduces catalytic activity 1.6-fold for ATP hydrolysis. Has a dominant negative mutator effect. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10077621,ECO:0000269|PubMed:16214425,ECO:0000269|PubMed:16600868;Dbxref=PMID:10077621,PMID:16214425,PMID:16600868	
+P25847	UniProtKB	Mutagenesis	694	694	.	.	.	Note=Defective in MMR and in NHTR. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10077621,ECO:0000269|PubMed:16214425,ECO:0000269|PubMed:16600868;Dbxref=PMID:10077621,PMID:16214425,PMID:16600868	
+P25847	UniProtKB	Mutagenesis	695	695	.	.	.	Note=Has a dominant negative mutator effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10077621;Dbxref=PMID:10077621	
+P25847	UniProtKB	Mutagenesis	716	716	.	.	.	Note=Defective in a mismatch repair assay. C->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10469597;Dbxref=PMID:10469597	
+P25847	UniProtKB	Mutagenesis	730	730	.	.	.	Note=Disruptes MutS alpha ATPase activity%2C but does not affect ATP binding or interactions with MutL alpha. Defective in MMR%2C but not in NHTR. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12875840;Dbxref=PMID:12875840	
+P25847	UniProtKB	Mutagenesis	742	742	.	.	.	Note=Defective in MMR%2C but not in NHTR. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644	
+P25847	UniProtKB	Mutagenesis	742	742	.	.	.	Note=Defective in MMR and in NHTR. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644	
+P25847	UniProtKB	Mutagenesis	768	768	.	.	.	Note=Reduces catalytic activity 50-fold for ATP hydrolysis. E->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12509278,ECO:0000269|PubMed:15513922,ECO:0000269|PubMed:16214425;Dbxref=PMID:12509278,PMID:15513922,PMID:16214425	
+P25847	UniProtKB	Mutagenesis	773	773	.	.	.	Note=Defective in MMR and in NHTR. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644	
+P25847	UniProtKB	Mutagenesis	855	855	.	.	.	Note=Defective in MMR%2C but not in NHTR. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644	
+P25847	UniProtKB	Mutagenesis	859	859	.	.	.	Note=Defective in MMR%2C but not in NHTR. A->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644	
+P25847	UniProtKB	Mutagenesis	862	862	.	.	.	Note=Defective in MMR%2C but not in NHTR. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644	
+P25847	UniProtKB	Mutagenesis	863	868	.	.	.	Note=Defective in MMR and in NHTR. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644	
+P25847	UniProtKB	Sequence conflict	957	964	.	.	.	Note=KYIKALLL->EIYKSPCCYN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P28737 1 362
+P28737	UniProtKB	Chain	1	362	.	.	.	ID=PRO_0000084757;Note=Protein MSP1	
+P28737	UniProtKB	Topological domain	1	12	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28737	UniProtKB	Transmembrane	13	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28737	UniProtKB	Topological domain	29	362	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28737	UniProtKB	Nucleotide binding	133	140	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53176 1 234
+P53176	UniProtKB	Chain	1	234	.	.	.	ID=PRO_0000207525;Note=Multicopy suppressor of SEC21 protein 27	
+P53176	UniProtKB	Topological domain	1	47	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53176	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53176	UniProtKB	Topological domain	69	72	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53176	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53176	UniProtKB	Topological domain	94	234	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53176	UniProtKB	Region	231	234	.	.	.	Note=COPI binding	
+P53176	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P39552	
+P53176	UniProtKB	Mutagenesis	231	232	.	.	.	Note=Abolishes binding to COPI coatomer complex. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12925749;Dbxref=PMID:12925749	
+##sequence-region Q03920 1 221
+Q03920	UniProtKB	Chain	1	221	.	.	.	ID=PRO_0000245840;Note=eRF1 methyltransferase catalytic subunit MTQ2	
+Q03920	UniProtKB	Region	50	54	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03920	UniProtKB	Region	122	125	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03920	UniProtKB	Binding site	77	77	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03920	UniProtKB	Binding site	122	122	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P48240 1 250
+P48240	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000139979;Note=Exosome complex component MTR3	
+P48240	UniProtKB	Compositional bias	216	222	.	.	.	Note=Asp/Glu-rich (acidic)	
+P48240	UniProtKB	Beta strand	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+P48240	UniProtKB	Beta strand	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+P48240	UniProtKB	Beta strand	45	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Beta strand	56	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Beta strand	69	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Beta strand	89	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+P48240	UniProtKB	Helix	107	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Helix	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Beta strand	133	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Helix	165	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Beta strand	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Beta strand	192	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Beta strand	199	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Helix	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Beta strand	209	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P48240	UniProtKB	Helix	223	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+##sequence-region Q12093 1 417
+Q12093	UniProtKB	Chain	1	417	.	.	.	ID=PRO_0000121711;Note=Mitochondrial tRNA-specific 2-thiouridylase 1	
+Q12093	UniProtKB	Nucleotide binding	32	39	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Region	122	124	.	.	.	Note=Interaction with target base in tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Region	179	181	.	.	.	Note=Interaction with tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Region	354	355	.	.	.	Note=Interaction with tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Active site	127	127	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Active site	229	229	.	.	.	Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Binding site	58	58	.	.	.	Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Binding site	154	154	.	.	.	Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Site	155	155	.	.	.	Note=Interaction with tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Site	281	281	.	.	.	Note=Interaction with tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Site	391	391	.	.	.	Note=Interaction with tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Disulfide bond	127	229	.	.	.	Note=Alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12093	UniProtKB	Mutagenesis	38	38	.	.	.	Note=Loss of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15509579;Dbxref=PMID:15509579	
+##sequence-region P36084 1 527
+P36084	UniProtKB	Chain	1	527	.	.	.	ID=PRO_0000081654;Note=Splicing factor MUD2	
+P36084	UniProtKB	Domain	424	511	.	.	.	Note=RRM	
+P36084	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P36084	UniProtKB	Sequence conflict	98	98	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32335 1 436
+P32335	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32335	UniProtKB	Chain	27	436	.	.	.	ID=PRO_0000096603;Note=Protein MSS51%2C mitochondrial	
+P32335	UniProtKB	Mutagenesis	167	167	.	.	.	Note=Partially suppresses the respiratory defect of SHY1 mutants by increasing COX1 translation. T->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11782424;Dbxref=PMID:11782424	
+P32335	UniProtKB	Mutagenesis	199	199	.	.	.	Note=Partially suppresses the respiratory defect of SHY1 mutants by increasing COX1 translation. F->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11782424;Dbxref=PMID:11782424	
+P32335	UniProtKB	Sequence conflict	210	210	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32335	UniProtKB	Sequence conflict	210	210	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39552 1 234
+P39552	UniProtKB	Chain	1	234	.	.	.	ID=PRO_0000207526;Note=Multicopy suppressor of SEC21 protein 28	
+P39552	UniProtKB	Topological domain	1	47	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39552	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39552	UniProtKB	Topological domain	69	72	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39552	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39552	UniProtKB	Topological domain	94	234	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39552	UniProtKB	Region	231	234	.	.	.	Note=COPI binding	
+P39552	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P0CY08 1 210
+P0CY08	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000049186;Note=Mating-type protein ALPHA2	
+P0CY08	UniProtKB	DNA binding	129	191	.	.	.	Note=Homeobox%3B TALE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108	
+P0CY08	UniProtKB	Region	1	102	.	.	.	Note=N-terminal domain	
+P0CY08	UniProtKB	Region	103	128	.	.	.	Note=Flexible linker	
+P0CY08	UniProtKB	Region	190	210	.	.	.	Note=C-terminal tail	
+P0CY08	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20110468;Dbxref=PMID:20110468	
+P0CY08	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Reduces the ability of ALPHA2 to repress transcription%2C but binds normally to DNA and MCM1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7995523;Dbxref=PMID:7995523	
+P0CY08	UniProtKB	Mutagenesis	9	9	.	.	.	Note=Reduces the ability of ALPHA2 to repress transcription%2C but binds normally to DNA and MCM1. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7995523;Dbxref=PMID:7995523	
+P0CY08	UniProtKB	Mutagenesis	10	10	.	.	.	Note=Reduces the ability of ALPHA2 to repress transcription%2C but binds normally to DNA and MCM1. Disrupts interaction with TUP1. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7995523;Dbxref=PMID:7995523	
+P0CY08	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Reduces the ability of alpha2 to repress transcription%2C but binds normally to DNA and MCM1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7995523;Dbxref=PMID:7995523	
+P0CY08	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035	
+P0CY08	UniProtKB	Mutagenesis	115	115	.	.	.	Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035	
+P0CY08	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035	
+P0CY08	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035	
+P0CY08	UniProtKB	Mutagenesis	118	118	.	.	.	Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035	
+P0CY08	UniProtKB	Mutagenesis	119	119	.	.	.	Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035	
+P0CY08	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035	
+P0CY08	UniProtKB	Mutagenesis	173	173	.	.	.	Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. Disrupts interaction with SSN6. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10759558;Dbxref=PMID:10759558	
+P0CY08	UniProtKB	Mutagenesis	181	181	.	.	.	Note=In ALPHA2-3A%3B defective in binding DNA alone or in complex with MCM1%2C but binds DNA normally in complex with A1%3B when associated with A-182 and A-185. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121651;Dbxref=PMID:12121651	
+P0CY08	UniProtKB	Mutagenesis	182	182	.	.	.	Note=In ALPHA2-3A%3B defective in binding DNA alone or in complex with MCM1%2C but binds DNA normally in complex with A1%3B when associated with A-181 and A-185. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121651;Dbxref=PMID:12121651	
+P0CY08	UniProtKB	Mutagenesis	185	185	.	.	.	Note=In ALPHA2-3A%3B defective in binding DNA alone or in complex with MCM1%2C but binds DNA normally in complex with A1%3B when associated with A-181 and A-182. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121651;Dbxref=PMID:12121651	
+P0CY08	UniProtKB	Mutagenesis	192	192	.	.	.	Note=Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7569974;Dbxref=PMID:7569974	
+P0CY08	UniProtKB	Mutagenesis	196	196	.	.	.	Note=Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. L->A%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2851482,ECO:0000269|PubMed:7569974;Dbxref=PMID:2851482,PMID:7569974	
+P0CY08	UniProtKB	Mutagenesis	199	199	.	.	.	Note=Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7569974;Dbxref=PMID:7569974	
+P0CY08	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7569974;Dbxref=PMID:7569974	
+P0CY08	UniProtKB	Sequence conflict	56	56	.	.	.	Note=G->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CY08	UniProtKB	Sequence conflict	150	150	.	.	.	Note=K->KK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CY08	UniProtKB	Sequence conflict	154	154	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CY08	UniProtKB	Beta strand	116	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM	
+P0CY08	UniProtKB	Beta strand	125	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM	
+P0CY08	UniProtKB	Helix	138	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K61	
+P0CY08	UniProtKB	Turn	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K61	
+P0CY08	UniProtKB	Helix	159	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K61	
+P0CY08	UniProtKB	Helix	173	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K61	
+P0CY08	UniProtKB	Helix	194	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LE8	
+P0CY08	UniProtKB	Beta strand	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LE8	
+##sequence-region P34246 1 357
+P34246	UniProtKB	Chain	1	357	.	.	.	ID=PRO_0000203161;Note=Maintenance of telomere capping protein 2	
+##sequence-region P38335 1 694
+P38335	UniProtKB	Chain	1	694	.	.	.	ID=PRO_0000202525;Note=Maintenance of telomere capping protein 4	
+P38335	UniProtKB	Transmembrane	655	675	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38335	UniProtKB	Compositional bias	226	240	.	.	.	Note=His-rich	
+P38335	UniProtKB	Compositional bias	268	275	.	.	.	Note=Poly-Asn	
+P38335	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38335	UniProtKB	Modified residue	263	263	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38335	UniProtKB	Modified residue	481	481	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38335	UniProtKB	Modified residue	491	491	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38335	UniProtKB	Modified residue	493	493	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32633 1 139
+P32633	UniProtKB	Chain	1	139	.	.	.	ID=PRO_0000202608;Note=Maintenance of telomere capping protein 7	
+P32633	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32633	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46151 1 657
+P46151	UniProtKB	Chain	1	657	.	.	.	ID=PRO_0000190255;Note=Methylenetetrahydrofolate reductase 1	
+P46151	UniProtKB	Nucleotide binding	18	23	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Nucleotide binding	49	50	.	.	.	Note=NAD and FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Nucleotide binding	108	110	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Nucleotide binding	129	130	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Active site	18	18	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Binding site	78	78	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Binding site	110	110	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Binding site	152	152	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Binding site	171	171	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Binding site	178	178	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Binding site	189	189	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Binding site	286	286	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46151	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46151	UniProtKB	Modified residue	301	301	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46151	UniProtKB	Modified residue	358	358	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46151	UniProtKB	Sequence conflict	110	111	.	.	.	Note=DP->NL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46151	UniProtKB	Sequence conflict	115	116	.	.	.	Note=ED->VV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46151	UniProtKB	Sequence conflict	119	119	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46151	UniProtKB	Sequence conflict	124	131	.	.	.	Note=ESPFKYAV->RLLNMRLF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53128 1 600
+P53128	UniProtKB	Chain	1	600	.	.	.	ID=PRO_0000190256;Note=Methylenetetrahydrofolate reductase 2	
+P53128	UniProtKB	Nucleotide binding	22	27	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Nucleotide binding	54	55	.	.	.	Note=NAD and FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Nucleotide binding	114	116	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Nucleotide binding	133	134	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Active site	22	22	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Binding site	84	84	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Binding site	116	116	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Binding site	156	156	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Binding site	171	171	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Binding site	178	178	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Binding site	189	189	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Binding site	282	282	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53128	UniProtKB	Sequence conflict	41	42	.	.	.	Note=RM->LA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53128	UniProtKB	Sequence conflict	48	48	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53128	UniProtKB	Sequence conflict	73	73	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53128	UniProtKB	Sequence conflict	152	154	.	.	.	Note=GVA->RC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53128	UniProtKB	Sequence conflict	183	183	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53128	UniProtKB	Sequence conflict	211	211	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53128	UniProtKB	Sequence conflict	233	243	.	.	.	Note=GQISIPQHFSS->ANLHPSTFLV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53128	UniProtKB	Sequence conflict	266	276	.	.	.	Note=MCQKLLDSGYV->CVKIARQWLR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06489 1 411
+Q06489	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06489	UniProtKB	Chain	2	411	.	.	.	ID=PRO_0000156110;Note=Methylthioribose-1-phosphate isomerase	
+Q06489	UniProtKB	Active site	280	280	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03119	
+Q06489	UniProtKB	Site	181	181	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03119	
+Q06489	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06489	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06489	UniProtKB	Beta strand	5	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	17	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Turn	23	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	38	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	53	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	88	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	111	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	129	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	173	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	188	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	194	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	223	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Turn	233	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	237	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	242	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	253	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	261	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	272	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	294	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	307	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	314	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	324	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	335	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	339	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Turn	347	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	362	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	377	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	384	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	388	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Beta strand	395	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+Q06489	UniProtKB	Helix	408	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W	
+##sequence-region Q06106 1 887
+Q06106	UniProtKB	Chain	1	887	.	.	.	ID=PRO_0000081647;Note=Multiple RNA-binding domain-containing protein 1	
+Q06106	UniProtKB	Domain	2	94	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q06106	UniProtKB	Domain	345	423	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q06106	UniProtKB	Domain	532	604	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q06106	UniProtKB	Domain	663	746	.	.	.	Note=RRM 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q06106	UniProtKB	Domain	763	840	.	.	.	Note=RRM 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q06106	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06106	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region Q12117 1 320
+Q12117	UniProtKB	Chain	1	320	.	.	.	ID=PRO_0000196285;Note=Protein MRH1	
+Q12117	UniProtKB	Topological domain	1	34	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Topological domain	56	62	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Topological domain	84	116	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Transmembrane	117	137	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Topological domain	138	141	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Topological domain	163	167	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Topological domain	189	204	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Transmembrane	205	225	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Topological domain	226	238	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Transmembrane	239	259	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Topological domain	260	320	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12117	UniProtKB	Compositional bias	300	318	.	.	.	Note=Lys-rich	
+Q12117	UniProtKB	Modified residue	289	289	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198	
+Q12117	UniProtKB	Modified residue	295	295	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198	
+Q12117	UniProtKB	Modified residue	299	299	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+##sequence-region P50873 1 501
+P50873	UniProtKB	Chain	1	501	.	.	.	ID=PRO_0000086399;Note=Serine/threonine-protein kinase MRK1	
+P50873	UniProtKB	Domain	164	447	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P50873	UniProtKB	Nucleotide binding	170	178	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P50873	UniProtKB	Active site	289	289	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P50873	UniProtKB	Binding site	193	193	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P50873	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P35719 1 219
+P35719	UniProtKB	Chain	1	219	.	.	.	ID=PRO_0000087699;Note=Uncharacterized protein MRP8	
+P35719	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35719	UniProtKB	Cross-link	137	137	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219	
+##sequence-region P47007 1 382
+P47007	UniProtKB	Transit peptide	1	12	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47007	UniProtKB	Chain	13	382	.	.	.	ID=PRO_0000203032;Note=MIOREX complex component 5	
+##sequence-region Q07349 1 420
+Q07349	UniProtKB	Chain	1	420	.	.	.	ID=PRO_0000202592;Note=MIOREX complex component 9	
+Q07349	UniProtKB	Transmembrane	125	145	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07349	UniProtKB	Transmembrane	149	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P13712 1 422
+P13712	UniProtKB	Chain	1	422	.	.	.	ID=PRO_0000051086;Note=Chromatin assembly factor 1 subunit p50	
+P13712	UniProtKB	Repeat	127	158	.	.	.	Note=WD 1	
+P13712	UniProtKB	Repeat	198	238	.	.	.	Note=WD 2	
+P13712	UniProtKB	Repeat	249	289	.	.	.	Note=WD 3	
+P13712	UniProtKB	Repeat	294	334	.	.	.	Note=WD 4	
+P13712	UniProtKB	Repeat	338	379	.	.	.	Note=WD 5	
+P13712	UniProtKB	Repeat	382	421	.	.	.	Note=WD 6	
+##sequence-region Q03162 1 620
+Q03162	UniProtKB	Chain	1	620	.	.	.	ID=PRO_0000218323;Note=MYND-type zinc finger protein MUB1	
+Q03162	UniProtKB	Zinc finger	514	555	.	.	.	Note=MYND-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00134	
+##sequence-region P50276 1 574
+P50276	UniProtKB	Chain	1	574	.	.	.	ID=PRO_0000096648;Note=High-affinity methionine permease	
+P50276	UniProtKB	Topological domain	1	61	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Topological domain	83	92	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Topological domain	114	140	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Topological domain	162	182	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Topological domain	204	207	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Topological domain	229	293	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Transmembrane	294	314	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Topological domain	315	340	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Transmembrane	341	361	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Topological domain	362	418	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Transmembrane	419	439	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Topological domain	440	455	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Transmembrane	456	476	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Topological domain	477	490	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Transmembrane	491	511	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Topological domain	512	574	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50276	UniProtKB	Modified residue	552	552	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P50276	UniProtKB	Modified residue	573	573	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50276	UniProtKB	Cross-link	28	28	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P38994 1 779
+P38994	UniProtKB	Chain	1	779	.	.	.	ID=PRO_0000185455;Note=Probable phosphatidylinositol 4-phosphate 5-kinase MSS4	
+P38994	UniProtKB	Domain	376	756	.	.	.	Note=PIPK;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00781	
+P38994	UniProtKB	Modified residue	207	207	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38994	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38994	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38994	UniProtKB	Modified residue	659	659	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38994	UniProtKB	Modified residue	661	661	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38994	UniProtKB	Sequence conflict	610	610	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03429 1 123
+Q03429	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03429	UniProtKB	Chain	25	123	.	.	.	ID=PRO_0000253826;Note=Mitochondrial zinc maintenance protein 1%2C mitochondrial	
+##sequence-region Q02642 1 157
+Q02642	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000213552;Note=Nascent polypeptide-associated complex subunit beta-1	
+Q02642	UniProtKB	Domain	38	103	.	.	.	Note=NAC-A/B;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00507	
+Q02642	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q99316 1 277
+Q99316	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99316	UniProtKB	Chain	23	277	.	.	.	ID=PRO_0000034182;Note=Protein disulfide isomerase MPD2	
+Q99316	UniProtKB	Domain	27	172	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+Q99316	UniProtKB	Motif	274	277	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138	
+Q99316	UniProtKB	Disulfide bond	56	59	.	.	.	Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+Q99316	UniProtKB	Mutagenesis	56	56	.	.	.	Note=Loss of function%3B when associated with S-59. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9367834;Dbxref=PMID:9367834	
+Q99316	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Loss of function%3B when associated with S-56. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9367834;Dbxref=PMID:9367834	
+##sequence-region Q06390 1 306
+Q06390	UniProtKB	Chain	1	306	.	.	.	ID=PRO_0000253821;Note=Methylated RNA-binding protein 1	
+Q06390	UniProtKB	Domain	155	290	.	.	.	Note=YTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00225	
+Q06390	UniProtKB	Region	161	163	.	.	.	Note=N6-methyladenosine binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4RCM,ECO:0000269|PubMed:26318451;Dbxref=PMID:26318451	
+Q06390	UniProtKB	Binding site	207	207	.	.	.	Note=N6-methyladenosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y5A9	
+Q06390	UniProtKB	Binding site	231	231	.	.	.	Note=N6-methyladenosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BYJ9	
+Q06390	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Abolishes binding to N6-methyladenosine (m6A)-containing RNAs. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26318451;Dbxref=PMID:26318451	
+Q06390	UniProtKB	Mutagenesis	231	231	.	.	.	Note=Abolishes binding to N6-methyladenosine (m6A)-containing RNAs. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26318451;Dbxref=PMID:26318451	
+Q06390	UniProtKB	Mutagenesis	273	273	.	.	.	Note=Abolishes binding to N6-methyladenosine (m6A)-containing RNAs. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26318451;Dbxref=PMID:26318451	
+Q06390	UniProtKB	Beta strand	156	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Helix	165	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Helix	181	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Beta strand	200	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Turn	207	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Beta strand	211	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Beta strand	223	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Helix	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Helix	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Beta strand	240	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Helix	253	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Turn	262	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Helix	269	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+Q06390	UniProtKB	Helix	280	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM	
+##sequence-region P25588 1 1096
+P25588	UniProtKB	Chain	1	1096	.	.	.	ID=PRO_0000096574;Note=Mediator of replication checkpoint protein 1	
+P25588	UniProtKB	Coiled coil	488	542	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25588	UniProtKB	Coiled coil	652	716	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25588	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25588	UniProtKB	Modified residue	409	409	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25588	UniProtKB	Modified residue	411	411	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25588	UniProtKB	Modified residue	434	434	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25588	UniProtKB	Modified residue	605	605	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P25588	UniProtKB	Modified residue	607	607	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25588	UniProtKB	Modified residue	609	609	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P25588	UniProtKB	Modified residue	801	801	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25588	UniProtKB	Modified residue	807	807	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25588	UniProtKB	Modified residue	911	911	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25588	UniProtKB	Sequence conflict	748	748	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25588	UniProtKB	Sequence conflict	808	808	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06815 1 381
+Q06815	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06815	UniProtKB	Chain	24	381	.	.	.	ID=PRO_0000042715;Note=Mannose 6-phosphate receptor-like protein 1	
+Q06815	UniProtKB	Topological domain	24	236	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06815	UniProtKB	Transmembrane	237	257	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06815	UniProtKB	Topological domain	258	381	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06815	UniProtKB	Modified residue	335	335	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06815	UniProtKB	Modified residue	339	339	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06815	UniProtKB	Modified residue	342	342	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06815	UniProtKB	Modified residue	371	371	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06815	UniProtKB	Modified residue	380	380	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06815	UniProtKB	Glycosylation	116	116	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06815	UniProtKB	Glycosylation	136	136	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06815	UniProtKB	Glycosylation	178	178	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06815	UniProtKB	Glycosylation	215	215	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25270 1 412
+P25270	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25270	UniProtKB	Chain	21	412	.	.	.	ID=PRO_0000058321;Note=rRNA methyltransferase 1%2C mitochondrial	
+##sequence-region P53123 1 320
+P53123	UniProtKB	Transit peptide	1	18	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53123	UniProtKB	Chain	19	320	.	.	.	ID=PRO_0000155588;Note=rRNA methyltransferase 2%2C mitochondrial	
+P53123	UniProtKB	Region	83	86	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UI43	
+P53123	UniProtKB	Region	178	179	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UI43	
+P53123	UniProtKB	Active site	264	264	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0C0R7	
+P53123	UniProtKB	Binding site	104	104	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UI43	
+P53123	UniProtKB	Binding site	203	203	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UI43	
+##sequence-region O75012 1 95
+O75012	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978	
+O75012	UniProtKB	Chain	2	95	.	.	.	ID=PRO_0000042818;Note=37S ribosomal protein MRP10%2C mitochondrial	
+O75012	UniProtKB	Domain	27	69	.	.	.	Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+O75012	UniProtKB	Motif	30	40	.	.	.	Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+O75012	UniProtKB	Motif	51	61	.	.	.	Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+O75012	UniProtKB	Disulfide bond	30	61	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+O75012	UniProtKB	Disulfide bond	40	51	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150	
+##sequence-region P10566 1 314
+P10566	UniProtKB	Chain	1	314	.	.	.	ID=PRO_0000090691;Note=Mitochondrial RNA-splicing protein MRS3	
+P10566	UniProtKB	Transmembrane	33	52	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10566	UniProtKB	Transmembrane	93	112	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10566	UniProtKB	Transmembrane	130	149	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10566	UniProtKB	Transmembrane	185	204	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10566	UniProtKB	Transmembrane	219	238	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10566	UniProtKB	Transmembrane	285	298	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10566	UniProtKB	Repeat	31	118	.	.	.	Note=Solcar 1	
+P10566	UniProtKB	Repeat	128	210	.	.	.	Note=Solcar 2	
+P10566	UniProtKB	Repeat	217	310	.	.	.	Note=Solcar 3	
+##sequence-region Q03079 1 207
+Q03079	UniProtKB	Transit peptide	1	46	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03079	UniProtKB	Chain	47	207	.	.	.	ID=PRO_0000238638;Note=MIOREX complex component 11	
+Q03079	UniProtKB	Topological domain	47	98	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q03079	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03079	UniProtKB	Topological domain	120	177	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q03079	UniProtKB	Transmembrane	178	198	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03079	UniProtKB	Topological domain	199	207	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+Q03079	UniProtKB	Sequence conflict	108	112	.	.	.	Note=ILPLF->NTTTV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38172 1 270
+P38172	UniProtKB	Transit peptide	1	12	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38172	UniProtKB	Chain	13	270	.	.	.	ID=PRO_0000202441;Note=MIOREX complex component 3	
+##sequence-region P36157 1 363
+P36157	UniProtKB	Chain	1	363	.	.	.	ID=PRO_0000203223;Note=Putative transcriptional activator MSA2	
+P36157	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36157	UniProtKB	Modified residue	292	292	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36157	UniProtKB	Sequence conflict	122	122	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32334 1 1306
+P32334	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32334	UniProtKB	Chain	22	1306	.	.	.	ID=PRO_0000096589;Note=Signaling mucin MSB2	
+P32334	UniProtKB	Topological domain	22	1185	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32334	UniProtKB	Transmembrane	1186	1206	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32334	UniProtKB	Topological domain	1207	1306	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32334	UniProtKB	Repeat	698	714	.	.	.	Note=1	
+P32334	UniProtKB	Repeat	715	731	.	.	.	Note=2	
+P32334	UniProtKB	Repeat	732	748	.	.	.	Note=3	
+P32334	UniProtKB	Repeat	749	765	.	.	.	Note=4	
+P32334	UniProtKB	Repeat	766	782	.	.	.	Note=5	
+P32334	UniProtKB	Repeat	783	799	.	.	.	Note=6	
+P32334	UniProtKB	Repeat	800	816	.	.	.	Note=7	
+P32334	UniProtKB	Region	698	816	.	.	.	Note=7 X 17 AA tandem repeats	
+P32334	UniProtKB	Compositional bias	37	956	.	.	.	Note=Ser-rich	
+P32334	UniProtKB	Compositional bias	1132	1150	.	.	.	Note=Poly-Ser	
+P32334	UniProtKB	Modified residue	1300	1300	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32334	UniProtKB	Glycosylation	30	30	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32334	UniProtKB	Glycosylation	859	859	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32334	UniProtKB	Glycosylation	885	885	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32334	UniProtKB	Glycosylation	945	945	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32334	UniProtKB	Glycosylation	1049	1049	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32334	UniProtKB	Glycosylation	1088	1088	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32334	UniProtKB	Glycosylation	1175	1175	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38694 1 644
+P38694	UniProtKB	Chain	1	644	.	.	.	ID=PRO_0000056596;Note=Putative aldehyde dehydrogenase-like protein YHR039C	
+P38694	UniProtKB	Active site	354	354	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P38694	UniProtKB	Active site	389	389	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P38694	UniProtKB	Site	248	248	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38694	UniProtKB	Glycosylation	15	15	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38694	UniProtKB	Glycosylation	565	565	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38694	UniProtKB	Glycosylation	627	627	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P10849 1 440
+P10849	UniProtKB	Transit peptide	1	15	.	.	.	Note=Mitochondrion	
+P10849	UniProtKB	Chain	16	440	.	.	.	ID=PRO_0000021790;Note=Mitochondrial transcription factor 2	
+##sequence-region P38860 1 518
+P38860	UniProtKB	Transit peptide	1	23	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38860	UniProtKB	Chain	24	518	.	.	.	ID=PRO_0000122468;Note=GTPase MTG2%2C mitochondrial	
+P38860	UniProtKB	Domain	340	512	.	.	.	Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P38860	UniProtKB	Nucleotide binding	346	353	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P38860	UniProtKB	Nucleotide binding	394	398	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P38860	UniProtKB	Nucleotide binding	460	463	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+##sequence-region P35198 1 433
+P35198	UniProtKB	Chain	1	433	.	.	.	ID=PRO_0000096625;Note=Protein MTH1	
+##sequence-region Q03677 1 179
+Q03677	UniProtKB	Chain	1	179	.	.	.	ID=PRO_0000162946;Note=1%2C2-dihydroxy-3-keto-5-methylthiopentene dioxygenase	
+Q03677	UniProtKB	Metal binding	85	85	.	.	.	Note=Iron or nickel;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03154	
+Q03677	UniProtKB	Metal binding	87	87	.	.	.	Note=Iron or nickel;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03154	
+Q03677	UniProtKB	Metal binding	91	91	.	.	.	Note=Iron or nickel;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03154	
+Q03677	UniProtKB	Metal binding	132	132	.	.	.	Note=Iron or nickel;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03154	
+Q03677	UniProtKB	Mutagenesis	24	24	.	.	.	Note=No loss of acireductone dioxygenase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15938715;Dbxref=PMID:15938715	
+Q03677	UniProtKB	Mutagenesis	45	45	.	.	.	Note=No loss of acireductone dioxygenase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15938715;Dbxref=PMID:15938715	
+Q03677	UniProtKB	Mutagenesis	91	91	.	.	.	Note=Loss of acireductone dioxygenase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15938715;Dbxref=PMID:15938715	
+Q03677	UniProtKB	Mutagenesis	151	151	.	.	.	Note=No loss of acireductone dioxygenase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15938715;Dbxref=PMID:15938715	
+##sequence-region P53070 1 669
+P53070	UniProtKB	Transit peptide	1	59	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53070	UniProtKB	Chain	60	669	.	.	.	ID=PRO_0000042687;Note=Mitochondrial translation optimization protein 1	
+P53070	UniProtKB	Mutagenesis	431	431	.	.	.	Note=Does not completely restore mitochondrial DNA-dependent respiratory chain activities in respiration-defective mutant cells. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22608499;Dbxref=PMID:22608499	
+##sequence-region P53944 1 314
+P53944	UniProtKB	Chain	1	314	.	.	.	ID=PRO_0000203448;Note=Mitochondrial N(5)-glutamine methyltransferase MTQ1	
+P53944	UniProtKB	Region	118	122	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53944	UniProtKB	Region	188	191	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53944	UniProtKB	Binding site	141	141	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53944	UniProtKB	Binding site	188	188	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P34232 1 184
+P34232	UniProtKB	Chain	1	184	.	.	.	ID=PRO_0000096634;Note=mRNA transport regulator MTR2	
+P34232	UniProtKB	Modified residue	125	125	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P34232	UniProtKB	Helix	15	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+P34232	UniProtKB	Helix	39	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+P34232	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+P34232	UniProtKB	Beta strand	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+P34232	UniProtKB	Beta strand	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+P34232	UniProtKB	Helix	62	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+P34232	UniProtKB	Beta strand	77	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+P34232	UniProtKB	Turn	89	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+P34232	UniProtKB	Beta strand	93	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+P34232	UniProtKB	Beta strand	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU	
+P34232	UniProtKB	Beta strand	145	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+P34232	UniProtKB	Helix	155	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+P34232	UniProtKB	Beta strand	166	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5	
+##sequence-region P48563 1 1636
+P48563	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P48563	UniProtKB	Chain	2	1636	.	.	.	ID=PRO_0000203372;Note=Protein MON2	
+P48563	UniProtKB	Region	60	410	.	.	.	Note=Golgi membrane targeting and interaction with ARL1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12052896;Dbxref=PMID:12052896	
+P48563	UniProtKB	Region	1501	1636	.	.	.	Note=Required for function in membrane trafficking	
+P48563	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P48563	UniProtKB	Modified residue	564	564	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48563	UniProtKB	Modified residue	567	567	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48563	UniProtKB	Modified residue	571	571	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q05812 1 728
+Q05812	UniProtKB	Chain	1	728	.	.	.	ID=PRO_0000096595;Note=Meiotic sister-chromatid recombination protein 3	
+Q05812	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05812	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05812	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05812	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q05812	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q05812	UniProtKB	Modified residue	363	363	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q05812	UniProtKB	Modified residue	646	646	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05812	UniProtKB	Modified residue	660	660	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53214 1 551
+P53214	UniProtKB	Signal peptide	1	35	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53214	UniProtKB	Chain	36	551	.	.	.	ID=PRO_0000202787;Note=Protein MTL1	
+P53214	UniProtKB	Topological domain	36	361	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53214	UniProtKB	Transmembrane	362	382	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53214	UniProtKB	Topological domain	383	551	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53214	UniProtKB	Compositional bias	11	356	.	.	.	Note=Ser-rich	
+P53214	UniProtKB	Compositional bias	468	474	.	.	.	Note=Poly-Asp	
+P53214	UniProtKB	Modified residue	481	481	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53214	UniProtKB	Modified residue	482	482	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53214	UniProtKB	Natural variant	264	264	.	.	.	Note=In strain: ATCC 204278. S->SSSSSSSSSSISLSSSSSSSSSSSSSSSS	
+P53214	UniProtKB	Natural variant	427	427	.	.	.	Note=In strain: SK1. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+##sequence-region Q08550 1 464
+Q08550	UniProtKB	Chain	1	464	.	.	.	ID=PRO_0000096555;Note=Meiotic plaque component protein 54	
+Q08550	UniProtKB	Coiled coil	99	119	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08550	UniProtKB	Coiled coil	156	193	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08550	UniProtKB	Coiled coil	231	365	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P29952 1 429
+P29952	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1377774;Dbxref=PMID:1377774	
+P29952	UniProtKB	Chain	2	429	.	.	.	ID=PRO_0000194247;Note=Mannose-6-phosphate isomerase	
+P29952	UniProtKB	Active site	300	300	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29952	UniProtKB	Metal binding	109	109	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29952	UniProtKB	Metal binding	111	111	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29952	UniProtKB	Metal binding	136	136	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29952	UniProtKB	Metal binding	281	281	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P29952	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1377774;Dbxref=PMID:1377774	
+P29952	UniProtKB	Modified residue	107	107	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P29952	UniProtKB	Sequence conflict	25	25	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11914 1 482
+P11914	UniProtKB	Transit peptide	1	13	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2007593;Dbxref=PMID:2007593	
+P11914	UniProtKB	Chain	14	482	.	.	.	ID=PRO_0000026773;Note=Mitochondrial-processing peptidase subunit alpha	
+P11914	UniProtKB	Sequence conflict	235	235	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11914	UniProtKB	Turn	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR8	
+P11914	UniProtKB	Beta strand	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	29	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	38	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Turn	54	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	60	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Turn	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	72	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR7	
+P11914	UniProtKB	Helix	77	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	91	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	111	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	129	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	150	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Turn	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	176	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	184	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	197	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	200	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	209	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	240	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	251	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	257	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	273	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	285	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	301	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Turn	306	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	311	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	327	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	337	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	343	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Turn	353	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	364	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	385	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	405	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	417	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Beta strand	443	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	450	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P11914	UniProtKB	Helix	456	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+##sequence-region P10507 1 462
+P10507	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2007593;Dbxref=PMID:2007593	
+P10507	UniProtKB	Chain	21	462	.	.	.	ID=PRO_0000026784;Note=Mitochondrial-processing peptidase subunit beta	
+P10507	UniProtKB	Active site	73	73	.	.	.	Note=Proton acceptor	
+P10507	UniProtKB	Metal binding	70	70	.	.	.	Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10096,ECO:0000269|PubMed:11470436;Dbxref=PMID:11470436	
+P10507	UniProtKB	Metal binding	74	74	.	.	.	Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10096,ECO:0000269|PubMed:11470436;Dbxref=PMID:11470436	
+P10507	UniProtKB	Metal binding	150	150	.	.	.	Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10096,ECO:0000269|PubMed:11470436;Dbxref=PMID:11470436	
+P10507	UniProtKB	Modified residue	243	243	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P10507	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Loss of activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11470436;Dbxref=PMID:11470436	
+P10507	UniProtKB	Beta strand	27	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	36	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	46	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Turn	63	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	68	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	78	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	85	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	98	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	105	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	119	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	137	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	158	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Turn	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	184	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	192	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	208	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	218	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	254	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	264	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	282	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	294	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Turn	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	302	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	308	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	321	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	334	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Turn	344	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	349	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	370	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	391	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	411	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	423	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	434	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Beta strand	439	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	447	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+P10507	UniProtKB	Helix	453	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6	
+##sequence-region P07266 1 363
+P07266	UniProtKB	Chain	1	363	.	.	.	ID=PRO_0000096580;Note=Mitochondrial RNA-splicing protein MRS1	
+P07266	UniProtKB	Sequence conflict	182	182	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07266	UniProtKB	Sequence conflict	318	318	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P23500 1 304
+P23500	UniProtKB	Chain	1	304	.	.	.	ID=PRO_0000090692;Note=Mitochondrial RNA-splicing protein MRS4	
+P23500	UniProtKB	Transmembrane	23	41	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23500	UniProtKB	Transmembrane	83	102	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23500	UniProtKB	Transmembrane	120	139	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23500	UniProtKB	Transmembrane	175	194	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23500	UniProtKB	Transmembrane	209	228	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23500	UniProtKB	Transmembrane	275	288	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23500	UniProtKB	Repeat	21	108	.	.	.	Note=Solcar 1	
+P23500	UniProtKB	Repeat	118	200	.	.	.	Note=Solcar 2	
+P23500	UniProtKB	Repeat	207	300	.	.	.	Note=Solcar 3	
+##sequence-region Q12467 1 430
+Q12467	UniProtKB	Transit peptide	1	27	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12467	UniProtKB	Chain	28	430	.	.	.	ID=PRO_0000238656;Note=MIOREX complex component 4	
+Q12467	UniProtKB	Transmembrane	403	420	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05473 1 314
+Q05473	UniProtKB	Chain	1	314	.	.	.	ID=PRO_0000253817;Note=MIOREX complex component 8	
+Q05473	UniProtKB	Domain	132	312	.	.	.	Note=EngB-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043	
+Q05473	UniProtKB	Nucleotide binding	140	147	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043	
+Q05473	UniProtKB	Nucleotide binding	173	177	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043	
+Q05473	UniProtKB	Nucleotide binding	191	194	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043	
+Q05473	UniProtKB	Nucleotide binding	253	256	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043	
+Q05473	UniProtKB	Nucleotide binding	290	292	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043	
+Q05473	UniProtKB	Metal binding	147	147	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043	
+Q05473	UniProtKB	Metal binding	175	175	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043	
+##sequence-region P21339 1 1137
+P21339	UniProtKB	Chain	1	1137	.	.	.	ID=PRO_0000096588;Note=Morphogenesis-related protein MSB1	
+P21339	UniProtKB	Modified residue	538	538	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P21339	UniProtKB	Modified residue	776	776	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P21339	UniProtKB	Modified residue	816	816	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q12317 1 492
+Q12317	UniProtKB	Chain	1	492	.	.	.	ID=PRO_0000208020;Note=GTPase-activating protein MSB4	
+Q12317	UniProtKB	Domain	147	367	.	.	.	Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163	
+Q12317	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Reduced GAP activity. R->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12913108;Dbxref=PMID:12913108	
+Q12317	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Reduced GAP activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12913108;Dbxref=PMID:12913108	
+##sequence-region Q03104 1 513
+Q03104	UniProtKB	Chain	1	513	.	.	.	ID=PRO_0000096591;Note=Meiotic sister chromatid recombination protein 1	
+Q03104	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+Q03104	UniProtKB	Modified residue	243	243	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+Q03104	UniProtKB	Sequence conflict	52	52	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38590 1 489
+P38590	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000094916;Note=Tyrosine-protein phosphatase MSG5	
+P38590	UniProtKB	Active site	319	319	.	.	.	Note=Phosphocysteine intermediate	
+P38590	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38590	UniProtKB	Modified residue	98	98	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38590	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38590	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38590	UniProtKB	Mutagenesis	319	319	.	.	.	Note=Loss of activity. C->A	
+P38590	UniProtKB	Sequence conflict	347	348	.	.	.	Note=NK->DE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03834 1 1242
+Q03834	UniProtKB	Chain	1	1242	.	.	.	ID=PRO_0000115213;Note=DNA mismatch repair protein MSH6	
+Q03834	UniProtKB	DNA binding	228	299	.	.	.	.	
+Q03834	UniProtKB	Nucleotide binding	982	989	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03834	UniProtKB	Region	305	421	.	.	.	Note=Mispair-binding domain	
+Q03834	UniProtKB	Motif	27	34	.	.	.	Note=PIP box	
+Q03834	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03834	UniProtKB	Modified residue	145	145	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03834	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03834	UniProtKB	Modified residue	201	201	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03834	UniProtKB	Modified residue	451	451	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03834	UniProtKB	Mutagenesis	26	27	.	.	.	Note=Partially functional in a mismatch repair assay%3B when associated with 33-AA-34. KQ->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11005803;Dbxref=PMID:11005803	
+Q03834	UniProtKB	Mutagenesis	33	34	.	.	.	Note=Abolishes interaction with PCNA (POL30)%2C but only causes a moderate mismatch repair defect. Partially functional in a mismatch repair assay%3B when associated with 26-AA-27. FF->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005803,ECO:0000269|PubMed:11062484;Dbxref=PMID:11005803,PMID:11062484	
+Q03834	UniProtKB	Mutagenesis	301	301	.	.	.	Note=Fully functional in a mismatch repair assay. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10537275;Dbxref=PMID:10537275	
+Q03834	UniProtKB	Mutagenesis	313	313	.	.	.	Note=Fully functional in a mismatch repair assay. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	337	337	.	.	.	Note=Shows defects in both homoduplex and mispair DNA binding and is only partially functional in a mismatch repair assay. F->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10347163,ECO:0000269|PubMed:10970737,ECO:0000269|PubMed:11641390;Dbxref=PMID:10347163,PMID:10970737,PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	337	337	.	.	.	Note=Partially functional in a mismatch repair assay. F->H%2CI%2CY;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10347163,ECO:0000269|PubMed:10970737,ECO:0000269|PubMed:11641390;Dbxref=PMID:10347163,PMID:10970737,PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	337	337	.	.	.	Note=Completely abolishes mismatch repair. F->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10347163,ECO:0000269|PubMed:10970737,ECO:0000269|PubMed:11641390;Dbxref=PMID:10347163,PMID:10970737,PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	337	337	.	.	.	Note=In MSH6-6%3B partially functional in a mismatch repair assay. F->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10347163,ECO:0000269|PubMed:10970737,ECO:0000269|PubMed:11641390;Dbxref=PMID:10347163,PMID:10970737,PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	339	339	.	.	.	Note=Defective in repairing 8-oxo-G-A mismatches. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11641390,ECO:0000269|PubMed:17141577;Dbxref=PMID:11641390,PMID:17141577	
+Q03834	UniProtKB	Mutagenesis	340	343	.	.	.	Note=In MSH6-340%3B shows defects in mispair DNA binding%2C but not in homoduplex DNA binding. LYEK->CFAE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10615127;Dbxref=PMID:10615127	
+Q03834	UniProtKB	Mutagenesis	368	368	.	.	.	Note=Moderately reduced activity in a mismatch repair assay. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	370	370	.	.	.	Note=Partially functional in a mismatch repair assay. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	393	393	.	.	.	Note=Moderately reduced activity in a mismatch repair assay. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	393	393	.	.	.	Note=In MSH6-5%3B partially functional in a mismatch repair assay. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	412	412	.	.	.	Note=Completely abolishes mismatch repair. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	412	412	.	.	.	Note=In MSH6-7%3B partially functional in a mismatch repair assay. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	421	421	.	.	.	Note=In PMS3-1%3B completely abolishes mismatch repair. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8600025;Dbxref=PMID:8600025	
+Q03834	UniProtKB	Mutagenesis	477	477	.	.	.	Note=Partially functional in a mismatch repair assay. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10537275;Dbxref=PMID:10537275	
+Q03834	UniProtKB	Mutagenesis	848	848	.	.	.	Note=Fully functional in a mismatch repair assay. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	852	852	.	.	.	Note=Moderately reduced activity in a mismatch repair assay. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390	
+Q03834	UniProtKB	Mutagenesis	987	987	.	.	.	Note=Has no defect in mismatch DNA binding%2C but lacks ATP-induced conformational change. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9819445;Dbxref=PMID:9819445	
+Q03834	UniProtKB	Mutagenesis	988	988	.	.	.	Note=Impairs ATP binding%3B reduces catalytic activity 13-fold for ATP hydrolysis. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16214425,ECO:0000269|PubMed:16600868;Dbxref=PMID:16214425,PMID:16600868	
+Q03834	UniProtKB	Mutagenesis	1036	1036	.	.	.	Note=In MSH6-4%3B defective for ATP-induced sliding clamp formation and assembly of ternary complexes with MutL alpha. S->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11986324,ECO:0000269|PubMed:16407100;Dbxref=PMID:11986324,PMID:16407100	
+Q03834	UniProtKB	Mutagenesis	1062	1062	.	.	.	Note=Reduces catalytic activity 13-fold for ATP hydrolysis. E->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12509278,ECO:0000269|PubMed:15513922,ECO:0000269|PubMed:16214425;Dbxref=PMID:12509278,PMID:15513922,PMID:16214425	
+Q03834	UniProtKB	Mutagenesis	1067	1067	.	.	.	Note=In MSH6-3%3B defective for ATP-induced sliding clamp formation and assembly of ternary complexes with MutL alpha. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11986324,ECO:0000269|PubMed:16407100;Dbxref=PMID:11986324,PMID:16407100	
+Q03834	UniProtKB	Mutagenesis	1096	1096	.	.	.	Note=In MSH6-9%3B shows normal mispair binding and dissociation%2C but fails to show complete mispair activation of the ATPase. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11986324;Dbxref=PMID:11986324	
+Q03834	UniProtKB	Mutagenesis	1142	1142	.	.	.	Note=In MSH6-2%3B defective for ATP-induced sliding clamp formation%2C but assembles ternary complexes with MutL alpha. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11986324,ECO:0000269|PubMed:16407100;Dbxref=PMID:11986324,PMID:16407100	
+##sequence-region P33749 1 630
+P33749	UniProtKB	Chain	1	630	.	.	.	ID=PRO_0000046811;Note=Zinc finger protein MSN4	
+P33749	UniProtKB	Zinc finger	573	596	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P33749	UniProtKB	Zinc finger	602	624	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P33749	UniProtKB	Motif	237	245	.	.	.	Note=9aaTAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618436;Dbxref=PMID:27618436	
+P33749	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P33749	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33749	UniProtKB	Modified residue	263	263	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P33749	UniProtKB	Modified residue	316	316	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33749	UniProtKB	Modified residue	319	319	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P33749	UniProtKB	Modified residue	479	479	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P33749	UniProtKB	Modified residue	558	558	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:19779198	
+##sequence-region Q99189 1 972
+Q99189	UniProtKB	Chain	1	972	.	.	.	ID=PRO_0000096632;Note=mRNA transport regulator MTR10	
+Q99189	UniProtKB	Compositional bias	196	201	.	.	.	Note=Poly-Ser	
+##sequence-region P47047 1 1073
+P47047	UniProtKB	Chain	1	1073	.	.	.	ID=PRO_0000102092;Note=ATP-dependent RNA helicase DOB1	
+P47047	UniProtKB	Domain	158	314	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P47047	UniProtKB	Domain	393	597	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P47047	UniProtKB	Nucleotide binding	171	178	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P47047	UniProtKB	Motif	262	265	.	.	.	Note=DEVH box	
+P47047	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P47047	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47047	UniProtKB	Modified residue	843	843	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47047	UniProtKB	Helix	8	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFD	
+P47047	UniProtKB	Beta strand	81	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XGJ	
+P47047	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XGJ	
+P47047	UniProtKB	Beta strand	119	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	152	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	166	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	177	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	194	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	202	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	219	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	233	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	239	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	252	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	256	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	264	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Turn	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	273	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	288	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	299	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	314	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	326	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	336	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	350	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	393	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	408	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	413	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QU4	
+P47047	UniProtKB	Helix	416	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QU4	
+P47047	UniProtKB	Helix	434	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	453	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	459	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	465	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	472	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	477	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QU4	
+P47047	UniProtKB	Helix	481	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	497	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	503	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	513	519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	521	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	526	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	534	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Turn	547	549	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	553	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	565	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	587	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	596	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XGJ	
+P47047	UniProtKB	Helix	601	607	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	609	635	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	642	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	667	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	671	673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	678	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Turn	685	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	688	700	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	713	715	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	716	727	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	732	734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	755	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	764	766	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	767	774	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	786	800	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	801	803	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XGJ	
+P47047	UniProtKB	Turn	810	814	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	819	837	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	839	841	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	843	845	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XGJ	
+P47047	UniProtKB	Helix	847	871	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	876	891	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	903	909	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	916	925	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Turn	926	930	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	933	944	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Beta strand	950	952	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	957	979	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	986	992	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	998	1006	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	1010	1015	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	1021	1043	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Turn	1044	1046	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	1048	1061	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+P47047	UniProtKB	Helix	1064	1067	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C	
+##sequence-region P39731 1 289
+P39731	UniProtKB	Chain	1	289	.	.	.	ID=PRO_0000096641;Note=Kinetochore-associated protein MTW1	
+P39731	UniProtKB	Coiled coil	105	147	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08750 1 479
+Q08750	UniProtKB	Chain	1	479	.	.	.	ID=PRO_0000255970;Note=Protein MUM3	
+Q08750	UniProtKB	Transmembrane	33	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08750	UniProtKB	Glycosylation	285	285	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P19524 1 1574
+P19524	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P19524	UniProtKB	Chain	2	1574	.	.	.	ID=PRO_0000123489;Note=Myosin-2	
+P19524	UniProtKB	Domain	70	781	.	.	.	Note=Myosin motor	
+P19524	UniProtKB	Domain	784	806	.	.	.	Note=IQ 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P19524	UniProtKB	Domain	807	831	.	.	.	Note=IQ 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P19524	UniProtKB	Domain	832	855	.	.	.	Note=IQ 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P19524	UniProtKB	Domain	856	879	.	.	.	Note=IQ 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P19524	UniProtKB	Domain	880	902	.	.	.	Note=IQ 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P19524	UniProtKB	Domain	903	932	.	.	.	Note=IQ 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P19524	UniProtKB	Domain	1226	1501	.	.	.	Note=Dilute;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00503	
+P19524	UniProtKB	Nucleotide binding	164	171	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19524	UniProtKB	Region	443	523	.	.	.	Note=Actin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19524	UniProtKB	Region	1087	1574	.	.	.	Note=Non alpha-helical%2C tail domain	
+P19524	UniProtKB	Coiled coil	933	1088	.	.	.	.	
+P19524	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P19524	UniProtKB	Modified residue	1097	1097	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P19524	UniProtKB	Modified residue	1121	1121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P19524	UniProtKB	Mutagenesis	511	511	.	.	.	Note=In MYO2-66%3B disrupts actin binding. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188749;Dbxref=PMID:8188749	
+P19524	UniProtKB	Mutagenesis	1189	1189	.	.	.	Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with G-1288%3B M-1500%3B S-1529%3B G-1546 and R-1559. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144	
+P19524	UniProtKB	Mutagenesis	1247	1247	.	.	.	Note=Intragenic suppressor of MYO2-2. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614	
+P19524	UniProtKB	Mutagenesis	1248	1248	.	.	.	Note=In MYO2-2%3B causes a vacuole inheritance defect. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9843969;Dbxref=PMID:9843969	
+P19524	UniProtKB	Mutagenesis	1262	1262	.	.	.	Note=Intragenic suppressor of MYO2-2. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614	
+P19524	UniProtKB	Mutagenesis	1264	1264	.	.	.	Note=Intragenic suppressor of MYO2-2. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614	
+P19524	UniProtKB	Mutagenesis	1268	1268	.	.	.	Note=Intragenic suppressor of MYO2-2. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614	
+P19524	UniProtKB	Mutagenesis	1274	1274	.	.	.	Note=Intragenic suppressor of MYO2-2. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614	
+P19524	UniProtKB	Mutagenesis	1275	1275	.	.	.	Note=Intragenic suppressor of MYO2-2. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614	
+P19524	UniProtKB	Mutagenesis	1288	1288	.	.	.	Note=Intragenic suppressor of MYO2-2. V->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12391144,ECO:0000269|PubMed:12642614;Dbxref=PMID:12391144,PMID:12642614	
+P19524	UniProtKB	Mutagenesis	1288	1288	.	.	.	Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with A-1189%3B M-1500%3B S-1529%3B G-1546 and R-1559. V->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12391144,ECO:0000269|PubMed:12642614;Dbxref=PMID:12391144,PMID:12642614	
+P19524	UniProtKB	Mutagenesis	1297	1297	.	.	.	Note=Causes a vacuole inheritance defect. D->G%2CN%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931864;Dbxref=PMID:10931864	
+P19524	UniProtKB	Mutagenesis	1301	1301	.	.	.	Note=Causes a vacuole inheritance defect. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931864;Dbxref=PMID:10931864	
+P19524	UniProtKB	Mutagenesis	1304	1304	.	.	.	Note=Causes a vacuole inheritance defect. N->D%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931864;Dbxref=PMID:10931864	
+P19524	UniProtKB	Mutagenesis	1307	1307	.	.	.	Note=Causes a vacuole inheritance defect. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931864;Dbxref=PMID:10931864	
+P19524	UniProtKB	Mutagenesis	1474	1474	.	.	.	Note=In MYO2-338%3B abolishes interaction with YPT11%3B when associated with G-1484 and G-1511. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144	
+P19524	UniProtKB	Mutagenesis	1484	1484	.	.	.	Note=In MYO2-338%3B abolishes interaction with YPT11%3B when associated with S-1474 and G-1511. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144	
+P19524	UniProtKB	Mutagenesis	1500	1500	.	.	.	Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with A-1189%3B G-1288%3B S-1529%3B G-1546 and R-1559. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144	
+P19524	UniProtKB	Mutagenesis	1511	1511	.	.	.	Note=In MYO2-338%3B abolishes interaction with YPT11%3B when associated with S-1474 and G-1484. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144	
+P19524	UniProtKB	Mutagenesis	1529	1529	.	.	.	Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with A-1189%3B G-1288%3B M-1500%3B G-1546 and R-1559. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144	
+P19524	UniProtKB	Mutagenesis	1546	1546	.	.	.	Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with A-1189%3B G-1288%3B M-1500%3B S-1529 and R-1559. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144	
+P19524	UniProtKB	Mutagenesis	1559	1559	.	.	.	Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with A-1189%3B G-1288%3B M-1500%3B S-1529 and G-1546. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144	
+P19524	UniProtKB	Helix	807	829	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45	
+P19524	UniProtKB	Helix	855	877	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M46	
+P19524	UniProtKB	Helix	1153	1165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1167	1176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Turn	1177	1181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1195	1198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1200	1214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1218	1237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1241	1243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1244	1271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1281	1325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Turn	1332	1335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1355	1371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1376	1399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1407	1426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1432	1435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1437	1445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1453	1462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Turn	1463	1465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1468	1477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1489	1504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1505	1507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1533	1536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+P19524	UniProtKB	Helix	1556	1567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H	
+##sequence-region P32492 1 1471
+P32492	UniProtKB	Chain	1	1471	.	.	.	ID=PRO_0000123491;Note=Myosin-4	
+P32492	UniProtKB	Domain	71	777	.	.	.	Note=Myosin motor	
+P32492	UniProtKB	Domain	781	801	.	.	.	Note=IQ 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P32492	UniProtKB	Domain	804	824	.	.	.	Note=IQ 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P32492	UniProtKB	Domain	829	849	.	.	.	Note=IQ 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P32492	UniProtKB	Domain	876	898	.	.	.	Note=IQ 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P32492	UniProtKB	Domain	899	928	.	.	.	Note=IQ 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P32492	UniProtKB	Domain	1164	1419	.	.	.	Note=Dilute;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00503	
+P32492	UniProtKB	Nucleotide binding	165	172	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32492	UniProtKB	Coiled coil	938	1063	.	.	.	.	
+P32492	UniProtKB	Helix	1104	1109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1111	1121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1128	1130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LL6	
+P32492	UniProtKB	Helix	1138	1152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1156	1176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Turn	1179	1181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1182	1193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1196	1204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1205	1207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LL6	
+P32492	UniProtKB	Helix	1217	1253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1255	1259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1262	1264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Beta strand	1265	1267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1270	1289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1294	1319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1325	1342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Turn	1343	1345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1350	1353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1354	1364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1370	1377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1385	1393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Beta strand	1398	1401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LL6	
+P32492	UniProtKB	Helix	1407	1423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1440	1442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+P32492	UniProtKB	Helix	1460	1467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI	
+##sequence-region P37293 1 288
+P37293	UniProtKB	Chain	1	288	.	.	.	ID=PRO_0000096740;Note=Putative N-terminal acetyltransferase 2	
+P37293	UniProtKB	Sequence conflict	61	61	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37293	UniProtKB	Sequence conflict	63	63	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37293	UniProtKB	Sequence conflict	218	218	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06504 1 195
+Q06504	UniProtKB	Chain	1	195	.	.	.	ID=PRO_0000074635;Note=N-terminal acetyltransferase B complex catalytic subunit NAT3	
+Q06504	UniProtKB	Domain	2	172	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+##sequence-region Q08689 1 176
+Q08689	UniProtKB	Chain	1	176	.	.	.	ID=PRO_0000240642;Note=N-alpha-acetyltransferase NAT5	
+Q08689	UniProtKB	Domain	14	176	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+Q08689	UniProtKB	Beta strand	5	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Helix	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Helix	16	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Helix	33	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Beta strand	59	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Beta strand	69	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Beta strand	90	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Helix	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Beta strand	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Helix	107	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Beta strand	126	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Helix	136	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Beta strand	148	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+Q08689	UniProtKB	Beta strand	165	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+##sequence-region Q08920 1 208
+Q08920	UniProtKB	Chain	1	208	.	.	.	ID=PRO_0000232990;Note=Nuclear cap-binding protein subunit 2	
+Q08920	UniProtKB	Domain	46	124	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q08920	UniProtKB	Region	118	122	.	.	.	Note=mRNA cap-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08920	UniProtKB	Region	129	133	.	.	.	Note=mRNA cap-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08920	UniProtKB	Region	139	140	.	.	.	Note=mRNA cap-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08920	UniProtKB	Binding site	24	24	.	.	.	Note=mRNA cap;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08920	UniProtKB	Binding site	49	49	.	.	.	Note=mRNA cap;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P16603 1 691
+P16603	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3139648;Dbxref=PMID:3139648	
+P16603	UniProtKB	Chain	2	691	.	.	.	ID=PRO_0000167608;Note=NADPH--cytochrome P450 reductase	
+P16603	UniProtKB	Topological domain	2	7	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16603	UniProtKB	Transmembrane	8	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16603	UniProtKB	Topological domain	25	691	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16603	UniProtKB	Domain	61	204	.	.	.	Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
+P16603	UniProtKB	Domain	266	529	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
+P16603	UniProtKB	Nucleotide binding	67	72	.	.	.	Note=FMN;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065,ECO:0000269|PubMed:19483672;Dbxref=PMID:16407065,PMID:19483672	
+P16603	UniProtKB	Nucleotide binding	116	119	.	.	.	Note=FMN;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065,ECO:0000269|PubMed:19483672;Dbxref=PMID:16407065,PMID:19483672	
+P16603	UniProtKB	Nucleotide binding	152	161	.	.	.	Note=FMN;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065,ECO:0000269|PubMed:19483672;Dbxref=PMID:16407065,PMID:19483672	
+P16603	UniProtKB	Nucleotide binding	439	442	.	.	.	Note=FAD;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065	
+P16603	UniProtKB	Nucleotide binding	457	459	.	.	.	Note=FAD;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065	
+P16603	UniProtKB	Nucleotide binding	476	479	.	.	.	Note=FAD;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065	
+P16603	UniProtKB	Nucleotide binding	610	611	.	.	.	Note=NADP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065	
+P16603	UniProtKB	Nucleotide binding	617	621	.	.	.	Note=NADP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065	
+P16603	UniProtKB	Binding site	78	78	.	.	.	Note=FMN%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065	
+P16603	UniProtKB	Binding site	187	187	.	.	.	Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212	
+P16603	UniProtKB	Binding site	187	187	.	.	.	Note=FMN%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065	
+P16603	UniProtKB	Binding site	285	285	.	.	.	Note=NADP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065	
+P16603	UniProtKB	Binding site	543	543	.	.	.	Note=NADP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065	
+P16603	UniProtKB	Binding site	646	646	.	.	.	Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065	
+P16603	UniProtKB	Binding site	691	691	.	.	.	Note=FAD;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065	
+P16603	UniProtKB	Cross-link	666	666	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P16603	UniProtKB	Natural variant	474	474	.	.	.	Note=V->G	
+P16603	UniProtKB	Sequence conflict	423	423	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16603	UniProtKB	Helix	50	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Beta strand	60	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Beta strand	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Helix	71	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Beta strand	91	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Helix	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Beta strand	109	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Beta strand	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Helix	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Helix	128	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Turn	139	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Beta strand	146	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Helix	162	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Beta strand	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Turn	187	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Helix	192	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO	
+P16603	UniProtKB	Beta strand	223	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BN4	
+P16603	UniProtKB	Beta strand	234	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BN4	
+P16603	UniProtKB	Helix	243	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	271	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	287	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	306	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	315	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	332	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	337	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	348	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	352	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	368	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	375	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BN4	
+P16603	UniProtKB	Helix	381	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	394	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	402	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	408	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	426	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	439	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Turn	447	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	453	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	469	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BF4	
+P16603	UniProtKB	Helix	477	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Turn	494	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	508	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Turn	511	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	519	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	536	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	542	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	546	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Turn	564	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BN4	
+P16603	UniProtKB	Beta strand	574	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Turn	587	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	592	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	600	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	603	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	620	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	628	635	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Turn	636	638	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	640	645	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	650	665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Helix	670	682	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+P16603	UniProtKB	Beta strand	685	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO	
+##sequence-region Q06389 1 190
+Q06389	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+Q06389	UniProtKB	Chain	2	190	.	.	.	ID=PRO_0000073795;Note=Calcium-binding protein NCS-1	
+Q06389	UniProtKB	Domain	24	59	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+Q06389	UniProtKB	Domain	60	95	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+Q06389	UniProtKB	Domain	96	131	.	.	.	Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+Q06389	UniProtKB	Domain	144	179	.	.	.	Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+Q06389	UniProtKB	Calcium binding	73	84	.	.	.	Note=1	
+Q06389	UniProtKB	Calcium binding	109	120	.	.	.	Note=2	
+Q06389	UniProtKB	Calcium binding	157	168	.	.	.	Note=3	
+Q06389	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10559922;Dbxref=PMID:10559922	
+Q06389	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Abolishes N-myristoylation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10559922;Dbxref=PMID:10559922	
+Q06389	UniProtKB	Beta strand	7	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JU0	
+Q06389	UniProtKB	Helix	11	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Turn	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Helix	24	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Helix	45	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Helix	63	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Beta strand	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Helix	82	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Helix	99	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Beta strand	113	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Helix	118	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Beta strand	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Helix	145	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Turn	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Beta strand	161	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Helix	166	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+Q06389	UniProtKB	Helix	179	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW	
+##sequence-region Q12366 1 352
+Q12366	UniProtKB	Chain	1	352	.	.	.	ID=PRO_0000268688;Note=Non-disjunction protein 1	
+##sequence-region P38757 1 446
+P38757	UniProtKB	Chain	1	446	.	.	.	ID=PRO_0000212579;Note=Nuclear envelope morphology protein 1	
+P38757	UniProtKB	Transmembrane	87	103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38757	UniProtKB	Domain	247	424	.	.	.	Note=FCP1 homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00336	
+P38757	UniProtKB	Mutagenesis	257	257	.	.	.	Note=Abolishes phosphatase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15889145;Dbxref=PMID:15889145	
+##sequence-region Q03264 1 515
+Q03264	UniProtKB	Chain	1	515	.	.	.	ID=PRO_0000218579;Note=RNA exonuclease NGL2	
+##sequence-region P0CX80 1 61
+P0CX80	UniProtKB	Propeptide	1	8	.	.	.	ID=PRO_0000018675	
+P0CX80	UniProtKB	Chain	9	61	.	.	.	ID=PRO_0000018676;Note=Copper metallothionein 1-1	
+P0CX80	UniProtKB	Metal binding	15	15	.	.	.	Note=Copper 1	
+P0CX80	UniProtKB	Metal binding	15	15	.	.	.	Note=Copper 2	
+P0CX80	UniProtKB	Metal binding	17	17	.	.	.	Note=Copper 1	
+P0CX80	UniProtKB	Metal binding	17	17	.	.	.	Note=Copper 3	
+P0CX80	UniProtKB	Metal binding	19	19	.	.	.	Note=Copper 4	
+P0CX80	UniProtKB	Metal binding	19	19	.	.	.	Note=Copper 5	
+P0CX80	UniProtKB	Metal binding	22	22	.	.	.	Note=Copper 3	
+P0CX80	UniProtKB	Metal binding	22	22	.	.	.	Note=Copper 4	
+P0CX80	UniProtKB	Metal binding	22	22	.	.	.	Note=Copper 6	
+P0CX80	UniProtKB	Metal binding	28	28	.	.	.	Note=Copper 2	
+P0CX80	UniProtKB	Metal binding	28	28	.	.	.	Note=Copper 6	
+P0CX80	UniProtKB	Metal binding	32	32	.	.	.	Note=Copper 1	
+P0CX80	UniProtKB	Metal binding	32	32	.	.	.	Note=Copper 7	
+P0CX80	UniProtKB	Metal binding	34	34	.	.	.	Note=Copper 3	
+P0CX80	UniProtKB	Metal binding	34	34	.	.	.	Note=Copper 7	
+P0CX80	UniProtKB	Metal binding	34	34	.	.	.	Note=Copper 8	
+P0CX80	UniProtKB	Metal binding	38	38	.	.	.	Note=Copper 5	
+P0CX80	UniProtKB	Metal binding	38	38	.	.	.	Note=Copper 8	
+P0CX80	UniProtKB	Metal binding	44	44	.	.	.	Note=Copper 4	
+P0CX80	UniProtKB	Metal binding	44	44	.	.	.	Note=Copper 8	
+P0CX80	UniProtKB	Metal binding	46	46	.	.	.	Note=Copper 6	
+P0CX80	UniProtKB	Metal binding	46	46	.	.	.	Note=Copper 7	
+P0CX80	UniProtKB	Cross-link	30	30	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX80	UniProtKB	Turn	20	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJU	
+P0CX80	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJU	
+P0CX80	UniProtKB	Turn	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AQR	
+P0CX80	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJU	
+##sequence-region P14908 1 341
+P14908	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1939277;Dbxref=PMID:1939277	
+P14908	UniProtKB	Chain	2	341	.	.	.	ID=PRO_0000096621;Note=Mitochondrial transcription factor 1	
+P14908	UniProtKB	Compositional bias	157	196	.	.	.	Note=Arg/Lys-rich (basic)	
+P14908	UniProtKB	Compositional bias	209	233	.	.	.	Note=Asp/Glu-rich (acidic)	
+P14908	UniProtKB	Compositional bias	246	260	.	.	.	Note=Asp/Glu-rich (acidic)	
+P14908	UniProtKB	Binding site	23	23	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026	
+P14908	UniProtKB	Binding site	77	77	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026	
+P14908	UniProtKB	Binding site	101	101	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026	
+P14908	UniProtKB	Binding site	137	137	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026	
+P14908	UniProtKB	Sequence conflict	79	79	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14908	UniProtKB	Sequence conflict	287	288	.	.	.	Note=QY->PI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14908	UniProtKB	Helix	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	26	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Turn	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Beta strand	49	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	59	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Beta strand	71	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	80	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Turn	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Beta strand	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	105	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Turn	112	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Beta strand	127	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	143	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	159	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Beta strand	164	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	174	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	191	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Beta strand	200	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	210	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	218	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	231	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Beta strand	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Beta strand	242	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	256	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Turn	268	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Turn	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	277	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	285	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Turn	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Turn	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+P14908	UniProtKB	Helix	308	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W	
+##sequence-region P08964 1 1928
+P08964	UniProtKB	Chain	1	1928	.	.	.	ID=PRO_0000123484;Note=Myosin-1	
+P08964	UniProtKB	Domain	75	791	.	.	.	Note=Myosin motor	
+P08964	UniProtKB	Domain	794	823	.	.	.	Note=IQ;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116	
+P08964	UniProtKB	Nucleotide binding	180	187	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08964	UniProtKB	Region	460	529	.	.	.	Note=Actin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08964	UniProtKB	Coiled coil	856	1911	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08964	UniProtKB	Sequence conflict	36	36	.	.	.	Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	46	46	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	46	46	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	59	59	.	.	.	Note=V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	59	59	.	.	.	Note=V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	86	86	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	330	330	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	330	330	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	343	343	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	343	343	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	421	426	.	.	.	Note=QQAKFI->TKLSSL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	515	515	.	.	.	Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	529	535	.	.	.	Note=SKGPPTG->ARGHDR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	529	535	.	.	.	Note=SKGPPTG->ARGHDR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	541	541	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	541	541	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	550	551	.	.	.	Note=TD->LM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	573	573	.	.	.	Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	582	582	.	.	.	Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	588	599	.	.	.	Note=EYTVEGWLSKNK->NTLWKAGYPKT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	599	599	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	627	632	.	.	.	Note=EKSSSA->GKNLLVC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	627	632	.	.	.	Note=EKSSSA->GKNLLVC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	695	695	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	695	695	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	736	742	.	.	.	Note=ENSTTTT->RKFNHHD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	756	756	.	.	.	Note=E->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	756	756	.	.	.	Note=E->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	773	784	.	.	.	Note=NTKLFFKAGVLA->ILTVFQKLEYWS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	793	794	.	.	.	Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	896	896	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	900	900	.	.	.	Note=N->NSQITKINTNITETPQSTYIGERPKRVICGN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	906	906	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	911	911	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	915	930	.	.	.	Note=NESLLNRVKTSSETLQ->RIAIKILKPAINIT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	934	939	.	.	.	Note=DDLVSE->MTLFL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	951	958	.	.	.	Note=AQNLEEAH->RKILKKLD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1002	1002	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1049	1049	.	.	.	Note=L->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1056	1056	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1060	1060	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1085	1085	.	.	.	Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1123	1123	.	.	.	Note=V->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1133	1133	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1144	1146	.	.	.	Note=KSN->NLI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1159	1168	.	.	.	Note=RETKEQEQKK->TRKKEEQDKE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1179	1204	.	.	.	Note=SKIKELEARLSQEISLNQYLNKRISG->ELKVKEWKARCHRKYLKSILKQKNIR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1224	1224	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1228	1228	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1253	1253	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1311	1323	.	.	.	Note=PDKESDINKLMLE->LTKSLILTNGNAS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1400	1400	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1454	1554	.	.	.	Note=SEQLDRLQKDLESTERQKELLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETLLE->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1568	1568	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1630	1646	.	.	.	Note=DLLKQLDHYTKVVEMLN->SEAARSLYKSGGNVD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1699	1705	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1725	1737	.	.	.	Note=TLQLQMEQNSRNG->NTTANGTKFKEW;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1754	1757	.	.	.	Note=FDDE->LMM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1777	1777	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1788	1788	.	.	.	Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1825	1825	.	.	.	Note=S->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1882	1882	.	.	.	Note=S->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08964	UniProtKB	Sequence conflict	1902	1904	.	.	.	Note=FWK->NSGKRLDADDL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04439 1 1219
+Q04439	UniProtKB	Chain	1	1219	.	.	.	ID=PRO_0000123492;Note=Myosin-5	
+Q04439	UniProtKB	Domain	36	715	.	.	.	Note=Myosin motor	
+Q04439	UniProtKB	Domain	719	739	.	.	.	Note=IQ 1	
+Q04439	UniProtKB	Domain	740	765	.	.	.	Note=IQ 2	
+Q04439	UniProtKB	Domain	771	961	.	.	.	Note=TH1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01093	
+Q04439	UniProtKB	Domain	1085	1147	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+Q04439	UniProtKB	Nucleotide binding	129	136	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04439	UniProtKB	Region	404	486	.	.	.	Note=Actin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04439	UniProtKB	Compositional bias	1000	1088	.	.	.	Note=Ala/Pro-rich	
+Q04439	UniProtKB	Compositional bias	1011	1016	.	.	.	Note=Poly-Pro	
+Q04439	UniProtKB	Compositional bias	1060	1063	.	.	.	Note=Poly-Ala	
+Q04439	UniProtKB	Compositional bias	1073	1081	.	.	.	Note=Poly-Pro	
+Q04439	UniProtKB	Compositional bias	1204	1218	.	.	.	Note=Asp/Glu-rich (acidic)	
+Q04439	UniProtKB	Modified residue	357	357	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:16478726;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:16478726	
+Q04439	UniProtKB	Modified residue	359	359	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q04439	UniProtKB	Modified residue	777	777	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16478726;Dbxref=PMID:16478726	
+Q04439	UniProtKB	Modified residue	992	992	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q04439	UniProtKB	Modified residue	1205	1205	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q04439	UniProtKB	Mutagenesis	164	164	.	.	.	Note=Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808026;Dbxref=PMID:12808026	
+Q04439	UniProtKB	Mutagenesis	168	168	.	.	.	Note=Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808026;Dbxref=PMID:12808026	
+Q04439	UniProtKB	Mutagenesis	209	209	.	.	.	Note=Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808026;Dbxref=PMID:12808026	
+Q04439	UniProtKB	Mutagenesis	357	357	.	.	.	Note=Leads to a depolarized actin cytoskeleton and a strong defect in the capacity to internalize STE2. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16478726;Dbxref=PMID:16478726	
+Q04439	UniProtKB	Mutagenesis	357	357	.	.	.	Note=No growth defect%2C but leads to a partially depolarized actin cytoskeleton. Accelerates the constitutive internalization of STE2. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16478726;Dbxref=PMID:16478726	
+Q04439	UniProtKB	Mutagenesis	377	377	.	.	.	Note=Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808026;Dbxref=PMID:12808026	
+Q04439	UniProtKB	Mutagenesis	472	472	.	.	.	Note=In MYO5-1%3B temperature sensitive loss of function. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8614799;Dbxref=PMID:8614799	
+Q04439	UniProtKB	Mutagenesis	1123	1123	.	.	.	Note=Abolishes interaction with BBC1 and VRP1. W->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10944111,ECO:0000269|PubMed:11901111;Dbxref=PMID:10944111,PMID:11901111	
+Q04439	UniProtKB	Beta strand	1089	1094	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUY	
+Q04439	UniProtKB	Beta strand	1112	1118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUY	
+Q04439	UniProtKB	Beta strand	1122	1130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUY	
+Q04439	UniProtKB	Beta strand	1134	1138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUY	
+Q04439	UniProtKB	Helix	1139	1141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUY	
+Q04439	UniProtKB	Beta strand	1142	1144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YP5	
+##sequence-region Q12387 1 796
+Q12387	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12387	UniProtKB	Chain	2	796	.	.	.	ID=PRO_0000079850;Note=N-terminal acetyltransferase B complex subunit MDM20	
+Q12387	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P38795 1 714
+P38795	UniProtKB	Chain	1	714	.	.	.	ID=PRO_0000152248;Note=Glutamine-dependent NAD(+) synthetase	
+P38795	UniProtKB	Domain	5	275	.	.	.	Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P38795	UniProtKB	Nucleotide binding	359	366	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38795	UniProtKB	Region	329	714	.	.	.	Note=Ligase	
+P38795	UniProtKB	Active site	45	45	.	.	.	Note=Proton acceptor%3B for glutaminase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WJJ3	
+P38795	UniProtKB	Active site	114	114	.	.	.	Note=For glutaminase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WJJ3	
+P38795	UniProtKB	Active site	175	175	.	.	.	Note=Nucleophile%3B for glutaminase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WJJ3	
+P38795	UniProtKB	Active site	361	361	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P12945 1 854
+P12945	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12945	UniProtKB	Chain	2	854	.	.	.	ID=PRO_0000096739;Note=N-terminal acetyltransferase A complex subunit NAT1	
+P12945	UniProtKB	Repeat	20	53	.	.	.	Note=TPR 1	
+P12945	UniProtKB	Repeat	54	87	.	.	.	Note=TPR 2	
+P12945	UniProtKB	Repeat	91	124	.	.	.	Note=TPR 3	
+P12945	UniProtKB	Repeat	126	162	.	.	.	Note=TPR 4	
+P12945	UniProtKB	Repeat	241	274	.	.	.	Note=TPR 5	
+P12945	UniProtKB	Repeat	384	417	.	.	.	Note=TPR 6	
+P12945	UniProtKB	Repeat	452	485	.	.	.	Note=TPR 7	
+P12945	UniProtKB	Repeat	728	761	.	.	.	Note=TPR 8	
+P12945	UniProtKB	Coiled coil	623	667	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12945	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12945	UniProtKB	Modified residue	674	674	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P12945	UniProtKB	Helix	24	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	36	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	54	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	70	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	91	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	107	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	126	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	141	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	159	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	175	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	198	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	220	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	240	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	257	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	275	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	291	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	309	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	314	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	322	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	344	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	356	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Turn	376	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	380	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	400	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	418	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	434	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	452	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	468	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Turn	478	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY	
+P12945	UniProtKB	Beta strand	484	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	488	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	497	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	536	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	571	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	575	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	585	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	596	600	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	602	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Turn	629	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY	
+P12945	UniProtKB	Helix	662	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Turn	674	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	683	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	691	698	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	700	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Turn	709	711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	714	721	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Turn	722	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	727	741	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Beta strand	743	745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY	
+P12945	UniProtKB	Helix	746	758	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Beta strand	763	765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	767	781	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Turn	782	784	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	787	791	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	797	805	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	810	818	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Turn	819	822	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Helix	827	837	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+P12945	UniProtKB	Turn	838	840	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY	
+P12945	UniProtKB	Helix	843	852	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH	
+##sequence-region P52919 1 319
+P52919	UniProtKB	Chain	1	319	.	.	.	ID=PRO_0000096745;Note=NAP1-binding protein	
+P52919	UniProtKB	Modified residue	251	251	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P52919	UniProtKB	Modified residue	260	260	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q12163 1 236
+Q12163	UniProtKB	Chain	1	236	.	.	.	ID=PRO_0000257822;Note=NAP1-binding protein 2	
+Q12163	UniProtKB	Domain	110	171	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+Q12163	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12163	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+Q12163	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12163	UniProtKB	Beta strand	113	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8	
+Q12163	UniProtKB	Beta strand	136	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8	
+Q12163	UniProtKB	Beta strand	147	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8	
+Q12163	UniProtKB	Beta strand	158	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8	
+Q12163	UniProtKB	Helix	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8	
+Q12163	UniProtKB	Beta strand	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8	
+##sequence-region Q12374 1 616
+Q12374	UniProtKB	Chain	1	616	.	.	.	ID=PRO_0000096754;Note=Nuclear control of ATPase protein 2	
+Q12374	UniProtKB	Transmembrane	321	341	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12374	UniProtKB	Transmembrane	488	508	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12374	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q02866 1 612
+Q02866	UniProtKB	Chain	1	612	.	.	.	ID=PRO_0000255969;Note=Protein MUK1	
+Q02866	UniProtKB	Domain	273	414	.	.	.	Note=VPS9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00550	
+Q02866	UniProtKB	Compositional bias	115	195	.	.	.	Note=Ser-rich	
+Q02866	UniProtKB	Compositional bias	512	554	.	.	.	Note=Ser-rich	
+Q02866	UniProtKB	Modified residue	67	67	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02866	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02866	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q02866	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q02197 1 733
+Q02197	UniProtKB	Chain	1	733	.	.	.	ID=PRO_0000084553;Note=N-alpha-acetyltransferase%2C 35 NatC auxiliary subunit	
+##sequence-region Q8TGN9 1 163
+Q8TGN9	UniProtKB	Chain	1	163	.	.	.	ID=PRO_0000299922;Note=Protein NAG1	
+Q8TGN9	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P27929 1 486
+P27929	UniProtKB	Chain	1	486	.	.	.	ID=PRO_0000030639;Note=37S ribosomal protein NAM9%2C mitochondrial	
+P27929	UniProtKB	Domain	103	172	.	.	.	Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182	
+P27929	UniProtKB	Mutagenesis	82	82	.	.	.	Note=In NAM9-1%3B suppressor for ocher mutations in mitochondrial DNA%2C possibly through decreasing the fidelity of translation. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7557422;Dbxref=PMID:7557422	
+P27929	UniProtKB	Mutagenesis	109	109	.	.	.	Note=In MNA6-3%3B causes temperature-dependent loss of the 15S rRNA. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10529174;Dbxref=PMID:10529174	
+P27929	UniProtKB	Mutagenesis	111	111	.	.	.	Note=In MNA6-1%3B causes temperature-dependent loss of the 15S rRNA. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10529174;Dbxref=PMID:10529174	
+P27929	UniProtKB	Mutagenesis	424	424	.	.	.	Note=In MNA6-4%3B causes temperature-dependent loss of the 15S rRNA. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10529174;Dbxref=PMID:10529174	
+P27929	UniProtKB	Mutagenesis	438	438	.	.	.	Note=In MNA6-2%3B causes temperature-dependent loss of the 15S rRNA. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10529174;Dbxref=PMID:10529174	
+##sequence-region P25293 1 417
+P25293	UniProtKB	Chain	1	417	.	.	.	ID=PRO_0000185659;Note=Nucleosome assembly protein	
+P25293	UniProtKB	DNA binding	330	356	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25293	UniProtKB	Region	143	362	.	.	.	Note=Interaction with NBA1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Compositional bias	168	180	.	.	.	Note=Asp/Glu-rich (acidic)	
+P25293	UniProtKB	Compositional bias	324	336	.	.	.	Note=Asp/Glu-rich (acidic)	
+P25293	UniProtKB	Compositional bias	366	403	.	.	.	Note=Asp/Glu-rich (acidic)	
+P25293	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25293	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25293	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25293	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25293	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25293	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P25293	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18086883;Dbxref=PMID:19779198,PMID:18086883	
+P25293	UniProtKB	Modified residue	98	98	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:18086883;Dbxref=PMID:18407956,PMID:18086883	
+P25293	UniProtKB	Modified residue	159	159	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18086883;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:18086883	
+P25293	UniProtKB	Modified residue	397	397	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Cross-link	50	50	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25293	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Predominantly cytoplasmic%3B when associated with A-159%2C A-177 and S-397. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Mutagenesis	159	159	.	.	.	Note=Significant reduction in phosphorylation%3B when associated with A-397. Complete inhibition of phosphorylation%3B when associated with A-177 and A-397. Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-177 and A-397. Predominantly cytoplasmic%3B when associated with S-99%2C A-177 and A-397. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Mutagenesis	159	159	.	.	.	Note=Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-177 and A-397. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Significant reduction in phosphorylation%3B when associated with A-397. Complete inhibition of phosphorylation%3B when associated with A-159 and A-397. Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-397. Predominantly cytoplasmic%3B when associated with S-99%2C A-159 and A-397. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-397. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Mutagenesis	397	397	.	.	.	Note=Significant reduction in phosphorylation%3B when associated with either A-159 or A-177. Complete inhibition of phosphorylation%3B when associated with A-159 and A-177. Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-177. Predominantly cytoplasmic%3B when associated with S-99%3B A-159 and A-177. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Mutagenesis	397	397	.	.	.	Note=Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-177. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883	
+P25293	UniProtKB	Sequence conflict	2	2	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25293	UniProtKB	Sequence conflict	103	104	.	.	.	Note=QS->LC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25293	UniProtKB	Sequence conflict	137	138	.	.	.	Note=RI->TM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25293	UniProtKB	Sequence conflict	384	384	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25293	UniProtKB	Turn	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	77	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	90	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Beta strand	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	147	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	188	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	210	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Beta strand	214	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Beta strand	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Beta strand	228	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Turn	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Beta strand	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Beta strand	246	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Beta strand	260	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Beta strand	265	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Turn	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Beta strand	285	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Turn	295	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z2R	
+P25293	UniProtKB	Beta strand	304	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	312	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Beta strand	327	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	332	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Turn	351	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	356	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+P25293	UniProtKB	Helix	363	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU	
+##sequence-region Q02820 1 53
+Q02820	UniProtKB	Chain	1	53	.	.	.	ID=PRO_0000096759;Note=Non-classical export protein 1	
+Q02820	UniProtKB	Transmembrane	7	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06568 1 189
+Q06568	UniProtKB	Chain	1	189	.	.	.	ID=PRO_0000240229;Note=Nuclear distribution protein nudE homolog 1	
+Q06568	UniProtKB	Coiled coil	4	121	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38236 1 366
+P38236	UniProtKB	Chain	1	366	.	.	.	ID=PRO_0000096647;Note=Protein MUM2	
+##sequence-region P38734 1 546
+P38734	UniProtKB	Chain	1	546	.	.	.	ID=PRO_0000096649;Note=Low-affinity methionine permease	
+P38734	UniProtKB	Topological domain	1	70	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	92	98	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	120	148	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	149	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	170	188	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	210	213	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	214	234	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	235	254	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	255	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	276	297	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	298	318	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	319	319	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	320	340	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	341	346	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	347	367	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	368	393	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	394	414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	415	423	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	424	444	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	445	459	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	460	480	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	481	494	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Transmembrane	495	515	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38734	UniProtKB	Topological domain	516	546	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P42939 1 101
+P42939	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000202845;Note=Multivesicular body sorting factor 12	
+P42939	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P42939	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P42939	UniProtKB	Mutagenesis	47	47	.	.	.	Note=Defective in MVB12 incorporation in ESCRT-I complex%3B reduces localization to MVBs%3B abolishes interaction with STP22 and SRN2%3B when associated with D-57. L->D	
+P42939	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Defective in MVB12 incorporation in ESCRT-I complex%3B when associated with D-57. C->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+P42939	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Defective in MVB12 incorporation in ESCRT-I complex%3B reduces localization to MVBs%3B abolishes interaction with STP22 and SRN2%3B when associated with D-47. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+P42939	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Defective in MVB12 incorporation in ESCRT-I complex%3B when associated with D-47. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+P42939	UniProtKB	Helix	4	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+P42939	UniProtKB	Beta strand	15	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+P42939	UniProtKB	Helix	41	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+P42939	UniProtKB	Helix	67	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+##sequence-region P25566 1 168
+P25566	UniProtKB	Chain	1	168	.	.	.	ID=PRO_0000140326;Note=Peptide methionine sulfoxide reductase 2	
+P25566	UniProtKB	Domain	40	168	.	.	.	Note=MsrB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126	
+P25566	UniProtKB	Active site	157	157	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126	
+P25566	UniProtKB	Metal binding	79	79	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126	
+P25566	UniProtKB	Metal binding	82	82	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126	
+P25566	UniProtKB	Metal binding	128	128	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126	
+P25566	UniProtKB	Metal binding	131	131	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126	
+P25566	UniProtKB	Disulfide bond	97	157	.	.	.	Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04751 1 285
+Q04751	UniProtKB	Chain	1	285	.	.	.	ID=PRO_0000074636;Note=N-alpha-acetyltransferase 40	
+Q04751	UniProtKB	Domain	88	274	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+Q04751	UniProtKB	Region	163	165	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6	
+Q04751	UniProtKB	Region	187	189	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6	
+Q04751	UniProtKB	Region	195	200	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6	
+Q04751	UniProtKB	Binding site	116	116	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6	
+Q04751	UniProtKB	Binding site	185	185	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6	
+Q04751	UniProtKB	Binding site	228	228	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6	
+Q04751	UniProtKB	Binding site	233	233	.	.	.	Note=Acetyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6	
+Q04751	UniProtKB	Site	186	186	.	.	.	Note=Essential for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6	
+##sequence-region Q03735 1 1134
+Q03735	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03735	UniProtKB	Chain	2	1134	.	.	.	ID=PRO_0000082034;Note=RNA-binding protein NAB6	
+Q03735	UniProtKB	Domain	653	726	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q03735	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03735	UniProtKB	Modified residue	464	464	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03735	UniProtKB	Modified residue	467	467	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53919 1 492
+P53919	UniProtKB	Chain	1	492	.	.	.	ID=PRO_0000203428;Note=H/ACA ribonucleoprotein complex non-core subunit NAF1	
+P53919	UniProtKB	Region	172	230	.	.	.	Note=RNA-binding	
+P53919	UniProtKB	Compositional bias	55	81	.	.	.	Note=Ser-rich	
+P53919	UniProtKB	Compositional bias	361	456	.	.	.	Note=Pro-rich	
+P53919	UniProtKB	Compositional bias	419	488	.	.	.	Note=Gln-rich	
+P53919	UniProtKB	Modified residue	255	255	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53919	UniProtKB	Natural variant	378	378	.	.	.	Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53919	UniProtKB	Natural variant	423	423	.	.	.	Note=In strain: YJM627. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53919	UniProtKB	Natural variant	424	424	.	.	.	Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53919	UniProtKB	Natural variant	426	426	.	.	.	Note=In strain: SK1%2C V1-09%2C YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326%2C YJM339%2C YJM627%2C YJM789 and YJM1129. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53919	UniProtKB	Natural variant	480	480	.	.	.	Note=In strain: V1-09 and YJM627. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53919	UniProtKB	Beta strand	137	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M	
+P53919	UniProtKB	Beta strand	150	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M	
+P53919	UniProtKB	Beta strand	169	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M	
+P53919	UniProtKB	Beta strand	177	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M	
+P53919	UniProtKB	Beta strand	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M	
+P53919	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M	
+P53919	UniProtKB	Beta strand	192	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M	
+P53919	UniProtKB	Helix	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M	
+P53919	UniProtKB	Helix	202	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M	
+P53919	UniProtKB	Turn	210	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M	
+P53919	UniProtKB	Beta strand	214	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M	
+##sequence-region P40360 1 574
+P40360	UniProtKB	Transit peptide	1	13	.	.	.	Note=Mitochondrion	
+P40360	UniProtKB	Chain	14	574	.	.	.	ID=PRO_0000203054;Note=Amino-acid acetyltransferase%2C mitochondrial	
+P40360	UniProtKB	Domain	392	560	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+##sequence-region P30771 1 971
+P30771	UniProtKB	Chain	1	971	.	.	.	ID=PRO_0000080713;Note=ATP-dependent helicase NAM7	
+P30771	UniProtKB	Zinc finger	61	208	.	.	.	Note=UPF1-type	
+P30771	UniProtKB	Nucleotide binding	430	437	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30771	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P30771	UniProtKB	Modified residue	869	869	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P30771	UniProtKB	Turn	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Turn	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Turn	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	88	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	94	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Turn	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	133	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Turn	149	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	166	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	171	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Turn	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	186	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	195	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	235	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	267	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	277	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	298	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	305	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	311	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	328	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	345	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	356	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	377	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	411	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	424	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	436	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	455	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	462	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	485	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	495	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	499	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	510	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	526	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	548	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	556	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	567	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	574	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	579	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Turn	587	589	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	590	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	609	613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Turn	614	617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	620	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	642	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	658	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Turn	663	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	682	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	697	701	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	703	718	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	723	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	726	731	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	733	746	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	751	755	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	757	761	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	762	765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	770	776	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	787	790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	792	799	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	800	810	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	812	815	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Helix	819	831	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	834	838	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+P30771	UniProtKB	Beta strand	841	844	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL	
+##sequence-region Q08229 1 501
+Q08229	UniProtKB	Chain	1	501	.	.	.	ID=PRO_0000235925;Note=Protein NBA1	
+Q08229	UniProtKB	Region	275	501	.	.	.	Note=Necessary for the normal cellular distribution and bud neck targeting	
+Q08229	UniProtKB	Compositional bias	405	424	.	.	.	Note=Lys-rich	
+Q08229	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08229	UniProtKB	Modified residue	208	208	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08229	UniProtKB	Modified residue	403	403	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P52920 1 328
+P52920	UniProtKB	Chain	1	328	.	.	.	ID=PRO_0000184947;Note=Cytosolic Fe-S cluster assembly factor NBP35	
+P52920	UniProtKB	Nucleotide binding	80	87	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03038	
+P52920	UniProtKB	Metal binding	27	27	.	.	.	Note=Iron-sulfur 1 (4Fe-4S)	
+P52920	UniProtKB	Metal binding	41	41	.	.	.	Note=Iron-sulfur 1 (4Fe-4S)	
+P52920	UniProtKB	Metal binding	44	44	.	.	.	Note=Iron-sulfur 1 (4Fe-4S)	
+P52920	UniProtKB	Metal binding	50	50	.	.	.	Note=Iron-sulfur 1 (4Fe-4S)	
+P52920	UniProtKB	Metal binding	253	253	.	.	.	Note=Iron-sulfur 2 (4Fe-4S)%3B shared with dimeric partner	
+P52920	UniProtKB	Metal binding	256	256	.	.	.	Note=Iron-sulfur 2 (4Fe-4S)%3B shared with dimeric partner	
+P52920	UniProtKB	Mutagenesis	27	27	.	.	.	Note=Supports growth%2C albeit at a lower rate. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766	
+P52920	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766	
+P52920	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Loss of function. C->A%2CG;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22362766,ECO:0000269|PubMed:9290212;Dbxref=PMID:22362766,PMID:9290212	
+P52920	UniProtKB	Mutagenesis	50	50	.	.	.	Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766	
+P52920	UniProtKB	Mutagenesis	86	86	.	.	.	Note=Lethal. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9290212;Dbxref=PMID:9290212	
+P52920	UniProtKB	Mutagenesis	234	234	.	.	.	Note=Does not impair function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766	
+P52920	UniProtKB	Mutagenesis	253	253	.	.	.	Note=Loss fo function and disrupts heterotetramer formation. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17401378,ECO:0000269|PubMed:22362766;Dbxref=PMID:17401378,PMID:22362766	
+P52920	UniProtKB	Mutagenesis	256	256	.	.	.	Note=Loss of function and disrupts heterotetramer formation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766	
+P52920	UniProtKB	Mutagenesis	295	295	.	.	.	Note=Does not impair function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766	
+P52920	UniProtKB	Sequence conflict	58	58	.	.	.	Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P46955 1 337
+P46955	UniProtKB	Compositional bias	61	64	.	.	.	Note=Poly-Thr	
+P46955	UniProtKB	Sequence conflict	292	292	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P34160 1 861
+P34160	UniProtKB	Chain	1	861	.	.	.	ID=PRO_0000087447;Note=Nuclear cap-binding protein complex subunit 1	
+P34160	UniProtKB	Domain	36	264	.	.	.	Note=MIF4G	
+P34160	UniProtKB	Motif	22	30	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34160	UniProtKB	Compositional bias	774	801	.	.	.	Note=Asp/Glu-rich (acidic)	
+P34160	UniProtKB	Compositional bias	802	825	.	.	.	Note=Arg/Lys-rich (basic)	
+P34160	UniProtKB	Sequence conflict	164	164	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P34160	UniProtKB	Sequence conflict	633	633	.	.	.	Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P34160	UniProtKB	Sequence conflict	704	704	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38205 1 684
+P38205	UniProtKB	Chain	1	684	.	.	.	ID=PRO_0000211820;Note=Multisite-specific tRNA:(cytosine-C(5))-methyltransferase	
+P38205	UniProtKB	Region	173	179	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P38205	UniProtKB	Active site	310	310	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P38205	UniProtKB	Binding site	202	202	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P38205	UniProtKB	Binding site	229	229	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P38205	UniProtKB	Binding site	257	257	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P38205	UniProtKB	Modified residue	426	426	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38205	UniProtKB	Modified residue	431	431	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38205	UniProtKB	Modified residue	667	667	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q07500 1 545
+Q07500	UniProtKB	Transit peptide	1	21	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07500	UniProtKB	Chain	22	545	.	.	.	ID=PRO_0000268687;Note=External NADH-ubiquinone oxidoreductase 2%2C mitochondrial	
+Q07500	UniProtKB	Nucleotide binding	99	129	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07500	UniProtKB	Nucleotide binding	260	296	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03503 1 176
+Q03503	UniProtKB	Chain	1	176	.	.	.	ID=PRO_0000074560;Note=N-alpha-acetyltransferase 30	
+Q03503	UniProtKB	Domain	3	159	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+##sequence-region P38996 1 802
+P38996	UniProtKB	Chain	1	802	.	.	.	ID=PRO_0000081657;Note=Nuclear polyadenylated RNA-binding protein 3	
+P38996	UniProtKB	Domain	330	401	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P38996	UniProtKB	Compositional bias	68	71	.	.	.	Note=Poly-Glu	
+P38996	UniProtKB	Compositional bias	87	93	.	.	.	Note=Poly-Glu	
+P38996	UniProtKB	Compositional bias	101	106	.	.	.	Note=Poly-Asp	
+P38996	UniProtKB	Compositional bias	108	115	.	.	.	Note=Poly-Glu	
+P38996	UniProtKB	Compositional bias	116	127	.	.	.	Note=Poly-Asp	
+P38996	UniProtKB	Compositional bias	128	137	.	.	.	Note=Poly-Glu	
+P38996	UniProtKB	Compositional bias	603	608	.	.	.	Note=Poly-Gln	
+P38996	UniProtKB	Compositional bias	644	648	.	.	.	Note=Poly-Pro	
+P38996	UniProtKB	Compositional bias	698	703	.	.	.	Note=Poly-Gln	
+P38996	UniProtKB	Compositional bias	723	728	.	.	.	Note=Poly-Gln	
+P38996	UniProtKB	Compositional bias	765	768	.	.	.	Note=Poly-Pro	
+P38996	UniProtKB	Compositional bias	769	784	.	.	.	Note=Poly-Gln	
+P38996	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38996	UniProtKB	Modified residue	451	451	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38996	UniProtKB	Sequence conflict	341	341	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38996	UniProtKB	Beta strand	331	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ	
+P38996	UniProtKB	Beta strand	339	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNR	
+P38996	UniProtKB	Helix	344	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ	
+P38996	UniProtKB	Helix	352	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ	
+P38996	UniProtKB	Beta strand	357	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ	
+P38996	UniProtKB	Beta strand	364	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ	
+P38996	UniProtKB	Helix	374	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ	
+P38996	UniProtKB	Beta strand	387	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ	
+P38996	UniProtKB	Turn	391	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KVI	
+P38996	UniProtKB	Beta strand	395	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ	
+##sequence-region P38879 1 174
+P38879	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378	
+P38879	UniProtKB	Chain	2	174	.	.	.	ID=PRO_0000135594;Note=Nascent polypeptide-associated complex subunit alpha	
+P38879	UniProtKB	Domain	15	73	.	.	.	Note=NAC-A/B;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00507	
+P38879	UniProtKB	Domain	135	174	.	.	.	Note=UBA	
+P38879	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378	
+P38879	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P23503 1 491
+P23503	UniProtKB	Chain	1	491	.	.	.	ID=PRO_0000096718;Note=Cytosolic Fe-S cluster assembly factor NAR1	
+P23503	UniProtKB	Metal binding	20	20	.	.	.	Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23503	UniProtKB	Metal binding	59	59	.	.	.	Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23503	UniProtKB	Metal binding	62	62	.	.	.	Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23503	UniProtKB	Metal binding	65	65	.	.	.	Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23503	UniProtKB	Metal binding	177	177	.	.	.	Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23503	UniProtKB	Metal binding	231	231	.	.	.	Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23503	UniProtKB	Metal binding	412	412	.	.	.	Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23503	UniProtKB	Metal binding	416	416	.	.	.	Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23503	UniProtKB	Mutagenesis	20	20	.	.	.	Note=Weakly reduced iron content and impaired maturation of cytosolic Fe/S proteins. Strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with A-62 or A-65. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603	
+P23503	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603	
+P23503	UniProtKB	Mutagenesis	62	62	.	.	.	Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603	
+P23503	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603	
+P23503	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Impaired maturation of cytosolic Fe/S proteins. Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with A-416. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603	
+P23503	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with S-412. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603	
+P23503	UniProtKB	Mutagenesis	231	231	.	.	.	Note=Impaired maturation of cytosolic Fe/S proteins. Strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with A-416. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603	
+P23503	UniProtKB	Mutagenesis	412	412	.	.	.	Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with S-177. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603	
+P23503	UniProtKB	Mutagenesis	416	416	.	.	.	Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with A-177 or A-231. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603	
+##sequence-region Q3E7Y6 1 73
+Q3E7Y6	UniProtKB	Chain	1	73	.	.	.	ID=PRO_0000245397;Note=N-terminal-borealin-like protein	
+##sequence-region Q12207 1 173
+Q12207	UniProtKB	Chain	1	173	.	.	.	ID=PRO_0000096760;Note=Non-classical export protein 2	
+Q12207	UniProtKB	Topological domain	1	10	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12207	UniProtKB	Transmembrane	11	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12207	UniProtKB	Topological domain	31	37	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12207	UniProtKB	Transmembrane	38	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12207	UniProtKB	Topological domain	63	75	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12207	UniProtKB	Transmembrane	76	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12207	UniProtKB	Topological domain	94	137	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12207	UniProtKB	Transmembrane	138	157	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12207	UniProtKB	Topological domain	158	173	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08887 1 554
+Q08887	UniProtKB	Chain	1	554	.	.	.	ID=PRO_0000268686;Note=Nuclear division defective protein 1	
+Q08887	UniProtKB	Compositional bias	96	113	.	.	.	Note=Gln-rich	
+Q08887	UniProtKB	Compositional bias	493	546	.	.	.	Note=Ser-rich	
+Q08887	UniProtKB	Modified residue	319	319	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:12865300;Dbxref=PMID:18407956,PMID:12865300	
+Q08887	UniProtKB	Mutagenesis	319	319	.	.	.	Note=Growth delay. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12865300;Dbxref=PMID:12865300	
+##sequence-region P36010 1 153
+P36010	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000137153;Note=Nucleoside diphosphate kinase	
+P36010	UniProtKB	Active site	119	119	.	.	.	Note=Pros-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36010	UniProtKB	Binding site	13	13	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36010	UniProtKB	Binding site	61	61	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36010	UniProtKB	Binding site	89	89	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36010	UniProtKB	Binding site	95	95	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36010	UniProtKB	Binding site	106	106	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36010	UniProtKB	Binding site	116	116	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36010	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36010	UniProtKB	Beta strand	7	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Helix	14	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Helix	22	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Beta strand	35	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Helix	46	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Helix	63	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Beta strand	74	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Helix	84	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Helix	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Helix	105	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Beta strand	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Helix	124	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+P36010	UniProtKB	Helix	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54	
+##sequence-region P25374 1 497
+P25374	UniProtKB	Transit peptide	1	33	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25374	UniProtKB	Chain	34	497	.	.	.	ID=PRO_0000001304;Note=Cysteine desulfurase%2C mitochondrial	
+P25374	UniProtKB	Region	168	169	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B9	
+P25374	UniProtKB	Region	296	298	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B9	
+P25374	UniProtKB	Active site	421	421	.	.	.	Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B7	
+P25374	UniProtKB	Metal binding	421	421	.	.	.	Note=Iron-sulfur (2Fe-2S)%3B via persulfide group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O29689	
+P25374	UniProtKB	Binding site	248	248	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O29689	
+P25374	UniProtKB	Binding site	276	276	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B9	
+P25374	UniProtKB	Binding site	336	336	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B9	
+P25374	UniProtKB	Modified residue	299	299	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B9	
+P25374	UniProtKB	Mutagenesis	191	191	.	.	.	Note=Exhibits constitutive up-regulation of the genes of the cellular iron uptake system. I->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10551871;Dbxref=PMID:10551871	
+P25374	UniProtKB	Sequence conflict	150	150	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99271 1 985
+Q99271	UniProtKB	Chain	1	985	.	.	.	ID=PRO_0000052407;Note=Na(+)/H(+) antiporter	
+Q99271	UniProtKB	Topological domain	1	12	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	34	36	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	37	57	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	58	70	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	92	105	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	127	128	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	129	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	150	176	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	198	203	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	225	244	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	245	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	266	294	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	295	315	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	316	319	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	320	340	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	341	361	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	362	382	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	383	410	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Transmembrane	411	431	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Topological domain	432	985	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99271	UniProtKB	Modified residue	568	568	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q99271	UniProtKB	Modified residue	765	765	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q99271	UniProtKB	Modified residue	768	768	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q99271	UniProtKB	Modified residue	774	774	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q00539 1 523
+Q00539	UniProtKB	Chain	1	523	.	.	.	ID=PRO_0000081659;Note=Protein NAM8	
+Q00539	UniProtKB	Domain	54	145	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q00539	UniProtKB	Domain	163	242	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q00539	UniProtKB	Domain	313	385	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q00539	UniProtKB	Sequence conflict	180	180	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00539	UniProtKB	Sequence conflict	208	209	.	.	.	Note=GF->VL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53914 1 1056
+P53914	UniProtKB	Chain	1	1056	.	.	.	ID=PRO_0000215890;Note=RNA cytidine acetyltransferase	
+P53914	UniProtKB	Domain	566	706	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03211	
+P53914	UniProtKB	Nucleotide binding	286	295	.	.	.	Note=ATP;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P76562,ECO:0000255|HAMAP-Rule:MF_03211	
+P53914	UniProtKB	Region	638	640	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P76562,ECO:0000255|HAMAP-Rule:MF_03211	
+P53914	UniProtKB	Region	645	651	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P76562,ECO:0000255|HAMAP-Rule:MF_03211	
+P53914	UniProtKB	Binding site	475	475	.	.	.	Note=ATP;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P76562,ECO:0000255|HAMAP-Rule:MF_03211	
+P53914	UniProtKB	Binding site	739	739	.	.	.	Note=Acetyl-CoA;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P76562,ECO:0000255|HAMAP-Rule:MF_03211	
+P53914	UniProtKB	Modified residue	1001	1001	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53914	UniProtKB	Modified residue	1007	1007	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53914	UniProtKB	Modified residue	1010	1010	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53914	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Reduces 18S rRNA acetylation by 80%25 and tRNA acetylation by 47%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25653167;Dbxref=PMID:25653167	
+P53914	UniProtKB	Mutagenesis	545	545	.	.	.	Note=Total loss of 18S rRNA acetylation and tRNA acetylation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25653167;Dbxref=PMID:25653167	
+P53914	UniProtKB	Mutagenesis	637	637	.	.	.	Note=Total loss of 18S rRNA acetylation and tRNA acetylation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25653167;Dbxref=PMID:25653167	
+##sequence-region P40096 1 142
+P40096	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000096755;Note=Negative cofactor 2 complex subunit alpha	
+P40096	UniProtKB	Domain	29	137	.	.	.	Note=Histone-fold	
+P40096	UniProtKB	Compositional bias	35	40	.	.	.	Note=Poly-Asn	
+P40096	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40096	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32500 1 655
+P32500	UniProtKB	Chain	1	655	.	.	.	ID=PRO_0000204862;Note=Nucleoporin NDC1	
+P32500	UniProtKB	Topological domain	1	33	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P32500	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32500	UniProtKB	Topological domain	55	58	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P32500	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32500	UniProtKB	Topological domain	80	88	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P32500	UniProtKB	Transmembrane	89	108	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32500	UniProtKB	Topological domain	109	109	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P32500	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32500	UniProtKB	Topological domain	131	190	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P32500	UniProtKB	Transmembrane	191	211	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32500	UniProtKB	Topological domain	212	224	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P32500	UniProtKB	Transmembrane	225	245	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32500	UniProtKB	Topological domain	246	655	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P32500	UniProtKB	Modified residue	401	401	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32500	UniProtKB	Modified residue	412	412	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40460 1 691
+P40460	UniProtKB	Chain	1	691	.	.	.	ID=PRO_0000202958;Note=Kinetochore protein NDC80	
+P40460	UniProtKB	Coiled coil	376	446	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40460	UniProtKB	Coiled coil	522	686	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40460	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40460	UniProtKB	Modified residue	248	248	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40460	UniProtKB	Mutagenesis	201	201	.	.	.	Note=Loss of function. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12386167;Dbxref=PMID:12386167	
+P40460	UniProtKB	Helix	122	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40460	UniProtKB	Helix	141	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40460	UniProtKB	Helix	159	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40460	UniProtKB	Helix	184	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40460	UniProtKB	Helix	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40460	UniProtKB	Helix	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40460	UniProtKB	Helix	215	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40460	UniProtKB	Turn	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40460	UniProtKB	Helix	267	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40460	UniProtKB	Helix	298	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40460	UniProtKB	Helix	621	679	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+##sequence-region P32831 1 672
+P32831	UniProtKB	Chain	1	672	.	.	.	ID=PRO_0000081660;Note=Negative growth regulatory protein NGR1	
+P32831	UniProtKB	Domain	36	159	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P32831	UniProtKB	Domain	192	271	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P32831	UniProtKB	Domain	360	432	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P32831	UniProtKB	Compositional bias	278	295	.	.	.	Note=Gln-rich	
+P32831	UniProtKB	Compositional bias	485	495	.	.	.	Note=Poly-Gln	
+P32831	UniProtKB	Compositional bias	566	672	.	.	.	Note=Asn/Met-rich	
+P32831	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32831	UniProtKB	Modified residue	524	524	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P32831	UniProtKB	Alternative sequence	1	1	.	.	.	ID=VSP_058122;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32831	UniProtKB	Sequence conflict	322	322	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32831	UniProtKB	Sequence conflict	568	568	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32831	UniProtKB	Sequence conflict	585	585	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32340 1 513
+P32340	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1735444;Dbxref=PMID:1735444	
+P32340	UniProtKB	Chain	27	513	.	.	.	ID=PRO_0000021793;Note=Rotenone-insensitive NADH-ubiquinone oxidoreductase%2C mitochondrial	
+P32340	UniProtKB	Nucleotide binding	55	85	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32340	UniProtKB	Nucleotide binding	229	265	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32340	UniProtKB	Natural variant	10	10	.	.	.	Note=K->R	
+P32340	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6G	
+P32340	UniProtKB	Beta strand	55	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	63	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Turn	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	78	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	91	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Turn	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	104	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	111	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	122	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	138	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	170	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6G	
+P32340	UniProtKB	Helix	188	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	193	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6G	
+P32340	UniProtKB	Helix	198	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	223	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	230	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	238	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	255	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	260	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	267	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	273	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	283	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	299	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	304	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	311	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G74	
+P32340	UniProtKB	Beta strand	325	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	333	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6G	
+P32340	UniProtKB	Helix	345	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	355	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	362	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	370	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	376	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	382	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	385	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	393	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	414	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	422	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	427	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	445	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	455	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Beta strand	464	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	472	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+P32340	UniProtKB	Helix	489	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H	
+##sequence-region P39744 1 710
+P39744	UniProtKB	Chain	1	710	.	.	.	ID=PRO_0000121054;Note=Nucleolar complex protein 2	
+P39744	UniProtKB	Compositional bias	101	104	.	.	.	Note=Poly-Ser	
+P39744	UniProtKB	Compositional bias	105	108	.	.	.	Note=Poly-Glu	
+P39744	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P39744	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39744	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P39744	UniProtKB	Modified residue	166	166	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P39744	UniProtKB	Modified residue	698	698	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P39744	UniProtKB	Modified residue	708	708	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P39744	UniProtKB	Sequence conflict	151	179	.	.	.	Note=DEGEDAERNSNIEEKSEQMELEKEKIELS->MKVKMLKETVILKKNLNKWSWKRKKLSFL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39744	UniProtKB	Sequence conflict	231	232	.	.	.	Note=FH->LD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39744	UniProtKB	Sequence conflict	333	333	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39744	UniProtKB	Sequence conflict	360	362	.	.	.	Note=TTY->QRT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39744	UniProtKB	Sequence conflict	542	542	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39744	UniProtKB	Sequence conflict	707	710	.	.	.	Note=MSDA->NVRRLTTQQDLIFCLEFNSIVYKCVNKRKVFFKAYISLCSHVLTCEHSKLSLVSWIFLYFGRFMDRKHVKRSMDLIKSNDVKQGTKMKEVRFTVIKFSKSFNSLKVPHEIDMIANITENFSTRYMISYCWKISSNLNLGAMFMDNNSWNNSFAAYGIVILIIFSALLQVVHQPL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25353 1 742
+P25353	UniProtKB	Chain	1	742	.	.	.	ID=PRO_0000202566;Note=Ectonucleotide pyrophosphatase/phosphodiesterase 1	
+P25353	UniProtKB	Topological domain	1	113	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25353	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25353	UniProtKB	Topological domain	135	742	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25353	UniProtKB	Region	168	545	.	.	.	Note=Phosphodiesterase	
+P25353	UniProtKB	Compositional bias	692	702	.	.	.	Note=Poly-Ser	
+P25353	UniProtKB	Active site	219	219	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25353	UniProtKB	Glycosylation	161	161	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25353	UniProtKB	Glycosylation	204	204	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25353	UniProtKB	Glycosylation	264	264	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25353	UniProtKB	Glycosylation	296	296	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25353	UniProtKB	Glycosylation	403	403	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53718 1 249
+P53718	UniProtKB	Chain	1	249	.	.	.	ID=PRO_0000203470;Note=Transcription factor NRM1	
+P53718	UniProtKB	Modified residue	145	145	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q08485 1 598
+Q08485	UniProtKB	Chain	1	598	.	.	.	ID=PRO_0000197927;Note=Nicotinamide riboside transporter 1	
+Q08485	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08485	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08485	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08485	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08485	UniProtKB	Transmembrane	197	217	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08485	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08485	UniProtKB	Transmembrane	273	293	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08485	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08485	UniProtKB	Transmembrane	395	415	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08485	UniProtKB	Transmembrane	447	467	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08485	UniProtKB	Transmembrane	484	504	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08485	UniProtKB	Modified residue	560	560	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08485	UniProtKB	Modified residue	572	572	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38632 1 267
+P38632	UniProtKB	Chain	1	267	.	.	.	ID=PRO_0000218991;Note=E3 SUMO-protein ligase MMS21	
+P38632	UniProtKB	Zinc finger	169	246	.	.	.	Note=SP-RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00452	
+P38632	UniProtKB	Sequence conflict	124	124	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38632	UniProtKB	Helix	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Helix	19	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Helix	31	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Helix	60	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Helix	108	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Beta strand	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Helix	122	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Helix	142	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Beta strand	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Turn	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Beta strand	192	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Beta strand	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Helix	206	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Helix	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Helix	232	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Beta strand	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+P38632	UniProtKB	Helix	239	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+##sequence-region Q05541 1 303
+Q05541	UniProtKB	Chain	1	303	.	.	.	ID=PRO_0000057962;Note=Non-structural maintenance of chromosome element 3	
+##sequence-region P53898 1 299
+P53898	UniProtKB	Chain	1	299	.	.	.	ID=PRO_0000203417;Note=Protein NSG2	
+P53898	UniProtKB	Topological domain	1	108	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53898	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53898	UniProtKB	Topological domain	130	161	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53898	UniProtKB	Transmembrane	162	182	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53898	UniProtKB	Topological domain	183	237	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53898	UniProtKB	Transmembrane	238	258	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53898	UniProtKB	Topological domain	259	268	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53898	UniProtKB	Transmembrane	269	289	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53898	UniProtKB	Topological domain	290	299	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53898	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q12457 1 570
+Q12457	UniProtKB	Chain	1	570	.	.	.	ID=PRO_0000242620;Note=RNA polymerase I termination factor	
+Q12457	UniProtKB	Domain	273	339	.	.	.	Note=Myb-like 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133	
+Q12457	UniProtKB	Domain	340	391	.	.	.	Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+Q12457	UniProtKB	Domain	392	486	.	.	.	Note=Myb-like 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133	
+Q12457	UniProtKB	Domain	493	549	.	.	.	Note=Myb-like 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133	
+Q12457	UniProtKB	DNA binding	367	389	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+Q12457	UniProtKB	Compositional bias	35	138	.	.	.	Note=Lys-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00012	
+Q12457	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P36052 1 402
+P36052	UniProtKB	Chain	1	402	.	.	.	ID=PRO_0000203142;Note=Protein arginine methyltransferase NDUFAF7 homolog%2C mitochondrial	
+##sequence-region Q06148 1 342
+Q06148	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000268689;Note=Non-homologous end-joining protein 1	
+Q06148	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06148	UniProtKB	Transmembrane	129	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06148	UniProtKB	Natural variant	17	17	.	.	.	Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6044%2C DBVPG6763%2C DBVPG6765%2C SK1%2C Y55 and YPS128. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060	
+Q06148	UniProtKB	Natural variant	21	21	.	.	.	Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060	
+Q06148	UniProtKB	Natural variant	65	65	.	.	.	Note=In strain: YPS128. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060	
+Q06148	UniProtKB	Natural variant	105	105	.	.	.	Note=In strain: YPS128. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060	
+Q06148	UniProtKB	Natural variant	161	161	.	.	.	Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060	
+Q06148	UniProtKB	Natural variant	204	204	.	.	.	Note=In strain: DBVPG6044 and Y55. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060	
+Q06148	UniProtKB	Natural variant	231	231	.	.	.	Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060	
+Q06148	UniProtKB	Natural variant	249	249	.	.	.	Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060	
+Q06148	UniProtKB	Natural variant	270	270	.	.	.	Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060	
+Q06148	UniProtKB	Natural variant	281	281	.	.	.	Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060	
+##sequence-region P25382 1 515
+P25382	UniProtKB	Chain	1	515	.	.	.	ID=PRO_0000051471;Note=Ribosome assembly protein 4	
+P25382	UniProtKB	Repeat	141	181	.	.	.	Note=WD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25382	UniProtKB	Repeat	184	223	.	.	.	Note=WD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25382	UniProtKB	Repeat	227	273	.	.	.	Note=WD 3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25382	UniProtKB	Repeat	276	314	.	.	.	Note=WD 4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25382	UniProtKB	Repeat	352	396	.	.	.	Note=WD 5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25382	UniProtKB	Repeat	400	439	.	.	.	Note=WD 6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25382	UniProtKB	Repeat	442	481	.	.	.	Note=WD 7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25382	UniProtKB	Repeat	484	515	.	.	.	Note=WD 8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25382	UniProtKB	Region	20	128	.	.	.	Note=Interaction with MDN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19737519;Dbxref=PMID:19737519	
+P25382	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Impairs interaction with MDN1. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19737519;Dbxref=PMID:19737519	
+P25382	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Impairs interaction with MDN1. Blocks progression of the nascent pre-60S subunit and subsequent export to the cytoplasm. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19737519;Dbxref=PMID:19737519	
+P25382	UniProtKB	Beta strand	34	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Helix	57	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Helix	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	117	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	146	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	156	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	168	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Turn	173	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	177	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	189	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	201	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	210	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Turn	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	232	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Helix	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	251	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	260	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Turn	265	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	269	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	281	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	290	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	301	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Helix	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	312	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	323	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Helix	331	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Helix	349	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	365	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	374	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	383	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Turn	388	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	395	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	405	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	414	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	426	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Turn	431	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	436	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	447	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	456	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	466	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Turn	473	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	477	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	489	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	500	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+P25382	UniProtKB	Beta strand	510	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU	
+##sequence-region P38798 1 1089
+P38798	UniProtKB	Chain	1	1089	.	.	.	ID=PRO_0000096873;Note=Nonsense-mediated mRNA decay protein 2	
+P38798	UniProtKB	Compositional bias	843	975	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P38798	UniProtKB	Sequence conflict	2	2	.	.	.	Note=D->YQQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38798	UniProtKB	Sequence conflict	2	2	.	.	.	Note=D->YQQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38798	UniProtKB	Helix	3	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	34	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	52	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	69	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	87	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	106	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	130	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	182	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	201	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	231	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+P38798	UniProtKB	Helix	277	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN	
+##sequence-region P47149 1 201
+P47149	UniProtKB	Chain	1	201	.	.	.	ID=PRO_0000096885;Note=Kinetochore-associated protein NNF1	
+P47149	UniProtKB	Sequence conflict	55	55	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47149	UniProtKB	Sequence conflict	89	89	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47149	UniProtKB	Sequence conflict	152	152	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47149	UniProtKB	Sequence conflict	164	165	.	.	.	Note=NE->KQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47149	UniProtKB	Sequence conflict	193	193	.	.	.	Note=M->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36059 1 337
+P36059	UniProtKB	Chain	1	337	.	.	.	ID=PRO_0000119053;Note=ATP-dependent (S)-NAD(P)H-hydrate dehydratase	
+P36059	UniProtKB	Domain	11	335	.	.	.	Note=YjeF C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157	
+P36059	UniProtKB	Nucleotide binding	218	222	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157	
+P36059	UniProtKB	Nucleotide binding	240	249	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157	
+P36059	UniProtKB	Region	182	188	.	.	.	Note=NAD(P)HX;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157	
+P36059	UniProtKB	Binding site	121	121	.	.	.	Note=NAD(P)HX%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157	
+P36059	UniProtKB	Binding site	250	250	.	.	.	Note=NAD(P)HX;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157	
+P36059	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36059	UniProtKB	Sequence conflict	182	182	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40165 1 246
+P40165	UniProtKB	Chain	1	246	.	.	.	ID=PRO_0000119061;Note=NAD(P)H-hydrate epimerase	
+P40165	UniProtKB	Domain	12	234	.	.	.	Note=YjeF N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159	
+P40165	UniProtKB	Region	69	73	.	.	.	Note=NAD(P)HX;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159	
+P40165	UniProtKB	Region	142	148	.	.	.	Note=NAD(P)HX;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159	
+P40165	UniProtKB	Metal binding	70	70	.	.	.	Note=Potassium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159	
+P40165	UniProtKB	Metal binding	138	138	.	.	.	Note=Potassium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159	
+P40165	UniProtKB	Metal binding	176	176	.	.	.	Note=Potassium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159	
+P40165	UniProtKB	Binding site	173	173	.	.	.	Note=NAD(P)HX;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159	
+P40165	UniProtKB	Helix	9	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Turn	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Helix	28	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Helix	54	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Beta strand	60	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Helix	69	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Beta strand	88	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Helix	100	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Helix	124	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Turn	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Beta strand	133	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Helix	153	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Turn	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Beta strand	169	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Turn	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Beta strand	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Beta strand	193	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Helix	203	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Turn	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Beta strand	214	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Helix	224	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+P40165	UniProtKB	Beta strand	242	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT	
+##sequence-region Q06162 1 153
+Q06162	UniProtKB	Chain	1	153	.	.	.	ID=PRO_0000096868;Note=Central kinetochore subunit NKP2	
+Q06162	UniProtKB	Coiled coil	86	128	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P48234 1 707
+P48234	UniProtKB	Chain	1	707	.	.	.	ID=PRO_0000051473;Note=Ribosome biogenesis protein ENP2	
+P48234	UniProtKB	Repeat	54	94	.	.	.	Note=WD 1	
+P48234	UniProtKB	Repeat	178	217	.	.	.	Note=WD 2	
+P48234	UniProtKB	Repeat	226	265	.	.	.	Note=WD 3	
+P48234	UniProtKB	Repeat	269	310	.	.	.	Note=WD 4	
+P48234	UniProtKB	Repeat	312	351	.	.	.	Note=WD 5	
+P48234	UniProtKB	Modified residue	529	529	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P48234	UniProtKB	Modified residue	550	550	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P48234	UniProtKB	Modified residue	555	555	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P48234	UniProtKB	Sequence conflict	678	678	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48234	UniProtKB	Sequence conflict	678	678	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07623 1 225
+Q07623	UniProtKB	Chain	1	225	.	.	.	ID=PRO_0000268691;Note=Nucleolar protein 6	
+Q07623	UniProtKB	Domain	78	155	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q07623	UniProtKB	Compositional bias	7	74	.	.	.	Note=Lys-rich	
+Q07623	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q07623	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07623	UniProtKB	Beta strand	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ	
+Q07623	UniProtKB	Helix	91	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ	
+Q07623	UniProtKB	Turn	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ	
+Q07623	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ	
+Q07623	UniProtKB	Helix	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ	
+Q07623	UniProtKB	Beta strand	114	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ	
+Q07623	UniProtKB	Helix	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ	
+Q07623	UniProtKB	Turn	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ	
+Q07623	UniProtKB	Helix	128	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ	
+Q07623	UniProtKB	Turn	137	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ	
+Q07623	UniProtKB	Beta strand	149	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ	
+##sequence-region P38082 1 220
+P38082	UniProtKB	Chain	1	220	.	.	.	ID=PRO_0000046813;Note=Probable transcriptional regulator NRG2	
+P38082	UniProtKB	Zinc finger	153	175	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P38082	UniProtKB	Zinc finger	181	205	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+##sequence-region P27476 1 414
+P27476	UniProtKB	Chain	1	414	.	.	.	ID=PRO_0000081690;Note=Nuclear localization sequence-binding protein	
+P27476	UniProtKB	Domain	168	246	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P27476	UniProtKB	Domain	267	345	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P27476	UniProtKB	Region	353	384	.	.	.	Note=RGG-box	
+P27476	UniProtKB	Region	366	384	.	.	.	Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P27476	UniProtKB	Compositional bias	29	136	.	.	.	Note=Asp/Glu/Ser-rich	
+P27476	UniProtKB	Modified residue	353	353	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P27476	UniProtKB	Modified residue	362	362	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P27476	UniProtKB	Modified residue	366	366	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P27476	UniProtKB	Modified residue	375	375	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P27476	UniProtKB	Modified residue	379	379	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+P27476	UniProtKB	Modified residue	382	382	.	.	.	Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332	
+##sequence-region Q08214 1 380
+Q08214	UniProtKB	Chain	1	380	.	.	.	ID=PRO_0000102238;Note=Endonuclease III homolog 2	
+Q08214	UniProtKB	Domain	228	252	.	.	.	Note=HhH;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183	
+Q08214	UniProtKB	Region	15	40	.	.	.	Note=Interaction with MLH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12042306;Dbxref=PMID:12042306	
+Q08214	UniProtKB	Motif	8	12	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08214	UniProtKB	Motif	376	380	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08214	UniProtKB	Active site	248	248	.	.	.	Note=Nucleophile%3B for N-glycosylase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183	
+Q08214	UniProtKB	Metal binding	319	319	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183	
+Q08214	UniProtKB	Metal binding	326	326	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183	
+Q08214	UniProtKB	Metal binding	329	329	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183	
+Q08214	UniProtKB	Metal binding	335	335	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183	
+Q08214	UniProtKB	Site	267	267	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183	
+Q08214	UniProtKB	Cross-link	194	194	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08214	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Abolishes interaction with MLH1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12042306;Dbxref=PMID:12042306	
+Q08214	UniProtKB	Mutagenesis	26	26	.	.	.	Note=Abolishes interaction with MLH1. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12042306;Dbxref=PMID:12042306	
+Q08214	UniProtKB	Mutagenesis	27	27	.	.	.	Note=Abolishes interaction with MLH1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12042306;Dbxref=PMID:12042306	
+##sequence-region P40215 1 560
+P40215	UniProtKB	Transit peptide	1	41	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40215	UniProtKB	Chain	42	560	.	.	.	ID=PRO_0000203306;Note=External NADH-ubiquinone oxidoreductase 1%2C mitochondrial	
+P40215	UniProtKB	Nucleotide binding	114	144	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40215	UniProtKB	Nucleotide binding	275	311	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03210 1 505
+Q03210	UniProtKB	Chain	1	505	.	.	.	ID=PRO_0000218580;Note=Probable RNA exonuclease NGL3	
+Q03210	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+##sequence-region P32495 1 156
+P32495	UniProtKB	Chain	1	156	.	.	.	ID=PRO_0000136776;Note=H/ACA ribonucleoprotein complex subunit 2	
+P32495	UniProtKB	Mutagenesis	56	56	.	.	.	Note=No effect. V->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11433018;Dbxref=PMID:11433018	
+P32495	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Significant growth impairment at 30 and 37 degrees Celsius. Impaired association with H/ACA snoRNAs. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11433018;Dbxref=PMID:11433018	
+P32495	UniProtKB	Mutagenesis	68	68	.	.	.	Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11433018;Dbxref=PMID:11433018	
+P32495	UniProtKB	Mutagenesis	76	77	.	.	.	Note=Lethal. Impaired association with H/ACA snoRNAs. Accumulation of NHP2 within the nucleolus. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11433018;Dbxref=PMID:11433018	
+P32495	UniProtKB	Mutagenesis	80	80	.	.	.	Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11433018;Dbxref=PMID:11433018	
+P32495	UniProtKB	Helix	37	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW	
+P32495	UniProtKB	Turn	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW	
+P32495	UniProtKB	Beta strand	56	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW	
+P32495	UniProtKB	Helix	60	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW	
+P32495	UniProtKB	Beta strand	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW	
+P32495	UniProtKB	Helix	86	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW	
+P32495	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW	
+P32495	UniProtKB	Helix	107	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW	
+P32495	UniProtKB	Beta strand	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBX	
+P32495	UniProtKB	Beta strand	121	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW	
+P32495	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW	
+P32495	UniProtKB	Beta strand	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBX	
+P32495	UniProtKB	Helix	139	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW	
+##sequence-region Q04121 1 633
+Q04121	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Chain	22	633	.	.	.	ID=PRO_0000052380;Note=Endosomal/prevacuolar sodium/hydrogen exchanger	
+Q04121	UniProtKB	Topological domain	22	61	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	83	85	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	107	117	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	139	152	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	174	189	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	190	211	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	212	217	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	218	238	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	239	258	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	259	279	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	280	288	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	289	308	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	309	313	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	314	333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	334	344	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	345	364	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	365	376	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	377	397	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	398	431	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	432	452	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Topological domain	453	457	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Transmembrane	458	478	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Motif	124	133	.	.	.	Note=Amiloride-binding	
+Q04121	UniProtKB	Compositional bias	23	50	.	.	.	Note=Asp-rich	
+Q04121	UniProtKB	Modified residue	490	490	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04121	UniProtKB	Modified residue	494	494	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04121	UniProtKB	Modified residue	498	498	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04121	UniProtKB	Modified residue	499	499	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04121	UniProtKB	Modified residue	569	569	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04121	UniProtKB	Glycosylation	420	420	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04121	UniProtKB	Glycosylation	515	515	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11036065;Dbxref=PMID:11036065	
+Q04121	UniProtKB	Glycosylation	550	550	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11036065;Dbxref=PMID:11036065	
+Q04121	UniProtKB	Glycosylation	563	563	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11036065;Dbxref=PMID:11036065	
+Q04121	UniProtKB	Mutagenesis	201	201	.	.	.	Note=Impairs protein-trafficking to the vacuole. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11102523;Dbxref=PMID:11102523	
+Q04121	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Impairs protein-trafficking to the vacuole. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11102523;Dbxref=PMID:11102523	
+Q04121	UniProtKB	Mutagenesis	230	230	.	.	.	Note=Impairs protein-trafficking to the vacuole. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11102523;Dbxref=PMID:11102523	
+Q04121	UniProtKB	Mutagenesis	355	355	.	.	.	Note=Impairs partially resistance to osmotic stress and hygromycin. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892	
+Q04121	UniProtKB	Mutagenesis	357	357	.	.	.	Note=Impairs resistance to osmotic stress and hygromycin%2C and blocks protein-trafficking to the vacuole. F->A%2CL%2CI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892	
+Q04121	UniProtKB	Mutagenesis	357	357	.	.	.	Note=Impairs partially resistance to osmotic stress and hygromycin. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892	
+Q04121	UniProtKB	Mutagenesis	361	361	.	.	.	Note=Impairs resistance to osmotic stress and hygromycin%2C and blocks protein-trafficking to the vacuole. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892	
+Q04121	UniProtKB	Mutagenesis	365	365	.	.	.	Note=Impairs resistance to osmotic stress and hygromycin%2C and blocks protein-trafficking to the vacuole. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892	
+Q04121	UniProtKB	Mutagenesis	369	369	.	.	.	Note=Impairs partially resistance to osmotic stress and hygromycin. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892	
+Q04121	UniProtKB	Mutagenesis	376	376	.	.	.	Note=Impairs resistance to osmotic stress and hygromycin. P->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892	
+##sequence-region P34077 1 839
+P34077	UniProtKB	Chain	1	839	.	.	.	ID=PRO_0000124787;Note=Nucleoporin NIC96	
+P34077	UniProtKB	Region	25	60	.	.	.	Note=Leucine zipper-like heptad repeat%2C required for interaction with NSP1	
+P34077	UniProtKB	Compositional bias	187	236	.	.	.	Note=Asn-rich	
+P34077	UniProtKB	Sequence conflict	59	59	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P34077	UniProtKB	Helix	206	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	234	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	248	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Turn	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	270	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	301	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Beta strand	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Beta strand	316	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Beta strand	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	333	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Turn	342	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	346	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	357	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	367	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Turn	375	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO	
+P34077	UniProtKB	Beta strand	384	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO	
+P34077	UniProtKB	Helix	388	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO	
+P34077	UniProtKB	Turn	398	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO	
+P34077	UniProtKB	Beta strand	402	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO	
+P34077	UniProtKB	Helix	406	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	420	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	426	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	432	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Beta strand	449	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO	
+P34077	UniProtKB	Helix	459	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	471	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	478	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	488	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	500	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	534	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Turn	543	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	550	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	559	562	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	566	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	586	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Beta strand	595	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO	
+P34077	UniProtKB	Helix	603	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	609	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	616	633	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	637	646	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	650	667	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Beta strand	675	679	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO	
+P34077	UniProtKB	Turn	681	683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	685	696	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	700	703	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	708	728	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	732	741	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	750	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO	
+P34077	UniProtKB	Helix	754	759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	760	762	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	765	768	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	771	790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	799	819	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	820	823	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+P34077	UniProtKB	Helix	826	833	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5	
+##sequence-region P32770 1 719
+P32770	UniProtKB	Chain	1	719	.	.	.	ID=PRO_0000081689;Note=Asparagine-rich protein	
+P32770	UniProtKB	Domain	226	322	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P32770	UniProtKB	Zinc finger	355	384	.	.	.	Note=RanBP2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00322	
+P32770	UniProtKB	Zinc finger	581	610	.	.	.	Note=RanBP2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00322	
+P32770	UniProtKB	Compositional bias	490	564	.	.	.	Note=Asn-rich	
+P32770	UniProtKB	Modified residue	345	345	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956	
+P32770	UniProtKB	Modified residue	455	455	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P32770	UniProtKB	Modified residue	630	630	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32770	UniProtKB	Sequence conflict	493	493	.	.	.	Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12181 1 623
+Q12181	UniProtKB	Chain	1	623	.	.	.	ID=PRO_0000167624;Note=NADPH-dependent diflavin oxidoreductase 1	
+Q12181	UniProtKB	Domain	7	168	.	.	.	Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178	
+Q12181	UniProtKB	Domain	224	491	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178	
+Q12181	UniProtKB	Nucleotide binding	13	18	.	.	.	Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178	
+Q12181	UniProtKB	Nucleotide binding	60	63	.	.	.	Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178	
+Q12181	UniProtKB	Nucleotide binding	106	115	.	.	.	Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178	
+Q12181	UniProtKB	Nucleotide binding	413	416	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178	
+Q12181	UniProtKB	Nucleotide binding	445	448	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178	
+Q12181	UniProtKB	Nucleotide binding	538	539	.	.	.	Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178	
+Q12181	UniProtKB	Binding site	142	142	.	.	.	Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178	
+Q12181	UniProtKB	Binding site	383	383	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178	
+Q12181	UniProtKB	Binding site	623	623	.	.	.	Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178	
+##sequence-region P53317 1 196
+P53317	UniProtKB	Chain	1	196	.	.	.	ID=PRO_0000202860;Note=Nucleolar protein 19	
+##sequence-region P37838 1 685
+P37838	UniProtKB	Chain	1	685	.	.	.	ID=PRO_0000081677;Note=Nucleolar protein 4	
+P37838	UniProtKB	Domain	26	103	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P37838	UniProtKB	Domain	147	225	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P37838	UniProtKB	Domain	290	383	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P37838	UniProtKB	Domain	462	612	.	.	.	Note=RRM 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P37838	UniProtKB	Compositional bias	241	267	.	.	.	Note=Asp/Glu-rich (acidic)	
+P37838	UniProtKB	Modified residue	247	247	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P37838	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P37838	UniProtKB	Natural variant	308	308	.	.	.	Note=P->A	
+##sequence-region Q12080 1 455
+Q12080	UniProtKB	Chain	1	455	.	.	.	ID=PRO_0000218965;Note=Ribosome biogenesis protein NOP53	
+Q12080	UniProtKB	Compositional bias	273	276	.	.	.	Note=Poly-Glu	
+Q12080	UniProtKB	Compositional bias	281	293	.	.	.	Note=Poly-Glu	
+Q12080	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P33755 1 580
+P33755	UniProtKB	Chain	1	580	.	.	.	ID=PRO_0000057944;Note=Nuclear protein localization protein 4	
+P33755	UniProtKB	Domain	237	377	.	.	.	Note=MPN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+P33755	UniProtKB	Mutagenesis	323	323	.	.	.	Note=In npl4-1%3B nuclear-targeted proteins accumulate in the cytoplasm. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11598205;Dbxref=PMID:11598205	
+##sequence-region P22211 1 790
+P22211	UniProtKB	Chain	1	790	.	.	.	ID=PRO_0000086445;Note=Nitrogen permease reactivator protein	
+P22211	UniProtKB	Domain	438	742	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22211	UniProtKB	Nucleotide binding	444	452	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22211	UniProtKB	Compositional bias	1	339	.	.	.	Note=Ser-rich (may play a regulatory role)	
+P22211	UniProtKB	Compositional bias	51	58	.	.	.	Note=Poly-Ser	
+P22211	UniProtKB	Compositional bias	782	786	.	.	.	Note=Poly-Lys	
+P22211	UniProtKB	Active site	561	561	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P22211	UniProtKB	Binding site	467	467	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P22211	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	111	111	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	125	125	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18980262;Dbxref=PMID:17330950,PMID:19779198,PMID:18980262	
+P22211	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18980262;Dbxref=PMID:19779198,PMID:18980262	
+P22211	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18980262;Dbxref=PMID:19779198,PMID:18980262	
+P22211	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	259	259	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	260	260	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	292	292	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	317	317	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	320	320	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	328	328	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	334	334	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22211	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	353	353	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	356	356	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Modified residue	357	357	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000269|PubMed:18980262;Dbxref=PMID:17330950,PMID:18980262	
+P22211	UniProtKB	Modified residue	385	385	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Mutagenesis	47	47	.	.	.	Note=Abolishes autophosphorylation%3B when associated with A-257 and A-357. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Mutagenesis	257	257	.	.	.	Note=Abolishes autophosphorylation%3B when associated with A-47 and A-357. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Mutagenesis	257	257	.	.	.	Note=Abolishes autophosphorylation. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Mutagenesis	357	357	.	.	.	Note=Abolishes autophosphorylation%3B when associated with A-47 and A-257. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262	
+P22211	UniProtKB	Sequence conflict	154	154	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22211	UniProtKB	Sequence conflict	277	277	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39683 1 429
+P39683	UniProtKB	Chain	1	429	.	.	.	ID=PRO_0000205862;Note=Nicotinate phosphoribosyltransferase	
+P39683	UniProtKB	Sequence conflict	131	137	.	.	.	Note=YEIPLLS->MRSLTV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39683	UniProtKB	Sequence conflict	144	158	.	.	.	Note=FKFVDIDWDYENQLE->LIVTSTGLRNHR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39683	UniProtKB	Sequence conflict	175	177	.	.	.	Note=SEF->RIH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39683	UniProtKB	Sequence conflict	243	243	.	.	.	Note=E->EL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39683	UniProtKB	Beta strand	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	14	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	31	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	47	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	67	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	82	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	101	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	111	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	132	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	156	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	185	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	203	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Turn	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	210	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	216	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	232	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	248	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	275	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	286	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	292	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	300	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	321	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	332	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	348	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	355	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	364	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	369	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Beta strand	376	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+P39683	UniProtKB	Helix	402	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP	
+##sequence-region P53915 1 240
+P53915	UniProtKB	Chain	1	240	.	.	.	ID=PRO_0000215898;Note=Nicotinamide riboside kinase	
+P53915	UniProtKB	Nucleotide binding	13	21	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6	
+P53915	UniProtKB	Nucleotide binding	162	164	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6	
+P53915	UniProtKB	Nucleotide binding	208	210	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6	
+P53915	UniProtKB	Region	39	42	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6	
+P53915	UniProtKB	Region	59	60	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6	
+P53915	UniProtKB	Region	164	165	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6	
+P53915	UniProtKB	Active site	39	39	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6	
+P53915	UniProtKB	Metal binding	20	20	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6	
+P53915	UniProtKB	Metal binding	39	39	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6	
+P53915	UniProtKB	Binding site	158	158	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6	
+P53915	UniProtKB	Binding site	159	159	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6	
+##sequence-region P53935 1 1240
+P53935	UniProtKB	Chain	1	1240	.	.	.	ID=PRO_0000203442;Note=Stress response protein NST1	
+P53935	UniProtKB	Coiled coil	616	777	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53935	UniProtKB	Compositional bias	506	554	.	.	.	Note=His-rich	
+P53935	UniProtKB	Compositional bias	989	1115	.	.	.	Note=Ser-rich	
+P53935	UniProtKB	Modified residue	266	266	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53935	UniProtKB	Natural variant	162	162	.	.	.	Note=In strain: SK1. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P53935	UniProtKB	Natural variant	208	208	.	.	.	Note=In strain: SK1. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P53935	UniProtKB	Natural variant	354	354	.	.	.	Note=In strain: SK1. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P53935	UniProtKB	Natural variant	899	899	.	.	.	Note=In strain: SK1. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+##sequence-region Q12311 1 748
+Q12311	UniProtKB	Chain	1	748	.	.	.	ID=PRO_0000268692;Note=NuA3 HAT complex component NTO1	
+Q12311	UniProtKB	Zinc finger	263	313	.	.	.	Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+Q12311	UniProtKB	Zinc finger	317	350	.	.	.	Note=C2HC pre-PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146	
+Q12311	UniProtKB	Zinc finger	374	439	.	.	.	Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146	
+Q12311	UniProtKB	Modified residue	728	728	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q02629 1 959
+Q02629	UniProtKB	Chain	1	959	.	.	.	ID=PRO_0000204830;Note=Nucleoporin NUP100/NSP100	
+Q02629	UniProtKB	Repeat	2	3	.	.	.	Note=FG 1	
+Q02629	UniProtKB	Repeat	9	10	.	.	.	Note=FG 2	
+Q02629	UniProtKB	Repeat	17	17	.	.	.	Note=FG 3	
+Q02629	UniProtKB	Repeat	21	24	.	.	.	Note=SLFG 1%3B approximate	
+Q02629	UniProtKB	Repeat	33	36	.	.	.	Note=SLFG 2	
+Q02629	UniProtKB	Repeat	51	54	.	.	.	Note=SLFG 3%3B approximate	
+Q02629	UniProtKB	Repeat	66	69	.	.	.	Note=SLFG 4	
+Q02629	UniProtKB	Repeat	77	80	.	.	.	Note=GLFG 1%3B approximate	
+Q02629	UniProtKB	Repeat	89	92	.	.	.	Note=SLFG 5%3B approximate	
+Q02629	UniProtKB	Repeat	105	106	.	.	.	Note=FG 4	
+Q02629	UniProtKB	Repeat	112	115	.	.	.	Note=GLFG 2%3B approximate	
+Q02629	UniProtKB	Repeat	131	134	.	.	.	Note=SLFG 6%3B approximate	
+Q02629	UniProtKB	Repeat	145	146	.	.	.	Note=FG 5	
+Q02629	UniProtKB	Repeat	157	160	.	.	.	Note=SLFG 7	
+Q02629	UniProtKB	Repeat	168	171	.	.	.	Note=GLFG 3%3B approximate	
+Q02629	UniProtKB	Repeat	175	178	.	.	.	Note=SLFG 8%3B approximate	
+Q02629	UniProtKB	Repeat	189	190	.	.	.	Note=FG 6	
+Q02629	UniProtKB	Repeat	202	205	.	.	.	Note=SLFG 9	
+Q02629	UniProtKB	Repeat	210	213	.	.	.	Note=SLFG 10%3B approximate	
+Q02629	UniProtKB	Repeat	220	223	.	.	.	Note=SLFG 11	
+Q02629	UniProtKB	Repeat	233	234	.	.	.	Note=FG 7	
+Q02629	UniProtKB	Repeat	242	245	.	.	.	Note=SLFG 12%3B approximate	
+Q02629	UniProtKB	Repeat	253	256	.	.	.	Note=SLFG 13	
+Q02629	UniProtKB	Repeat	271	274	.	.	.	Note=GLFG 4	
+Q02629	UniProtKB	Repeat	287	290	.	.	.	Note=GLFG 5	
+Q02629	UniProtKB	Repeat	300	303	.	.	.	Note=GLFG 6%3B approximate	
+Q02629	UniProtKB	Repeat	318	321	.	.	.	Note=SLFG 14	
+Q02629	UniProtKB	Repeat	333	336	.	.	.	Note=GLFG 7	
+Q02629	UniProtKB	Repeat	345	348	.	.	.	Note=GLFG 8	
+Q02629	UniProtKB	Repeat	358	361	.	.	.	Note=GLFG 9	
+Q02629	UniProtKB	Repeat	379	382	.	.	.	Note=GLFG 10	
+Q02629	UniProtKB	Repeat	393	396	.	.	.	Note=GLFG 11	
+Q02629	UniProtKB	Repeat	405	408	.	.	.	Note=SLFG 15	
+Q02629	UniProtKB	Repeat	417	420	.	.	.	Note=SLFG 16	
+Q02629	UniProtKB	Repeat	436	439	.	.	.	Note=SLFG 17	
+Q02629	UniProtKB	Repeat	448	449	.	.	.	Note=FG 8	
+Q02629	UniProtKB	Repeat	462	465	.	.	.	Note=SLFG 18	
+Q02629	UniProtKB	Repeat	474	477	.	.	.	Note=SLFG 19%3B approximate	
+Q02629	UniProtKB	Repeat	490	493	.	.	.	Note=GLFG 12	
+Q02629	UniProtKB	Repeat	506	509	.	.	.	Note=GLFG 13	
+Q02629	UniProtKB	Repeat	523	526	.	.	.	Note=GLFG 14	
+Q02629	UniProtKB	Repeat	542	543	.	.	.	Note=FG 9	
+Q02629	UniProtKB	Repeat	550	553	.	.	.	Note=GLFG 15	
+Q02629	UniProtKB	Repeat	569	570	.	.	.	Note=FG 10	
+Q02629	UniProtKB	Domain	814	956	.	.	.	Note=Peptidase S59;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00765	
+Q02629	UniProtKB	Region	816	955	.	.	.	Note=Nucleoporin RNA-binding motif (NRM)	
+Q02629	UniProtKB	Compositional bias	32	386	.	.	.	Note=Asn-rich	
+Q02629	UniProtKB	Compositional bias	37	43	.	.	.	Note=Poly-Asn	
+Q02629	UniProtKB	Compositional bias	52	570	.	.	.	Note=Gly-rich	
+Q02629	UniProtKB	Compositional bias	312	317	.	.	.	Note=Poly-Asn	
+Q02629	UniProtKB	Compositional bias	337	390	.	.	.	Note=Gln-rich	
+Q02629	UniProtKB	Compositional bias	387	390	.	.	.	Note=Poly-Gln	
+Q02629	UniProtKB	Modified residue	763	763	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q02629	UniProtKB	Modified residue	783	783	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q92317 1 146
+Q92317	UniProtKB	Chain	1	146	.	.	.	ID=PRO_0000255268;Note=Negative cofactor 2 complex subunit beta	
+Q92317	UniProtKB	Modified residue	135	135	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q92317	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q92317	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P38626 1 284
+P38626	UniProtKB	Chain	1	284	.	.	.	ID=PRO_0000167627;Note=NADH-cytochrome b5 reductase 1	
+P38626	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38626	UniProtKB	Domain	38	142	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+P38626	UniProtKB	Nucleotide binding	122	137	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38626	UniProtKB	Nucleotide binding	148	180	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38830 1 627
+P38830	UniProtKB	Chain	1	627	.	.	.	ID=PRO_0000096772;Note=Meiosis-specific transcription factor NDT80	
+P38830	UniProtKB	DNA binding	28	335	.	.	.	Note=NDT80;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00850	
+P38830	UniProtKB	Site	58	58	.	.	.	Note=Interaction with DNA	
+P38830	UniProtKB	Site	111	111	.	.	.	Note=Interaction with DNA	
+P38830	UniProtKB	Site	177	177	.	.	.	Note=Interaction with DNA	
+P38830	UniProtKB	Site	208	208	.	.	.	Note=Interaction with DNA	
+P38830	UniProtKB	Site	254	254	.	.	.	Note=Interaction with DNA	
+P38830	UniProtKB	Site	326	326	.	.	.	Note=Interaction with DNA	
+P38830	UniProtKB	Mutagenesis	50	50	.	.	.	Note=Reduces DNA-binding by 70%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15161958;Dbxref=PMID:15161958	
+P38830	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Reduces DNA-binding by 50%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15161958;Dbxref=PMID:15161958	
+P38830	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Reduces DNA-binding by 65%25. P->A	
+P38830	UniProtKB	Mutagenesis	58	58	.	.	.	Note=Reduces DNA-binding by 65%25. R->A	
+P38830	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Reduces DNA-binding by 86%25. S->A	
+P38830	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Reduces DNA-binding by 67%25. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15161958;Dbxref=PMID:15161958	
+P38830	UniProtKB	Mutagenesis	110	110	.	.	.	Note=No effect on DNA-binding but strongly reduces progress through meiosis and sporulation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384578;Dbxref=PMID:12384578	
+P38830	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Reduces DNA-binding by 95%25 and abolishes sporulation. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12384578,ECO:0000269|PubMed:15161958;Dbxref=PMID:12384578,PMID:15161958	
+P38830	UniProtKB	Mutagenesis	113	113	.	.	.	Note=Reduces DNA-binding by 80%25 and abolishes sporulation. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12384578,ECO:0000269|PubMed:15161958;Dbxref=PMID:12384578,PMID:15161958	
+P38830	UniProtKB	Mutagenesis	173	173	.	.	.	Note=Reduces DNA-binding by 80%25 and strongly reduces progress through meiosis and sporulation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384578;Dbxref=PMID:12384578	
+P38830	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Reduces DNA-binding by 50%25 but does not abolish sporulation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384578;Dbxref=PMID:12384578	
+P38830	UniProtKB	Mutagenesis	177	177	.	.	.	Note=Reduces DNA-binding by 96%25 and abolishes sporulation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384578;Dbxref=PMID:12384578	
+P38830	UniProtKB	Mutagenesis	202	202	.	.	.	Note=No effect on DNA-binding but strongly reduces progress through meiosis and sporulation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384578;Dbxref=PMID:12384578	
+P38830	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Reduces DNA-binding by 50%25 and abolishes sporulation. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12384578,ECO:0000269|PubMed:15161958;Dbxref=PMID:12384578,PMID:15161958	
+P38830	UniProtKB	Mutagenesis	254	254	.	.	.	Note=Reduces DNA-binding by 93%25 and abolishes sporulation. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12384578,ECO:0000269|PubMed:15161958;Dbxref=PMID:12384578,PMID:15161958	
+P38830	UniProtKB	Mutagenesis	326	326	.	.	.	Note=Reduces DNA-binding by 50%25 and abolishes sporulation. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12384578,ECO:0000269|PubMed:15161958;Dbxref=PMID:12384578,PMID:15161958	
+P38830	UniProtKB	Sequence conflict	200	200	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38830	UniProtKB	Sequence conflict	213	213	.	.	.	Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38830	UniProtKB	Sequence conflict	225	225	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38830	UniProtKB	Sequence conflict	267	267	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38830	UniProtKB	Sequence conflict	363	363	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38830	UniProtKB	Sequence conflict	493	493	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38830	UniProtKB	Sequence conflict	568	568	.	.	.	Note=P->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38830	UniProtKB	Beta strand	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Turn	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Helix	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	70	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Turn	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	90	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	105	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	114	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Helix	127	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Turn	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MN4	
+P38830	UniProtKB	Beta strand	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EVG	
+P38830	UniProtKB	Beta strand	152	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Turn	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M7U	
+P38830	UniProtKB	Beta strand	170	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Helix	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Helix	198	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Turn	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Helix	210	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Helix	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Helix	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Helix	237	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	241	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	273	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Helix	285	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M6U	
+P38830	UniProtKB	Beta strand	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M6U	
+P38830	UniProtKB	Beta strand	297	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	303	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Beta strand	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Helix	328	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+P38830	UniProtKB	Helix	332	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN	
+##sequence-region P33420 1 868
+P33420	UniProtKB	Chain	1	868	.	.	.	ID=PRO_0000083525;Note=Protein NIP100	
+P33420	UniProtKB	Domain	34	84	.	.	.	Note=CAP-Gly;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00045	
+P33420	UniProtKB	Coiled coil	101	175	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33420	UniProtKB	Coiled coil	207	375	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33420	UniProtKB	Coiled coil	645	776	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40447 1 199
+P40447	UniProtKB	Chain	1	199	.	.	.	ID=PRO_0000204049;Note=Putative nitrilase-like protein NIT1	
+P40447	UniProtKB	Domain	2	199	.	.	.	Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P40447	UniProtKB	Active site	44	44	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P40447	UniProtKB	Active site	135	135	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P40447	UniProtKB	Active site	169	169	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054,ECO:0000255|PROSITE-ProRule:PRU10105	
+P40447	UniProtKB	Sequence conflict	4	4	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40447	UniProtKB	Sequence conflict	106	106	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40447	UniProtKB	Sequence conflict	173	173	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P49954 1 291
+P49954	UniProtKB	Chain	1	291	.	.	.	ID=PRO_0000213256;Note=Probable hydrolase NIT3	
+P49954	UniProtKB	Domain	11	264	.	.	.	Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P49954	UniProtKB	Active site	53	53	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P49954	UniProtKB	Active site	128	128	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P49954	UniProtKB	Active site	169	169	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P49954	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P49954	UniProtKB	Beta strand	4	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	11	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Helix	25	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	46	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Turn	53	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Helix	61	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Helix	78	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	99	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Turn	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	109	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	122	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Helix	143	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	155	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	162	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Helix	169	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Helix	175	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	186	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Helix	199	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	217	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	247	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Beta strand	253	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+P49954	UniProtKB	Helix	264	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89	
+##sequence-region Q06178 1 401
+Q06178	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000135018;Note=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1	
+Q06178	UniProtKB	Nucleotide binding	172	174	.	.	.	Note=ATP;Ontology_term=ECO:0000250,ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66,ECO:0000250|UniProtKB:Q9HAN9	
+Q06178	UniProtKB	Nucleotide binding	288	290	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66	
+Q06178	UniProtKB	Nucleotide binding	356	359	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66	
+Q06178	UniProtKB	Region	212	214	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9	
+Q06178	UniProtKB	Region	250	253	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9	
+Q06178	UniProtKB	Region	300	301	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9	
+Q06178	UniProtKB	Compositional bias	61	67	.	.	.	Note=Poly-His	
+Q06178	UniProtKB	Binding site	181	181	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66	
+Q06178	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q06178	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q06178	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q06178	UniProtKB	Modified residue	111	111	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38861 1 518
+P38861	UniProtKB	Chain	1	518	.	.	.	ID=PRO_0000096874;Note=60S ribosomal export protein NMD3	
+P38861	UniProtKB	Motif	399	415	.	.	.	Note=Nuclear localization signal	
+P38861	UniProtKB	Motif	493	502	.	.	.	Note=Nuclear export signal	
+P38861	UniProtKB	Sequence conflict	94	94	.	.	.	Note=K->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P46970 1 1048
+P46970	UniProtKB	Chain	1	1048	.	.	.	ID=PRO_0000096880;Note=Nonsense-mediated mRNA decay protein 5	
+P46970	UniProtKB	Domain	24	104	.	.	.	Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115	
+P46970	UniProtKB	Modified residue	977	977	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46970	UniProtKB	Sequence conflict	258	258	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46970	UniProtKB	Sequence conflict	517	517	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08213 1 363
+Q08213	UniProtKB	Chain	1	363	.	.	.	ID=PRO_0000218578;Note=RNA exonuclease NGL1	
+##sequence-region P53939 1 407
+P53939	UniProtKB	Chain	1	407	.	.	.	ID=PRO_0000203447;Note=Protein NIS1	
+P53939	UniProtKB	Motif	391	398	.	.	.	Note=SUMO-binding	
+P53939	UniProtKB	Modified residue	260	260	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53939	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53939	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53939	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P34909 1 587
+P34909	UniProtKB	Chain	1	587	.	.	.	ID=PRO_0000081681;Note=General negative regulator of transcription subunit 4	
+P34909	UniProtKB	Domain	137	228	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P34909	UniProtKB	Zinc finger	33	78	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P34909	UniProtKB	Zinc finger	229	256	.	.	.	Note=C3H1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723	
+P34909	UniProtKB	Coiled coil	94	128	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34909	UniProtKB	Modified residue	310	310	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34909	UniProtKB	Modified residue	312	312	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34909	UniProtKB	Modified residue	326	326	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34909	UniProtKB	Modified residue	360	360	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34909	UniProtKB	Cross-link	270	270	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P34909	UniProtKB	Turn	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE	
+P34909	UniProtKB	Turn	42	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE	
+P34909	UniProtKB	Helix	58	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE	
+P34909	UniProtKB	Beta strand	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE	
+P34909	UniProtKB	Turn	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE	
+##sequence-region P32494 1 702
+P32494	UniProtKB	Chain	1	702	.	.	.	ID=PRO_0000064448;Note=Chromatin-remodeling complexes subunit NGG1	
+P32494	UniProtKB	Motif	606	618	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32494	UniProtKB	Modified residue	134	134	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32494	UniProtKB	Modified residue	407	407	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32494	UniProtKB	Modified residue	464	464	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32494	UniProtKB	Sequence conflict	520	520	.	.	.	Note=K->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11633 1 99
+P11633	UniProtKB	Chain	1	99	.	.	.	ID=PRO_0000048566;Note=Non-histone chromosomal protein 6B	
+P11633	UniProtKB	DNA binding	27	95	.	.	.	Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267	
+P11633	UniProtKB	Sequence conflict	30	30	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11633	UniProtKB	Sequence conflict	30	30	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47016 1 307
+P47016	UniProtKB	Chain	1	307	.	.	.	ID=PRO_0000213255;Note=Probable hydrolase NIT2	
+P47016	UniProtKB	Domain	6	285	.	.	.	Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P47016	UniProtKB	Active site	45	45	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P47016	UniProtKB	Active site	127	127	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P47016	UniProtKB	Active site	169	169	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00054,ECO:0000269|PubMed:23897470;Dbxref=PMID:23897470	
+P47016	UniProtKB	Binding site	173	173	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23897470;Dbxref=PMID:23897470	
+P47016	UniProtKB	Binding site	199	199	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23897470;Dbxref=PMID:23897470	
+P47016	UniProtKB	Mutagenesis	169	169	.	.	.	Note=Abolishes enzyme activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23897470;Dbxref=PMID:23897470	
+P47016	UniProtKB	Beta strand	5	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Helix	19	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	39	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Helix	54	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Helix	64	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	87	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Helix	98	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	108	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	121	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	162	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Helix	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Helix	175	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	187	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Helix	197	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	223	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Helix	233	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Turn	243	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	251	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	257	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	265	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Beta strand	277	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Helix	285	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Helix	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+P47016	UniProtKB	Turn	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5	
+##sequence-region Q6Q547 1 58
+Q6Q547	UniProtKB	Chain	1	58	.	.	.	ID=PRO_0000149013;Note=H/ACA ribonucleoprotein complex subunit 3	
+Q6Q547	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q6Q547	UniProtKB	Cross-link	28	28	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q6Q547	UniProtKB	Beta strand	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+Q6Q547	UniProtKB	Beta strand	8	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y2Y	
+Q6Q547	UniProtKB	Beta strand	13	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+Q6Q547	UniProtKB	Beta strand	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+Q6Q547	UniProtKB	Beta strand	32	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y2Y	
+Q6Q547	UniProtKB	Beta strand	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQA	
+Q6Q547	UniProtKB	Helix	42	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28	
+Q6Q547	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y2Y	
+##sequence-region Q99207 1 810
+Q99207	UniProtKB	Chain	1	810	.	.	.	ID=PRO_0000137163;Note=Nucleolar complex protein 14	
+##sequence-region Q01560 1 414
+Q01560	UniProtKB	Chain	1	414	.	.	.	ID=PRO_0000081676;Note=Nucleolar protein 3	
+Q01560	UniProtKB	Domain	125	195	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q01560	UniProtKB	Domain	200	275	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q01560	UniProtKB	Compositional bias	280	398	.	.	.	Note=Arg/Gly-rich	
+Q01560	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q01560	UniProtKB	Modified residue	224	224	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q01560	UniProtKB	Beta strand	125	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO	
+Q01560	UniProtKB	Helix	138	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO	
+Q01560	UniProtKB	Turn	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO	
+Q01560	UniProtKB	Beta strand	153	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO	
+Q01560	UniProtKB	Beta strand	160	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO	
+Q01560	UniProtKB	Helix	168	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO	
+Q01560	UniProtKB	Beta strand	189	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO	
+Q01560	UniProtKB	Beta strand	200	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR	
+Q01560	UniProtKB	Helix	213	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR	
+Q01560	UniProtKB	Beta strand	228	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR	
+Q01560	UniProtKB	Beta strand	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR	
+Q01560	UniProtKB	Beta strand	241	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR	
+Q01560	UniProtKB	Helix	248	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR	
+Q01560	UniProtKB	Beta strand	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR	
+Q01560	UniProtKB	Beta strand	266	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR	
+##sequence-region Q12499 1 511
+Q12499	UniProtKB	Chain	1	511	.	.	.	ID=PRO_0000219029;Note=Nucleolar protein 58	
+Q12499	UniProtKB	Domain	283	403	.	.	.	Note=Nop;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00690	
+Q12499	UniProtKB	Coiled coil	435	511	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12499	UniProtKB	Compositional bias	441	511	.	.	.	Note=Asp/Glu/Lys-rich	
+Q12499	UniProtKB	Cross-link	281	281	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P47077 1 666
+P47077	UniProtKB	Chain	1	666	.	.	.	ID=PRO_0000075939;Note=Nucleolar protein 9	
+P47077	UniProtKB	Domain	23	435	.	.	.	Note=PUM-HD	
+P47077	UniProtKB	Repeat	92	127	.	.	.	Note=Pumilio 1	
+P47077	UniProtKB	Repeat	128	163	.	.	.	Note=Pumilio 2	
+P47077	UniProtKB	Repeat	188	223	.	.	.	Note=Pumilio 3	
+P47077	UniProtKB	Repeat	286	326	.	.	.	Note=Pumilio 4	
+P47077	UniProtKB	Repeat	334	368	.	.	.	Note=Pumilio 5	
+P47077	UniProtKB	Repeat	369	407	.	.	.	Note=Pumilio 6	
+P47077	UniProtKB	Repeat	511	548	.	.	.	Note=Pumilio 7	
+P47077	UniProtKB	Repeat	549	587	.	.	.	Note=Pumilio 8	
+P47077	UniProtKB	Helix	58	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	79	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Turn	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	97	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Turn	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	107	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	119	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Turn	128	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	133	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	142	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	178	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	193	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	202	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	256	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Beta strand	278	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	287	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Turn	298	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	301	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	311	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	319	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Beta strand	328	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	333	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	346	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	361	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	376	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Turn	383	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	386	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	399	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	410	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	413	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	421	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Turn	434	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WTY	
+P47077	UniProtKB	Helix	439	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Beta strand	455	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WTY	
+P47077	UniProtKB	Helix	460	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	467	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	482	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	499	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	514	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	526	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	536	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	541	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	552	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	555	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	564	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Turn	575	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	579	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	593	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	600	608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	611	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+P47077	UniProtKB	Helix	618	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD	
+##sequence-region P39923 1 615
+P39923	UniProtKB	Chain	1	615	.	.	.	ID=PRO_0000213321;Note=Nitrogen permease regulator 2	
+P39923	UniProtKB	Compositional bias	354	420	.	.	.	Note=Ser-rich	
+P39923	UniProtKB	Modified residue	362	362	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39923	UniProtKB	Sequence conflict	225	225	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53164 1 384
+P53164	UniProtKB	Chain	1	384	.	.	.	ID=PRO_0000056961;Note=NADH pyrophosphatase	
+P53164	UniProtKB	Domain	219	351	.	.	.	Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794	
+P53164	UniProtKB	Motif	257	278	.	.	.	Note=Nudix box	
+P53164	UniProtKB	Metal binding	272	272	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53164	UniProtKB	Metal binding	276	276	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53164	UniProtKB	Sequence conflict	44	44	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08972 1 1196
+Q08972	UniProtKB	Chain	1	1196	.	.	.	ID=PRO_0000268690;Note=[NU+] prion formation protein 1	
+Q08972	UniProtKB	Domain	570	786	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q08972	UniProtKB	Domain	812	1129	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q08972	UniProtKB	Domain	942	1003	.	.	.	Note=Chromo;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00053	
+Q08972	UniProtKB	Nucleotide binding	604	611	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q08972	UniProtKB	Nucleotide binding	846	853	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q08972	UniProtKB	Compositional bias	61	104	.	.	.	Note=Tyr-rich	
+Q08972	UniProtKB	Compositional bias	70	95	.	.	.	Note=Asn-rich	
+Q08972	UniProtKB	Modified residue	443	443	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08972	UniProtKB	Modified residue	1191	1191	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P0CE68 1 1218
+P0CE68	UniProtKB	Chain	1	1218	.	.	.	ID=PRO_0000093462;Note=ABC transporter NFT1	
+P0CE68	UniProtKB	Topological domain	1	29	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	30	50	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	51	103	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	125	130	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	152	169	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	170	190	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	191	201	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	223	302	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	303	323	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	324	351	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	352	374	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	375	449	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	450	470	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	471	481	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	482	504	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	505	558	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	559	579	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	580	584	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	585	605	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	606	953	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	954	974	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	975	1013	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	1014	1034	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	1035	1082	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	1083	1105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	1106	1109	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	1110	1132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Topological domain	1133	1197	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE68	UniProtKB	Transmembrane	1198	1218	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Domain	311	621	.	.	.	Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Domain	651	892	.	.	.	Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P0CE68	UniProtKB	Domain	961	1218	.	.	.	Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P0CE68	UniProtKB	Nucleotide binding	686	693	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P0CE68	UniProtKB	Glycosylation	4	4	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32860 1 256
+P32860	UniProtKB	Motif	196	199	.	.	.	Note=CxxC motif;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:27532773;Dbxref=PMID:27532773	
+P32860	UniProtKB	Mutagenesis	194	194	.	.	.	Note=Dominant negative mutant%3B cells show a severe synthetic sick phenotype on glycerol/lactate medium. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773	
+P32860	UniProtKB	Mutagenesis	196	199	.	.	.	Note=Loss of function. Abolished homodimerization. CTSC->ATSA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773	
+P32860	UniProtKB	Beta strand	24	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL	
+P32860	UniProtKB	Beta strand	32	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL	
+P32860	UniProtKB	Beta strand	53	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL	
+P32860	UniProtKB	Helix	60	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL	
+P32860	UniProtKB	Helix	67	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL	
+P32860	UniProtKB	Beta strand	79	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL	
+P32860	UniProtKB	Beta strand	86	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL	
+P32860	UniProtKB	Helix	99	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL	
+P32860	UniProtKB	Beta strand	118	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL	
+##sequence-region Q03435 1 203
+Q03435	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03435	UniProtKB	Chain	2	203	.	.	.	ID=PRO_0000048567;Note=Non-histone protein 10	
+Q03435	UniProtKB	DNA binding	94	158	.	.	.	Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267	
+Q03435	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P53081 1 288
+P53081	UniProtKB	Chain	1	288	.	.	.	ID=PRO_0000147356;Note=NGG1-interacting factor 3	
+P53081	UniProtKB	Sequence conflict	53	53	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53920 1 997
+P53920	UniProtKB	Chain	1	997	.	.	.	ID=PRO_0000203429;Note=Pro-apoptotic serine protease NMA111	
+P53920	UniProtKB	Domain	300	378	.	.	.	Note=PDZ 1	
+P53920	UniProtKB	Domain	779	854	.	.	.	Note=PDZ 2	
+P53920	UniProtKB	Region	83	273	.	.	.	Note=Serine protease	
+P53920	UniProtKB	Active site	121	121	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53920	UniProtKB	Active site	152	152	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53920	UniProtKB	Active site	235	235	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53920	UniProtKB	Natural variant	162	162	.	.	.	Note=In strain: YJM269%2C YJM270 and YJM1129. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53920	UniProtKB	Natural variant	241	241	.	.	.	Note=In strain: YJM269 and YJM270. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53920	UniProtKB	Natural variant	331	331	.	.	.	Note=In strain: YJM326. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53920	UniProtKB	Natural variant	343	343	.	.	.	Note=In strain: YJM269 and YJM270. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53920	UniProtKB	Natural variant	386	386	.	.	.	Note=In strain: YJM269%2C YJM270 and YJM1129. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53920	UniProtKB	Natural variant	457	457	.	.	.	Note=In strain: YJM269 and YJM270. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53920	UniProtKB	Natural variant	530	530	.	.	.	Note=In strain: YJM627. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53920	UniProtKB	Natural variant	580	580	.	.	.	Note=In strain: YJM627. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53920	UniProtKB	Natural variant	621	621	.	.	.	Note=In strain: YJM269 and YJM270. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53920	UniProtKB	Natural variant	942	942	.	.	.	Note=In strain: YJM627. P->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730	
+P53920	UniProtKB	Mutagenesis	235	235	.	.	.	Note=Impairs BIR1 degradation and death-promoting activity. S->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14657274,ECO:0000269|PubMed:16608876;Dbxref=PMID:14657274,PMID:16608876	
+##sequence-region Q12129 1 218
+Q12129	UniProtKB	Chain	1	218	.	.	.	ID=PRO_0000096879;Note=Nonsense-mediated decay protein 4	
+##sequence-region P53253 1 936
+P53253	UniProtKB	Chain	1	936	.	.	.	ID=PRO_0000202809;Note=Protein NNF2	
+P53253	UniProtKB	Topological domain	1	41	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53253	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53253	UniProtKB	Topological domain	63	120	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53253	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53253	UniProtKB	Topological domain	142	245	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53253	UniProtKB	Transmembrane	246	266	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53253	UniProtKB	Topological domain	267	936	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53253	UniProtKB	Cross-link	10	10	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region Q08444 1 459
+Q08444	UniProtKB	Chain	1	459	.	.	.	ID=PRO_0000270554;Note=20S-pre-rRNA D-site endonuclease NOB1	
+Q08444	UniProtKB	Domain	10	115	.	.	.	Note=PINc	
+Q08444	UniProtKB	Metal binding	304	304	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08444	UniProtKB	Metal binding	307	307	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08444	UniProtKB	Metal binding	323	323	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08444	UniProtKB	Metal binding	326	326	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08444	UniProtKB	Mutagenesis	92	92	.	.	.	Note=No 20S cleavage. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15388878;Dbxref=PMID:15388878	
+Q08444	UniProtKB	Mutagenesis	110	110	.	.	.	Note=No change in activity or growth. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15388878;Dbxref=PMID:15388878	
+Q08444	UniProtKB	Mutagenesis	279	279	.	.	.	Note=Temperature-sensitive. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502737;Dbxref=PMID:12502737	
+Q08444	UniProtKB	Mutagenesis	280	280	.	.	.	Note=Temperature-sensitive. Q->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502737;Dbxref=PMID:12502737	
+Q08444	UniProtKB	Mutagenesis	281	281	.	.	.	Note=Temperature-sensitive. M->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502737;Dbxref=PMID:12502737	
+##sequence-region Q06512 1 552
+Q06512	UniProtKB	Chain	1	552	.	.	.	ID=PRO_0000173491;Note=Nucleolar complex protein 4	
+##sequence-region Q08208 1 459
+Q08208	UniProtKB	Chain	1	459	.	.	.	ID=PRO_0000081675;Note=Nucleolar protein 12	
+Q08208	UniProtKB	Domain	279	371	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q08208	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08208	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08208	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q12460 1 504
+Q12460	UniProtKB	Chain	1	504	.	.	.	ID=PRO_0000219030;Note=Nucleolar protein 56	
+Q12460	UniProtKB	Domain	299	417	.	.	.	Note=Nop;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00690	
+Q12460	UniProtKB	Compositional bias	443	504	.	.	.	Note=Asp/Glu/Lys-rich	
+Q12460	UniProtKB	Modified residue	321	321	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12460	UniProtKB	Mutagenesis	333	333	.	.	.	Note=Reduced growth rate at all temperatures%3B when associated with R-385. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372940;Dbxref=PMID:9372940	
+Q12460	UniProtKB	Mutagenesis	355	355	.	.	.	Note=At 37 degrees%2C growth slows after 6 to 8 hours and cell division stops after 20 hours. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372940;Dbxref=PMID:9372940	
+Q12460	UniProtKB	Mutagenesis	385	385	.	.	.	Note=Reduced growth rate at all temperatures%3B when associated with A-333. M->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372940;Dbxref=PMID:9372940	
+##sequence-region Q12408 1 173
+Q12408	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12408	UniProtKB	Propeptide	22	34	.	.	.	ID=PRO_0000019897;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12408	UniProtKB	Chain	35	173	.	.	.	ID=PRO_0000019898;Note=Phosphatidylglycerol/phosphatidylinositol transfer protein	
+##sequence-region Q06287 1 252
+Q06287	UniProtKB	Chain	1	252	.	.	.	ID=PRO_0000158612;Note=Ribosomal RNA small subunit methyltransferase NEP1	
+Q06287	UniProtKB	Region	212	214	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18063569,ECO:0000269|PubMed:21087996;Dbxref=PMID:18063569,PMID:21087996	
+Q06287	UniProtKB	Region	227	232	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18063569,ECO:0000269|PubMed:21087996;Dbxref=PMID:18063569,PMID:21087996	
+Q06287	UniProtKB	Binding site	180	180	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18063569,ECO:0000269|PubMed:21087996;Dbxref=PMID:18063569,PMID:21087996	
+Q06287	UniProtKB	Binding site	207	207	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18063569,ECO:0000269|PubMed:21087996;Dbxref=PMID:18063569,PMID:21087996	
+Q06287	UniProtKB	Site	88	88	.	.	.	Note=Interaction with substrate rRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21087996;Dbxref=PMID:21087996	
+Q06287	UniProtKB	Site	90	90	.	.	.	Note=Stabilizes Arg-88;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:21087996;Dbxref=PMID:21087996	
+Q06287	UniProtKB	Site	129	129	.	.	.	Note=Interaction with substrate rRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21087996;Dbxref=PMID:21087996	
+Q06287	UniProtKB	Site	132	132	.	.	.	Note=Interaction with substrate rRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21087996;Dbxref=PMID:21087996	
+Q06287	UniProtKB	Site	136	136	.	.	.	Note=Interaction with substrate rRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21087996;Dbxref=PMID:21087996	
+Q06287	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Loss of substrate rRNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18208838;Dbxref=PMID:18208838	
+Q06287	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Loss of substrate rRNA binding. No effect on growth. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18063569;Dbxref=PMID:18063569	
+Q06287	UniProtKB	Mutagenesis	90	90	.	.	.	Note=Loses its exclusive nucleolar localization and mislocalizes to the cytoplasm. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20972225;Dbxref=PMID:20972225	
+Q06287	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Loss of substrate rRNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18208838;Dbxref=PMID:18208838	
+Q06287	UniProtKB	Mutagenesis	132	132	.	.	.	Note=Loss of substrate rRNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18208838;Dbxref=PMID:18208838	
+Q06287	UniProtKB	Mutagenesis	136	136	.	.	.	Note=Loss of substrate rRNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18208838;Dbxref=PMID:18208838	
+Q06287	UniProtKB	Mutagenesis	214	214	.	.	.	Note=Almost complete loss of SAM binding. No effect on growth and ribosome biogenesis. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18063569;Dbxref=PMID:18063569	
+Q06287	UniProtKB	Mutagenesis	232	232	.	.	.	Note=Almost complete loss of SAM binding. No effect on growth and ribosome biogenesis. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18063569;Dbxref=PMID:18063569	
+Q06287	UniProtKB	Mutagenesis	237	237	.	.	.	Note=Almost complete loss of SAM binding. No effect on growth and ribosome biogenesis. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18063569;Dbxref=PMID:18063569	
+Q06287	UniProtKB	Sequence conflict	114	114	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06287	UniProtKB	Beta strand	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3J	
+Q06287	UniProtKB	Beta strand	41	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Beta strand	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIN	
+Q06287	UniProtKB	Beta strand	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIN	
+Q06287	UniProtKB	Turn	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Helix	74	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Helix	89	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Helix	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Beta strand	110	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Beta strand	121	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Helix	134	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Beta strand	148	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Beta strand	155	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Helix	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Beta strand	173	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Helix	189	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Beta strand	201	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Beta strand	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Turn	216	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Beta strand	222	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+Q06287	UniProtKB	Helix	234	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII	
+##sequence-region P47035 1 1189
+P47035	UniProtKB	Chain	1	1189	.	.	.	ID=PRO_0000096784;Note=Nucleolar protein NET1	
+P47035	UniProtKB	Compositional bias	192	199	.	.	.	Note=Poly-Thr	
+P47035	UniProtKB	Compositional bias	328	335	.	.	.	Note=Poly-Ser	
+P47035	UniProtKB	Compositional bias	415	418	.	.	.	Note=Poly-Ser	
+P47035	UniProtKB	Compositional bias	982	988	.	.	.	Note=Poly-Ser	
+P47035	UniProtKB	Compositional bias	993	1000	.	.	.	Note=Poly-Ser	
+P47035	UniProtKB	Compositional bias	1171	1174	.	.	.	Note=Poly-Lys	
+P47035	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47035	UniProtKB	Modified residue	166	166	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47035	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47035	UniProtKB	Modified residue	252	252	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47035	UniProtKB	Modified residue	437	437	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47035	UniProtKB	Modified residue	439	439	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47035	UniProtKB	Modified residue	447	447	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47035	UniProtKB	Modified residue	452	452	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47035	UniProtKB	Modified residue	497	497	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47035	UniProtKB	Modified residue	676	676	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P47035	UniProtKB	Modified residue	830	830	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47035	UniProtKB	Modified residue	1042	1042	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47035	UniProtKB	Modified residue	1056	1056	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47035	UniProtKB	Modified residue	1059	1059	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P11632 1 93
+P11632	UniProtKB	Chain	1	93	.	.	.	ID=PRO_0000048565;Note=Non-histone chromosomal protein 6A	
+P11632	UniProtKB	DNA binding	21	89	.	.	.	Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267	
+P11632	UniProtKB	Mutagenesis	18	18	.	.	.	Note=Does not affect affinity for DNA. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494	
+P11632	UniProtKB	Mutagenesis	21	21	.	.	.	Note=Shows a 4-fold reduced affinity for DNA. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494	
+P11632	UniProtKB	Mutagenesis	28	28	.	.	.	Note=Shows a strongly reduced affinity for linear and circular DNA. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494	
+P11632	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Unable to form 75 bp microcircles. M->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494	
+P11632	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Does not affect affinity for DNA. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494	
+P11632	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Shows a strongly reduced affinity for linear and circular DNA. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494	
+P11632	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J5N	
+P11632	UniProtKB	Helix	27	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7	
+P11632	UniProtKB	Turn	38	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7	
+P11632	UniProtKB	Helix	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7	
+P11632	UniProtKB	Turn	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7	
+P11632	UniProtKB	Helix	55	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7	
+P11632	UniProtKB	Helix	63	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7	
+P11632	UniProtKB	Helix	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7	
+P11632	UniProtKB	Helix	83	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7	
+##sequence-region Q07896 1 663
+Q07896	UniProtKB	Chain	1	663	.	.	.	ID=PRO_0000173483;Note=Nucleolar complex-associated protein 3	
+Q07896	UniProtKB	Coiled coil	363	408	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07896	UniProtKB	Modified residue	395	395	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q03790 1 475
+Q03790	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03790	UniProtKB	Chain	2	475	.	.	.	ID=PRO_0000204871;Note=Nucleoporin NUP53	
+Q03790	UniProtKB	Repeat	124	125	.	.	.	Note=FG 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785	
+Q03790	UniProtKB	Domain	247	352	.	.	.	Note=RRM Nup35-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00804	
+Q03790	UniProtKB	Repeat	264	265	.	.	.	Note=FG 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785	
+Q03790	UniProtKB	Repeat	273	274	.	.	.	Note=FG 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785	
+Q03790	UniProtKB	Repeat	470	471	.	.	.	Note=FG 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785	
+Q03790	UniProtKB	Region	405	438	.	.	.	Note=PSE1 binding	
+Q03790	UniProtKB	Region	449	475	.	.	.	Note=Required for nuclear membrane association and proliferation	
+Q03790	UniProtKB	Compositional bias	24	41	.	.	.	Note=Gln-rich	
+Q03790	UniProtKB	Compositional bias	115	147	.	.	.	Note=Asn-rich	
+Q03790	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03790	UniProtKB	Modified residue	101	101	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03790	UniProtKB	Modified residue	297	297	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03790	UniProtKB	Modified residue	438	438	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P46673 1 744
+P46673	UniProtKB	Chain	1	744	.	.	.	ID=PRO_0000204885;Note=Nucleoporin NUP85	
+P46673	UniProtKB	Compositional bias	646	652	.	.	.	Note=Poly-Leu	
+P46673	UniProtKB	Sequence conflict	101	101	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46673	UniProtKB	Sequence conflict	471	471	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46673	UniProtKB	Beta strand	41	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3P	
+P46673	UniProtKB	Beta strand	67	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Beta strand	77	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Beta strand	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	102	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	119	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	135	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	170	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Beta strand	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	201	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	221	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Beta strand	237	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	243	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	258	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Turn	266	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	272	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	279	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	300	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	326	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	343	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	353	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	368	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	371	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Beta strand	388	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	391	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	403	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	406	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	414	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Beta strand	454	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	461	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Turn	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	482	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Beta strand	493	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	497	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	508	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	516	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	532	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P46673	UniProtKB	Helix	545	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+##sequence-region P36023 1 863
+P36023	UniProtKB	Chain	1	863	.	.	.	ID=PRO_0000115002;Note=Oleate activated transcription factor 3	
+P36023	UniProtKB	DNA binding	18	47	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region Q03028 1 310
+Q03028	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000090648;Note=Mitochondrial 2-oxodicarboxylate carrier 1	
+Q03028	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03028	UniProtKB	Transmembrane	78	97	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03028	UniProtKB	Transmembrane	126	146	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03028	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03028	UniProtKB	Transmembrane	219	239	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03028	UniProtKB	Transmembrane	281	301	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03028	UniProtKB	Repeat	9	108	.	.	.	Note=Solcar 1	
+Q03028	UniProtKB	Repeat	120	204	.	.	.	Note=Solcar 2	
+Q03028	UniProtKB	Repeat	213	300	.	.	.	Note=Solcar 3	
+##sequence-region P32473 1 366
+P32473	UniProtKB	Transit peptide	1	33	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8433986;Dbxref=PMID:8433986	
+P32473	UniProtKB	Chain	34	366	.	.	.	ID=PRO_0000020461;Note=Pyruvate dehydrogenase E1 component subunit beta%2C mitochondrial	
+P32473	UniProtKB	Binding site	95	95	.	.	.	Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32473	UniProtKB	Sequence conflict	160	160	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53397 1 376
+P53397	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000058595;Note=N-glycosylase/DNA lyase	
+P53397	UniProtKB	Active site	241	241	.	.	.	Note=Schiff-base intermediate with DNA	
+P53397	UniProtKB	Binding site	134	134	.	.	.	Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53397	UniProtKB	Binding site	139	139	.	.	.	Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53397	UniProtKB	Binding site	189	189	.	.	.	Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53397	UniProtKB	Binding site	258	258	.	.	.	Note=8-oxoguanine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53397	UniProtKB	Binding site	260	260	.	.	.	Note=8-oxoguanine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53397	UniProtKB	Binding site	262	262	.	.	.	Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53397	UniProtKB	Binding site	320	320	.	.	.	Note=8-oxoguanine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53397	UniProtKB	Binding site	324	324	.	.	.	Note=8-oxoguanine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53397	UniProtKB	Mutagenesis	241	241	.	.	.	Note=Abolishes both DNA glycosylase and AP lyase activity. K->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677220,ECO:0000269|PubMed:9241232;Dbxref=PMID:10677220,PMID:9241232	
+P53397	UniProtKB	Mutagenesis	241	241	.	.	.	Note=Diminishes both DNA glycosylase and AP lyase activity. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677220,ECO:0000269|PubMed:9241232;Dbxref=PMID:10677220,PMID:9241232	
+##sequence-region Q08962 1 181
+Q08962	UniProtKB	Chain	1	181	.	.	.	ID=PRO_0000218776;Note=60S ribosome subunit biogenesis protein NIP7	
+Q08962	UniProtKB	Domain	94	170	.	.	.	Note=PUA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00161	
+Q08962	UniProtKB	Mutagenesis	161	164	.	.	.	Note=Reduces RNA-binding ability in vitro. IVAF->AVAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18001138;Dbxref=PMID:18001138	
+##sequence-region Q12493 1 238
+Q12493	UniProtKB	Chain	1	238	.	.	.	ID=PRO_0000096867;Note=Central kinetochore subunit NKP1	
+Q12493	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P14743 1 455
+P14743	UniProtKB	Chain	1	455	.	.	.	ID=PRO_0000064248;Note=Glycylpeptide N-tetradecanoyltransferase	
+P14743	UniProtKB	Region	38	41	.	.	.	Note=Myristoyl CoA-binding	
+P14743	UniProtKB	Region	168	204	.	.	.	Note=Myristoyl CoA-binding	
+P14743	UniProtKB	Active site	455	455	.	.	.	Note=Proton acceptor%3B via carboxylate	
+P14743	UniProtKB	Mutagenesis	99	99	.	.	.	Note=In NMT1-72%3B temperature-sensitive mutant with myristic acid auxotrophy. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8416952;Dbxref=PMID:8416952	
+P14743	UniProtKB	Mutagenesis	169	169	.	.	.	Note=Reduces the chemical transformation rate%3B when associated with A-205. N->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11478885;Dbxref=PMID:11478885	
+P14743	UniProtKB	Mutagenesis	170	170	.	.	.	Note=Reduces the chemical transformation rate%3B when associated with A-171. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11478885;Dbxref=PMID:11478885	
+P14743	UniProtKB	Mutagenesis	171	171	.	.	.	Note=Reduces the chemical transformation rate%3B when associated with A-170. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11478885;Dbxref=PMID:11478885	
+P14743	UniProtKB	Mutagenesis	202	202	.	.	.	Note=Reduces affinity for both substrate and myristoyl-CoA. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8955162;Dbxref=PMID:8955162	
+P14743	UniProtKB	Mutagenesis	205	205	.	.	.	Note=Reduces the chemical transformation rate%3B when associated with L-169. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11478885;Dbxref=PMID:11478885	
+P14743	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Reduces affinity for substrate%2C but not for myristoyl-CoA. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8955162;Dbxref=PMID:8955162	
+P14743	UniProtKB	Mutagenesis	328	328	.	.	.	Note=Moderately reduces affinity for myristoyl-CoA%2C but not for substrate. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8955162;Dbxref=PMID:8955162	
+P14743	UniProtKB	Mutagenesis	404	404	.	.	.	Note=Moderately reduces affinity for substrate%2C but not for myristoyl-CoA. N->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8955162;Dbxref=PMID:8955162	
+P14743	UniProtKB	Mutagenesis	426	426	.	.	.	Note=Reduces affinity for myristoyl-CoA%2C but not for substrate. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8955162;Dbxref=PMID:8955162	
+P14743	UniProtKB	Mutagenesis	451	451	.	.	.	Note=In NMT1-181%3B temperature-sensitive with myristic acid auxotrophy. Reduces affinity for myristoyl-CoA. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2045414;Dbxref=PMID:2045414	
+P14743	UniProtKB	Mutagenesis	454	455	.	.	.	Note=Reduces chemical transformation rate 400-fold. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11478885;Dbxref=PMID:11478885	
+P14743	UniProtKB	Helix	6	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P6E	
+P14743	UniProtKB	Helix	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NMT	
+P14743	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	79	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P6G	
+P14743	UniProtKB	Helix	89	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	117	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	134	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Turn	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	145	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	161	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IID	
+P14743	UniProtKB	Helix	183	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Turn	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	202	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	214	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	226	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IID	
+P14743	UniProtKB	Helix	243	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	266	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	269	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	283	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	291	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P6E	
+P14743	UniProtKB	Helix	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	311	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	323	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	347	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Turn	357	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	367	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	394	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Helix	404	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Turn	407	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	414	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	434	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Beta strand	440	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+P14743	UniProtKB	Turn	444	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC	
+##sequence-region P36003 1 928
+P36003	UniProtKB	Chain	1	928	.	.	.	ID=PRO_0000086152;Note=Nitrogen network kinase 1	
+P36003	UniProtKB	Domain	449	912	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P36003	UniProtKB	Nucleotide binding	455	463	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P36003	UniProtKB	Active site	580	580	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P36003	UniProtKB	Binding site	478	478	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P36003	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36003	UniProtKB	Modified residue	179	179	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36003	UniProtKB	Modified residue	405	405	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36003	UniProtKB	Modified residue	426	426	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36003	UniProtKB	Modified residue	737	737	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P36003	UniProtKB	Modified residue	739	739	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q02892 1 647
+Q02892	UniProtKB	Chain	1	647	.	.	.	ID=PRO_0000195035;Note=Nucleolar GTP-binding protein 1	
+Q02892	UniProtKB	Domain	168	340	.	.	.	Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+Q02892	UniProtKB	Nucleotide binding	174	181	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+Q02892	UniProtKB	Nucleotide binding	220	224	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+Q02892	UniProtKB	Nucleotide binding	288	291	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+Q02892	UniProtKB	Modified residue	563	563	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P06100 1 191
+P06100	UniProtKB	Chain	1	191	.	.	.	ID=PRO_0000198336;Note=General negative regulator of transcription subunit 2	
+P06100	UniProtKB	Beta strand	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Helix	35	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Helix	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Beta strand	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Helix	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Beta strand	88	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Turn	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Helix	101	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Helix	109	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Helix	123	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Beta strand	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Turn	141	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Beta strand	145	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Beta strand	161	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Turn	173	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Beta strand	177	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+P06100	UniProtKB	Helix	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+##sequence-region Q12514 1 560
+Q12514	UniProtKB	Chain	1	560	.	.	.	ID=PRO_0000198338;Note=General negative regulator of transcription subunit 5	
+Q12514	UniProtKB	Coiled coil	3	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12514	UniProtKB	Coiled coil	37	71	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12514	UniProtKB	Coiled coil	124	177	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12514	UniProtKB	Modified residue	306	306	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12514	UniProtKB	Modified residue	377	377	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12514	UniProtKB	Cross-link	338	338	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q12514	UniProtKB	Turn	348	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Helix	353	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Helix	356	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Helix	367	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Helix	378	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Helix	394	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Turn	459	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Helix	464	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Helix	474	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Helix	488	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Beta strand	504	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Turn	507	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Beta strand	512	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Beta strand	532	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Turn	537	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Beta strand	542	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+Q12514	UniProtKB	Helix	554	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6	
+##sequence-region P38742 1 1146
+P38742	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38742	UniProtKB	Chain	26	1146	.	.	.	ID=PRO_0000202882;Note=Nitrogen permease regulator 3	
+P38742	UniProtKB	Compositional bias	149	315	.	.	.	Note=Ser-rich	
+P38742	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P38742	UniProtKB	Modified residue	486	486	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38742	UniProtKB	Modified residue	987	987	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q03718 1 556
+Q03718	UniProtKB	Chain	1	556	.	.	.	ID=PRO_0000057963;Note=Non-structural maintenance of chromosome element 5	
+##sequence-region P32499 1 720
+P32499	UniProtKB	Chain	1	720	.	.	.	ID=PRO_0000204903;Note=Nucleoporin NUP2	
+P32499	UniProtKB	Repeat	67	69	.	.	.	Note=FXF 1	
+P32499	UniProtKB	Repeat	189	192	.	.	.	Note=FXFG 1	
+P32499	UniProtKB	Repeat	216	218	.	.	.	Note=FXF 2	
+P32499	UniProtKB	Repeat	247	249	.	.	.	Note=FXF 3	
+P32499	UniProtKB	Repeat	285	288	.	.	.	Note=FXFG 2	
+P32499	UniProtKB	Repeat	302	305	.	.	.	Note=FXFG 3	
+P32499	UniProtKB	Repeat	318	321	.	.	.	Note=FXFG 4	
+P32499	UniProtKB	Repeat	352	354	.	.	.	Note=FXF 4	
+P32499	UniProtKB	Repeat	369	372	.	.	.	Note=FXFG 5	
+P32499	UniProtKB	Repeat	386	389	.	.	.	Note=FXFG 6	
+P32499	UniProtKB	Repeat	438	441	.	.	.	Note=FXFG 7	
+P32499	UniProtKB	Repeat	474	477	.	.	.	Note=FXFG 8	
+P32499	UniProtKB	Repeat	493	496	.	.	.	Note=FXFG 9	
+P32499	UniProtKB	Repeat	511	514	.	.	.	Note=FXFG 10	
+P32499	UniProtKB	Repeat	524	527	.	.	.	Note=FXFG 11	
+P32499	UniProtKB	Repeat	550	552	.	.	.	Note=FXF 5	
+P32499	UniProtKB	Domain	583	720	.	.	.	Note=RanBD1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00164	
+P32499	UniProtKB	Region	35	50	.	.	.	Note=Interaction with SRP1 NLS binding site 1	
+P32499	UniProtKB	Compositional bias	333	377	.	.	.	Note=Ser-rich	
+P32499	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P32499	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P32499	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32499	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32499	UniProtKB	Modified residue	203	203	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P32499	UniProtKB	Modified residue	205	205	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P32499	UniProtKB	Modified residue	348	348	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32499	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32499	UniProtKB	Modified residue	361	361	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32499	UniProtKB	Modified residue	581	581	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32499	UniProtKB	Modified residue	590	590	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32499	UniProtKB	Sequence conflict	137	137	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32499	UniProtKB	Sequence conflict	370	370	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32499	UniProtKB	Sequence conflict	418	418	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32499	UniProtKB	Turn	12	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C1T	
+P32499	UniProtKB	Helix	34	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C1T	
+P32499	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UN0	
+##sequence-region P49686 1 430
+P49686	UniProtKB	Chain	1	430	.	.	.	ID=PRO_0000204866;Note=Nucleoporin NUP42	
+P49686	UniProtKB	Repeat	2	5	.	.	.	Note=SXFG 1	
+P49686	UniProtKB	Repeat	38	46	.	.	.	Note=SAFGXPXFG 1	
+P49686	UniProtKB	Repeat	58	66	.	.	.	Note=SAFGXPXFG 2	
+P49686	UniProtKB	Repeat	78	81	.	.	.	Note=SXFG 2	
+P49686	UniProtKB	Repeat	90	98	.	.	.	Note=SAFGXPXFG 3	
+P49686	UniProtKB	Repeat	112	120	.	.	.	Note=SAFGXPXFG 4	
+P49686	UniProtKB	Repeat	124	125	.	.	.	Note=FG 1	
+P49686	UniProtKB	Repeat	134	135	.	.	.	Note=FG 2	
+P49686	UniProtKB	Repeat	143	151	.	.	.	Note=SAFGXPXFG 5	
+P49686	UniProtKB	Repeat	168	171	.	.	.	Note=SXFG 3	
+P49686	UniProtKB	Repeat	182	185	.	.	.	Note=SXFG 4	
+P49686	UniProtKB	Repeat	200	208	.	.	.	Note=SAFGXPXFG 6	
+P49686	UniProtKB	Repeat	215	218	.	.	.	Note=SXFG 5	
+P49686	UniProtKB	Repeat	232	235	.	.	.	Note=SXFG 6	
+P49686	UniProtKB	Repeat	259	262	.	.	.	Note=SXFG 7	
+P49686	UniProtKB	Repeat	277	280	.	.	.	Note=SXFG 8	
+P49686	UniProtKB	Repeat	296	297	.	.	.	Note=FG 3	
+P49686	UniProtKB	Repeat	312	315	.	.	.	Note=SXFG 9	
+P49686	UniProtKB	Repeat	319	322	.	.	.	Note=FG 4	
+P49686	UniProtKB	Repeat	339	340	.	.	.	Note=FG 5	
+P49686	UniProtKB	Repeat	361	364	.	.	.	Note=FG 6	
+P49686	UniProtKB	Region	121	230	.	.	.	Note=Interactions with CRM1 and GFD1	
+P49686	UniProtKB	Region	365	430	.	.	.	Note=Interaction with GLE1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10610322;Dbxref=PMID:10610322	
+P49686	UniProtKB	Compositional bias	269	273	.	.	.	Note=Poly-Asn	
+P49686	UniProtKB	Compositional bias	423	426	.	.	.	Note=Poly-Pro	
+P49686	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P49686	UniProtKB	Modified residue	298	298	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P49686	UniProtKB	Sequence conflict	331	331	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P49686	UniProtKB	Sequence conflict	419	419	.	.	.	Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P48837 1 541
+P48837	UniProtKB	Chain	1	541	.	.	.	ID=PRO_0000204877;Note=Nucleoporin NUP57	
+P48837	UniProtKB	Repeat	2	3	.	.	.	Note=FG 1	
+P48837	UniProtKB	Repeat	11	12	.	.	.	Note=FG 2	
+P48837	UniProtKB	Repeat	21	24	.	.	.	Note=FXFG 1	
+P48837	UniProtKB	Repeat	39	42	.	.	.	Note=FXFG 2	
+P48837	UniProtKB	Repeat	56	57	.	.	.	Note=FG 3	
+P48837	UniProtKB	Repeat	65	66	.	.	.	Note=FG 4	
+P48837	UniProtKB	Repeat	76	79	.	.	.	Note=GLFG 1	
+P48837	UniProtKB	Repeat	103	106	.	.	.	Note=GLFG 2	
+P48837	UniProtKB	Repeat	120	123	.	.	.	Note=GLFG 3	
+P48837	UniProtKB	Repeat	132	135	.	.	.	Note=GLFG 4	
+P48837	UniProtKB	Repeat	147	150	.	.	.	Note=GLFG 5	
+P48837	UniProtKB	Repeat	175	178	.	.	.	Note=GLFG 6	
+P48837	UniProtKB	Repeat	190	193	.	.	.	Note=GLFG 7	
+P48837	UniProtKB	Repeat	204	207	.	.	.	Note=GLFG 8	
+P48837	UniProtKB	Repeat	220	223	.	.	.	Note=GLFG 9	
+P48837	UniProtKB	Coiled coil	398	425	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48837	UniProtKB	Compositional bias	3	223	.	.	.	Note=Gly-rich	
+P48837	UniProtKB	Compositional bias	26	31	.	.	.	Note=Poly-Asn	
+P48837	UniProtKB	Compositional bias	127	130	.	.	.	Note=Poly-Thr	
+P48837	UniProtKB	Compositional bias	217	220	.	.	.	Note=Poly-Gly	
+P48837	UniProtKB	Compositional bias	224	291	.	.	.	Note=Gln-rich	
+P48837	UniProtKB	Compositional bias	258	266	.	.	.	Note=Poly-Gln	
+P48837	UniProtKB	Compositional bias	277	280	.	.	.	Note=Poly-Gln	
+##sequence-region Q05166 1 528
+Q05166	UniProtKB	Chain	1	528	.	.	.	ID=PRO_0000204878;Note=Nucleoporin ASM4	
+Q05166	UniProtKB	Repeat	2	3	.	.	.	Note=FG 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785	
+Q05166	UniProtKB	Repeat	61	62	.	.	.	Note=FG 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785	
+Q05166	UniProtKB	Repeat	195	196	.	.	.	Note=FG 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785	
+Q05166	UniProtKB	Domain	265	394	.	.	.	Note=RRM Nup35-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00804	
+Q05166	UniProtKB	Repeat	274	275	.	.	.	Note=FG 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785	
+Q05166	UniProtKB	Repeat	291	292	.	.	.	Note=FG 5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785	
+Q05166	UniProtKB	Repeat	523	524	.	.	.	Note=FG 6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785	
+Q05166	UniProtKB	Coiled coil	490	510	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05166	UniProtKB	Compositional bias	19	49	.	.	.	Note=Gln-rich	
+Q05166	UniProtKB	Compositional bias	28	46	.	.	.	Note=Poly-Gln	
+Q05166	UniProtKB	Compositional bias	63	178	.	.	.	Note=Asn-rich	
+Q05166	UniProtKB	Compositional bias	84	87	.	.	.	Note=Poly-Asn	
+Q05166	UniProtKB	Modified residue	458	458	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05166	UniProtKB	Modified residue	464	464	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05166	UniProtKB	Sequence conflict	114	114	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q05166	UniProtKB	Sequence conflict	171	171	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q05166	UniProtKB	Sequence conflict	446	528	.	.	.	Note=PAGHAGNPTNISSPIVANSPNKRLDVIDGKLPFMQNAGPNSNIPNLLRNLESKMRQQEAKYRNNEPAGFTHKLSNWLFGWNDL->LPVMLVIQQIFQVQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12066 1 484
+Q12066	UniProtKB	Chain	1	484	.	.	.	ID=PRO_0000202586;Note=Nuclear rim protein 1	
+Q12066	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12066	UniProtKB	Transmembrane	252	272	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12066	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12066	UniProtKB	Modified residue	417	417	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12066	UniProtKB	Modified residue	474	474	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32332 1 324
+P32332	UniProtKB	Chain	1	324	.	.	.	ID=PRO_0000090689;Note=Mitochondrial oxaloacetate transport protein	
+P32332	UniProtKB	Transmembrane	26	46	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32332	UniProtKB	Transmembrane	79	99	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32332	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32332	UniProtKB	Transmembrane	193	213	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32332	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32332	UniProtKB	Transmembrane	284	305	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32332	UniProtKB	Repeat	20	111	.	.	.	Note=Solcar 1	
+P32332	UniProtKB	Repeat	126	218	.	.	.	Note=Solcar 2	
+P32332	UniProtKB	Repeat	227	312	.	.	.	Note=Solcar 3	
+##sequence-region P39720 1 1047
+P39720	UniProtKB	Chain	1	1047	.	.	.	ID=PRO_0000114990;Note=Oleate-activated transcription factor 1	
+P39720	UniProtKB	DNA binding	66	93	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P39720	UniProtKB	Motif	1034	1042	.	.	.	Note=9aaTAD	
+P39720	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39720	UniProtKB	Sequence conflict	70	70	.	.	.	Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39720	UniProtKB	Sequence conflict	447	447	.	.	.	Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39720	UniProtKB	Sequence conflict	588	588	.	.	.	Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53949 1 197
+P53949	UniProtKB	Chain	1	197	.	.	.	ID=PRO_0000203451;Note=Tyrosine-protein phosphatase-like protein OCA2	
+P53949	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53949	UniProtKB	Sequence conflict	11	11	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07913 1 336
+Q07913	UniProtKB	Chain	1	336	.	.	.	ID=PRO_0000114116;Note=Non-structural maintenance of chromosomes element 1	
+Q07913	UniProtKB	Zinc finger	268	327	.	.	.	Note=NSE1-type	
+##sequence-region P38837 1 291
+P38837	UniProtKB	Chain	1	291	.	.	.	ID=PRO_0000202918;Note=Protein NSG1	
+P38837	UniProtKB	Topological domain	1	96	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38837	UniProtKB	Transmembrane	97	117	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38837	UniProtKB	Topological domain	118	156	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38837	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38837	UniProtKB	Topological domain	178	230	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38837	UniProtKB	Transmembrane	231	251	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38837	UniProtKB	Topological domain	252	261	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38837	UniProtKB	Transmembrane	262	282	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38837	UniProtKB	Topological domain	283	291	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38837	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P38837	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38837	UniProtKB	Sequence conflict	8	8	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12143 1 216
+Q12143	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12143	UniProtKB	Chain	2	216	.	.	.	ID=PRO_0000057965;Note=Kinetochore-associated protein NSL1	
+Q12143	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12143	UniProtKB	Sequence conflict	212	212	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P14907 1 823
+P14907	UniProtKB	Chain	1	823	.	.	.	ID=PRO_0000204865;Note=Nucleoporin NSP1	
+P14907	UniProtKB	Repeat	13	16	.	.	.	Note=FSFG 1	
+P14907	UniProtKB	Repeat	36	37	.	.	.	Note=FG 1	
+P14907	UniProtKB	Repeat	43	44	.	.	.	Note=FG 2	
+P14907	UniProtKB	Repeat	64	65	.	.	.	Note=FG 3	
+P14907	UniProtKB	Repeat	74	75	.	.	.	Note=FG 4	
+P14907	UniProtKB	Repeat	84	85	.	.	.	Note=FG 5	
+P14907	UniProtKB	Repeat	94	95	.	.	.	Note=FG 6	
+P14907	UniProtKB	Repeat	104	105	.	.	.	Note=FG 7	
+P14907	UniProtKB	Repeat	123	124	.	.	.	Note=FG 8	
+P14907	UniProtKB	Repeat	142	143	.	.	.	Note=FG 9	
+P14907	UniProtKB	Repeat	147	148	.	.	.	Note=FG 10	
+P14907	UniProtKB	Repeat	168	169	.	.	.	Note=FG 11	
+P14907	UniProtKB	Repeat	179	182	.	.	.	Note=FSFG 2	
+P14907	UniProtKB	Repeat	217	220	.	.	.	Note=FSFG 3	
+P14907	UniProtKB	Repeat	239	240	.	.	.	Note=FG 12	
+P14907	UniProtKB	Repeat	268	269	.	.	.	Note=FG 13	
+P14907	UniProtKB	Repeat	284	287	.	.	.	Note=FSFG 4	
+P14907	UniProtKB	Repeat	303	306	.	.	.	Note=FSFG 5	
+P14907	UniProtKB	Repeat	322	325	.	.	.	Note=FSFG 6	
+P14907	UniProtKB	Repeat	341	344	.	.	.	Note=FSFG 7	
+P14907	UniProtKB	Repeat	360	363	.	.	.	Note=FSFG 8	
+P14907	UniProtKB	Repeat	379	382	.	.	.	Note=FSFG 9	
+P14907	UniProtKB	Repeat	398	401	.	.	.	Note=FSFG 10	
+P14907	UniProtKB	Repeat	417	420	.	.	.	Note=FSFG 11	
+P14907	UniProtKB	Repeat	436	439	.	.	.	Note=FSFG 12	
+P14907	UniProtKB	Repeat	455	458	.	.	.	Note=FSFG 13	
+P14907	UniProtKB	Repeat	474	477	.	.	.	Note=FSFG 14	
+P14907	UniProtKB	Repeat	493	496	.	.	.	Note=FSFG 15	
+P14907	UniProtKB	Repeat	512	515	.	.	.	Note=FSFG 16	
+P14907	UniProtKB	Repeat	531	534	.	.	.	Note=FSFG 17	
+P14907	UniProtKB	Repeat	550	553	.	.	.	Note=FSFG 18	
+P14907	UniProtKB	Repeat	571	572	.	.	.	Note=FG 14	
+P14907	UniProtKB	Repeat	588	591	.	.	.	Note=FSFG 19%3B approximate	
+P14907	UniProtKB	Region	673	738	.	.	.	Note=Competitive binding site of NUP57 and NUP82	
+P14907	UniProtKB	Region	740	823	.	.	.	Note=Required for association with NUP57 subcomplex	
+P14907	UniProtKB	Coiled coil	630	823	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14907	UniProtKB	Compositional bias	2	175	.	.	.	Note=Asn-rich	
+P14907	UniProtKB	Compositional bias	308	628	.	.	.	Note=Lys-rich	
+P14907	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14907	UniProtKB	Modified residue	361	361	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14907	UniProtKB	Modified residue	456	456	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14907	UniProtKB	Modified residue	631	631	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P35729 1 1037
+P35729	UniProtKB	Chain	1	1037	.	.	.	ID=PRO_0000204836;Note=Nucleoporin NUP120	
+P35729	UniProtKB	Region	131	152	.	.	.	Note=Leucine-zipper 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35729	UniProtKB	Region	290	311	.	.	.	Note=Leucine-zipper 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35729	UniProtKB	Modified residue	417	417	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P35729	UniProtKB	Beta strand	2	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	11	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	16	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	55	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR	
+P35729	UniProtKB	Beta strand	67	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	78	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	92	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H7N	
+P35729	UniProtKB	Helix	104	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	108	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	114	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	128	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	135	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	158	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	163	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	170	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR	
+P35729	UniProtKB	Beta strand	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR	
+P35729	UniProtKB	Beta strand	187	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	203	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	216	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H7N	
+P35729	UniProtKB	Beta strand	223	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	233	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	242	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	248	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	252	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	259	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	280	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	293	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	297	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H7N	
+P35729	UniProtKB	Beta strand	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	318	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	330	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR	
+P35729	UniProtKB	Beta strand	348	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	360	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	370	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	375	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	383	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR	
+P35729	UniProtKB	Helix	386	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	406	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	417	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	429	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	440	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	460	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	467	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	470	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	480	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	489	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	495	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	505	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	522	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	538	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	542	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H7N	
+P35729	UniProtKB	Helix	546	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	558	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	564	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	579	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	589	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	609	639	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Turn	644	647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	648	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	672	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	681	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Beta strand	685	688	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR	
+P35729	UniProtKB	Helix	695	711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+P35729	UniProtKB	Helix	719	728	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F	
+##sequence-region P40064 1 1391
+P40064	UniProtKB	Chain	1	1391	.	.	.	ID=PRO_0000204848;Note=Nucleoporin NUP157	
+P40064	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40064	UniProtKB	Modified residue	1034	1034	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40064	UniProtKB	Helix	90	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	122	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	138	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	161	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	167	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	171	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	179	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	191	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	201	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	214	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	218	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	244	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	260	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	267	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	271	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	284	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	303	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	341	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	349	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	353	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	363	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	372	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	381	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	401	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	406	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	418	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	431	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	447	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	483	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	500	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	503	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	506	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	536	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	545	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	555	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	567	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	581	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	584	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	589	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	593	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	600	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	617	623	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	624	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	629	635	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	637	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	655	667	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	670	672	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	707	719	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Turn	720	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	726	729	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Beta strand	745	747	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	749	768	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	770	772	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	787	815	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	816	818	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	819	829	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	838	845	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	849	853	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	857	872	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+P40064	UniProtKB	Helix	879	890	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC	
+##sequence-region P40477 1 1460
+P40477	UniProtKB	Chain	1	1460	.	.	.	ID=PRO_0000204849;Note=Nucleoporin NUP159	
+P40477	UniProtKB	Repeat	228	231	.	.	.	Note=FG 1	
+P40477	UniProtKB	Repeat	267	270	.	.	.	Note=PXFG 1	
+P40477	UniProtKB	Repeat	462	470	.	.	.	Note=SXFGXPXFG 1	
+P40477	UniProtKB	Repeat	503	511	.	.	.	Note=SXFGXPXFG 2%3B approximate	
+P40477	UniProtKB	Repeat	522	530	.	.	.	Note=SXFGXPXFG 3%3B approximate	
+P40477	UniProtKB	Repeat	532	535	.	.	.	Note=PXFG 2	
+P40477	UniProtKB	Repeat	548	556	.	.	.	Note=SXFGXPXFG 4	
+P40477	UniProtKB	Repeat	558	561	.	.	.	Note=PXFG 3	
+P40477	UniProtKB	Repeat	574	582	.	.	.	Note=SXFGXPXFG 5	
+P40477	UniProtKB	Repeat	584	587	.	.	.	Note=PXFG 4	
+P40477	UniProtKB	Repeat	600	608	.	.	.	Note=SXFGXPXFG 6	
+P40477	UniProtKB	Repeat	610	613	.	.	.	Note=SXFG 1	
+P40477	UniProtKB	Repeat	624	632	.	.	.	Note=SXFGXPXFG 7%3B approximate	
+P40477	UniProtKB	Repeat	642	645	.	.	.	Note=FG 2	
+P40477	UniProtKB	Repeat	687	690	.	.	.	Note=FG 3	
+P40477	UniProtKB	Repeat	704	707	.	.	.	Note=FXFG 1	
+P40477	UniProtKB	Repeat	709	712	.	.	.	Note=SXFG 2	
+P40477	UniProtKB	Repeat	728	731	.	.	.	Note=FXFG 2	
+P40477	UniProtKB	Repeat	842	845	.	.	.	Note=PXFG 5	
+P40477	UniProtKB	Repeat	873	876	.	.	.	Note=FXFG 3	
+P40477	UniProtKB	Region	1	500	.	.	.	Note=Interaction with DBP5	
+P40477	UniProtKB	Region	497	701	.	.	.	Note=Interactions with CRM1 and GLE1	
+P40477	UniProtKB	Region	1223	1460	.	.	.	Note=Interaction with NUP82;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9736720;Dbxref=PMID:9736720	
+P40477	UniProtKB	Coiled coil	1279	1320	.	.	.	.	
+P40477	UniProtKB	Coiled coil	1383	1418	.	.	.	.	
+P40477	UniProtKB	Compositional bias	455	766	.	.	.	Note=Ser-rich	
+P40477	UniProtKB	Modified residue	404	404	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40477	UniProtKB	Modified residue	657	657	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40477	UniProtKB	Modified residue	724	724	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40477	UniProtKB	Modified residue	735	735	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40477	UniProtKB	Modified residue	745	745	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40477	UniProtKB	Modified residue	803	803	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40477	UniProtKB	Modified residue	805	805	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40477	UniProtKB	Modified residue	819	819	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40477	UniProtKB	Modified residue	889	889	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40477	UniProtKB	Modified residue	940	940	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40477	UniProtKB	Beta strand	10	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	17	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Turn	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	50	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	58	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Helix	64	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	81	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	89	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	98	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	118	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	128	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	135	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	145	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Turn	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	157	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	171	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	183	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	192	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Helix	203	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Turn	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	213	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	245	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	256	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	278	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	292	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	309	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Helix	318	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Turn	328	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	336	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	364	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	372	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP	
+P40477	UniProtKB	Beta strand	1118	1123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1	
+P40477	UniProtKB	Helix	1436	1454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+##sequence-region P08466 1 329
+P08466	UniProtKB	Chain	1	329	.	.	.	ID=PRO_0000178670;Note=Mitochondrial nuclease	
+P08466	UniProtKB	Active site	138	138	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10047	
+P08466	UniProtKB	Metal binding	170	170	.	.	.	Note=Magnesium or manganese%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P40010 1 520
+P40010	UniProtKB	Chain	1	520	.	.	.	ID=PRO_0000122452;Note=Nuclear GTP-binding protein NUG1	
+P40010	UniProtKB	Domain	165	343	.	.	.	Note=CP-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01058	
+P40010	UniProtKB	Nucleotide binding	213	216	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40010	UniProtKB	Nucleotide binding	287	294	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40010	UniProtKB	Nucleotide binding	336	339	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40010	UniProtKB	Modified residue	337	337	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q00402 1 2748
+Q00402	UniProtKB	Chain	1	2748	.	.	.	ID=PRO_0000057997;Note=Nuclear migration protein NUM1	
+Q00402	UniProtKB	Repeat	593	656	.	.	.	Note=1	
+Q00402	UniProtKB	Repeat	657	727	.	.	.	Note=2	
+Q00402	UniProtKB	Repeat	728	798	.	.	.	Note=3	
+Q00402	UniProtKB	Repeat	799	862	.	.	.	Note=4	
+Q00402	UniProtKB	Repeat	863	926	.	.	.	Note=5	
+Q00402	UniProtKB	Repeat	927	990	.	.	.	Note=6	
+Q00402	UniProtKB	Repeat	991	1054	.	.	.	Note=7	
+Q00402	UniProtKB	Repeat	1055	1118	.	.	.	Note=8	
+Q00402	UniProtKB	Repeat	1119	1182	.	.	.	Note=9	
+Q00402	UniProtKB	Repeat	1183	1246	.	.	.	Note=10	
+Q00402	UniProtKB	Repeat	1247	1310	.	.	.	Note=11	
+Q00402	UniProtKB	Repeat	1311	1374	.	.	.	Note=12	
+Q00402	UniProtKB	Repeat	1375	1384	.	.	.	Note=13%3B truncated	
+Q00402	UniProtKB	Domain	2573	2683	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+Q00402	UniProtKB	Region	593	1384	.	.	.	Note=13 X tandem repeats	
+Q00402	UniProtKB	Modified residue	611	611	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q00402	UniProtKB	Modified residue	675	675	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q00402	UniProtKB	Modified residue	746	746	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q00402	UniProtKB	Modified residue	881	881	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q00402	UniProtKB	Modified residue	945	945	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q00402	UniProtKB	Modified residue	1009	1009	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q00402	UniProtKB	Modified residue	1201	1201	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q00402	UniProtKB	Modified residue	1265	1265	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q00402	UniProtKB	Modified residue	1329	1329	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q00402	UniProtKB	Modified residue	2162	2162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00402	UniProtKB	Modified residue	2164	2164	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00402	UniProtKB	Modified residue	2197	2197	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q00402	UniProtKB	Modified residue	2217	2217	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00402	UniProtKB	Modified residue	2220	2220	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q00402	UniProtKB	Modified residue	2221	2221	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q00402	UniProtKB	Modified residue	2360	2360	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00402	UniProtKB	Modified residue	2424	2424	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00402	UniProtKB	Modified residue	2494	2494	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00402	UniProtKB	Modified residue	2545	2545	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00402	UniProtKB	Sequence conflict	1570	1570	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00402	UniProtKB	Sequence conflict	1822	1822	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00402	UniProtKB	Sequence conflict	1960	1962	.	.	.	Note=KAS->RHL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00402	UniProtKB	Sequence conflict	1971	1972	.	.	.	Note=KD->RN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00402	UniProtKB	Sequence conflict	2049	2049	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00402	UniProtKB	Sequence conflict	2637	2637	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39705 1 539
+P39705	UniProtKB	Chain	1	539	.	.	.	ID=PRO_0000204879;Note=Nucleoporin NUP60	
+P39705	UniProtKB	Repeat	399	401	.	.	.	Note=FXF 1	
+P39705	UniProtKB	Repeat	427	429	.	.	.	Note=FXF 2	
+P39705	UniProtKB	Repeat	469	471	.	.	.	Note=FXF 3	
+P39705	UniProtKB	Repeat	509	511	.	.	.	Note=FXF 4	
+P39705	UniProtKB	Coiled coil	91	118	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39705	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P39705	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39705	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39705	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39705	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39705	UniProtKB	Modified residue	171	171	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39705	UniProtKB	Modified residue	214	214	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39705	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39705	UniProtKB	Modified residue	352	352	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39705	UniProtKB	Modified residue	360	360	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39705	UniProtKB	Modified residue	374	374	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39705	UniProtKB	Modified residue	382	382	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39705	UniProtKB	Modified residue	460	460	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39705	UniProtKB	Modified residue	480	480	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39705	UniProtKB	Modified residue	483	483	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P40368 1 713
+P40368	UniProtKB	Chain	1	713	.	.	.	ID=PRO_0000204883;Note=Nucleoporin NUP82	
+P40368	UniProtKB	Region	1	409	.	.	.	Note=Interaction with NUP116;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891509;Dbxref=PMID:10891509	
+P40368	UniProtKB	Region	463	713	.	.	.	Note=Interaction with NSP1 and NUP159;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9843582;Dbxref=PMID:9843582	
+P40368	UniProtKB	Coiled coil	582	713	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40368	UniProtKB	Motif	607	623	.	.	.	Note=Bipartite nuclear localization signal	
+P40368	UniProtKB	Beta strand	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TKN	
+P40368	UniProtKB	Turn	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TKN	
+P40368	UniProtKB	Beta strand	24	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Turn	30	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	34	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	42	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Turn	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	55	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Turn	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	70	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	85	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Helix	103	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	110	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Helix	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	119	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TKN	
+P40368	UniProtKB	Beta strand	127	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Helix	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	141	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	151	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	164	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	171	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	182	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	194	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	204	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	214	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Helix	220	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Helix	243	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Turn	265	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	269	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Helix	274	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	286	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Helix	293	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	299	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	308	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	313	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Turn	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	323	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	347	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	372	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	378	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Helix	387	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Helix	403	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	413	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	425	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	434	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+P40368	UniProtKB	Beta strand	445	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP	
+##sequence-region P38881 1 321
+P38881	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38881	UniProtKB	Chain	23	321	.	.	.	ID=PRO_0000202937;Note=Nucleus-vacuole junction protein 1	
+P38881	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38881	UniProtKB	Region	73	125	.	.	.	Note=TSC13-binding	
+P38881	UniProtKB	Region	139	195	.	.	.	Note=OSH1-binding	
+P38881	UniProtKB	Region	233	321	.	.	.	Note=VAC8-binding	
+P38881	UniProtKB	Compositional bias	235	303	.	.	.	Note=Ser-rich	
+P38881	UniProtKB	Modified residue	156	156	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P38881	UniProtKB	Modified residue	199	199	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38881	UniProtKB	Modified residue	285	285	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38881	UniProtKB	Modified residue	298	298	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40354 1 457
+P40354	UniProtKB	Chain	1	457	.	.	.	ID=PRO_0000204068;Note=Protein N-terminal amidase	
+P40354	UniProtKB	Domain	19	453	.	.	.	Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P40354	UniProtKB	Active site	63	63	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P40354	UniProtKB	Active site	136	136	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+P40354	UniProtKB	Active site	187	187	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054	
+##sequence-region P38302 1 140
+P38302	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000057974;Note=Pre-mRNA-splicing factor NTC20	
+P38302	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P31378 1 399
+P31378	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183	
+P31378	UniProtKB	Chain	27	399	.	.	.	ID=PRO_0000001744;Note=Endonuclease III homolog 1	
+P31378	UniProtKB	Domain	223	247	.	.	.	Note=HhH;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183	
+P31378	UniProtKB	Motif	14	37	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31378	UniProtKB	Active site	243	243	.	.	.	Note=Nucleophile%3B for N-glycosylase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183	
+P31378	UniProtKB	Site	262	262	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183	
+P31378	UniProtKB	Cross-link	194	194	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31378	UniProtKB	Mutagenesis	3	6	.	.	.	Note=In NTG1(mts)%3B reduces mitochondrial localization by 40%25. KISK->EISE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20194111;Dbxref=PMID:20194111	
+P31378	UniProtKB	Mutagenesis	15	16	.	.	.	Note=In NTG1(nls1)%3B reduces nuclear localization by 60%25. KR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20194111;Dbxref=PMID:20194111	
+P31378	UniProtKB	Mutagenesis	33	34	.	.	.	Note=In NTG1(nls2)%3B reduces nuclear localization by 60%25. KR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20194111;Dbxref=PMID:20194111	
+P31378	UniProtKB	Mutagenesis	243	243	.	.	.	Note=Abolishes cleavage of substrate oligonucleotides. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20194111;Dbxref=PMID:20194111	
+P31378	UniProtKB	Mutagenesis	364	364	.	.	.	Note=Cannot properly relocalize in response to oxidative stress. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19029246;Dbxref=PMID:19029246	
+##sequence-region P49687 1 1317
+P49687	UniProtKB	Chain	1	605	.	.	.	ID=PRO_0000019927;Note=Nucleoporin NUP145N	
+P49687	UniProtKB	Chain	606	1317	.	.	.	ID=PRO_0000019928;Note=Nucleoporin NUP145C	
+P49687	UniProtKB	Repeat	12	13	.	.	.	Note=FG 1	
+P49687	UniProtKB	Repeat	39	42	.	.	.	Note=GLFG 1	
+P49687	UniProtKB	Repeat	79	80	.	.	.	Note=FG 2	
+P49687	UniProtKB	Repeat	89	92	.	.	.	Note=GLFG 2	
+P49687	UniProtKB	Repeat	106	107	.	.	.	Note=FG 3	
+P49687	UniProtKB	Repeat	136	139	.	.	.	Note=GLFG 3	
+P49687	UniProtKB	Repeat	154	157	.	.	.	Note=GLFG 4	
+P49687	UniProtKB	Repeat	168	171	.	.	.	Note=GLFG 5	
+P49687	UniProtKB	Repeat	181	184	.	.	.	Note=GLFG 6	
+P49687	UniProtKB	Repeat	193	196	.	.	.	Note=GLFG 7%3B approximate	
+P49687	UniProtKB	Repeat	206	209	.	.	.	Note=GLFG 8	
+P49687	UniProtKB	Domain	458	605	.	.	.	Note=Peptidase S59;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00765	
+P49687	UniProtKB	Region	398	523	.	.	.	Note=Required for autocatalytic cleavage	
+P49687	UniProtKB	Region	460	604	.	.	.	Note=Nucleoporin RNA-binding motif (NRM)	
+P49687	UniProtKB	Motif	369	385	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P49687	UniProtKB	Compositional bias	43	145	.	.	.	Note=Asn-rich	
+P49687	UniProtKB	Compositional bias	140	145	.	.	.	Note=Poly-Asn	
+P49687	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P49687	UniProtKB	Modified residue	403	403	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P49687	UniProtKB	Modified residue	404	404	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P49687	UniProtKB	Modified residue	414	414	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P49687	UniProtKB	Modified residue	667	667	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P49687	UniProtKB	Modified residue	679	679	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P49687	UniProtKB	Modified residue	689	689	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P49687	UniProtKB	Modified residue	751	751	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P49687	UniProtKB	Mutagenesis	604	604	.	.	.	Note=Loss of autocatalytic cleavage%3B when associated with L-608. H->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9305650;Dbxref=PMID:9305650	
+P49687	UniProtKB	Mutagenesis	605	605	.	.	.	Note=Loss of autocatalytic cleavage%3B when associated with R-608. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9305650;Dbxref=PMID:9305650	
+P49687	UniProtKB	Mutagenesis	606	606	.	.	.	Note=Loss of autocatalytic cleavage. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10542288;Dbxref=PMID:10542288	
+P49687	UniProtKB	Mutagenesis	608	608	.	.	.	Note=Loss of autocatalytic cleavage%3B when associated with P-604. W->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9305650;Dbxref=PMID:9305650	
+P49687	UniProtKB	Mutagenesis	608	608	.	.	.	Note=Loss of autocatalytic cleavage%3B when associated with F-605. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9305650;Dbxref=PMID:9305650	
+P49687	UniProtKB	Sequence conflict	281	282	.	.	.	Note=NA->QR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P49687	UniProtKB	Sequence conflict	1142	1142	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P49687	UniProtKB	Sequence conflict	1310	1316	.	.	.	Note=LMKCTYK->FEVYI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P49687	UniProtKB	Helix	454	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KES	
+P49687	UniProtKB	Beta strand	461	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Helix	467	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Helix	477	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Beta strand	480	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Beta strand	485	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Turn	489	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Beta strand	492	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Helix	503	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Helix	509	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Turn	515	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Beta strand	518	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Turn	522	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Beta strand	525	528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Turn	532	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Beta strand	546	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Turn	558	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Helix	570	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Beta strand	584	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Turn	593	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Beta strand	597	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP	
+P49687	UniProtKB	Turn	731	733	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P49687	UniProtKB	Helix	738	746	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Turn	747	749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Beta strand	757	759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P49687	UniProtKB	Turn	761	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG0	
+P49687	UniProtKB	Beta strand	765	769	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P49687	UniProtKB	Beta strand	772	775	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG0	
+P49687	UniProtKB	Helix	788	791	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	793	801	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Beta strand	803	807	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Beta strand	809	812	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P49687	UniProtKB	Beta strand	814	819	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	823	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	835	846	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	859	881	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	883	891	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	896	904	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Turn	905	907	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	909	918	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	922	931	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	936	948	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Turn	950	952	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P49687	UniProtKB	Helix	958	968	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Beta strand	971	974	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG0	
+P49687	UniProtKB	Helix	979	983	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	987	996	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Turn	997	1002	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P49687	UniProtKB	Helix	1005	1015	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	1023	1032	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	1034	1036	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+P49687	UniProtKB	Helix	1037	1045	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	1053	1064	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	1073	1089	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	1093	1100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	1106	1119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	1122	1124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Turn	1126	1129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	1132	1135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+P49687	UniProtKB	Helix	1140	1157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1	
+##sequence-region P38219 1 394
+P38219	UniProtKB	Chain	1	394	.	.	.	ID=PRO_0000122462;Note=Obg-like ATPase 1	
+P38219	UniProtKB	Domain	21	285	.	.	.	Note=OBG-type G	
+P38219	UniProtKB	Nucleotide binding	30	35	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03167	
+P38219	UniProtKB	Metal binding	34	34	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38219	UniProtKB	Metal binding	55	55	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38219	UniProtKB	Binding site	233	233	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03167	
+P38219	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38219	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38219	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38219	UniProtKB	Cross-link	98	98	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P53204 1 395
+P53204	UniProtKB	Chain	1	395	.	.	.	ID=PRO_0000135019;Note=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2	
+P53204	UniProtKB	Nucleotide binding	166	168	.	.	.	Note=ATP;Ontology_term=ECO:0000250,ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66,ECO:0000250|UniProtKB:Q9HAN9	
+P53204	UniProtKB	Nucleotide binding	282	284	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66	
+P53204	UniProtKB	Nucleotide binding	350	353	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66	
+P53204	UniProtKB	Region	206	208	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9	
+P53204	UniProtKB	Region	244	247	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9	
+P53204	UniProtKB	Region	294	295	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9	
+P53204	UniProtKB	Binding site	175	175	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66	
+P53204	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53204	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53204	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53883 1 403
+P53883	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P53883	UniProtKB	Chain	2	403	.	.	.	ID=PRO_0000082036;Note=Nucleolar protein 13	
+P53883	UniProtKB	Domain	125	219	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P53883	UniProtKB	Domain	239	317	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P53883	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P53883	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956	
+P53883	UniProtKB	Modified residue	105	105	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53883	UniProtKB	Modified residue	335	335	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53883	UniProtKB	Sequence conflict	296	296	.	.	.	Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53927 1 220
+P53927	UniProtKB	Chain	1	220	.	.	.	ID=PRO_0000082035;Note=Ribosome biogenesis protein 15	
+P53927	UniProtKB	Domain	91	169	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P53927	UniProtKB	Beta strand	89	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P	
+P53927	UniProtKB	Helix	104	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P	
+P53927	UniProtKB	Helix	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P	
+P53927	UniProtKB	Beta strand	117	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P	
+P53927	UniProtKB	Turn	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P	
+P53927	UniProtKB	Beta strand	131	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P	
+P53927	UniProtKB	Helix	142	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P	
+P53927	UniProtKB	Beta strand	163	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P	
+P53927	UniProtKB	Helix	173	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P	
+P53927	UniProtKB	Helix	181	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P	
+P53927	UniProtKB	Turn	187	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P	
+##sequence-region P25655 1 2108
+P25655	UniProtKB	Chain	1	2108	.	.	.	ID=PRO_0000096955;Note=General negative regulator of transcription subunit 1	
+P25655	UniProtKB	Coiled coil	795	813	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25655	UniProtKB	Coiled coil	1021	1046	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25655	UniProtKB	Compositional bias	1009	1046	.	.	.	Note=Gln-rich	
+P25655	UniProtKB	Compositional bias	1300	1329	.	.	.	Note=Gln-rich	
+P25655	UniProtKB	Modified residue	2102	2102	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956	
+P25655	UniProtKB	Sequence conflict	526	526	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25655	UniProtKB	Sequence conflict	569	569	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25655	UniProtKB	Helix	194	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	201	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	234	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	249	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	254	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	275	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	288	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	301	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Turn	316	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	323	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Beta strand	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	347	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Turn	359	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	367	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	384	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	395	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	405	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	424	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	427	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	437	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	457	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	468	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	479	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	484	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	495	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Turn	505	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	508	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Turn	530	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	536	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	553	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	571	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Turn	574	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	581	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Beta strand	589	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	595	609	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	615	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	631	647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	648	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	656	671	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	677	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	698	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	710	716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	718	727	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	729	733	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Helix	735	743	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B	
+P25655	UniProtKB	Beta strand	765	767	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P25655	UniProtKB	Helix	783	795	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Turn	798	800	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	801	811	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	814	816	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	817	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Turn	828	831	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	833	835	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	836	846	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	849	867	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	872	874	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	877	890	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	892	894	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Turn	900	902	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	905	914	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	918	929	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	930	932	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Beta strand	936	939	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	943	958	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	963	975	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+P25655	UniProtKB	Helix	980	982	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89	
+##sequence-region P06102 1 836
+P06102	UniProtKB	Chain	1	836	.	.	.	ID=PRO_0000198337;Note=General negative regulator of transcription subunit 3	
+P06102	UniProtKB	Coiled coil	36	68	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06102	UniProtKB	Coiled coil	119	195	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06102	UniProtKB	Coiled coil	255	292	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06102	UniProtKB	Coiled coil	803	831	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06102	UniProtKB	Modified residue	303	303	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06102	UniProtKB	Modified residue	307	307	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06102	UniProtKB	Modified residue	322	322	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P06102	UniProtKB	Modified residue	446	446	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06102	UniProtKB	Modified residue	450	450	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P06102	UniProtKB	Modified residue	565	565	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P06102	UniProtKB	Modified residue	569	569	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06102	UniProtKB	Modified residue	571	571	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06102	UniProtKB	Modified residue	657	657	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P06102	UniProtKB	Cross-link	535	535	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P06102	UniProtKB	Sequence conflict	106	106	.	.	.	Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06102	UniProtKB	Sequence conflict	593	593	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06102	UniProtKB	Sequence conflict	725	725	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06102	UniProtKB	Sequence conflict	827	836	.	.	.	Note=KQLKQGKISV->ETIETGKN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39997 1 493
+P39997	UniProtKB	Chain	1	493	.	.	.	ID=PRO_0000202612;Note=Ectonucleotide pyrophosphatase/phosphodiesterase 2	
+P39997	UniProtKB	Topological domain	1	28	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39997	UniProtKB	Transmembrane	29	45	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39997	UniProtKB	Topological domain	46	493	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39997	UniProtKB	Region	76	438	.	.	.	Note=Phosphodiesterase	
+P39997	UniProtKB	Active site	127	127	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39997	UniProtKB	Glycosylation	62	62	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39997	UniProtKB	Glycosylation	69	69	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39997	UniProtKB	Glycosylation	112	112	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39997	UniProtKB	Glycosylation	153	153	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39997	UniProtKB	Glycosylation	441	441	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39997	UniProtKB	Sequence conflict	125	125	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53617 1 575
+P53617	UniProtKB	Chain	1	575	.	.	.	ID=PRO_0000081688;Note=Protein NRD1	
+P53617	UniProtKB	Domain	1	153	.	.	.	Note=CID;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00724	
+P53617	UniProtKB	Domain	339	409	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P53617	UniProtKB	Compositional bias	541	544	.	.	.	Note=Poly-Ala	
+P53617	UniProtKB	Compositional bias	567	574	.	.	.	Note=Poly-Gln	
+P53617	UniProtKB	Modified residue	263	263	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53617	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53617	UniProtKB	Modified residue	271	271	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53617	UniProtKB	Helix	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LO6	
+P53617	UniProtKB	Helix	7	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Helix	16	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Helix	26	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Helix	39	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Helix	43	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Helix	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Helix	62	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Helix	94	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Helix	118	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Turn	135	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Turn	143	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Helix	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ	
+P53617	UniProtKB	Beta strand	331	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Beta strand	340	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Beta strand	347	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Helix	352	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Beta strand	356	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Beta strand	365	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Turn	372	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Beta strand	376	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Helix	384	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Beta strand	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Beta strand	401	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Helix	418	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Helix	426	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Helix	429	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Beta strand	440	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Beta strand	445	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+P53617	UniProtKB	Helix	450	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88	
+##sequence-region P40007 1 231
+P40007	UniProtKB	Chain	1	231	.	.	.	ID=PRO_0000202619;Note=Nucleolar protein 16	
+P40007	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P40007	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P40991 1 618
+P40991	UniProtKB	Chain	1	618	.	.	.	ID=PRO_0000211819;Note=25S rRNA (cytosine(2870)-C(5))-methyltransferase	
+P40991	UniProtKB	Region	353	359	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P40991	UniProtKB	Active site	478	478	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P40991	UniProtKB	Binding site	377	377	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P40991	UniProtKB	Binding site	404	404	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P40991	UniProtKB	Binding site	421	421	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P40991	UniProtKB	Modified residue	580	580	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40991	UniProtKB	Mutagenesis	424	424	.	.	.	Note=Cannot complement loss of wild type NOP2. C->A%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23913415,ECO:0000269|PubMed:9854021;Dbxref=PMID:23913415,PMID:9854021	
+P40991	UniProtKB	Mutagenesis	478	478	.	.	.	Note=Fails to ctalyze the C-5 methylation of the C2870 residue and strongly affects 60S biogenesis. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23913415,ECO:0000269|PubMed:9854021;Dbxref=PMID:23913415,PMID:9854021	
+P40991	UniProtKB	Sequence conflict	216	216	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40991	UniProtKB	Sequence conflict	577	577	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08287 1 484
+Q08287	UniProtKB	Chain	1	484	.	.	.	ID=PRO_0000081678;Note=60S ribosome subunit biogenesis protein NOP8	
+Q08287	UniProtKB	Domain	7	83	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q08287	UniProtKB	Compositional bias	280	290	.	.	.	Note=Poly-Glu	
+Q08287	UniProtKB	Modified residue	234	234	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08287	UniProtKB	Modified residue	239	239	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08287	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08287	UniProtKB	Modified residue	370	370	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P40078 1 261
+P40078	UniProtKB	Chain	1	261	.	.	.	ID=PRO_0000202648;Note=Ribosome biogenesis protein NSA2	
+P40078	UniProtKB	Turn	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJV	
+##sequence-region P43124 1 402
+P43124	UniProtKB	Chain	1	402	.	.	.	ID=PRO_0000214100;Note=Non-structural maintenance of chromosome element 4	
+##sequence-region Q04958 1 1679
+Q04958	UniProtKB	Chain	1	1679	.	.	.	ID=PRO_0000172528;Note=Lysophospholipase NTE1	
+Q04958	UniProtKB	Topological domain	1	49	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04958	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04958	UniProtKB	Topological domain	71	103	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04958	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04958	UniProtKB	Topological domain	125	1679	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04958	UniProtKB	Domain	1373	1537	.	.	.	Note=PNPLA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+Q04958	UniProtKB	Nucleotide binding	803	947	.	.	.	Note=cNMP 1	
+Q04958	UniProtKB	Nucleotide binding	943	1074	.	.	.	Note=cNMP 2	
+Q04958	UniProtKB	Motif	1377	1382	.	.	.	Note=GXGXXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+Q04958	UniProtKB	Motif	1404	1408	.	.	.	Note=GXSXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+Q04958	UniProtKB	Motif	1524	1526	.	.	.	Note=DGA/G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+Q04958	UniProtKB	Compositional bias	259	297	.	.	.	Note=Asp-rich	
+Q04958	UniProtKB	Compositional bias	713	718	.	.	.	Note=Poly-Ser	
+Q04958	UniProtKB	Active site	1406	1406	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+Q04958	UniProtKB	Active site	1524	1524	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+Q04958	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04958	UniProtKB	Modified residue	312	312	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04958	UniProtKB	Modified residue	632	632	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04958	UniProtKB	Modified residue	634	634	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04958	UniProtKB	Modified residue	653	653	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04958	UniProtKB	Modified residue	661	661	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04958	UniProtKB	Modified residue	670	670	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04958	UniProtKB	Modified residue	680	680	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04958	UniProtKB	Modified residue	739	739	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04958	UniProtKB	Modified residue	803	803	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04958	UniProtKB	Mutagenesis	1406	1406	.	.	.	Note=Loss of esterase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044461;Dbxref=PMID:15044461	
+##sequence-region P33331 1 125
+P33331	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P33331	UniProtKB	Chain	2	125	.	.	.	ID=PRO_0000194792;Note=Nuclear transport factor 2	
+P33331	UniProtKB	Domain	8	121	.	.	.	Note=NTF2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00137	
+P33331	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P33331	UniProtKB	Cross-link	53	53	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P33331	UniProtKB	Helix	5	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7	
+P33331	UniProtKB	Helix	24	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7	
+P33331	UniProtKB	Beta strand	31	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7	
+P33331	UniProtKB	Beta strand	42	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7	
+P33331	UniProtKB	Helix	47	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7	
+P33331	UniProtKB	Beta strand	62	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7	
+P33331	UniProtKB	Beta strand	80	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7	
+P33331	UniProtKB	Beta strand	97	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7	
+P33331	UniProtKB	Beta strand	111	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7	
+##sequence-region P36118 1 322
+P36118	UniProtKB	Chain	1	322	.	.	.	ID=PRO_0000203201;Note=Pre-mRNA-splicing factor NTR2	
+P36118	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P36118	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36118	UniProtKB	Modified residue	197	197	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P36161 1 1157
+P36161	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36161	UniProtKB	Chain	2	1157	.	.	.	ID=PRO_0000204841;Note=Nucleoporin NUP133	
+P36161	UniProtKB	Region	44	236	.	.	.	Note=Required for normal NPC distribution	
+P36161	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36161	UniProtKB	Helix	951	965	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	973	975	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	978	992	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Beta strand	993	995	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	999	1006	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	1012	1025	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	1026	1028	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	1031	1049	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	1056	1067	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	1070	1073	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	1081	1084	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	1087	1089	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	1092	1099	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Beta strand	1102	1104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	1106	1123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	1124	1127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Helix	1128	1141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Beta strand	1144	1149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Turn	1150	1153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+P36161	UniProtKB	Beta strand	1154	1157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO	
+##sequence-region P38181 1 1502
+P38181	UniProtKB	Chain	1	1502	.	.	.	ID=PRO_0000204854;Note=Nucleoporin NUP170	
+P38181	UniProtKB	Region	233	261	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38181	UniProtKB	Modified residue	1247	1247	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38181	UniProtKB	Helix	1001	1015	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1022	1032	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1045	1056	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1060	1075	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1079	1086	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Beta strand	1089	1093	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1095	1114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1146	1149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Beta strand	1150	1152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1155	1167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1171	1176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1182	1188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1196	1201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1203	1206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1210	1221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Beta strand	1222	1225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1229	1242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1262	1264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1265	1281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Beta strand	1283	1285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P	
+P38181	UniProtKB	Helix	1287	1299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1304	1310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Turn	1311	1316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1318	1327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1333	1350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1357	1378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Turn	1382	1384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1387	1401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1404	1406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Turn	1409	1412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1413	1419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1423	1435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1442	1458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1460	1463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1469	1472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Turn	1479	1481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+P38181	UniProtKB	Helix	1483	1491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q	
+##sequence-region P47054 1 1683
+P47054	UniProtKB	Chain	1	1683	.	.	.	ID=PRO_0000204858;Note=Nucleoporin NUP192	
+P47054	UniProtKB	Coiled coil	31	58	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47054	UniProtKB	Helix	6	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	22	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Turn	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	48	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Beta strand	54	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Beta strand	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	68	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	87	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	102	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	129	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	139	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	173	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Beta strand	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	211	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	228	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	234	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	242	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	249	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	266	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	272	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Turn	293	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	302	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	307	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	318	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	332	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	344	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	358	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	425	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	447	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Beta strand	463	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	469	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	477	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	493	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	498	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Beta strand	503	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	506	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	520	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	537	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Beta strand	549	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	555	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	603	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	625	642	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	650	660	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	665	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	669	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	689	699	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	703	716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Turn	738	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Beta strand	745	749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	750	758	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	761	766	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	770	789	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	794	797	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	815	821	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	824	831	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	834	845	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	861	884	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	886	893	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	909	916	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	921	929	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+P47054	UniProtKB	Helix	935	949	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ	
+##sequence-region P53742 1 486
+P53742	UniProtKB	Chain	1	486	.	.	.	ID=PRO_0000215817;Note=Nucleolar GTP-binding protein 2	
+P53742	UniProtKB	Domain	212	373	.	.	.	Note=CP-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01058	
+P53742	UniProtKB	Nucleotide binding	322	329	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53742	UniProtKB	Nucleotide binding	366	370	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53742	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53742	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53742	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q12200 1 1170
+Q12200	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Chain	20	1170	.	.	.	ID=PRO_0000268685;Note=Niemann-Pick type C-related protein 1	
+Q12200	UniProtKB	Transmembrane	260	280	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	341	361	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	556	576	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	585	605	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	616	636	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	667	687	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	698	718	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	752	772	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	1000	1020	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	1027	1047	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	1054	1074	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	1099	1119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Transmembrane	1133	1153	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Domain	557	717	.	.	.	Note=SSD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00199	
+Q12200	UniProtKB	Glycosylation	123	123	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Glycosylation	145	145	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Glycosylation	178	178	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Glycosylation	314	314	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Glycosylation	401	401	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Glycosylation	513	513	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Glycosylation	900	900	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Glycosylation	940	940	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12200	UniProtKB	Mutagenesis	718	718	.	.	.	Note=Sphingolipids mislocalization and no growth at 38 degrees Celsius. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14970192;Dbxref=PMID:14970192	
+##sequence-region Q03125 1 231
+Q03125	UniProtKB	Chain	1	231	.	.	.	ID=PRO_0000046812;Note=Transcriptional regulator NRG1	
+Q03125	UniProtKB	Zinc finger	174	196	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q03125	UniProtKB	Zinc finger	202	226	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q03125	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P39081 1 626
+P39081	UniProtKB	Chain	1	626	.	.	.	ID=PRO_0000058247;Note=Protein PCF11	
+P39081	UniProtKB	Domain	4	139	.	.	.	Note=CID;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00724	
+P39081	UniProtKB	Region	1	130	.	.	.	Note=Interaction with RBP1 CTD (CID)	
+P39081	UniProtKB	Compositional bias	234	253	.	.	.	Note=Poly-Gln	
+P39081	UniProtKB	Compositional bias	470	473	.	.	.	Note=Poly-Thr	
+P39081	UniProtKB	Mutagenesis	66	66	.	.	.	Note=Loss of interaction with RBP1 CTD. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12727883;Dbxref=PMID:12727883	
+P39081	UniProtKB	Mutagenesis	68	70	.	.	.	Note=Loss of interaction with RBP1 CTD. DSI->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12727883;Dbxref=PMID:12727883	
+P39081	UniProtKB	Sequence conflict	286	288	.	.	.	Note=NSL->ILS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39081	UniProtKB	Sequence conflict	515	515	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39081	UniProtKB	Helix	3	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9	
+P39081	UniProtKB	Helix	24	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9	
+P39081	UniProtKB	Helix	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9	
+P39081	UniProtKB	Helix	41	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9	
+P39081	UniProtKB	Helix	57	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9	
+P39081	UniProtKB	Helix	78	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9	
+P39081	UniProtKB	Helix	86	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9	
+P39081	UniProtKB	Helix	99	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9	
+P39081	UniProtKB	Helix	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9	
+P39081	UniProtKB	Helix	125	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9	
+P39081	UniProtKB	Helix	486	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+P39081	UniProtKB	Helix	495	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4	
+P39081	UniProtKB	Helix	543	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX	
+P39081	UniProtKB	Beta strand	550	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX	
+P39081	UniProtKB	Beta strand	561	564	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX	
+P39081	UniProtKB	Turn	565	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX	
+P39081	UniProtKB	Beta strand	569	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX	
+P39081	UniProtKB	Turn	577	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX	
+P39081	UniProtKB	Beta strand	581	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX	
+P39081	UniProtKB	Beta strand	587	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX	
+P39081	UniProtKB	Beta strand	593	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX	
+P39081	UniProtKB	Helix	597	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX	
+##sequence-region P51533 1 1564
+P51533	UniProtKB	Chain	1	1564	.	.	.	ID=PRO_0000093443;Note=ATP-dependent permease PDR10	
+P51533	UniProtKB	Topological domain	1	587	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	588	608	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	624	644	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	674	694	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	699	719	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	732	752	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	841	861	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Topological domain	862	1304	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	1305	1325	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	1340	1360	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	1390	1410	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	1426	1446	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	1459	1479	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Transmembrane	1491	1511	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Topological domain	1512	1564	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51533	UniProtKB	Domain	174	430	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P51533	UniProtKB	Domain	923	1166	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P51533	UniProtKB	Nucleotide binding	959	966	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P51533	UniProtKB	Compositional bias	73	80	.	.	.	Note=Poly-Ser	
+P51533	UniProtKB	Compositional bias	568	572	.	.	.	Note=Poly-Thr	
+P51533	UniProtKB	Compositional bias	845	848	.	.	.	Note=Poly-Lys	
+P51533	UniProtKB	Glycosylation	754	754	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q02785 1 1511
+Q02785	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q02785	UniProtKB	Chain	2	1511	.	.	.	ID=PRO_0000093445;Note=ATP-dependent permease PDR12	
+Q02785	UniProtKB	Topological domain	2	508	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	509	529	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	530	548	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	549	569	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	570	597	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	598	618	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	619	622	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	623	643	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	644	657	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	658	678	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	679	765	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	766	786	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	787	1182	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	1183	1203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	1204	1204	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	1205	1225	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	1226	1254	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	1255	1275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	1276	1291	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	1292	1312	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	1313	1318	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	1319	1339	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	1340	1444	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Transmembrane	1445	1465	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Topological domain	1466	1511	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Domain	144	397	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q02785	UniProtKB	Domain	836	1084	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q02785	UniProtKB	Nucleotide binding	878	885	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q02785	UniProtKB	Nucleotide binding	972	979	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+Q02785	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q02785	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02785	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q02785	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q02785	UniProtKB	Glycosylation	1405	1405	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02785	UniProtKB	Cross-link	426	426	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region P38855 1 283
+P38855	UniProtKB	Chain	1	283	.	.	.	ID=PRO_0000202929;Note=Peroxisomal membrane protein PEX18	
+##sequence-region Q07418 1 342
+Q07418	UniProtKB	Chain	1	339	.	.	.	ID=PRO_0000218763;Note=Peroxisomal membrane protein import receptor PEX19	
+Q07418	UniProtKB	Propeptide	340	342	.	.	.	ID=PRO_0000396705;Note=Removed in mature form;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q07418	UniProtKB	Compositional bias	311	314	.	.	.	Note=Poly-Glu	
+Q07418	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q07418	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q07418	UniProtKB	Modified residue	339	339	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q07418	UniProtKB	Lipidation	339	339	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9418908;Dbxref=PMID:9418908	
+Q07418	UniProtKB	Mutagenesis	339	339	.	.	.	Note=Prevents farnesylation. C->S%2CR;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16791427,ECO:0000269|PubMed:9418908;Dbxref=PMID:16791427,PMID:9418908	
+##sequence-region Q06169 1 523
+Q06169	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06169	UniProtKB	Chain	2	523	.	.	.	ID=PRO_0000252270;Note=Peroxisomal membrane protein PEX30	
+Q06169	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06169	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06169	UniProtKB	Transmembrane	184	204	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06169	UniProtKB	Transmembrane	207	227	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06169	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06169	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06169	UniProtKB	Modified residue	420	420	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06169	UniProtKB	Modified residue	424	424	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06169	UniProtKB	Sequence conflict	257	257	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40005 1 111
+P40005	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000124841;Note=Prefoldin subunit 2	
+P40005	UniProtKB	Coiled coil	1	36	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40005	UniProtKB	Coiled coil	72	92	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40005	UniProtKB	Sequence conflict	59	59	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08959 1 321
+Q08959	UniProtKB	Chain	1	321	.	.	.	ID=PRO_0000234365;Note=Phosphatidylglycerol phospholipase C	
+Q08959	UniProtKB	Transmembrane	297	315	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08959	UniProtKB	Domain	2	251	.	.	.	Note=GP-PDE	
+##sequence-region Q05637 1 104
+Q05637	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000262734;Note=Phosphate metabolism protein 6	
+Q05637	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P07269 1 559
+P07269	UniProtKB	Chain	1	559	.	.	.	ID=PRO_0000049247;Note=Regulatory protein PHO2	
+P07269	UniProtKB	DNA binding	77	136	.	.	.	Note=Homeobox;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108	
+P07269	UniProtKB	Compositional bias	23	52	.	.	.	Note=Gln-rich (involved in transcriptional activation)	
+P07269	UniProtKB	Modified residue	542	542	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P17442 1 1178
+P17442	UniProtKB	Chain	1	1178	.	.	.	ID=PRO_0000067075;Note=Phosphate system positive regulatory protein PHO81	
+P17442	UniProtKB	Domain	1	169	.	.	.	Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714	
+P17442	UniProtKB	Repeat	423	452	.	.	.	Note=ANK 1	
+P17442	UniProtKB	Repeat	458	487	.	.	.	Note=ANK 2	
+P17442	UniProtKB	Repeat	506	535	.	.	.	Note=ANK 3	
+P17442	UniProtKB	Repeat	556	586	.	.	.	Note=ANK 4	
+P17442	UniProtKB	Repeat	591	620	.	.	.	Note=ANK 5	
+P17442	UniProtKB	Repeat	624	653	.	.	.	Note=ANK 6	
+P17442	UniProtKB	Domain	871	1178	.	.	.	Note=GP-PDE	
+P17442	UniProtKB	Compositional bias	198	253	.	.	.	Note=Asn/Asp-rich	
+P17442	UniProtKB	Compositional bias	231	248	.	.	.	Note=Poly-Asn	
+P17442	UniProtKB	Modified residue	956	956	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P17442	UniProtKB	Sequence conflict	248	248	.	.	.	Note=N->NN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17442	UniProtKB	Sequence conflict	728	728	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17442	UniProtKB	Sequence conflict	762	762	.	.	.	Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17442	UniProtKB	Sequence conflict	845	845	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17442	UniProtKB	Sequence conflict	873	873	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17442	UniProtKB	Sequence conflict	920	920	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17442	UniProtKB	Sequence conflict	984	984	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25360 1 923
+P25360	UniProtKB	Chain	1	923	.	.	.	ID=PRO_0000172517;Note=Inorganic phosphate transporter PHO87	
+P25360	UniProtKB	Topological domain	1	461	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	462	482	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	483	493	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	494	514	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	515	537	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	538	558	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	559	583	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	584	604	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	605	627	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	628	648	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	649	667	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	668	688	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	689	707	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	708	728	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	729	735	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	736	756	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	757	767	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	768	788	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	789	802	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	803	823	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	824	849	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	850	870	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	871	898	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Transmembrane	899	919	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Topological domain	920	923	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Domain	1	334	.	.	.	Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714	
+P25360	UniProtKB	Glycosylation	162	162	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Glycosylation	202	202	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Glycosylation	274	274	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25360	UniProtKB	Cross-link	102	102	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25360	UniProtKB	Sequence conflict	72	72	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06216 1 648
+Q06216	UniProtKB	Chain	1	648	.	.	.	ID=PRO_0000071519;Note=Serine/threonine-protein phosphatase 1 regulatory subunit PIG1	
+Q06216	UniProtKB	Domain	201	331	.	.	.	Note=CBM21;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00491	
+Q06216	UniProtKB	Compositional bias	41	51	.	.	.	Note=Poly-Ser	
+Q06216	UniProtKB	Sequence conflict	228	228	.	.	.	Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38768 1 344
+P38768	UniProtKB	Chain	1	344	.	.	.	ID=PRO_0000058440;Note=Protein interacting with Hsp90 1	
+P38768	UniProtKB	Beta strand	29	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Beta strand	35	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Beta strand	58	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Helix	78	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Beta strand	100	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Beta strand	109	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Helix	119	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Helix	129	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Beta strand	149	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Beta strand	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Beta strand	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Beta strand	164	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Beta strand	171	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Helix	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Helix	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH	
+P38768	UniProtKB	Beta strand	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MNJ	
+P38768	UniProtKB	Beta strand	267	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P38768	UniProtKB	Beta strand	275	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P38768	UniProtKB	Beta strand	280	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P38768	UniProtKB	Beta strand	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MNJ	
+P38768	UniProtKB	Beta strand	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P38768	UniProtKB	Turn	303	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P38768	UniProtKB	Beta strand	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P38768	UniProtKB	Beta strand	311	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P38768	UniProtKB	Beta strand	315	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P38768	UniProtKB	Turn	326	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P38768	UniProtKB	Beta strand	330	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P38768	UniProtKB	Turn	335	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P38768	UniProtKB	Beta strand	339	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+##sequence-region Q12057 1 282
+Q12057	UniProtKB	Chain	1	282	.	.	.	ID=PRO_0000058442;Note=[PSI+] induction protein 2	
+Q12057	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12057	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12057	UniProtKB	Glycosylation	91	91	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12057	UniProtKB	Glycosylation	132	132	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12057	UniProtKB	Glycosylation	276	276	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46999 1 287
+P46999	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46999	UniProtKB	Propeptide	22	62	.	.	.	ID=PRO_0000377623;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46999	UniProtKB	Chain	63	287	.	.	.	ID=PRO_0000014333;Note=Cell wall protein PIR5	
+P46999	UniProtKB	Repeat	62	80	.	.	.	Note=PIR1/2/3 1	
+P46999	UniProtKB	Repeat	81	99	.	.	.	Note=PIR1/2/3 2	
+P46999	UniProtKB	Repeat	104	122	.	.	.	Note=PIR1/2/3 3	
+P46999	UniProtKB	Repeat	144	162	.	.	.	Note=PIR1/2/3 4	
+P46999	UniProtKB	Site	62	63	.	.	.	Note=Cleavage%3B by KEX2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46999	UniProtKB	Site	72	72	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46999	UniProtKB	Site	91	91	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46999	UniProtKB	Site	114	114	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46999	UniProtKB	Site	154	154	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03407 1 766
+Q03407	UniProtKB	Chain	1	766	.	.	.	ID=PRO_0000086552;Note=Serine/threonine-protein kinase PKH1	
+Q03407	UniProtKB	Domain	125	391	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03407	UniProtKB	Nucleotide binding	135	137	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q03407	UniProtKB	Nucleotide binding	204	206	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q03407	UniProtKB	Region	156	201	.	.	.	Note=PIF-pocket;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q03407	UniProtKB	Active site	249	249	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q03407	UniProtKB	Binding site	154	154	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q03407	UniProtKB	Binding site	210	210	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q03407	UniProtKB	Binding site	253	253	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q03407	UniProtKB	Binding site	267	267	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q03407	UniProtKB	Modified residue	294	294	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03407	UniProtKB	Modified residue	296	296	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198	
+##sequence-region P39105 1 664
+P39105	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Chain	23	634	.	.	.	ID=PRO_0000024646;Note=Lysophospholipase 1	
+P39105	UniProtKB	Propeptide	635	664	.	.	.	ID=PRO_0000372442;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Domain	35	586	.	.	.	Note=PLA2c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00555	
+P39105	UniProtKB	Compositional bias	587	629	.	.	.	Note=Ala/Ser-rich	
+P39105	UniProtKB	Lipidation	634	634	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	26	26	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	33	33	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	52	52	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	78	78	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	92	92	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	123	123	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	160	160	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	170	170	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	215	215	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	277	277	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	307	307	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	345	345	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	388	388	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	459	459	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	489	489	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	513	513	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	541	541	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	565	565	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Glycosylation	582	582	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39105	UniProtKB	Sequence conflict	32	32	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39105	UniProtKB	Sequence conflict	93	93	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39105	UniProtKB	Sequence conflict	494	494	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03674 1 706
+Q03674	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Chain	20	680	.	.	.	ID=PRO_0000024647;Note=Lysophospholipase 2	
+Q03674	UniProtKB	Propeptide	681	706	.	.	.	ID=PRO_0000372443;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Domain	36	588	.	.	.	Note=PLA2c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00555	
+Q03674	UniProtKB	Compositional bias	369	372	.	.	.	Note=Poly-Asp	
+Q03674	UniProtKB	Compositional bias	657	667	.	.	.	Note=Poly-Ser	
+Q03674	UniProtKB	Compositional bias	671	674	.	.	.	Note=Poly-Ser	
+Q03674	UniProtKB	Lipidation	680	680	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	47	47	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	80	80	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	94	94	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	125	125	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	162	162	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	181	181	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	193	193	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	217	217	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	279	279	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	309	309	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	365	365	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	390	390	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	491	491	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	515	515	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	524	524	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	543	543	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	567	567	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	584	584	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	598	598	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	630	630	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	634	634	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	642	642	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	648	648	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	652	652	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03674	UniProtKB	Glycosylation	658	658	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32383 1 869
+P32383	UniProtKB	Chain	1	869	.	.	.	ID=PRO_0000088514;Note=1-phosphatidylinositol 4%2C5-bisphosphate phosphodiesterase 1	
+P32383	UniProtKB	Domain	269	304	.	.	.	Note=EF-hand;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P32383	UniProtKB	Domain	382	520	.	.	.	Note=PI-PLC X-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00270	
+P32383	UniProtKB	Domain	590	709	.	.	.	Note=PI-PLC Y-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00271	
+P32383	UniProtKB	Domain	734	846	.	.	.	Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+P32383	UniProtKB	Calcium binding	282	293	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P32383	UniProtKB	Active site	395	395	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00270	
+P32383	UniProtKB	Active site	439	439	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00270	
+P32383	UniProtKB	Binding site	518	518	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32383	UniProtKB	Binding site	520	520	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32383	UniProtKB	Binding site	614	614	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32383	UniProtKB	Binding site	643	643	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32383	UniProtKB	Sequence conflict	159	159	.	.	.	Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32383	UniProtKB	Sequence conflict	181	181	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32383	UniProtKB	Sequence conflict	581	581	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12511 1 572
+Q12511	UniProtKB	Domain	153	543	.	.	.	Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082	
+Q12511	UniProtKB	Metal binding	197	197	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12511	UniProtKB	Metal binding	197	197	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12511	UniProtKB	Metal binding	198	198	.	.	.	Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12511	UniProtKB	Metal binding	424	424	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12511	UniProtKB	Metal binding	480	480	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P25646 1 442
+P25646	UniProtKB	Transit peptide	1	34	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25646	UniProtKB	Chain	35	442	.	.	.	ID=PRO_0000057788;Note=[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2%2C mitochondrial	
+P25646	UniProtKB	Domain	35	411	.	.	.	Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082	
+##sequence-region P53844 1 350
+P53844	UniProtKB	Chain	1	350	.	.	.	ID=PRO_0000210746;Note=Phosphatidylinositol transfer protein PDR17	
+P53844	UniProtKB	Domain	139	297	.	.	.	Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056	
+##sequence-region P27801 1 918
+P27801	UniProtKB	Chain	1	918	.	.	.	ID=PRO_0000055993;Note=Vacuolar membrane protein PEP3	
+P27801	UniProtKB	Repeat	585	741	.	.	.	Note=CHCR	
+P27801	UniProtKB	Zinc finger	826	851	.	.	.	Note=RING-type%3B atypical	
+P27801	UniProtKB	Modified residue	907	907	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P27801	UniProtKB	Beta strand	3	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Turn	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	22	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	29	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	35	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	49	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	63	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	75	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	84	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	91	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	103	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	123	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	134	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	149	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	158	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	166	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	184	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	199	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	206	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Turn	237	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	242	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Helix	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	260	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	267	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	277	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Turn	283	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	288	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	310	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Turn	317	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	321	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Beta strand	330	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+P27801	UniProtKB	Helix	338	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY	
+##sequence-region P40335 1 379
+P40335	UniProtKB	Chain	1	379	.	.	.	ID=PRO_0000073015;Note=Carboxypeptidase Y-deficient protein 8	
+P40335	UniProtKB	Modified residue	216	216	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40335	UniProtKB	Sequence conflict	189	189	.	.	.	Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40335	UniProtKB	Sequence conflict	286	286	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99373 1 253
+Q99373	UniProtKB	Transit peptide	1	36	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99373	UniProtKB	Chain	37	253	.	.	.	ID=PRO_0000240390;Note=Protein PET20%2C mitochondrial	
+##sequence-region Q04370 1 399
+Q04370	UniProtKB	Chain	1	399	.	.	.	ID=PRO_0000218617;Note=Peroxisome assembly protein 12	
+Q04370	UniProtKB	Transmembrane	270	286	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04370	UniProtKB	Zinc finger	334	373	.	.	.	Note=RING-type%3B degenerate	
+Q04370	UniProtKB	Sequence conflict	37	37	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08215 1 383
+Q08215	UniProtKB	Chain	1	383	.	.	.	ID=PRO_0000270567;Note=Peroxisomal membrane protein PEX15	
+Q08215	UniProtKB	Topological domain	1	331	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08215	UniProtKB	Transmembrane	332	349	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08215	UniProtKB	Topological domain	350	383	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08215	UniProtKB	Mutagenesis	22	22	.	.	.	Note=No interaction with PEX6. L->F%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808025;Dbxref=PMID:12808025	
+Q08215	UniProtKB	Mutagenesis	47	47	.	.	.	Note=No interaction with PEX6. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808025;Dbxref=PMID:12808025	
+Q08215	UniProtKB	Mutagenesis	50	50	.	.	.	Note=No interaction with PEX6. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808025;Dbxref=PMID:12808025	
+##sequence-region P53203 1 462
+P53203	UniProtKB	Chain	1	462	.	.	.	ID=PRO_0000202779;Note=Peroxisomal membrane protein PEX31	
+P53203	UniProtKB	Topological domain	1	90	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53203	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53203	UniProtKB	Topological domain	112	175	.	.	.	Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53203	UniProtKB	Transmembrane	176	196	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53203	UniProtKB	Topological domain	197	462	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53203	UniProtKB	Modified residue	432	432	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P53203	UniProtKB	Modified residue	435	435	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P33760 1 1030
+P33760	UniProtKB	Chain	1	1030	.	.	.	ID=PRO_0000084621;Note=Peroxisomal ATPase PEX6	
+P33760	UniProtKB	Nucleotide binding	772	779	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33760	UniProtKB	Region	478	683	.	.	.	Note=AAA-cassette D1	
+P33760	UniProtKB	Region	767	956	.	.	.	Note=AAA-cassette D2	
+P33760	UniProtKB	Mutagenesis	489	489	.	.	.	Note=In PEX6pA1%3B decreased binding to PEX15. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12808025,ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078;Dbxref=PMID:12808025,PMID:15634331,PMID:16007078	
+P33760	UniProtKB	Mutagenesis	778	778	.	.	.	Note=In PEX6pA2%3B increased amount of peroxisome-bound PEX6. Results in accumulation of PEX5 on peroxisomal membranes. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12808025,ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078;Dbxref=PMID:12808025,PMID:15634331,PMID:16007078	
+P33760	UniProtKB	Mutagenesis	831	831	.	.	.	Note=In PEX6pB2%3B increased amount of peroxisome-bound PEX6. Results in accumulation of PEX5 on peroxisomal membranes. D->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12808025,ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078;Dbxref=PMID:12808025,PMID:15634331,PMID:16007078	
+##sequence-region P42836 1 336
+P42836	UniProtKB	Chain	1	336	.	.	.	ID=PRO_0000212959;Note=Palmitoyltransferase PFA3	
+P42836	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42836	UniProtKB	Transmembrane	7	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42836	UniProtKB	Topological domain	30	37	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42836	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42836	UniProtKB	Topological domain	59	147	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42836	UniProtKB	Transmembrane	148	168	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42836	UniProtKB	Topological domain	169	188	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42836	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42836	UniProtKB	Topological domain	210	336	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42836	UniProtKB	Domain	104	154	.	.	.	Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067	
+P42836	UniProtKB	Mutagenesis	134	134	.	.	.	Note=Abolishes autopalmitoylation and VAC8 palmitoylation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16186255;Dbxref=PMID:16186255	
+##sequence-region Q12006 1 378
+Q12006	UniProtKB	Chain	1	378	.	.	.	ID=PRO_0000212972;Note=Palmitoyltransferase PFA4	
+Q12006	UniProtKB	Topological domain	1	9	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12006	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03199	
+Q12006	UniProtKB	Topological domain	31	40	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12006	UniProtKB	Transmembrane	41	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03199	
+Q12006	UniProtKB	Topological domain	62	119	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12006	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03199	
+Q12006	UniProtKB	Topological domain	141	164	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q12006	UniProtKB	Transmembrane	165	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03199	
+Q12006	UniProtKB	Topological domain	186	378	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+Q12006	UniProtKB	Domain	78	128	.	.	.	Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067	
+Q12006	UniProtKB	Active site	108	108	.	.	.	Note=S-palmitoyl cysteine intermediate;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000305|PubMed:26224664;Dbxref=PMID:26224664	
+Q12006	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Causes mislocalization of chitin synthase CHS3 (PubMed:16818716). Reduces%2C but does not abolish catalytic activity. Lacks autopalmitoylation (PubMed:26224664). C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16818716,ECO:0000269|PubMed:26224664;Dbxref=PMID:16818716,PMID:26224664	
+Q12006	UniProtKB	Mutagenesis	108	108	.	.	.	Note=Reduces%2C but does not abolish catalytic activity. Lacks autopalmitoylation. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26224664;Dbxref=PMID:26224664	
+##sequence-region Q03289 1 374
+Q03289	UniProtKB	Chain	1	374	.	.	.	ID=PRO_0000212983;Note=Palmitoyltransferase PFA5	
+Q03289	UniProtKB	Topological domain	1	13	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03289	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03289	UniProtKB	Topological domain	35	55	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03289	UniProtKB	Transmembrane	56	76	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03289	UniProtKB	Topological domain	77	173	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03289	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03289	UniProtKB	Topological domain	195	217	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03289	UniProtKB	Transmembrane	218	238	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03289	UniProtKB	Topological domain	239	374	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03289	UniProtKB	Domain	129	179	.	.	.	Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067	
+##sequence-region P46988 1 109
+P46988	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P46988	UniProtKB	Chain	2	109	.	.	.	ID=PRO_0000124834;Note=Prefoldin subunit 1	
+P46988	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P46988	UniProtKB	Sequence conflict	74	74	.	.	.	Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P52553 1 114
+P52553	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P52553	UniProtKB	Chain	2	114	.	.	.	ID=PRO_0000124855;Note=Prefoldin subunit 6	
+P52553	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P32452 1 334
+P32452	UniProtKB	Chain	1	334	.	.	.	ID=PRO_0000119206;Note=Putative prephenate dehydratase	
+P32452	UniProtKB	Domain	7	224	.	.	.	Note=Prephenate dehydratase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00517	
+P32452	UniProtKB	Domain	244	322	.	.	.	Note=ACT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007	
+##sequence-region P07270 1 312
+P07270	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000127422;Note=Phosphate system positive regulatory protein PHO4	
+P07270	UniProtKB	Domain	250	306	.	.	.	Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981	
+P07270	UniProtKB	Region	1	31	.	.	.	Note=Interaction with PHO80	
+P07270	UniProtKB	Region	75	99	.	.	.	Note=Transcription activation domain	
+P07270	UniProtKB	Region	156	200	.	.	.	Note=Interaction with PHO80	
+P07270	UniProtKB	Region	201	218	.	.	.	Note=Interaction with PHO2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7957107;Dbxref=PMID:7957107	
+P07270	UniProtKB	Region	203	227	.	.	.	Note=Involved in oligomerization	
+P07270	UniProtKB	Motif	75	83	.	.	.	Note=9aaTAD	
+P07270	UniProtKB	Motif	140	166	.	.	.	Note=Nuclear localization signal	
+P07270	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320381,ECO:0000269|PubMed:8539622;Dbxref=PMID:10320381,PMID:8539622	
+P07270	UniProtKB	Modified residue	114	114	.	.	.	Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320381,ECO:0000269|PubMed:8539622;Dbxref=PMID:10320381,PMID:8539622	
+P07270	UniProtKB	Modified residue	128	128	.	.	.	Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320381,ECO:0000269|PubMed:8539622;Dbxref=PMID:10320381,PMID:8539622	
+P07270	UniProtKB	Modified residue	152	152	.	.	.	Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320381,ECO:0000269|PubMed:8539622;Dbxref=PMID:10320381,PMID:8539622	
+P07270	UniProtKB	Modified residue	204	204	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07270	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10320381,ECO:0000269|PubMed:8539622;Dbxref=PMID:17330950,PMID:19779198,PMID:10320381,PMID:8539622	
+P07270	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P07270	UniProtKB	Modified residue	243	243	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P07270	UniProtKB	Sequence conflict	269	269	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07270	UniProtKB	Sequence conflict	269	269	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07270	UniProtKB	Sequence conflict	310	310	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07270	UniProtKB	Helix	254	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A0A	
+P07270	UniProtKB	Helix	260	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A0A	
+P07270	UniProtKB	Helix	279	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A0A	
+P07270	UniProtKB	Helix	294	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A0A	
+##sequence-region P20052 1 293
+P20052	UniProtKB	Chain	1	293	.	.	.	ID=PRO_0000080502;Note=PHO85 cyclin PHO80	
+P20052	UniProtKB	Modified residue	234	234	.	.	.	Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15057567;Dbxref=PMID:15057567	
+P20052	UniProtKB	Modified residue	267	267	.	.	.	Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15057567;Dbxref=PMID:15057567	
+P20052	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Temperature-sensitive allele. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3283704;Dbxref=PMID:3283704	
+P20052	UniProtKB	Mutagenesis	229	229	.	.	.	Note=In PHO80-1. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2269431;Dbxref=PMID:2269431	
+P20052	UniProtKB	Sequence conflict	65	65	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20052	UniProtKB	Sequence conflict	247	247	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20052	UniProtKB	Sequence conflict	247	247	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20052	UniProtKB	Sequence conflict	254	254	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20052	UniProtKB	Sequence conflict	254	254	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20052	UniProtKB	Sequence conflict	292	292	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20052	UniProtKB	Sequence conflict	292	292	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20052	UniProtKB	Beta strand	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PK9	
+P20052	UniProtKB	Helix	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Helix	32	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Helix	77	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Helix	92	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Turn	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PK9	
+P20052	UniProtKB	Helix	119	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Helix	141	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Helix	152	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Turn	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Helix	176	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Helix	210	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Helix	216	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Helix	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P20052	UniProtKB	Beta strand	242	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PK9	
+##sequence-region P38361 1 574
+P38361	UniProtKB	Chain	1	574	.	.	.	ID=PRO_0000080781;Note=Phosphate permease PHO89	
+P38361	UniProtKB	Transmembrane	6	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38361	UniProtKB	Transmembrane	44	64	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38361	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38361	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38361	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38361	UniProtKB	Transmembrane	185	205	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38361	UniProtKB	Transmembrane	223	243	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38361	UniProtKB	Transmembrane	355	375	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38361	UniProtKB	Transmembrane	399	419	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38361	UniProtKB	Transmembrane	448	468	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38361	UniProtKB	Transmembrane	504	524	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38361	UniProtKB	Transmembrane	542	562	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P06738 1 902
+P06738	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1613787;Dbxref=PMID:1613787	
+P06738	UniProtKB	Chain	2	902	.	.	.	ID=PRO_0000188545;Note=Glycogen phosphorylase	
+P06738	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:1092346,ECO:0000269|PubMed:1613787;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198,PMID:1092346,PMID:1613787	
+P06738	UniProtKB	Modified residue	333	333	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P06738	UniProtKB	Modified residue	751	751	.	.	.	Note=N6-(pyridoxal phosphate)lysine	
+P06738	UniProtKB	Sequence conflict	167	168	.	.	.	Note=DL->EG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	167	168	.	.	.	Note=DL->EG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	326	326	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	326	326	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	440	441	.	.	.	Note=VG->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	440	441	.	.	.	Note=VG->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	508	508	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	508	508	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	524	524	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	524	524	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	578	578	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	578	578	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	876	876	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Sequence conflict	876	876	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06738	UniProtKB	Helix	35	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	47	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	64	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	88	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	121	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	134	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	158	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	172	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	188	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	207	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	220	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	227	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Turn	235	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	244	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	277	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	297	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	313	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	326	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	337	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	345	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	380	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	384	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Turn	392	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	395	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	412	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	423	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	432	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	437	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	440	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	448	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	474	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	481	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	486	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	490	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	493	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	501	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	509	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Turn	518	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	521	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	529	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	532	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	541	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Turn	545	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	550	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	566	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	571	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	585	607	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Turn	608	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	620	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	624	630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	634	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	638	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	662	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	672	677	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	685	701	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	705	707	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	710	716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	721	727	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	728	730	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	732	736	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	747	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Turn	754	756	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	758	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	766	774	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	776	778	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Beta strand	779	783	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	786	798	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	805	813	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Turn	824	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	828	836	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Turn	838	841	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	843	863	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	865	879	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	880	882	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+P06738	UniProtKB	Helix	884	894	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP	
+##sequence-region P40187 1 538
+P40187	UniProtKB	Chain	1	538	.	.	.	ID=PRO_0000071522;Note=GSY2-interacting protein PIG2	
+P40187	UniProtKB	Domain	384	508	.	.	.	Note=CBM21;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00491	
+P40187	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P40187	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P40187	UniProtKB	Modified residue	296	296	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40187	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40187	UniProtKB	Sequence conflict	537	537	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06149 1 701
+Q06149	UniProtKB	Chain	1	701	.	.	.	ID=PRO_0000114963;Note=Transcription factor PDR8	
+Q06149	UniProtKB	DNA binding	31	59	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+Q06149	UniProtKB	Compositional bias	272	278	.	.	.	Note=Poly-Ser	
+##sequence-region Q06608 1 200
+Q06608	UniProtKB	Chain	1	200	.	.	.	ID=PRO_0000257818;Note=Pyridoxamine 5'-phosphate oxidase homolog	
+Q06608	UniProtKB	Binding site	60	60	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06608	UniProtKB	Binding site	68	68	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06608	UniProtKB	Binding site	125	125	.	.	.	Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P12868 1 1029
+P12868	UniProtKB	Chain	1	1029	.	.	.	ID=PRO_0000055995;Note=E3 ubiquitin-protein ligase PEP5	
+P12868	UniProtKB	Repeat	406	583	.	.	.	Note=CHCR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01006	
+P12868	UniProtKB	Zinc finger	928	973	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P12868	UniProtKB	Sequence conflict	37	37	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12868	UniProtKB	Sequence conflict	619	625	.	.	.	Note=VFYSYKT->MFFTVTKH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12868	UniProtKB	Sequence conflict	769	770	.	.	.	Note=TK->KQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39684 1 611
+P39684	UniProtKB	Chain	1	611	.	.	.	ID=PRO_0000081724;Note=Protein PES4	
+P39684	UniProtKB	Domain	91	169	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P39684	UniProtKB	Domain	179	247	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P39684	UniProtKB	Domain	303	379	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P39684	UniProtKB	Domain	393	471	.	.	.	Note=RRM 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P39684	UniProtKB	Compositional bias	54	64	.	.	.	Note=Poly-Ser	
+P39684	UniProtKB	Sequence conflict	124	124	.	.	.	Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39684	UniProtKB	Sequence conflict	541	611	.	.	.	Note=QVRRGIDFMRFPSATRDENVHGIAEYIFDTYWNRDVLILDKFLSLLNSSPYHEGVLQKQIEEAASSLGFKR->ASKKRYRFHEISKCH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12252 1 991
+Q12252	UniProtKB	Chain	1	991	.	.	.	ID=PRO_0000262735;Note=Phosphate metabolism protein 7	
+Q12252	UniProtKB	Topological domain	1	9	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Topological domain	31	91	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Topological domain	113	138	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Transmembrane	139	159	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Topological domain	160	388	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Transmembrane	389	409	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Topological domain	410	437	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Transmembrane	438	458	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Topological domain	459	471	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Transmembrane	472	492	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Topological domain	493	523	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Transmembrane	524	544	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Topological domain	545	582	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Transmembrane	583	603	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Topological domain	604	604	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Transmembrane	605	625	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Topological domain	626	637	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Transmembrane	638	658	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Topological domain	659	661	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Transmembrane	662	682	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Topological domain	683	991	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12252	UniProtKB	Glycosylation	132	132	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53297 1 722
+P53297	UniProtKB	Chain	1	722	.	.	.	ID=PRO_0000058244;Note=PAB1-binding protein 1	
+P53297	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53297	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53297	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53297	UniProtKB	Modified residue	436	436	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P53297	UniProtKB	Cross-link	344	344	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P38151 1 413
+P38151	UniProtKB	Chain	1	413	.	.	.	ID=PRO_0000050122;Note=PAB1-binding protein 2	
+P38151	UniProtKB	Domain	66	130	.	.	.	Note=KH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P38151	UniProtKB	Domain	148	213	.	.	.	Note=KH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P38151	UniProtKB	Domain	330	394	.	.	.	Note=KH 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+##sequence-region P06169 1 563
+P06169	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10545125,ECO:0000269|PubMed:9298649;Dbxref=PMID:10545125,PMID:9298649	
+P06169	UniProtKB	Chain	2	563	.	.	.	ID=PRO_0000090770;Note=Pyruvate decarboxylase isozyme 1	
+P06169	UniProtKB	Region	390	476	.	.	.	Note=Thiamine pyrophosphate binding	
+P06169	UniProtKB	Metal binding	444	444	.	.	.	Note=Magnesium	
+P06169	UniProtKB	Metal binding	471	471	.	.	.	Note=Magnesium	
+P06169	UniProtKB	Metal binding	473	473	.	.	.	Note=Magnesium%3B via carbonyl oxygen	
+P06169	UniProtKB	Binding site	28	28	.	.	.	Note=Substrate	
+P06169	UniProtKB	Binding site	115	115	.	.	.	Note=Substrate	
+P06169	UniProtKB	Binding site	157	157	.	.	.	Note=Substrate%3B allosteric site	
+P06169	UniProtKB	Binding site	477	477	.	.	.	Note=Substrate	
+P06169	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10545125,ECO:0000269|PubMed:9298649;Dbxref=PMID:10545125,PMID:9298649	
+P06169	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P06169	UniProtKB	Modified residue	266	266	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P06169	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06169	UniProtKB	Modified residue	353	353	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P06169	UniProtKB	Modified residue	522	522	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06169	UniProtKB	Modified residue	526	526	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P06169	UniProtKB	Cross-link	212	212	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P06169	UniProtKB	Cross-link	233	233	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P06169	UniProtKB	Cross-link	269	269	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P06169	UniProtKB	Cross-link	332	332	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P06169	UniProtKB	Cross-link	484	484	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P06169	UniProtKB	Cross-link	505	505	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P06169	UniProtKB	Cross-link	520	520	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P06169	UniProtKB	Mutagenesis	291	291	.	.	.	Note=In PDC1-8%3B reduces catalytic activity to 10%25 but retains autoregulatory activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7050079;Dbxref=PMID:7050079	
+P06169	UniProtKB	Sequence conflict	55	55	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	106	106	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	106	106	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	106	106	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	106	106	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	115	115	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	143	143	.	.	.	Note=A->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	143	143	.	.	.	Note=A->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	143	143	.	.	.	Note=A->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	145	146	.	.	.	Note=AP->PQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	206	206	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	208	208	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	253	253	.	.	.	Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	253	253	.	.	.	Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	253	253	.	.	.	Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	253	253	.	.	.	Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	336	336	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	336	336	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	336	336	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	336	336	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	538	538	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	538	538	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	538	538	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	538	538	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Sequence conflict	545	563	.	.	.	Note=APQNLVEQAKLTAATNAKQ->CSTKLG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06169	UniProtKB	Beta strand	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	6	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	31	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	51	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	76	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	95	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	104	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPB	
+P06169	UniProtKB	Beta strand	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPB	
+P06169	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	124	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	134	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Turn	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	145	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	163	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	178	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	194	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	212	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	220	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	228	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	242	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Turn	246	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	259	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	265	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	270	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	280	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Turn	291	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	306	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	311	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	319	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	326	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Turn	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	367	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Turn	375	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	383	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	390	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	395	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	405	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Turn	410	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	417	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	438	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	444	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	451	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	454	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	465	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	475	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	486	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	495	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	498	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	505	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	515	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Turn	525	528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Beta strand	531	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+P06169	UniProtKB	Helix	547	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8	
+##sequence-region P38848 1 579
+P38848	UniProtKB	Chain	1	579	.	.	.	ID=PRO_0000202925;Note=Peroxisomal membrane protein PEX28	
+P38848	UniProtKB	Topological domain	1	243	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38848	UniProtKB	Transmembrane	244	264	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38848	UniProtKB	Topological domain	265	392	.	.	.	Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38848	UniProtKB	Transmembrane	393	413	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38848	UniProtKB	Topological domain	414	579	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38848	UniProtKB	Compositional bias	2	114	.	.	.	Note=Ser-rich	
+P38848	UniProtKB	Glycosylation	361	361	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32800 1 271
+P32800	UniProtKB	Chain	1	271	.	.	.	ID=PRO_0000030724;Note=Peroxisomal biogenesis factor 2	
+P32800	UniProtKB	Zinc finger	222	259	.	.	.	Note=RING-type	
+P32800	UniProtKB	Alternative sequence	1	46	.	.	.	ID=VSP_018874;Note=In isoform Short. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38292 1 413
+P38292	UniProtKB	Chain	1	413	.	.	.	ID=PRO_0000202502;Note=Peroxisomal membrane protein PEX32	
+P38292	UniProtKB	Topological domain	1	66	.	.	.	Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38292	UniProtKB	Transmembrane	67	87	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38292	UniProtKB	Topological domain	88	103	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38292	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38292	UniProtKB	Topological domain	125	181	.	.	.	Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38292	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38292	UniProtKB	Topological domain	203	413	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38292	UniProtKB	Sequence conflict	165	165	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P28795 1 441
+P28795	UniProtKB	Chain	1	441	.	.	.	ID=PRO_0000208747;Note=Peroxisomal biogenesis factor 3	
+P28795	UniProtKB	Topological domain	1	17	.	.	.	Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28795	UniProtKB	Transmembrane	18	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28795	UniProtKB	Topological domain	40	441	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P35056 1 612
+P35056	UniProtKB	Chain	1	612	.	.	.	ID=PRO_0000106316;Note=Peroxisomal targeting signal receptor	
+P35056	UniProtKB	Repeat	64	97	.	.	.	Note=TPR 1	
+P35056	UniProtKB	Repeat	313	346	.	.	.	Note=TPR 2	
+P35056	UniProtKB	Repeat	347	380	.	.	.	Note=TPR 3	
+P35056	UniProtKB	Repeat	381	418	.	.	.	Note=TPR 4	
+P35056	UniProtKB	Repeat	419	456	.	.	.	Note=TPR 5	
+P35056	UniProtKB	Repeat	457	490	.	.	.	Note=TPR 6	
+P35056	UniProtKB	Repeat	491	524	.	.	.	Note=TPR 7	
+P35056	UniProtKB	Repeat	525	558	.	.	.	Note=TPR 8	
+P35056	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898	
+P35056	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P35056	UniProtKB	Cross-link	6	6	.	.	.	Note=Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898	
+P35056	UniProtKB	Cross-link	18	18	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898	
+P35056	UniProtKB	Cross-link	24	24	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898	
+P35056	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Loss of UBE2D2-independent ubiquitination. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898	
+P35056	UniProtKB	Mutagenesis	18	18	.	.	.	Note=Loss of UBE2D2-dependent ubiquitination. No effect on its function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898	
+P35056	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Loss of UBE2D2-dependent ubiquitination. No effect on its function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898	
+##sequence-region P53900 1 129
+P53900	UniProtKB	Chain	1	129	.	.	.	ID=PRO_0000124848;Note=Prefoldin subunit 4	
+P53900	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P53872 1 204
+P53872	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53872	UniProtKB	Chain	21	174	.	.	.	ID=PRO_0000203402;Note=Hydrophilin YNL190W	
+P53872	UniProtKB	Propeptide	175	204	.	.	.	ID=PRO_0000424804;Note=Removed in mature form	
+P53872	UniProtKB	Compositional bias	7	163	.	.	.	Note=Thr-rich	
+P53872	UniProtKB	Lipidation	174	174	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10383953;Dbxref=PMID:10383953	
+P53872	UniProtKB	Glycosylation	55	55	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53872	UniProtKB	Glycosylation	64	64	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53872	UniProtKB	Glycosylation	75	75	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53872	UniProtKB	Glycosylation	84	84	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53872	UniProtKB	Glycosylation	95	95	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53872	UniProtKB	Glycosylation	104	104	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53872	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53872	UniProtKB	Glycosylation	124	124	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53872	UniProtKB	Glycosylation	135	135	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53872	UniProtKB	Glycosylation	144	144	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53872	UniProtKB	Glycosylation	155	155	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53896 1 198
+P53896	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53896	UniProtKB	Chain	24	198	.	.	.	ID=PRO_0000203415;Note=GPI mannosyltransferase 2 subunit PGA1	
+P53896	UniProtKB	Topological domain	24	163	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53896	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53896	UniProtKB	Topological domain	185	198	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53896	UniProtKB	Glycosylation	72	72	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53896	UniProtKB	Glycosylation	80	80	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12746 1 312
+Q12746	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000167628;Note=Plasma membrane-associated coenzyme Q6 reductase PGA3	
+Q12746	UniProtKB	Topological domain	1	15	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12746	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12746	UniProtKB	Topological domain	37	39	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12746	UniProtKB	Transmembrane	40	60	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12746	UniProtKB	Topological domain	61	179	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12746	UniProtKB	Transmembrane	180	200	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12746	UniProtKB	Topological domain	201	312	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12746	UniProtKB	Domain	70	173	.	.	.	Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716	
+Q12746	UniProtKB	Nucleotide binding	153	168	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12746	UniProtKB	Nucleotide binding	179	211	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P25578 1 521
+P25578	UniProtKB	Chain	1	521	.	.	.	ID=PRO_0000056827;Note=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase	
+P25578	UniProtKB	Domain	177	203	.	.	.	Note=PLD phosphodiesterase 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P25578	UniProtKB	Domain	419	457	.	.	.	Note=PLD phosphodiesterase 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P25578	UniProtKB	Nucleotide binding	91	98	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25578	UniProtKB	Active site	182	182	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P25578	UniProtKB	Active site	184	184	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P25578	UniProtKB	Active site	189	189	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P25578	UniProtKB	Sequence conflict	498	498	.	.	.	Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P18898 1 376
+P18898	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000119775;Note=Geranylgeranyl transferase type-1 subunit beta	
+P18898	UniProtKB	Repeat	128	179	.	.	.	Note=PFTB 1	
+P18898	UniProtKB	Repeat	192	231	.	.	.	Note=PFTB 2	
+P18898	UniProtKB	Repeat	259	301	.	.	.	Note=PFTB 3	
+P18898	UniProtKB	Repeat	310	353	.	.	.	Note=PFTB 4	
+P18898	UniProtKB	Region	216	218	.	.	.	Note=Geranylgeranyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18898	UniProtKB	Region	280	283	.	.	.	Note=Geranylgeranyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18898	UniProtKB	Region	289	292	.	.	.	Note=Geranylgeranyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18898	UniProtKB	Compositional bias	138	180	.	.	.	Note=Cys-rich	
+P18898	UniProtKB	Metal binding	286	286	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18898	UniProtKB	Metal binding	288	288	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18898	UniProtKB	Metal binding	341	341	.	.	.	Note=Zinc%3B via tele nitrogen%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P18898	UniProtKB	Mutagenesis	328	328	.	.	.	Note=Defect in nuclear division and bud formation. G->S	
+##sequence-region P39535 1 881
+P39535	UniProtKB	Chain	1	881	.	.	.	ID=PRO_0000172518;Note=Low-affinity phosphate transporter PHO90	
+P39535	UniProtKB	Transmembrane	417	437	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Transmembrane	456	476	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Transmembrane	493	513	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Transmembrane	514	534	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Transmembrane	539	559	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Transmembrane	581	601	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Transmembrane	663	683	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Transmembrane	691	711	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Transmembrane	718	738	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Transmembrane	758	778	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Transmembrane	805	825	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Transmembrane	854	874	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39535	UniProtKB	Domain	1	288	.	.	.	Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714	
+##sequence-region P05066 1 565
+P05066	UniProtKB	Domain	75	226	.	.	.	Note=Photolyase/cryptochrome alpha/beta	
+P05066	UniProtKB	Nucleotide binding	338	342	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05066	UniProtKB	Nucleotide binding	482	484	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05066	UniProtKB	Region	384	391	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05066	UniProtKB	Region	451	452	.	.	.	Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05066	UniProtKB	Binding site	326	326	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05066	UniProtKB	Binding site	514	514	.	.	.	Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05066	UniProtKB	Site	416	416	.	.	.	Note=Electron transfer via tryptophanyl radical;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05066	UniProtKB	Site	469	469	.	.	.	Note=Electron transfer via tryptophanyl radical;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05066	UniProtKB	Site	492	492	.	.	.	Note=Electron transfer via tryptophanyl radical;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05066	UniProtKB	Mutagenesis	387	387	.	.	.	Note=Reduces substrate binding 100-fold. Reduces quantum yield for dimer photolysis 3-fold. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8344951;Dbxref=PMID:8344951	
+P05066	UniProtKB	Mutagenesis	463	463	.	.	.	Note=Reduces substrate binding 100-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8344951;Dbxref=PMID:8344951	
+P05066	UniProtKB	Mutagenesis	507	507	.	.	.	Note=Reduces substrate binding 100-fold. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8344951;Dbxref=PMID:8344951	
+P05066	UniProtKB	Mutagenesis	517	517	.	.	.	Note=Reduces substrate binding 10-fold. K->A	
+P05066	UniProtKB	Sequence conflict	77	77	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05066	UniProtKB	Sequence conflict	165	165	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05066	UniProtKB	Sequence conflict	169	169	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05066	UniProtKB	Sequence conflict	200	200	.	.	.	Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05066	UniProtKB	Sequence conflict	351	351	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05066	UniProtKB	Sequence conflict	365	365	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05066	UniProtKB	Sequence conflict	473	473	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32854 1 288
+P32854	UniProtKB	Chain	1	288	.	.	.	ID=PRO_0000210271;Note=Syntaxin PEP12	
+P32854	UniProtKB	Topological domain	1	268	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32854	UniProtKB	Transmembrane	269	288	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32854	UniProtKB	Domain	195	257	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+P32854	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P32854	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32854	UniProtKB	Mutagenesis	271	271	.	.	.	Note=Increases ubiquitination by TUL1. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11788821;Dbxref=PMID:11788821	
+P32854	UniProtKB	Sequence conflict	13	13	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32854	UniProtKB	Sequence conflict	89	89	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38921 1 284
+P38921	UniProtKB	Chain	1	284	.	.	.	ID=PRO_0000090686;Note=Putative mitochondrial carrier protein PET8	
+P38921	UniProtKB	Transmembrane	5	25	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38921	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38921	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38921	UniProtKB	Transmembrane	153	169	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38921	UniProtKB	Transmembrane	194	214	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38921	UniProtKB	Transmembrane	252	272	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38921	UniProtKB	Repeat	2	75	.	.	.	Note=Solcar 1	
+P38921	UniProtKB	Repeat	92	178	.	.	.	Note=Solcar 2	
+P38921	UniProtKB	Repeat	192	271	.	.	.	Note=Solcar 3	
+##sequence-region P40155 1 199
+P40155	UniProtKB	Chain	1	199	.	.	.	ID=PRO_0000058333;Note=Peroxisomal membrane protein PEX17	
+##sequence-region Q02969 1 394
+Q02969	UniProtKB	Chain	1	394	.	.	.	ID=PRO_0000270568;Note=Peroxisomal membrane protein PEX25	
+Q02969	UniProtKB	Topological domain	1	366	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02969	UniProtKB	Transmembrane	367	383	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02969	UniProtKB	Topological domain	384	394	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02969	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q02969	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q02969	UniProtKB	Modified residue	289	289	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+Q02969	UniProtKB	Sequence conflict	8	8	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08580 1 376
+Q08580	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000270569;Note=Peroxisomal membrane protein PEX27	
+Q08580	UniProtKB	Compositional bias	130	138	.	.	.	Note=Poly-Leu	
+##sequence-region P53248 1 589
+P53248	UniProtKB	Chain	1	589	.	.	.	ID=PRO_0000058343;Note=Peroxisomal biogenesis factor 8	
+P53248	UniProtKB	Motif	587	589	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53903 1 129
+P53903	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5	
+P53903	UniProtKB	Chain	2	129	.	.	.	ID=PRO_0000203421;Note=Processing of GAS1 and ALP protein 2	
+P53903	UniProtKB	Transmembrane	23	42	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53903	UniProtKB	Coiled coil	43	116	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53903	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5	
+P53903	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P40025 1 321
+P40025	UniProtKB	Chain	1	321	.	.	.	ID=PRO_0000202627;Note=Phosphate metabolism protein 8	
+##sequence-region Q06651 1 286
+Q06651	UniProtKB	Chain	1	286	.	.	.	ID=PRO_0000245839;Note=E3 ubiquitin-protein ligase PIB1	
+Q06651	UniProtKB	Zinc finger	17	88	.	.	.	Note=FYVE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
+Q06651	UniProtKB	Zinc finger	225	283	.	.	.	Note=RING-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q06651	UniProtKB	Mutagenesis	23	23	.	.	.	Note=Abolishes endosomal targeting. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11526110;Dbxref=PMID:11526110	
+Q06651	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Abolishes E3 activity%2C strongly reduces zinc binding and destabilizes the protein%2C but no effect on subcellular location. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11526110;Dbxref=PMID:11526110	
+Q06651	UniProtKB	Sequence conflict	166	166	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07271 1 859
+P07271	UniProtKB	Transit peptide	1	45	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8253734;Dbxref=PMID:8253734	
+P07271	UniProtKB	Chain	46	859	.	.	.	ID=PRO_0000013269;Note=ATP-dependent DNA helicase PIF1	
+P07271	UniProtKB	Nucleotide binding	258	265	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03176	
+P07271	UniProtKB	DNA binding	727	746	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03176	
+P07271	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07271	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07271	UniProtKB	Modified residue	169	169	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07271	UniProtKB	Modified residue	584	584	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07271	UniProtKB	Alternative sequence	1	39	.	.	.	ID=VSP_034601;Note=In isoform Nuclear. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07271	UniProtKB	Mutagenesis	1	1	.	.	.	Note=In PIF1-m1%3B loss of mitochondrial function. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8287473;Dbxref=PMID:8287473	
+P07271	UniProtKB	Mutagenesis	40	40	.	.	.	Note=In PIF1-m2%3B loss of nuclear function. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8287473;Dbxref=PMID:8287473	
+P07271	UniProtKB	Mutagenesis	264	264	.	.	.	Note=Abolishes helicase activity resulting in elongated telomeres%3B binds normally to DNA substrates. K->A%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10926538,ECO:0000269|PubMed:16121131,ECO:0000269|PubMed:16816432;Dbxref=PMID:10926538,PMID:16121131,PMID:16816432	
+P07271	UniProtKB	Sequence conflict	309	309	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07271	UniProtKB	Sequence conflict	322	322	.	.	.	Note=V->VG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07271	UniProtKB	Sequence conflict	426	426	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07271	UniProtKB	Sequence conflict	800	801	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P19657 1 947
+P19657	UniProtKB	Chain	1	947	.	.	.	ID=PRO_0000046272;Note=Plasma membrane ATPase 2	
+P19657	UniProtKB	Topological domain	1	144	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Topological domain	166	169	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Transmembrane	170	189	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Topological domain	190	320	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Transmembrane	321	342	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Topological domain	343	353	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Transmembrane	354	376	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Topological domain	377	748	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Transmembrane	749	767	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Topological domain	768	783	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Transmembrane	784	803	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Topological domain	804	853	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Transmembrane	854	874	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Topological domain	875	886	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Transmembrane	887	903	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Topological domain	904	947	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P19657	UniProtKB	Compositional bias	33	47	.	.	.	Note=Poly-Ser	
+P19657	UniProtKB	Compositional bias	62	91	.	.	.	Note=Asp/Glu-rich (acidic)	
+P19657	UniProtKB	Active site	407	407	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19657	UniProtKB	Metal binding	663	663	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19657	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P19657	UniProtKB	Sequence conflict	944	944	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P87284 1 55
+P87284	UniProtKB	Chain	1	55	.	.	.	ID=PRO_0000193987;Note=Plasma membrane proteolipid 3	
+P87284	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87284	UniProtKB	Transmembrane	31	51	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P14242 1 873
+P14242	UniProtKB	Chain	1	873	.	.	.	ID=PRO_0000245571;Note=DNA mismatch repair protein PMS1	
+P14242	UniProtKB	Region	1	357	.	.	.	Note=DNA- and ATP-binding	
+P14242	UniProtKB	Region	661	873	.	.	.	Note=Interaction with MLH1	
+P14242	UniProtKB	Modified residue	393	393	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14242	UniProtKB	Modified residue	566	566	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14242	UniProtKB	Natural variant	41	41	.	.	.	Note=In strain: SK1 and YJM421. N->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108	
+P14242	UniProtKB	Natural variant	112	112	.	.	.	Note=In strain: SK1 and YJM421. I->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108	
+P14242	UniProtKB	Natural variant	384	384	.	.	.	Note=In strain: SK1%2C YJM320%2C YJM339 and YJM421. F->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108	
+P14242	UniProtKB	Natural variant	392	392	.	.	.	Note=In strain: YJM320. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579	
+P14242	UniProtKB	Natural variant	400	400	.	.	.	Note=In strain: SK1%2C YJM320%2C YJM339 and YJM421. T->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108	
+P14242	UniProtKB	Natural variant	401	401	.	.	.	Note=In strain: YJM320 and YJM421. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579	
+P14242	UniProtKB	Natural variant	416	416	.	.	.	Note=In strain: SK1%2C YJM320%2C YJM339 and YJM421. T->TCEGT	
+P14242	UniProtKB	Natural variant	458	458	.	.	.	Note=In strain: EAY1068. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773	
+P14242	UniProtKB	Natural variant	475	475	.	.	.	Note=In strain: YJM339. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579	
+P14242	UniProtKB	Natural variant	513	513	.	.	.	Note=In strain: SK1. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P14242	UniProtKB	Natural variant	564	564	.	.	.	Note=In strain: YJM320. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579	
+P14242	UniProtKB	Natural variant	768	768	.	.	.	Note=In strain: YJM320. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579	
+P14242	UniProtKB	Natural variant	818	818	.	.	.	Note=In strain: SK1 and YJM320%3B forms a non-functional heterodimer with MHL1 from strain S288c%2C resulting in an accumulation of mutations in spore progeny of crosses between these strains. R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108	
+P14242	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Reduces ATPase activity by 62%25. Displays 60-fold increase in spontaneous mutation accumulation. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10938116,ECO:0000269|PubMed:11717305;Dbxref=PMID:10938116,PMID:11717305	
+P14242	UniProtKB	Mutagenesis	34	34	.	.	.	Note=Reduces ATPase activity by 84%25. Displays 11000-fold increase in spontaneous mutation accumulation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11717305;Dbxref=PMID:11717305	
+P14242	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704	
+P14242	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Displays an increase in spontaneous mutation accumulation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10938116;Dbxref=PMID:10938116	
+P14242	UniProtKB	Mutagenesis	297	297	.	.	.	Note=Displays a 60-fold increase in spontaneous mutation accumulation. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12682353;Dbxref=PMID:12682353	
+P14242	UniProtKB	Mutagenesis	851	851	.	.	.	Note=Confers a strong defect in the repair of primer strand-specific 1-bp loops during DNA replication%2C but not during meoitic recombination. Does not impair heterodimer formation. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227575;Dbxref=PMID:16227575	
+P14242	UniProtKB	Mutagenesis	857	857	.	.	.	Note=Confers a strong defect in the repair of primer strand-specific 1-bp loops during DNA replication%2C but not during meoitic recombination. Does not impair heterodimer formation. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227575;Dbxref=PMID:16227575	
+P14242	UniProtKB	Sequence conflict	695	695	.	.	.	Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14242	UniProtKB	Sequence conflict	861	861	.	.	.	Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14242	UniProtKB	Helix	13	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Helix	24	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	41	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Turn	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	53	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Helix	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Turn	69	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Helix	98	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	106	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	120	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	131	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	140	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Turn	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Helix	155	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Helix	165	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	187	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	199	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Helix	211	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Turn	221	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	227	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Helix	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	259	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	274	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	288	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Helix	293	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	314	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Helix	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Beta strand	330	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Helix	341	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L	
+P14242	UniProtKB	Helix	650	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Helix	653	665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Helix	668	672	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Beta strand	675	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Turn	681	683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Beta strand	684	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Beta strand	695	701	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Helix	702	717	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Beta strand	722	731	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Helix	739	742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Helix	747	750	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Beta strand	767	773	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Helix	782	794	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Helix	806	819	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Helix	829	838	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Helix	839	841	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Beta strand	842	844	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Beta strand	853	860	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+P14242	UniProtKB	Helix	869	871	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W	
+##sequence-region P47190 1 753
+P47190	UniProtKB	Chain	1	753	.	.	.	ID=PRO_0000121493;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 3	
+P47190	UniProtKB	Topological domain	1	50	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Topological domain	72	148	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Transmembrane	149	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Topological domain	170	174	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Topological domain	196	235	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Transmembrane	236	256	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Topological domain	257	282	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Transmembrane	283	303	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Topological domain	304	602	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Transmembrane	603	623	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Topological domain	624	639	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Transmembrane	640	660	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Topological domain	661	665	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Transmembrane	666	686	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Topological domain	687	703	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Transmembrane	704	724	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Topological domain	725	753	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Domain	332	387	.	.	.	Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P47190	UniProtKB	Domain	401	457	.	.	.	Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P47190	UniProtKB	Domain	465	523	.	.	.	Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P47190	UniProtKB	Glycosylation	124	124	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Glycosylation	324	324	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Glycosylation	398	398	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47190	UniProtKB	Sequence conflict	397	397	.	.	.	Note=E->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47190	UniProtKB	Sequence conflict	567	567	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P52867 1 743
+P52867	UniProtKB	Chain	1	743	.	.	.	ID=PRO_0000121495;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 5	
+P52867	UniProtKB	Topological domain	1	46	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Transmembrane	47	67	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Topological domain	68	129	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Transmembrane	130	150	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Topological domain	151	158	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Transmembrane	159	179	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Topological domain	180	180	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Transmembrane	181	201	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Topological domain	202	231	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Topological domain	253	264	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Transmembrane	265	285	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Topological domain	286	583	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Transmembrane	584	604	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Topological domain	605	623	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Transmembrane	624	644	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Topological domain	645	646	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Transmembrane	647	667	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Topological domain	668	683	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Transmembrane	684	704	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Topological domain	705	743	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Domain	320	374	.	.	.	Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P52867	UniProtKB	Domain	384	444	.	.	.	Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P52867	UniProtKB	Domain	454	510	.	.	.	Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P52867	UniProtKB	Glycosylation	33	33	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Glycosylation	213	213	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Glycosylation	380	380	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52867	UniProtKB	Glycosylation	386	386	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P42934 1 759
+P42934	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P42934	UniProtKB	Chain	2	759	.	.	.	ID=PRO_0000121496;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 6	
+P42934	UniProtKB	Topological domain	2	58	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Transmembrane	59	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Topological domain	80	164	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Transmembrane	165	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Topological domain	186	194	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Transmembrane	195	215	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Topological domain	216	251	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Transmembrane	252	272	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Topological domain	273	293	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Transmembrane	294	314	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Topological domain	315	618	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Transmembrane	619	639	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Topological domain	640	656	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Transmembrane	657	677	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Topological domain	678	686	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Transmembrane	687	707	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Topological domain	708	715	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Transmembrane	716	736	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Topological domain	737	759	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Domain	340	394	.	.	.	Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P42934	UniProtKB	Domain	409	467	.	.	.	Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P42934	UniProtKB	Domain	482	540	.	.	.	Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P42934	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P42934	UniProtKB	Glycosylation	156	156	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Glycosylation	404	404	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42934	UniProtKB	Glycosylation	481	481	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05788 1 311
+Q05788	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q05788	UniProtKB	Chain	2	311	.	.	.	ID=PRO_0000184538;Note=Purine nucleoside phosphorylase	
+Q05788	UniProtKB	Region	101	103	.	.	.	Note=Phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859	
+Q05788	UniProtKB	Binding site	46	46	.	.	.	Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859	
+Q05788	UniProtKB	Binding site	81	81	.	.	.	Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859	
+Q05788	UniProtKB	Binding site	134	134	.	.	.	Note=Phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859	
+Q05788	UniProtKB	Binding site	219	219	.	.	.	Note=Purine nucleoside;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859	
+Q05788	UniProtKB	Binding site	238	238	.	.	.	Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859	
+Q05788	UniProtKB	Binding site	261	261	.	.	.	Note=Purine nucleoside;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859	
+Q05788	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q05788	UniProtKB	Modified residue	275	275	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P47180 1 361
+P47180	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47180	UniProtKB	Chain	19	361	.	.	.	ID=PRO_0000024797;Note=Polygalacturonase	
+P47180	UniProtKB	Repeat	155	185	.	.	.	Note=PbH1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47180	UniProtKB	Repeat	186	207	.	.	.	Note=PbH1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47180	UniProtKB	Repeat	208	228	.	.	.	Note=PbH1 3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47180	UniProtKB	Repeat	237	258	.	.	.	Note=PbH1 4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47180	UniProtKB	Repeat	266	288	.	.	.	Note=PbH1 5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47180	UniProtKB	Active site	200	200	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74213	
+P47180	UniProtKB	Active site	222	222	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10052	
+P47180	UniProtKB	Glycosylation	318	318	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P47180	UniProtKB	Glycosylation	330	330	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P47180	UniProtKB	Disulfide bond	27	43	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74213	
+P47180	UniProtKB	Disulfide bond	202	218	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74213	
+P47180	UniProtKB	Disulfide bond	350	361	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74213	
+P47180	UniProtKB	Sequence conflict	23	23	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P37012 1 569
+P37012	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P37012	UniProtKB	Chain	2	569	.	.	.	ID=PRO_0000147797;Note=Phosphoglucomutase 2	
+P37012	UniProtKB	Region	119	120	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Region	294	295	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Region	378	380	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Active site	119	119	.	.	.	Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Metal binding	119	119	.	.	.	Note=Magnesium%3B via phosphate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Metal binding	290	290	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Metal binding	292	292	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Metal binding	294	294	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Binding site	20	20	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Binding site	24	24	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Binding site	132	132	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Binding site	359	359	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Binding site	391	391	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Binding site	522	522	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P37012	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P37012	UniProtKB	Modified residue	111	111	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P37012	UniProtKB	Modified residue	117	117	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P37012	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P37012	UniProtKB	Sequence conflict	27	27	.	.	.	Note=T->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37012	UniProtKB	Sequence conflict	32	32	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P37012	UniProtKB	Sequence conflict	272	272	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03262 1 622
+Q03262	UniProtKB	Chain	1	622	.	.	.	ID=PRO_0000148022;Note=Phosphoribomutase	
+Q03262	UniProtKB	Region	158	159	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Region	329	330	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Region	428	430	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Active site	158	158	.	.	.	Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Metal binding	158	158	.	.	.	Note=Magnesium%3B via phosphate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Metal binding	325	325	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Metal binding	327	327	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Metal binding	329	329	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Binding site	57	57	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Binding site	61	61	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Binding site	168	168	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Binding site	404	404	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Binding site	442	442	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+Q03262	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q03262	UniProtKB	Mutagenesis	158	158	.	.	.	Note=Loss of function. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18042468;Dbxref=PMID:18042468	
+Q03262	UniProtKB	Mutagenesis	326	326	.	.	.	Note=No effect. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18042468;Dbxref=PMID:18042468	
+##sequence-region P40961 1 287
+P40961	UniProtKB	Chain	1	287	.	.	.	ID=PRO_0000213883;Note=Prohibitin-1	
+P40961	UniProtKB	Coiled coil	180	224	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525670;Dbxref=PMID:15525670	
+P40961	UniProtKB	Sequence conflict	43	43	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40961	UniProtKB	Sequence conflict	222	222	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40961	UniProtKB	Sequence conflict	225	225	.	.	.	Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P50085 1 310
+P50085	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000213888;Note=Prohibitin-2	
+P50085	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50085	UniProtKB	Coiled coil	212	253	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525670;Dbxref=PMID:15525670	
+##sequence-region P36093 1 366
+P36093	UniProtKB	Chain	1	366	.	.	.	ID=PRO_0000058377;Note=Putative transcription factor PHD1	
+P36093	UniProtKB	Domain	186	292	.	.	.	Note=HTH APSES-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630	
+P36093	UniProtKB	DNA binding	220	241	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630	
+##sequence-region P50947 1 330
+P50947	UniProtKB	Chain	1	330	.	.	.	ID=PRO_0000203440;Note=Transcriptional regulatory protein PHO23	
+P50947	UniProtKB	Zinc finger	280	329	.	.	.	Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+P50947	UniProtKB	Metal binding	283	283	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Metal binding	285	285	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Metal binding	296	296	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Metal binding	301	301	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Metal binding	307	307	.	.	.	Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Metal binding	310	310	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Metal binding	323	323	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Metal binding	326	326	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Binding site	282	282	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Binding site	293	293	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Binding site	297	297	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Binding site	305	305	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53	
+P50947	UniProtKB	Natural variant	8	8	.	.	.	Note=In strain: SK1. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P50947	UniProtKB	Natural variant	35	35	.	.	.	Note=In strain: SK1. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+##sequence-region P25297 1 587
+P25297	UniProtKB	Chain	1	587	.	.	.	ID=PRO_0000050477;Note=Inorganic phosphate transporter PHO84	
+P25297	UniProtKB	Topological domain	1	67	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	89	108	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	130	133	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	134	154	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	155	156	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	178	201	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	223	250	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	251	271	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	272	345	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	346	366	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	367	395	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	396	416	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	417	419	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	420	440	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	441	442	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	443	463	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	464	485	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	486	506	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	507	522	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Transmembrane	523	543	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Topological domain	544	587	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25297	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25297	UniProtKB	Modified residue	303	303	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25297	UniProtKB	Modified residue	316	316	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25297	UniProtKB	Modified residue	317	317	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25297	UniProtKB	Modified residue	321	321	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25297	UniProtKB	Modified residue	577	577	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P25297	UniProtKB	Modified residue	579	579	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25297	UniProtKB	Modified residue	581	581	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25297	UniProtKB	Cross-link	6	6	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P25297	UniProtKB	Cross-link	298	298	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P25297	UniProtKB	Sequence conflict	162	162	.	.	.	Note=A->AHSPAINFVA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25297	UniProtKB	Sequence conflict	353	353	.	.	.	Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P46956 1 311
+P46956	UniProtKB	Chain	1	311	.	.	.	ID=PRO_0000058404;Note=Inorganic phosphate transporter PHO86	
+P46956	UniProtKB	Topological domain	1	70	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46956	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46956	UniProtKB	Topological domain	92	117	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46956	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46956	UniProtKB	Topological domain	139	311	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46956	UniProtKB	Sequence conflict	8	8	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38264 1 188
+P38264	UniProtKB	Chain	1	188	.	.	.	ID=PRO_0000058405;Note=SRP-independent targeting protein 3	
+P38264	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38264	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P27514 1 894
+P27514	UniProtKB	Chain	1	894	.	.	.	ID=PRO_0000172519;Note=Low-affinity phosphate transporter PHO91	
+P27514	UniProtKB	Transmembrane	430	450	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	474	494	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	511	531	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	557	577	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	602	622	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	642	662	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	682	702	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	706	726	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	738	758	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	777	797	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	799	819	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	824	844	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Transmembrane	874	894	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P27514	UniProtKB	Domain	1	256	.	.	.	Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714	
+P27514	UniProtKB	Modified residue	295	295	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P27514	UniProtKB	Modified residue	311	311	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P27514	UniProtKB	Modified residue	312	312	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q03306 1 898
+Q03306	UniProtKB	Chain	1	898	.	.	.	ID=PRO_0000086554;Note=Serine/threonine-protein kinase PKH3	
+Q03306	UniProtKB	Domain	11	293	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03306	UniProtKB	Nucleotide binding	17	25	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03306	UniProtKB	Active site	138	138	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q03306	UniProtKB	Binding site	41	41	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03306	UniProtKB	Modified residue	696	696	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03306	UniProtKB	Modified residue	753	753	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03306	UniProtKB	Modified residue	871	871	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P33333 1 303
+P33333	UniProtKB	Chain	1	303	.	.	.	ID=PRO_0000208189;Note=Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase	
+P33333	UniProtKB	Transmembrane	16	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33333	UniProtKB	Motif	82	87	.	.	.	Note=HXXXXD motif	
+P33333	UniProtKB	Natural variant	44	44	.	.	.	Note=In allele suppressor SLC1-1. Q->L	
+P33333	UniProtKB	Sequence conflict	115	115	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P05030 1 918
+P05030	UniProtKB	Chain	1	918	.	.	.	ID=PRO_0000046271;Note=Plasma membrane ATPase 1	
+P05030	UniProtKB	Topological domain	1	115	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Topological domain	137	140	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Transmembrane	141	160	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Topological domain	161	291	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Transmembrane	292	313	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Topological domain	314	325	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Transmembrane	326	347	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Topological domain	348	719	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Transmembrane	720	738	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Topological domain	739	754	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Transmembrane	755	774	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Topological domain	775	824	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Transmembrane	825	845	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Topological domain	846	857	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Transmembrane	858	874	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Topological domain	875	918	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P05030	UniProtKB	Compositional bias	5	17	.	.	.	Note=Poly-Ser	
+P05030	UniProtKB	Compositional bias	31	78	.	.	.	Note=Asp/Glu-rich (acidic)	
+P05030	UniProtKB	Compositional bias	39	44	.	.	.	Note=Poly-Asp	
+P05030	UniProtKB	Compositional bias	585	590	.	.	.	Note=Poly-Gly	
+P05030	UniProtKB	Active site	378	378	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05030	UniProtKB	Metal binding	634	634	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05030	UniProtKB	Metal binding	638	638	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P05030	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P05030	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P05030	UniProtKB	Modified residue	911	911	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P05030	UniProtKB	Modified residue	912	912	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P05030	UniProtKB	Modified residue	918	918	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P05030	UniProtKB	Cross-link	252	252	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05030	UniProtKB	Cross-link	555	555	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538	
+P05030	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Normal activity. E->L%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Activity reduced to 23%25. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	233	233	.	.	.	Note=Activity reduced to 33%25. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	271	271	.	.	.	Note=Normal activity. R->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	335	335	.	.	.	Note=Activity reduced to 53%25. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	378	378	.	.	.	Note=Activity reduced to 67%25. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	378	378	.	.	.	Note=Activity reduced to 73%25. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	378	378	.	.	.	Note=Activity reduced to 49%25. D->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	474	474	.	.	.	Note=Activity reduced to 19%25. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	534	534	.	.	.	Note=Activity reduced to 37%25. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	560	560	.	.	.	Note=Activity reduced to 24%25. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	638	638	.	.	.	Note=Activity reduced to 24%25. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+P05030	UniProtKB	Mutagenesis	848	848	.	.	.	Note=Normal activity. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955	
+##sequence-region P53238 1 335
+P53238	UniProtKB	Chain	1	335	.	.	.	ID=PRO_0000073720;Note=Peflin	
+P53238	UniProtKB	Domain	144	192	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53238	UniProtKB	Domain	198	223	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53238	UniProtKB	Domain	224	259	.	.	.	Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53238	UniProtKB	Domain	260	300	.	.	.	Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53238	UniProtKB	Domain	301	332	.	.	.	Note=EF-hand 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53238	UniProtKB	Calcium binding	170	181	.	.	.	Note=1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53238	UniProtKB	Calcium binding	237	248	.	.	.	Note=2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P53238	UniProtKB	Mutagenesis	218	218	.	.	.	Note=Induces EGTA and SDS sensitivity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17640275;Dbxref=PMID:17640275	
+P53238	UniProtKB	Sequence conflict	324	324	.	.	.	Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32609 1 515
+P32609	UniProtKB	Chain	1	515	.	.	.	ID=PRO_0000046858;Note=Vacuolar segregation protein PEP7	
+P32609	UniProtKB	Zinc finger	6	29	.	.	.	Note=C2H2-type	
+P32609	UniProtKB	Zinc finger	72	137	.	.	.	Note=FYVE-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
+P32609	UniProtKB	Zinc finger	215	297	.	.	.	Note=FYVE-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
+P32609	UniProtKB	Sequence conflict	366	366	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53261 1 605
+P53261	UniProtKB	Chain	1	605	.	.	.	ID=PRO_0000186192;Note=Pescadillo homolog	
+P53261	UniProtKB	Domain	355	449	.	.	.	Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03028	
+P53261	UniProtKB	Region	51	484	.	.	.	Note=Sufficient for interaction with ERB1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448671;Dbxref=PMID:18448671	
+P53261	UniProtKB	Coiled coil	294	342	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03028	
+P53261	UniProtKB	Coiled coil	530	605	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03028	
+P53261	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53261	UniProtKB	Modified residue	308	308	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53261	UniProtKB	Mutagenesis	380	380	.	.	.	Note=Temperature sensitive mutant. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110181;Dbxref=PMID:12110181	
+P53261	UniProtKB	Mutagenesis	431	431	.	.	.	Note=Temperature sensitive mutant. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110181;Dbxref=PMID:12110181	
+##sequence-region P39718 1 180
+P39718	UniProtKB	Chain	1	180	.	.	.	ID=PRO_0000058339;Note=Peroxisome assembly protein 22	
+P39718	UniProtKB	Transmembrane	15	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39718	UniProtKB	Beta strand	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Helix	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Helix	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Turn	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Beta strand	83	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Turn	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Beta strand	94	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Helix	100	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Turn	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Helix	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Beta strand	115	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Helix	121	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Beta strand	134	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Helix	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Beta strand	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9P	
+P39718	UniProtKB	Helix	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9P	
+P39718	UniProtKB	Helix	158	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Beta strand	163	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+P39718	UniProtKB	Helix	171	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M	
+##sequence-region P16861 1 987
+P16861	UniProtKB	Chain	1	987	.	.	.	ID=PRO_0000112045;Note=ATP-dependent 6-phosphofructokinase subunit alpha	
+P16861	UniProtKB	Nucleotide binding	278	279	.	.	.	Note=ATP;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A796,ECO:0000255|HAMAP-Rule:MF_03184	
+P16861	UniProtKB	Nucleotide binding	308	311	.	.	.	Note=ATP;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A796,ECO:0000255|HAMAP-Rule:MF_03184	
+P16861	UniProtKB	Region	1	580	.	.	.	Note=N-terminal catalytic PFK domain 1;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Region	354	356	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Region	398	400	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Region	488	491	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Region	581	594	.	.	.	Note=Interdomain linker;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Region	595	987	.	.	.	Note=C-terminal regulatory PFK domain 2;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Region	722	726	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Region	767	769	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Region	859	862	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Active site	356	356	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A796,ECO:0000255|HAMAP-Rule:MF_03184	
+P16861	UniProtKB	Metal binding	309	309	.	.	.	Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A796,ECO:0000255|HAMAP-Rule:MF_03184	
+P16861	UniProtKB	Binding site	215	215	.	.	.	Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A796,ECO:0000255|HAMAP-Rule:MF_03184	
+P16861	UniProtKB	Binding site	391	391	.	.	.	Note=Substrate%3B shared with subunit beta;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Binding site	455	455	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Binding site	482	482	.	.	.	Note=Substrate%3B shared with subunit beta;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Binding site	665	665	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Binding site	760	760	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate%3B shared with subunit beta;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Binding site	827	827	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Binding site	853	853	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate%3B shared with subunit beta;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Binding site	952	952	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16861	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P16861	UniProtKB	Modified residue	166	166	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P16861	UniProtKB	Modified residue	179	179	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P16861	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P16861	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P16861	UniProtKB	Modified residue	192	192	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P16861	UniProtKB	Modified residue	217	217	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P16861	UniProtKB	Modified residue	450	450	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P16861	UniProtKB	Cross-link	89	89	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P16861	UniProtKB	Cross-link	625	625	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P16861	UniProtKB	Mutagenesis	309	309	.	.	.	Note=Reduces maximal activity of the holoenzyme by 50%25. Completely abolishes catalytic activity%3B when associated with 'S-348' in subunit beta. D->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627	
+P16861	UniProtKB	Mutagenesis	356	356	.	.	.	Note=Reduces maximal activity of the holoenzyme by 50%25. Completely abolishes catalytic activity%3B when associated with 'S-348' in subunit beta. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627	
+P16861	UniProtKB	Mutagenesis	447	447	.	.	.	Note=Reduces maximal activity of the holoenzyme by less than 25%25. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627	
+P16861	UniProtKB	Mutagenesis	488	488	.	.	.	Note=Increases the KM for fructose 6-phosphate 20 fold. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627	
+P16861	UniProtKB	Mutagenesis	724	724	.	.	.	Note=Abolishes sensitivity of the holoenzyme to fructose 2%2C6-bisphosphate activation%3B when associated with 'D-718' in subunit beta. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663166;Dbxref=PMID:8663166	
+P16861	UniProtKB	Mutagenesis	728	728	.	.	.	Note=Drastically reduces sensitivity of the holoenzyme to ATP inhibition. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11221662;Dbxref=PMID:11221662	
+P16861	UniProtKB	Mutagenesis	859	859	.	.	.	Note=Reduces sensitivity of the holoenzyme to fructose 2%2C6-bisphosphate activation%3B when associated with 'S-853' in subunit beta. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663166;Dbxref=PMID:8663166	
+P16861	UniProtKB	Beta strand	207	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	220	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	237	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	244	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	254	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	260	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	266	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	281	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	285	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	300	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	309	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	322	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	331	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Turn	337	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	347	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	368	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	392	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	404	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	416	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	421	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Turn	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	430	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	449	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	467	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	481	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	487	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	497	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	524	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	538	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	557	562	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	568	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	595	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	608	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	625	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	632	639	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	642	644	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Turn	647	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	653	655	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	668	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	672	681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	685	692	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	693	705	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Turn	706	708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	710	713	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	716	721	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	736	757	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	758	766	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	773	780	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Turn	781	783	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	785	788	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	790	792	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	796	812	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	821	826	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	831	833	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	835	846	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	849	856	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	858	862	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	868	890	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	921	923	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	924	930	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	933	938	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	939	942	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Turn	948	951	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Beta strand	953	955	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	960	969	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16861	UniProtKB	Helix	972	978	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+##sequence-region P16862 1 959
+P16862	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8223596;Dbxref=PMID:8223596	
+P16862	UniProtKB	Chain	2	959	.	.	.	ID=PRO_0000112046;Note=ATP-dependent 6-phosphofructokinase subunit beta	
+P16862	UniProtKB	Nucleotide binding	270	271	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184	
+P16862	UniProtKB	Nucleotide binding	300	303	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184	
+P16862	UniProtKB	Region	2	573	.	.	.	Note=N-terminal catalytic PFK domain 1;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Region	346	348	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Region	390	392	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Region	481	484	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Region	574	587	.	.	.	Note=Interdomain linker;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Region	588	959	.	.	.	Note=C-terminal regulatory PFK domain 2;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Region	716	720	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Region	761	763	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Region	853	856	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Active site	348	348	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184	
+P16862	UniProtKB	Metal binding	301	301	.	.	.	Note=Magnesium%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184	
+P16862	UniProtKB	Binding site	206	206	.	.	.	Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184	
+P16862	UniProtKB	Binding site	383	383	.	.	.	Note=Substrate%3B shared with subunit alpha;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Binding site	447	447	.	.	.	Note=Substrate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Binding site	475	475	.	.	.	Note=Substrate%3B shared with subunit alpha;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Binding site	658	658	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Binding site	754	754	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate%3B shared with subunit alpha;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184	
+P16862	UniProtKB	Binding site	847	847	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate%3B shared with subunit alpha;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184	
+P16862	UniProtKB	Binding site	935	935	.	.	.	Note=Allosteric activator fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708	
+P16862	UniProtKB	Modified residue	152	152	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P16862	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P16862	UniProtKB	Modified residue	171	171	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P16862	UniProtKB	Modified residue	803	803	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P16862	UniProtKB	Mutagenesis	301	301	.	.	.	Note=Reduces maximal activity of the holoenzyme by 30%25. D->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627	
+P16862	UniProtKB	Mutagenesis	348	348	.	.	.	Note=Reduces maximal activity of the holoenzyme by 50%25. Completely abolishes catalytic activity%3B when associated with 'T-309' or 'S-356' in subunit alpha. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627	
+P16862	UniProtKB	Mutagenesis	439	439	.	.	.	Note=Reduces maximal activity of the holoenzyme by less than 25%25. R->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627	
+P16862	UniProtKB	Mutagenesis	481	481	.	.	.	Note=Increases the KM for fructose 6-phosphate 50 fold. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627	
+P16862	UniProtKB	Mutagenesis	718	718	.	.	.	Note=Abolishes sensitivity of the holoenzyme to fructose 2%2C6-bisphosphate activation%3B when associated with 'D-724' in subunit alpha. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663166;Dbxref=PMID:8663166	
+P16862	UniProtKB	Mutagenesis	722	722	.	.	.	Note=Drastically reduces sensitivity of the holoenzyme to ATP inhibition. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11221662;Dbxref=PMID:11221662	
+P16862	UniProtKB	Mutagenesis	853	853	.	.	.	Note=Reduces sensitivity of the holoenzyme to fructose 2%2C6-bisphosphate activation%3B when associated with 'S-859' in subunit alpha. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663166;Dbxref=PMID:8663166	
+P16862	UniProtKB	Sequence conflict	137	137	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16862	UniProtKB	Sequence conflict	880	880	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16862	UniProtKB	Beta strand	198	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	211	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	228	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	235	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Turn	244	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	247	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	252	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	277	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	294	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	301	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	329	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	339	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	360	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	384	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	396	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	408	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	421	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	441	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	459	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	474	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	480	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	490	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	517	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	526	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	531	546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	550	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	561	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	581	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	588	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	601	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	618	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	625	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	635	637	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	640	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	646	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	661	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	666	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	679	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	687	697	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Turn	698	702	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	704	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	712	715	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	730	751	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	752	760	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	767	776	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	779	782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Turn	784	786	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	790	807	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	815	820	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	821	823	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	829	840	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	845	850	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	852	856	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	862	881	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	884	889	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	890	894	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	901	904	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	907	911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	913	915	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	918	921	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	922	928	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	932	934	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Beta strand	935	939	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+P16862	UniProtKB	Helix	943	952	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O	
+##sequence-region P00560 1 416
+P00560	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P00560	UniProtKB	Chain	2	416	.	.	.	ID=PRO_0000145893;Note=Phosphoglycerate kinase	
+P00560	UniProtKB	Nucleotide binding	371	374	.	.	.	Note=ATP	
+P00560	UniProtKB	Region	24	26	.	.	.	Note=Substrate binding	
+P00560	UniProtKB	Region	63	66	.	.	.	Note=Substrate binding	
+P00560	UniProtKB	Binding site	39	39	.	.	.	Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6765200,ECO:0000269|PubMed:8672447;Dbxref=PMID:6765200,PMID:8672447	
+P00560	UniProtKB	Binding site	122	122	.	.	.	Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6765200,ECO:0000269|PubMed:8672447;Dbxref=PMID:6765200,PMID:8672447	
+P00560	UniProtKB	Binding site	169	169	.	.	.	Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6765200,ECO:0000269|PubMed:8672447;Dbxref=PMID:6765200,PMID:8672447	
+P00560	UniProtKB	Binding site	218	218	.	.	.	Note=ATP	
+P00560	UniProtKB	Binding site	311	311	.	.	.	Note=ATP%3B via carbonyl oxygen	
+P00560	UniProtKB	Binding site	335	335	.	.	.	Note=ATP	
+P00560	UniProtKB	Binding site	342	342	.	.	.	Note=ATP	
+P00560	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P00560	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00560	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00560	UniProtKB	Modified residue	130	130	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00560	UniProtKB	Modified residue	154	154	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P00560	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00560	UniProtKB	Modified residue	203	203	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00560	UniProtKB	Modified residue	241	241	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00560	UniProtKB	Modified residue	298	298	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00560	UniProtKB	Modified residue	318	318	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00560	UniProtKB	Modified residue	331	331	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P00560	UniProtKB	Modified residue	392	392	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P00560	UniProtKB	Cross-link	82	82	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00560	UniProtKB	Cross-link	197	197	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00560	UniProtKB	Cross-link	258	258	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00560	UniProtKB	Cross-link	274	274	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00560	UniProtKB	Cross-link	302	302	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00560	UniProtKB	Mutagenesis	22	22	.	.	.	Note=2-fold reduction of Vmax. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1628654;Dbxref=PMID:1628654	
+P00560	UniProtKB	Mutagenesis	22	22	.	.	.	Note=7-fold reduction of Vmax. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1628654;Dbxref=PMID:1628654	
+P00560	UniProtKB	Sequence conflict	185	185	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00560	UniProtKB	Sequence conflict	191	191	.	.	.	Note=E->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00560	UniProtKB	Helix	9	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG	
+P00560	UniProtKB	Beta strand	18	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG	
+P00560	UniProtKB	Beta strand	29	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG	
+P00560	UniProtKB	Helix	38	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG	
+P00560	UniProtKB	Beta strand	56	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG	
+P00560	UniProtKB	Beta strand	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGK	
+P00560	UniProtKB	Helix	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG	
+P00560	UniProtKB	Helix	78	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	101	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGK	
+P00560	UniProtKB	Beta strand	114	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Turn	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	129	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	136	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	142	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	157	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	172	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	182	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	186	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	204	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Turn	216	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	219	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	230	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	239	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	247	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGK	
+P00560	UniProtKB	Helix	258	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	277	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	282	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	296	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Turn	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	304	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGK	
+P00560	UniProtKB	Beta strand	310	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	316	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	330	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	344	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	348	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	366	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	373	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	384	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Beta strand	387	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	395	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+P00560	UniProtKB	Helix	407	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8	
+##sequence-region P33401 1 570
+P33401	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P33401	UniProtKB	Chain	2	570	.	.	.	ID=PRO_0000147796;Note=Phosphoglucomutase 1	
+P33401	UniProtKB	Region	120	121	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Region	295	296	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Region	379	381	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Active site	120	120	.	.	.	Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Metal binding	120	120	.	.	.	Note=Magnesium%3B via phosphate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Metal binding	291	291	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Metal binding	293	293	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Metal binding	295	295	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Binding site	20	20	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Binding site	24	24	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Binding site	133	133	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Binding site	360	360	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Binding site	392	392	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Binding site	523	523	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949	
+P33401	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P33401	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P0CE93 1 120
+P0CE93	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE93	UniProtKB	Chain	21	120	.	.	.	ID=PRO_0000392928;Note=Seripauperin-11	
+##sequence-region P40585 1 124
+P40585	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40585	UniProtKB	Chain	21	124	.	.	.	ID=PRO_0000033246;Note=Seripauperin-15	
+##sequence-region P0CE85 1 124
+P0CE85	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CE85	UniProtKB	Chain	21	124	.	.	.	ID=PRO_0000033249;Note=Seripauperin-19	
+P0CE85	UniProtKB	Sequence conflict	18	18	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CE86 1 164
+P0CE86	UniProtKB	Chain	1	164	.	.	.	ID=PRO_0000392931;Note=Seripauperin-21	
+P0CE86	UniProtKB	Alternative sequence	1	40	.	.	.	ID=VSP_038855;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CE86	UniProtKB	Sequence conflict	24	26	.	.	.	Note=HFF->PSL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32612 1 120
+P32612	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000203779;Note=Seripauperin-2	
+P32612	UniProtKB	Transmembrane	7	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43575 1 122
+P43575	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000203782;Note=Seripauperin-5	
+P43575	UniProtKB	Transmembrane	7	24	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E770 1 120
+Q3E770	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E770	UniProtKB	Chain	21	120	.	.	.	ID=PRO_0000248410;Note=Seripauperin-9	
+##sequence-region Q3E833 1 88
+Q3E833	UniProtKB	Chain	1	88	.	.	.	ID=PRO_0000245368;Note=EKC/KEOPS complex subunit PCC1	
+Q3E833	UniProtKB	Beta strand	11	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA	
+Q3E833	UniProtKB	Helix	22	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA	
+Q3E833	UniProtKB	Turn	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA	
+Q3E833	UniProtKB	Beta strand	43	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA	
+Q3E833	UniProtKB	Beta strand	53	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA	
+Q3E833	UniProtKB	Helix	63	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA	
+##sequence-region P16467 1 563
+P16467	UniProtKB	Chain	1	563	.	.	.	ID=PRO_0000090771;Note=Pyruvate decarboxylase isozyme 2	
+P16467	UniProtKB	Region	390	476	.	.	.	Note=Thiamine pyrophosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16467	UniProtKB	Metal binding	444	444	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16467	UniProtKB	Metal binding	471	471	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16467	UniProtKB	Metal binding	473	473	.	.	.	Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16467	UniProtKB	Binding site	28	28	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16467	UniProtKB	Binding site	115	115	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16467	UniProtKB	Binding site	157	157	.	.	.	Note=Substrate%3B allosteric site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16467	UniProtKB	Binding site	477	477	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16467	UniProtKB	Sequence conflict	35	35	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16467	UniProtKB	Sequence conflict	143	143	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16467	UniProtKB	Sequence conflict	207	207	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16467	UniProtKB	Sequence conflict	222	222	.	.	.	Note=A->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16467	UniProtKB	Sequence conflict	341	341	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16467	UniProtKB	Sequence conflict	373	373	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P10834 1 293
+P10834	UniProtKB	Chain	1	293	.	.	.	ID=PRO_0000058319;Note=Protein PET54	
+##sequence-region Q05568 1 337
+Q05568	UniProtKB	Chain	1	337	.	.	.	ID=PRO_0000056381;Note=Peroxisome biogenesis factor 10	
+Q05568	UniProtKB	Zinc finger	286	327	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q05568	UniProtKB	Sequence conflict	183	183	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38244 1 976
+P38244	UniProtKB	Chain	1	976	.	.	.	ID=PRO_0000174140;Note=Vacuolar membrane protease	
+P38244	UniProtKB	Topological domain	1	15	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23679341;Dbxref=PMID:23679341	
+P38244	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38244	UniProtKB	Topological domain	37	359	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23679341;Dbxref=PMID:23679341	
+P38244	UniProtKB	Transmembrane	360	380	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38244	UniProtKB	Topological domain	381	392	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341	
+P38244	UniProtKB	Transmembrane	393	412	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38244	UniProtKB	Topological domain	413	428	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341	
+P38244	UniProtKB	Transmembrane	429	449	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38244	UniProtKB	Topological domain	450	461	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341	
+P38244	UniProtKB	Transmembrane	462	482	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38244	UniProtKB	Topological domain	483	496	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341	
+P38244	UniProtKB	Transmembrane	497	517	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38244	UniProtKB	Topological domain	518	627	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341	
+P38244	UniProtKB	Transmembrane	628	648	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38244	UniProtKB	Topological domain	649	668	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341	
+P38244	UniProtKB	Transmembrane	669	689	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38244	UniProtKB	Topological domain	690	692	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341	
+P38244	UniProtKB	Transmembrane	693	713	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38244	UniProtKB	Topological domain	714	976	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23679341;Dbxref=PMID:23679341	
+P38244	UniProtKB	Active site	200	200	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P38244	UniProtKB	Metal binding	156	156	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P38244	UniProtKB	Metal binding	168	168	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P38244	UniProtKB	Metal binding	168	168	.	.	.	Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P38244	UniProtKB	Metal binding	201	201	.	.	.	Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P38244	UniProtKB	Metal binding	226	226	.	.	.	Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P38244	UniProtKB	Metal binding	300	300	.	.	.	Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P38244	UniProtKB	Site	299	299	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561	
+P38244	UniProtKB	Glycosylation	96	96	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P38244	UniProtKB	Glycosylation	121	121	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P38244	UniProtKB	Glycosylation	189	189	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P38244	UniProtKB	Glycosylation	217	217	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P38244	UniProtKB	Glycosylation	656	656	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P38244	UniProtKB	Glycosylation	768	768	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P38244	UniProtKB	Glycosylation	796	796	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P38244	UniProtKB	Glycosylation	811	811	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P38244	UniProtKB	Glycosylation	866	866	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P38244	UniProtKB	Glycosylation	937	937	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+P38244	UniProtKB	Sequence conflict	832	832	.	.	.	Note=N->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38244	UniProtKB	Sequence conflict	832	832	.	.	.	Note=N->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P42841 1 465
+P42841	UniProtKB	Chain	1	465	.	.	.	ID=PRO_0000051122;Note=Polyadenylation factor subunit 2	
+P42841	UniProtKB	Repeat	133	163	.	.	.	Note=WD 1	
+P42841	UniProtKB	Repeat	175	205	.	.	.	Note=WD 2	
+P42841	UniProtKB	Repeat	217	247	.	.	.	Note=WD 3	
+P42841	UniProtKB	Repeat	259	290	.	.	.	Note=WD 4	
+P42841	UniProtKB	Repeat	348	378	.	.	.	Note=WD 5	
+P42841	UniProtKB	Sequence conflict	2	2	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q00618 1 327
+Q00618	UniProtKB	Chain	1	327	.	.	.	ID=PRO_0000119756;Note=Geranylgeranyl transferase type-2 subunit alpha	
+Q00618	UniProtKB	Repeat	44	78	.	.	.	Note=PFTA 1	
+Q00618	UniProtKB	Repeat	84	118	.	.	.	Note=PFTA 2	
+Q00618	UniProtKB	Repeat	123	157	.	.	.	Note=PFTA 3	
+Q00618	UniProtKB	Repeat	163	197	.	.	.	Note=PFTA 4	
+Q00618	UniProtKB	Repeat	207	241	.	.	.	Note=PFTA 5	
+##sequence-region P20133 1 325
+P20133	UniProtKB	Chain	1	325	.	.	.	ID=PRO_0000119777;Note=Geranylgeranyl transferase type-2 subunit beta	
+P20133	UniProtKB	Repeat	9	50	.	.	.	Note=PFTB 1	
+P20133	UniProtKB	Repeat	57	99	.	.	.	Note=PFTB 2	
+P20133	UniProtKB	Repeat	109	150	.	.	.	Note=PFTB 3	
+P20133	UniProtKB	Repeat	157	198	.	.	.	Note=PFTB 4	
+P20133	UniProtKB	Repeat	208	249	.	.	.	Note=PFTB 5	
+P20133	UniProtKB	Repeat	256	298	.	.	.	Note=PFTB 6	
+P20133	UniProtKB	Region	183	185	.	.	.	Note=Geranylgeranyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20133	UniProtKB	Region	228	240	.	.	.	Note=Geranylgeranyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20133	UniProtKB	Metal binding	234	234	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20133	UniProtKB	Metal binding	234	234	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20133	UniProtKB	Metal binding	236	236	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20133	UniProtKB	Metal binding	236	236	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20133	UniProtKB	Metal binding	286	286	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20133	UniProtKB	Metal binding	286	286	.	.	.	Note=Zinc%3B via tele nitrogen%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20133	UniProtKB	Sequence conflict	22	22	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20133	UniProtKB	Sequence conflict	22	22	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38744 1 120
+P38744	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000063064;Note=Putative pterin-4-alpha-carbinolamine dehydratase	
+##sequence-region P39104 1 1066
+P39104	UniProtKB	Chain	1	1066	.	.	.	ID=PRO_0000088834;Note=Phosphatidylinositol 4-kinase PIK1	
+P39104	UniProtKB	Domain	1	133	.	.	.	Note=PIK helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00878	
+P39104	UniProtKB	Domain	793	1041	.	.	.	Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269	
+P39104	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P39104	UniProtKB	Modified residue	236	236	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P39104	UniProtKB	Modified residue	384	384	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39104	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39104	UniProtKB	Modified residue	396	396	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39104	UniProtKB	Modified residue	592	592	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39104	UniProtKB	Helix	126	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JU0	
+P39104	UniProtKB	Helix	156	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JU0	
+##sequence-region P53252 1 339
+P53252	UniProtKB	Chain	1	339	.	.	.	ID=PRO_0000058441;Note=Sphingolipid long chain base-responsive protein PIL1	
+P53252	UniProtKB	Compositional bias	21	25	.	.	.	Note=Poly-Pro	
+P53252	UniProtKB	Compositional bias	279	323	.	.	.	Note=Glu-rich	
+P53252	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53252	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53252	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53252	UniProtKB	Modified residue	98	98	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53252	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53252	UniProtKB	Modified residue	230	230	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53252	UniProtKB	Modified residue	233	233	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198	
+P53252	UniProtKB	Modified residue	299	299	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53252	UniProtKB	Cross-link	29	29	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q03178 1 341
+Q03178	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9301021;Dbxref=PMID:9301021	
+Q03178	UniProtKB	Propeptide	19	63	.	.	.	ID=PRO_0000033254;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9301021;Dbxref=PMID:9301021	
+Q03178	UniProtKB	Chain	64	341	.	.	.	ID=PRO_0000033255;Note=Cell wall mannoprotein PIR1	
+Q03178	UniProtKB	Repeat	64	82	.	.	.	Note=PIR1/2/3 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03178	UniProtKB	Repeat	83	101	.	.	.	Note=PIR1/2/3 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03178	UniProtKB	Repeat	102	125	.	.	.	Note=PIR1/2/3 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03178	UniProtKB	Repeat	126	144	.	.	.	Note=PIR1/2/3 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03178	UniProtKB	Repeat	145	163	.	.	.	Note=PIR1/2/3 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03178	UniProtKB	Repeat	164	182	.	.	.	Note=PIR1/2/3 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03178	UniProtKB	Repeat	183	201	.	.	.	Note=PIR1/2/3 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03178	UniProtKB	Repeat	202	220	.	.	.	Note=PIR1/2/3 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03178	UniProtKB	Site	63	64	.	.	.	Note=Cleavage%3B by KEX2	
+Q03178	UniProtKB	Site	74	74	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03178	UniProtKB	Site	93	93	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03178	UniProtKB	Site	112	112	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03178	UniProtKB	Site	136	136	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03178	UniProtKB	Site	155	155	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03178	UniProtKB	Site	174	174	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03178	UniProtKB	Site	193	193	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03178	UniProtKB	Site	212	212	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03180 1 325
+Q03180	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9301021;Dbxref=PMID:9301021	
+Q03180	UniProtKB	Propeptide	19	67	.	.	.	ID=PRO_0000033256;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8314797;Dbxref=PMID:8314797	
+Q03180	UniProtKB	Chain	68	325	.	.	.	ID=PRO_0000033257;Note=Cell wall mannoprotein PIR3	
+Q03180	UniProtKB	Repeat	68	91	.	.	.	Note=PIR1/2/3 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03180	UniProtKB	Repeat	92	109	.	.	.	Note=PIR1/2/3 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03180	UniProtKB	Repeat	110	127	.	.	.	Note=PIR1/2/3 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03180	UniProtKB	Repeat	128	145	.	.	.	Note=PIR1/2/3 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03180	UniProtKB	Repeat	146	163	.	.	.	Note=PIR1/2/3 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03180	UniProtKB	Repeat	164	181	.	.	.	Note=PIR1/2/3 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03180	UniProtKB	Repeat	182	199	.	.	.	Note=PIR1/2/3 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03180	UniProtKB	Repeat	200	217	.	.	.	Note=PIR1/2/3 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q03180	UniProtKB	Site	67	68	.	.	.	Note=Cleavage%3B by KEX2	
+Q03180	UniProtKB	Site	76	76	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03180	UniProtKB	Site	102	102	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03180	UniProtKB	Site	120	120	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03180	UniProtKB	Site	138	138	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03180	UniProtKB	Site	156	156	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03180	UniProtKB	Site	174	174	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03180	UniProtKB	Site	192	192	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03180	UniProtKB	Site	209	209	.	.	.	Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03180	UniProtKB	Natural variant	113	113	.	.	.	Note=In strain: RAY-3AD. V->A	
+Q03180	UniProtKB	Natural variant	117	117	.	.	.	Note=In strain: RAY-3AD. T->S	
+Q03180	UniProtKB	Natural variant	144	144	.	.	.	Note=In strain: RAY-3AD. S->STAAAVSQITDGQVQAAKSTAAAASQISDGQVQAAKS	
+##sequence-region P06197 1 220
+P06197	UniProtKB	Chain	1	220	.	.	.	ID=PRO_0000056807;Note=CDP-diacylglycerol--inositol 3-phosphatidyltransferase	
+P06197	UniProtKB	Topological domain	1	20	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P06197	UniProtKB	Transmembrane	21	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06197	UniProtKB	Topological domain	42	45	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P06197	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06197	UniProtKB	Topological domain	67	75	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P06197	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06197	UniProtKB	Topological domain	97	98	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P06197	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06197	UniProtKB	Topological domain	120	145	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P06197	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06197	UniProtKB	Topological domain	167	170	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P06197	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06197	UniProtKB	Topological domain	192	220	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+##sequence-region Q12236 1 1081
+Q12236	UniProtKB	Chain	1	1081	.	.	.	ID=PRO_0000086158;Note=Serine/threonine-protein kinase PKH2	
+Q12236	UniProtKB	Domain	179	443	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12236	UniProtKB	Nucleotide binding	189	191	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q12236	UniProtKB	Nucleotide binding	258	260	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q12236	UniProtKB	Region	210	255	.	.	.	Note=PIF-pocket;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q12236	UniProtKB	Active site	303	303	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q12236	UniProtKB	Binding site	208	208	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q12236	UniProtKB	Binding site	264	264	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q12236	UniProtKB	Binding site	307	307	.	.	.	Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q12236	UniProtKB	Binding site	321	321	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530	
+Q12236	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12236	UniProtKB	Modified residue	619	619	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12236	UniProtKB	Modified residue	1009	1009	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q03880 1 122
+Q03880	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000203297;Note=V-type ATPase assembly factor PKR1	
+Q03880	UniProtKB	Topological domain	1	20	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03880	UniProtKB	Transmembrane	21	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03880	UniProtKB	Topological domain	42	46	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03880	UniProtKB	Transmembrane	47	67	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03880	UniProtKB	Topological domain	68	122	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P52960 1 996
+P52960	UniProtKB	Chain	1	996	.	.	.	ID=PRO_0000114964;Note=Peroxisome proliferation transcriptional regulator	
+P52960	UniProtKB	DNA binding	25	52	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P52960	UniProtKB	Motif	985	993	.	.	.	Note=9aaTAD	
+##sequence-region Q04383 1 521
+Q04383	UniProtKB	Chain	1	521	.	.	.	ID=PRO_0000262747;Note=Protein PLM2	
+Q04383	UniProtKB	Domain	102	156	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+Q04383	UniProtKB	Modified residue	281	281	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04383	UniProtKB	Modified residue	295	295	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+Q04383	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04383	UniProtKB	Modified residue	384	384	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38197 1 257
+P38197	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38197	UniProtKB	Chain	2	257	.	.	.	ID=PRO_0000163213;Note=Pyridoxal phosphate homeostasis protein	
+P38197	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38197	UniProtKB	Modified residue	49	49	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03225,ECO:0000269|PubMed:12499548;Dbxref=PMID:12499548	
+P38197	UniProtKB	Sequence conflict	8	8	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38197	UniProtKB	Helix	9	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Beta strand	43	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Helix	53	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Beta strand	66	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Helix	72	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Beta strand	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Helix	99	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Beta strand	108	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Helix	117	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Beta strand	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1B54	
+P38197	UniProtKB	Beta strand	137	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Beta strand	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Beta strand	151	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Helix	157	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Beta strand	174	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Helix	197	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Beta strand	218	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Turn	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Helix	227	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Beta strand	236	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+P38197	UniProtKB	Helix	242	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5	
+##sequence-region Q07930 1 204
+Q07930	UniProtKB	Chain	1	204	.	.	.	ID=PRO_0000058466;Note=Pre-mRNA leakage protein 1	
+Q07930	UniProtKB	Domain	104	172	.	.	.	Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086	
+Q07930	UniProtKB	Sequence conflict	15	15	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q07930	UniProtKB	Helix	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC	
+Q07930	UniProtKB	Helix	61	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+Q07930	UniProtKB	Helix	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+Q07930	UniProtKB	Beta strand	78	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+Q07930	UniProtKB	Helix	85	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+Q07930	UniProtKB	Beta strand	93	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+Q07930	UniProtKB	Beta strand	102	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+Q07930	UniProtKB	Beta strand	128	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+Q07930	UniProtKB	Beta strand	141	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+Q07930	UniProtKB	Beta strand	151	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+Q07930	UniProtKB	Beta strand	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JKD	
+Q07930	UniProtKB	Beta strand	184	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+Q07930	UniProtKB	Helix	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+Q07930	UniProtKB	Beta strand	197	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS	
+##sequence-region Q12412 1 539
+Q12412	UniProtKB	Chain	1	539	.	.	.	ID=PRO_0000191740;Note=Protein PNS1	
+Q12412	UniProtKB	Topological domain	1	81	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Topological domain	103	129	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Transmembrane	130	150	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Topological domain	151	157	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Transmembrane	158	178	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Topological domain	179	182	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Topological domain	204	226	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Transmembrane	227	247	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Topological domain	248	274	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Transmembrane	275	295	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Topological domain	296	332	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Transmembrane	333	353	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Topological domain	354	371	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Topological domain	393	436	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Transmembrane	437	457	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Topological domain	458	473	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Transmembrane	474	494	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Topological domain	495	539	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Glycosylation	259	259	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12412	UniProtKB	Sequence conflict	181	181	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07951 1 179
+Q07951	UniProtKB	Chain	1	179	.	.	.	ID=PRO_0000247202;Note=Proteasome chaperone 3	
+Q07951	UniProtKB	Beta strand	3	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q07951	UniProtKB	Beta strand	26	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q07951	UniProtKB	Beta strand	38	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q07951	UniProtKB	Beta strand	50	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q07951	UniProtKB	Helix	84	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q07951	UniProtKB	Beta strand	95	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q07951	UniProtKB	Helix	109	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q07951	UniProtKB	Beta strand	140	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q07951	UniProtKB	Helix	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q07951	UniProtKB	Helix	162	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+##sequence-region P25576 1 258
+P25576	UniProtKB	Chain	1	258	.	.	.	ID=PRO_0000202549;Note=Nicotinamide mononucleotide adenylyltransferase	
+P25576	UniProtKB	Nucleotide binding	34	36	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66	
+P25576	UniProtKB	Nucleotide binding	138	140	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66	
+P25576	UniProtKB	Nucleotide binding	224	227	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66	
+P25576	UniProtKB	Binding site	43	43	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66	
+##sequence-region Q04049 1 632
+Q04049	UniProtKB	Chain	1	632	.	.	.	ID=PRO_0000268698;Note=DNA polymerase eta	
+Q04049	UniProtKB	Domain	26	309	.	.	.	Note=UmuC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00216	
+Q04049	UniProtKB	Region	625	632	.	.	.	Note=POL30-binding	
+Q04049	UniProtKB	Metal binding	30	30	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00216	
+Q04049	UniProtKB	Metal binding	155	155	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00216	
+Q04049	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Abolishes DNA polymerase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238937;Dbxref=PMID:11238937	
+Q04049	UniProtKB	Mutagenesis	34	34	.	.	.	Note=Alters translesion activity. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15024063;Dbxref=PMID:15024063	
+Q04049	UniProtKB	Mutagenesis	39	39	.	.	.	Note=Abolishes DNA polymerase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238937;Dbxref=PMID:11238937	
+Q04049	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Decreases efficiency of nucleotide incorporation. Y->F%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665597;Dbxref=PMID:12665597	
+Q04049	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Decreases efficiency of nucleotide incorporation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665597;Dbxref=PMID:12665597	
+Q04049	UniProtKB	Mutagenesis	155	155	.	.	.	Note=Abolishes DNA polymerase activity and increases UV-induced mutations. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238937;Dbxref=PMID:11238937	
+Q04049	UniProtKB	Mutagenesis	156	156	.	.	.	Note=Decreases efficiency of nucleotide incorporation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238937;Dbxref=PMID:11238937	
+Q04049	UniProtKB	Mutagenesis	279	279	.	.	.	Note=Decreases efficiency of nucleotide incorporation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665597;Dbxref=PMID:12665597	
+Q04049	UniProtKB	Mutagenesis	627	627	.	.	.	Note=Abolishes POL30-binding%3B when associated with A-628. F->A	
+Q04049	UniProtKB	Mutagenesis	628	628	.	.	.	Note=Abolishes POL30-binding%3B when associated with A-627. F->A	
+Q04049	UniProtKB	Beta strand	1	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	6	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Turn	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R8K	
+Q04049	UniProtKB	Beta strand	26	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	34	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	51	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	58	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Turn	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	77	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	88	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	100	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OHB	
+Q04049	UniProtKB	Helix	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OHA	
+Q04049	UniProtKB	Beta strand	123	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	129	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	149	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	156	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	162	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	188	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	203	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	210	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	219	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	233	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	260	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	268	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Turn	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JIH	
+Q04049	UniProtKB	Beta strand	280	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	288	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	291	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	302	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JIH	
+Q04049	UniProtKB	Helix	311	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	324	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	327	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	339	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	352	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WTF	
+Q04049	UniProtKB	Turn	357	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OHA	
+Q04049	UniProtKB	Helix	364	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFH	
+Q04049	UniProtKB	Helix	367	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Turn	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	395	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Turn	403	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	409	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	436	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	454	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	466	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Helix	469	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Turn	488	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+Q04049	UniProtKB	Beta strand	497	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI	
+##sequence-region Q12445 1 299
+Q12445	UniProtKB	Chain	1	299	.	.	.	ID=PRO_0000204911;Note=Nucleoporin POM34	
+Q12445	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12445	UniProtKB	Transmembrane	133	153	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12445	UniProtKB	Modified residue	270	270	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12445	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12445	UniProtKB	Modified residue	292	292	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12445	UniProtKB	Modified residue	294	294	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:18407956,PMID:19779198	
+Q12445	UniProtKB	Sequence conflict	191	191	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P28005 1 173
+P28005	UniProtKB	Chain	1	173	.	.	.	ID=PRO_0000140015;Note=Ribonuclease P/MRP protein subunit POP5	
+##sequence-region P23287 1 553
+P23287	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P23287	UniProtKB	Chain	2	553	.	.	.	ID=PRO_0000058836;Note=Serine/threonine-protein phosphatase 2B catalytic subunit A1	
+P23287	UniProtKB	Active site	180	180	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23287	UniProtKB	Metal binding	119	119	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23287	UniProtKB	Metal binding	121	121	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23287	UniProtKB	Metal binding	147	147	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23287	UniProtKB	Metal binding	147	147	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23287	UniProtKB	Metal binding	179	179	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23287	UniProtKB	Metal binding	228	228	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23287	UniProtKB	Metal binding	317	317	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23287	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P23287	UniProtKB	Natural variant	45	46	.	.	.	Note=In strain: S288c / GRF88. PI->SY	
+P23287	UniProtKB	Helix	455	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LHI	
+P23287	UniProtKB	Helix	460	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LHI	
+##sequence-region P39966 1 464
+P39966	UniProtKB	Chain	1	464	.	.	.	ID=PRO_0000057775;Note=Protein phosphatase 2C homolog 2	
+P39966	UniProtKB	Domain	23	292	.	.	.	Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082	
+P39966	UniProtKB	Metal binding	62	62	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39966	UniProtKB	Metal binding	62	62	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39966	UniProtKB	Metal binding	63	63	.	.	.	Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39966	UniProtKB	Metal binding	234	234	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39966	UniProtKB	Metal binding	283	283	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39966	UniProtKB	Modified residue	376	376	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39966	UniProtKB	Modified residue	380	380	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53691 1 371
+P53691	UniProtKB	Chain	1	371	.	.	.	ID=PRO_0000064173;Note=Peptidyl-prolyl cis-trans isomerase CPR6	
+P53691	UniProtKB	Domain	7	174	.	.	.	Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156	
+P53691	UniProtKB	Repeat	219	252	.	.	.	Note=TPR 1	
+P53691	UniProtKB	Repeat	270	303	.	.	.	Note=TPR 2	
+P53691	UniProtKB	Repeat	308	341	.	.	.	Note=TPR 3	
+P53691	UniProtKB	Sequence conflict	12	12	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12326 1 303
+Q12326	UniProtKB	Chain	1	303	.	.	.	ID=PRO_0000179841;Note=Phosphoglycerate mutase 3	
+Q12326	UniProtKB	Region	13	20	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12326	UniProtKB	Region	26	27	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12326	UniProtKB	Region	120	123	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12326	UniProtKB	Region	147	148	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12326	UniProtKB	Region	236	237	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12326	UniProtKB	Active site	14	14	.	.	.	Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12326	UniProtKB	Active site	120	120	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12326	UniProtKB	Binding site	70	70	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12326	UniProtKB	Binding site	131	131	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12326	UniProtKB	Site	235	235	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+##sequence-region Q02890 1 363
+Q02890	UniProtKB	Chain	1	363	.	.	.	ID=PRO_0000248996;Note=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase	
+Q02890	UniProtKB	Active site	191	191	.	.	.	Note=Nucleophile	
+Q02890	UniProtKB	Active site	218	218	.	.	.	.	
+Q02890	UniProtKB	Active site	235	235	.	.	.	.	
+Q02890	UniProtKB	Metal binding	129	129	.	.	.	Note=Zinc	
+Q02890	UniProtKB	Metal binding	132	132	.	.	.	Note=Zinc	
+Q02890	UniProtKB	Metal binding	165	165	.	.	.	Note=Zinc	
+Q02890	UniProtKB	Metal binding	168	168	.	.	.	Note=Zinc	
+Q02890	UniProtKB	Binding site	238	238	.	.	.	Note=Substrate	
+Q02890	UniProtKB	Mutagenesis	123	123	.	.	.	Note=No effect. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Abolishes enzyme activity. C->A%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	132	132	.	.	.	Note=Abolishes enzyme activity. C->A%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	165	165	.	.	.	Note=Abolishes enzyme activity. C->A%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	168	168	.	.	.	Note=Abolishes enzyme activity. C->A%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	174	174	.	.	.	Note=No effect. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	177	177	.	.	.	Note=No effect. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	187	187	.	.	.	Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	189	189	.	.	.	Note=No effect. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	191	191	.	.	.	Note=Abolishes enzyme activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	194	194	.	.	.	Note=No effect. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	198	198	.	.	.	Note=No effect. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	199	199	.	.	.	Note=No effect. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	203	203	.	.	.	Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	206	206	.	.	.	Note=No effect. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	210	210	.	.	.	Note=Abolishes enzyme activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	212	212	.	.	.	Note=No effect. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	218	218	.	.	.	Note=Abolishes enzyme activity. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10831608,ECO:0000269|PubMed:11812789;Dbxref=PMID:10831608,PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	218	218	.	.	.	Note=In png1-1%3B abolishes enzyme activity. H->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10831608,ECO:0000269|PubMed:11812789;Dbxref=PMID:10831608,PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	220	220	.	.	.	Note=Abolishes enzyme activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	220	220	.	.	.	Note=No effect. W->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	222	222	.	.	.	Note=Abolishes enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	224	224	.	.	.	Note=No effect. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	230	230	.	.	.	Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	231	231	.	.	.	Note=Abolishes enzyme activity. W->A	
+Q02890	UniProtKB	Mutagenesis	231	231	.	.	.	Note=No effect. W->F	
+Q02890	UniProtKB	Mutagenesis	234	234	.	.	.	Note=No effect. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	235	235	.	.	.	Note=Abolishes enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	242	242	.	.	.	Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	251	251	.	.	.	Note=No effect. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	253	253	.	.	.	Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	257	257	.	.	.	Note=Abolishes enzyme activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	261	261	.	.	.	Note=Abolishes enzyme activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	264	264	.	.	.	Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	266	266	.	.	.	Note=No effect. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	268	268	.	.	.	Note=Abolishes enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	273	273	.	.	.	Note=Abolishes enzyme activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	281	281	.	.	.	Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	347	347	.	.	.	Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	354	354	.	.	.	Note=No effect. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Mutagenesis	358	358	.	.	.	Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789	
+Q02890	UniProtKB	Helix	13	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3W	
+Q02890	UniProtKB	Helix	36	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Helix	50	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Helix	69	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Helix	81	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Helix	103	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	138	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Helix	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	154	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Turn	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	171	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Helix	180	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Helix	191	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Turn	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	209	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Turn	215	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	218	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Turn	226	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	230	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Turn	236	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Helix	246	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	258	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	265	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Helix	270	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	275	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Helix	286	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Helix	306	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z	
+Q02890	UniProtKB	Beta strand	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ESW	
+##sequence-region P53833 1 195
+P53833	UniProtKB	Chain	1	195	.	.	.	ID=PRO_0000058516;Note=Ribonucleases P/MRP protein subunit POP3	
+##sequence-region P38208 1 133
+P38208	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000058521;Note=Ribonucleases P/MRP protein subunit POP8	
+##sequence-region P20604 1 311
+P20604	UniProtKB	Chain	1	311	.	.	.	ID=PRO_0000058881;Note=Serine/threonine-protein phosphatase PP1-1	
+P20604	UniProtKB	Active site	115	115	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20604	UniProtKB	Metal binding	53	53	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20604	UniProtKB	Metal binding	55	55	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20604	UniProtKB	Metal binding	82	82	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20604	UniProtKB	Metal binding	82	82	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20604	UniProtKB	Metal binding	114	114	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20604	UniProtKB	Metal binding	164	164	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20604	UniProtKB	Metal binding	238	238	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20604	UniProtKB	Mutagenesis	35	35	.	.	.	Note=Reduced interaction with TAP42. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259	
+P20604	UniProtKB	Mutagenesis	37	38	.	.	.	Note=Nearly no interaction with TAP42. EE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259	
+P20604	UniProtKB	Mutagenesis	38	38	.	.	.	Note=Normal interaction with TAP42. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259	
+P20604	UniProtKB	Mutagenesis	40	40	.	.	.	Note=Normal interaction with TAP42. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259	
+##sequence-region P32345 1 308
+P32345	UniProtKB	Chain	1	308	.	.	.	ID=PRO_0000058875;Note=Serine/threonine-protein phosphatase 4 catalytic subunit	
+P32345	UniProtKB	Active site	112	112	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32345	UniProtKB	Metal binding	51	51	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32345	UniProtKB	Metal binding	53	53	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32345	UniProtKB	Metal binding	79	79	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32345	UniProtKB	Metal binding	79	79	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32345	UniProtKB	Metal binding	111	111	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32345	UniProtKB	Metal binding	161	161	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32345	UniProtKB	Metal binding	235	235	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32345	UniProtKB	Sequence conflict	245	245	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11491 1 566
+P11491	UniProtKB	Topological domain	1	33	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2676517;Dbxref=PMID:2676517	
+P11491	UniProtKB	Transmembrane	34	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P11491	UniProtKB	Active site	123	123	.	.	.	Note=Phosphoserine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10042	
+P11491	UniProtKB	Metal binding	75	75	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11491	UniProtKB	Metal binding	75	75	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11491	UniProtKB	Metal binding	174	174	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11491	UniProtKB	Metal binding	176	176	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11491	UniProtKB	Metal binding	325	325	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11491	UniProtKB	Metal binding	330	330	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11491	UniProtKB	Metal binding	334	334	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11491	UniProtKB	Metal binding	373	373	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11491	UniProtKB	Metal binding	374	374	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11491	UniProtKB	Metal binding	484	484	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P11491	UniProtKB	Modified residue	123	123	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P11491	UniProtKB	Glycosylation	268	268	.	.	.	Note=N-linked (GlcNAc...) asparagine	
+P11491	UniProtKB	Glycosylation	401	401	.	.	.	Note=N-linked (GlcNAc...) asparagine	
+P11491	UniProtKB	Sequence conflict	5	5	.	.	.	Note=T->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11491	UniProtKB	Sequence conflict	55	55	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11491	UniProtKB	Sequence conflict	59	59	.	.	.	Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11491	UniProtKB	Sequence conflict	132	132	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11491	UniProtKB	Sequence conflict	271	271	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11491	UniProtKB	Sequence conflict	328	328	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11491	UniProtKB	Sequence conflict	447	447	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04004 1 230
+Q04004	UniProtKB	Chain	1	230	.	.	.	ID=PRO_0000120172;Note=Phosducin-like protein 1	
+Q04004	UniProtKB	Region	81	230	.	.	.	Note=Thioredoxin fold;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04004	UniProtKB	Coiled coil	25	79	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04004	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P32634 1 1753
+P32634	UniProtKB	Chain	1	1753	.	.	.	ID=PRO_0000119141;Note=Negative regulator of sporulation PMD1	
+P32634	UniProtKB	Repeat	143	198	.	.	.	Note=Kelch 1	
+P32634	UniProtKB	Repeat	206	253	.	.	.	Note=Kelch 2	
+P32634	UniProtKB	Modified residue	298	298	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32634	UniProtKB	Modified residue	838	838	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32634	UniProtKB	Modified residue	1289	1289	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32634	UniProtKB	Modified residue	1307	1307	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32634	UniProtKB	Modified residue	1356	1356	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32634	UniProtKB	Modified residue	1664	1664	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198	
+##sequence-region P35999 1 772
+P35999	UniProtKB	Transit peptide	1	37	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35999	UniProtKB	Chain	38	772	.	.	.	ID=PRO_0000028583;Note=Mitochondrial intermediate peptidase	
+P35999	UniProtKB	Active site	559	559	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P35999	UniProtKB	Metal binding	558	558	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P35999	UniProtKB	Metal binding	562	562	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P35999	UniProtKB	Metal binding	587	587	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35999	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Affects protein stability%2C but has no effect on peptidase activity. C->S%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	557	557	.	.	.	Note=Affects protein stability. F->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	558	558	.	.	.	Note=Abolishes proteolytic activity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	559	559	.	.	.	Note=Abolishes proteolytic activity. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	561	561	.	.	.	Note=Affects protein stability. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	562	562	.	.	.	Note=Abolishes proteolytic activity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	565	565	.	.	.	Note=Temperature sensitive%3B abolishes proteolytic activity for RIP1%2C but not for COX4. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	578	578	.	.	.	Note=Temperature sensitive%3B abolishes proteolytic activity for RIP1%2C but not for COX4. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	581	581	.	.	.	Note=Affects protein stability%2C but has no effect on peptidase activity. C->S%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	584	584	.	.	.	Note=No effect. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	587	587	.	.	.	Note=Abolishes proteolytic activity. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	589	589	.	.	.	Note=No effect. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	590	590	.	.	.	Note=Affects protein stability. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Mutagenesis	594	594	.	.	.	Note=No effect. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696	
+P35999	UniProtKB	Sequence conflict	343	350	.	.	.	Note=MAKNPKDV->WQDRRC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35999	UniProtKB	Sequence conflict	694	702	.	.	.	Note=YGATYYSYL->SGQLITATY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32903 1 40
+P32903	UniProtKB	Propeptide	1	2	.	.	.	ID=PRO_0000022071;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1532582;Dbxref=PMID:1532582	
+P32903	UniProtKB	Chain	3	40	.	.	.	ID=PRO_0000022072;Note=Plasma membrane ATPase proteolipid 1	
+P32903	UniProtKB	Transmembrane	3	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32903	UniProtKB	Topological domain	27	40	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q06644 1 662
+Q06644	UniProtKB	Chain	1	662	.	.	.	ID=PRO_0000121497;Note=Probable dolichyl-phosphate-mannose--protein mannosyltransferase 7	
+Q06644	UniProtKB	Topological domain	1	26	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Topological domain	48	159	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Transmembrane	160	180	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Topological domain	181	195	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Transmembrane	196	216	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Topological domain	217	235	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Transmembrane	236	256	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Topological domain	257	482	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Transmembrane	483	503	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Topological domain	504	565	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Transmembrane	566	586	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Topological domain	587	617	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Transmembrane	618	638	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Topological domain	639	662	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06644	UniProtKB	Domain	289	344	.	.	.	Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+Q06644	UniProtKB	Domain	359	418	.	.	.	Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+Q06644	UniProtKB	Domain	432	488	.	.	.	Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+Q06644	UniProtKB	Glycosylation	347	347	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53184 1 216
+P53184	UniProtKB	Chain	1	216	.	.	.	ID=PRO_0000206558;Note=Nicotinamidase	
+P53184	UniProtKB	Active site	8	8	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53184	UniProtKB	Active site	122	122	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53184	UniProtKB	Active site	167	167	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53184	UniProtKB	Metal binding	51	51	.	.	.	Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2H0R,ECO:0000269|PubMed:17382284;Dbxref=PMID:17382284	
+P53184	UniProtKB	Metal binding	53	53	.	.	.	Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2H0R,ECO:0000269|PubMed:17382284;Dbxref=PMID:17382284	
+P53184	UniProtKB	Metal binding	94	94	.	.	.	Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2H0R,ECO:0000269|PubMed:17382284;Dbxref=PMID:17382284	
+P53184	UniProtKB	Beta strand	2	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Helix	11	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Helix	25	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Helix	29	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Helix	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Beta strand	43	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Helix	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Beta strand	72	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Beta strand	85	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Helix	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Helix	106	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Beta strand	118	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Beta strand	132	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Helix	145	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Beta strand	156	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Turn	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Helix	167	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Beta strand	181	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Helix	196	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+P53184	UniProtKB	Beta strand	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E	
+##sequence-region Q99216 1 274
+Q99216	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000270553;Note=Pre-rRNA-processing protein PNO1	
+Q99216	UniProtKB	Domain	195	247	.	.	.	Note=KH	
+Q99216	UniProtKB	Compositional bias	35	41	.	.	.	Note=Poly-Asp	
+Q99216	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q99216	UniProtKB	Modified residue	51	51	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q99216	UniProtKB	Mutagenesis	203	203	.	.	.	Note=Temperature-sensitive. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502737;Dbxref=PMID:12502737	
+Q99216	UniProtKB	Mutagenesis	235	235	.	.	.	Note=Accumulation of aberrant 22S and 23S rRNA intermediates. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12736301;Dbxref=PMID:12736301	
+##sequence-region P19881 1 312
+P19881	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000058481;Note=4-nitrophenylphosphatase	
+P19881	UniProtKB	Sequence conflict	50	50	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19881	UniProtKB	Sequence conflict	96	96	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19881	UniProtKB	Sequence conflict	284	284	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P19881	UniProtKB	Sequence conflict	306	306	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36040 1 267
+P36040	UniProtKB	Chain	1	267	.	.	.	ID=PRO_0000203132;Note=Proteasome assembly chaperone 2	
+P36040	UniProtKB	Beta strand	3	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Helix	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Helix	14	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Beta strand	28	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Beta strand	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Beta strand	67	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Turn	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Beta strand	80	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Helix	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Helix	95	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Helix	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Beta strand	113	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Helix	183	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Helix	220	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Helix	247	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P36040	UniProtKB	Helix	258	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+##sequence-region Q12164 1 279
+Q12164	UniProtKB	Chain	1	279	.	.	.	ID=PRO_0000247116;Note=Pore membrane protein of 33 kDa	
+Q12164	UniProtKB	Topological domain	1	31	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12164	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12164	UniProtKB	Topological domain	53	56	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12164	UniProtKB	Transmembrane	57	79	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12164	UniProtKB	Topological domain	80	124	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12164	UniProtKB	Transmembrane	125	145	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12164	UniProtKB	Topological domain	146	180	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12164	UniProtKB	Transmembrane	181	201	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12164	UniProtKB	Topological domain	202	203	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12164	UniProtKB	Transmembrane	204	221	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12164	UniProtKB	Topological domain	222	279	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32838 1 368
+P32838	UniProtKB	Chain	1	368	.	.	.	ID=PRO_0000058876;Note=Serine/threonine-protein phosphatase PP2A-like PPG1	
+P32838	UniProtKB	Active site	111	111	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32838	UniProtKB	Metal binding	50	50	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32838	UniProtKB	Metal binding	52	52	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32838	UniProtKB	Metal binding	78	78	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32838	UniProtKB	Metal binding	78	78	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32838	UniProtKB	Metal binding	110	110	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32838	UniProtKB	Metal binding	161	161	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32838	UniProtKB	Metal binding	247	247	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32838	UniProtKB	Sequence conflict	126	126	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32838	UniProtKB	Sequence conflict	154	154	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38693 1 467
+P38693	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38693	UniProtKB	Chain	18	467	.	.	.	ID=PRO_0000023957;Note=Acid phosphatase PHO12	
+P38693	UniProtKB	Active site	75	75	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38693	UniProtKB	Active site	338	338	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38693	UniProtKB	Glycosylation	97	97	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38693	UniProtKB	Glycosylation	162	162	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38693	UniProtKB	Glycosylation	192	192	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38693	UniProtKB	Glycosylation	250	250	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38693	UniProtKB	Glycosylation	315	315	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38693	UniProtKB	Glycosylation	356	356	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38693	UniProtKB	Glycosylation	390	390	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38693	UniProtKB	Glycosylation	439	439	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38693	UniProtKB	Glycosylation	445	445	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38693	UniProtKB	Glycosylation	461	461	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08108 1 686
+Q08108	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Chain	27	659	.	.	.	ID=PRO_0000024648;Note=Lysophospholipase 3	
+Q08108	UniProtKB	Propeptide	660	686	.	.	.	ID=PRO_0000372444;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Domain	39	592	.	.	.	Note=PLA2c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00555	
+Q08108	UniProtKB	Compositional bias	627	643	.	.	.	Note=Poly-Ser	
+Q08108	UniProtKB	Lipidation	659	659	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	56	56	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	129	129	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	166	166	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	221	221	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	283	283	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	313	313	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	351	351	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	495	495	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	519	519	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	547	547	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	571	571	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	588	588	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08108	UniProtKB	Glycosylation	614	614	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P05375 1 206
+P05375	UniProtKB	Chain	1	206	.	.	.	ID=PRO_0000193924;Note=Phosphatidyl-N-methylethanolamine N-methyltransferase	
+P05375	UniProtKB	Topological domain	1	20	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216	
+P05375	UniProtKB	Intramembrane	21	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216	
+P05375	UniProtKB	Topological domain	42	53	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216	
+P05375	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216	
+P05375	UniProtKB	Topological domain	75	101	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216	
+P05375	UniProtKB	Transmembrane	102	122	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216	
+P05375	UniProtKB	Topological domain	123	165	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216	
+P05375	UniProtKB	Transmembrane	166	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216	
+P05375	UniProtKB	Topological domain	187	206	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216	
+P05375	UniProtKB	Region	106	108	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216	
+P05375	UniProtKB	Region	188	189	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216	
+##sequence-region P41812 1 875
+P41812	UniProtKB	Chain	1	875	.	.	.	ID=PRO_0000058514;Note=Ribonucleases P/MRP protein subunit POP1	
+P41812	UniProtKB	Modified residue	524	524	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q06494 1 345
+Q06494	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000257816;Note=Putative pyridoxal reductase	
+Q06494	UniProtKB	Active site	60	60	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P00950 1 247
+P00950	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8	
+P00950	UniProtKB	Chain	2	247	.	.	.	ID=PRO_0000179839;Note=Phosphoglycerate mutase 1	
+P00950	UniProtKB	Region	8	15	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10369755,ECO:0000269|PubMed:10531478,ECO:0000269|PubMed:6115412;Dbxref=PMID:10369755,PMID:10531478,PMID:6115412	
+P00950	UniProtKB	Region	21	22	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10369755,ECO:0000269|PubMed:10531478;Dbxref=PMID:10369755,PMID:10531478	
+P00950	UniProtKB	Region	87	90	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10369755,ECO:0000269|PubMed:6115412;Dbxref=PMID:10369755,PMID:6115412	
+P00950	UniProtKB	Region	114	115	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10369755;Dbxref=PMID:10369755	
+P00950	UniProtKB	Region	183	184	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10369755,ECO:0000269|PubMed:6115412;Dbxref=PMID:10369755,PMID:6115412	
+P00950	UniProtKB	Compositional bias	233	242	.	.	.	Note=Ala-rich	
+P00950	UniProtKB	Active site	9	9	.	.	.	Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10064712,ECO:0000269|PubMed:10531478,ECO:0000269|PubMed:6115412,ECO:0000269|PubMed:9512715;Dbxref=PMID:10064712,PMID:10531478,PMID:6115412,PMID:9512715	
+P00950	UniProtKB	Active site	87	87	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10064712;Dbxref=PMID:10064712	
+P00950	UniProtKB	Binding site	60	60	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10531478;Dbxref=PMID:10531478	
+P00950	UniProtKB	Binding site	98	98	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10369755;Dbxref=PMID:10369755	
+P00950	UniProtKB	Site	182	182	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10064712;Dbxref=PMID:10064712	
+P00950	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00950	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00950	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P00950	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00950	UniProtKB	Modified residue	128	128	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00950	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00950	UniProtKB	Modified residue	197	197	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P00950	UniProtKB	Cross-link	31	31	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00950	UniProtKB	Cross-link	57	57	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00950	UniProtKB	Cross-link	71	71	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00950	UniProtKB	Cross-link	139	139	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00950	UniProtKB	Cross-link	175	175	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00950	UniProtKB	Cross-link	191	191	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P00950	UniProtKB	Mutagenesis	169	169	.	.	.	Note=Causes dissociation of the homotetramer to dimers at low concentrations. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8240286;Dbxref=PMID:8240286	
+P00950	UniProtKB	Mutagenesis	182	182	.	.	.	Note=Reduces kcat of the mutase reaction 10000-fold. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1386023;Dbxref=PMID:1386023	
+P00950	UniProtKB	Beta strand	3	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Helix	13	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Helix	30	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Beta strand	51	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Helix	59	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Beta strand	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Helix	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Helix	98	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Beta strand	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGM	
+P00950	UniProtKB	Beta strand	126	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGM	
+P00950	UniProtKB	Helix	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Helix	152	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Helix	167	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Beta strand	177	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Helix	183	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Turn	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Helix	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Beta strand	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGM	
+P00950	UniProtKB	Beta strand	212	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Turn	218	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGM	
+P00950	UniProtKB	Beta strand	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Beta strand	227	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+P00950	UniProtKB	Turn	231	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF	
+##sequence-region P33775 1 817
+P33775	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P33775	UniProtKB	Chain	2	817	.	.	.	ID=PRO_0000121491;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 1	
+P33775	UniProtKB	Topological domain	2	50	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Transmembrane	51	70	.	.	.	Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Topological domain	71	135	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Transmembrane	136	154	.	.	.	Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Topological domain	155	179	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Transmembrane	180	200	.	.	.	Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Topological domain	201	234	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Transmembrane	235	259	.	.	.	Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Topological domain	260	273	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Transmembrane	274	291	.	.	.	Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Topological domain	292	584	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Transmembrane	585	605	.	.	.	Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Topological domain	606	685	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Transmembrane	686	710	.	.	.	Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Topological domain	711	817	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156	
+P33775	UniProtKB	Domain	324	378	.	.	.	Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P33775	UniProtKB	Domain	388	448	.	.	.	Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P33775	UniProtKB	Domain	459	514	.	.	.	Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P33775	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P33775	UniProtKB	Glycosylation	390	390	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33775	UniProtKB	Glycosylation	513	513	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33775	UniProtKB	Glycosylation	743	743	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33775	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Reduces mannosyltransferase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10764776;Dbxref=PMID:10764776	
+P33775	UniProtKB	Mutagenesis	77	78	.	.	.	Note=Impairs mannosyltransferase activity. DE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21956107;Dbxref=PMID:21956107	
+P33775	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Decreases substrate-binding and reduces mannosyltransferase activity. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10764776,ECO:0000269|PubMed:21956107;Dbxref=PMID:10764776,PMID:21956107	
+P33775	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Moderately decreases complex formation with PMT2. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21956107;Dbxref=PMID:21956107	
+P33775	UniProtKB	Mutagenesis	100	100	.	.	.	Note=Moderately decreases complex formation with PMT2. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21956107;Dbxref=PMID:21956107	
+P33775	UniProtKB	Mutagenesis	138	138	.	.	.	Note=Impairs complex formation with PMT2. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10764776;Dbxref=PMID:10764776	
+P33775	UniProtKB	Mutagenesis	408	408	.	.	.	Note=Reduces mannosyltransferase activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10764776;Dbxref=PMID:10764776	
+##sequence-region P31382 1 759
+P31382	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P31382	UniProtKB	Chain	2	759	.	.	.	ID=PRO_0000121492;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 2	
+P31382	UniProtKB	Topological domain	2	64	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Topological domain	86	167	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Topological domain	189	198	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Topological domain	220	251	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Transmembrane	252	272	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Topological domain	273	289	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Transmembrane	290	310	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Topological domain	311	609	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Transmembrane	610	630	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Topological domain	631	647	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Transmembrane	648	668	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Topological domain	669	676	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Transmembrane	677	697	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Topological domain	698	710	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Transmembrane	711	731	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Topological domain	732	759	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Domain	339	394	.	.	.	Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P31382	UniProtKB	Domain	407	463	.	.	.	Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P31382	UniProtKB	Domain	471	529	.	.	.	Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P31382	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P31382	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P31382	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P31382	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P31382	UniProtKB	Glycosylation	131	131	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Glycosylation	155	155	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31382	UniProtKB	Glycosylation	403	403	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P46971 1 762
+P46971	UniProtKB	Chain	1	762	.	.	.	ID=PRO_0000121494;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 4	
+P46971	UniProtKB	Topological domain	1	53	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Topological domain	75	136	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Transmembrane	137	157	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Topological domain	158	166	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Transmembrane	167	187	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Topological domain	188	189	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Transmembrane	190	210	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Topological domain	211	217	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Transmembrane	218	238	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Topological domain	239	242	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Topological domain	264	283	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Transmembrane	284	304	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Topological domain	305	593	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Transmembrane	594	614	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Topological domain	615	635	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Transmembrane	636	656	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Topological domain	657	716	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Transmembrane	717	737	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Topological domain	738	762	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46971	UniProtKB	Domain	331	391	.	.	.	Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P46971	UniProtKB	Domain	399	458	.	.	.	Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P46971	UniProtKB	Domain	464	521	.	.	.	Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131	
+P46971	UniProtKB	Glycosylation	759	759	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39685 1 1337
+P39685	UniProtKB	Chain	1	1337	.	.	.	ID=PRO_0000204910;Note=Nucleoporin POM152	
+P39685	UniProtKB	Topological domain	1	110	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:16847258,ECO:0000305|PubMed:9988776;Dbxref=PMID:16847258,PMID:9988776	
+P39685	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39685	UniProtKB	Topological domain	132	148	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:16847258,ECO:0000305|PubMed:9988776;Dbxref=PMID:16847258,PMID:9988776	
+P39685	UniProtKB	Transmembrane	149	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39685	UniProtKB	Topological domain	170	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:16847258,ECO:0000305|PubMed:9988776;Dbxref=PMID:16847258,PMID:9988776	
+P39685	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39685	UniProtKB	Topological domain	194	1337	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:16847258,ECO:0000305|PubMed:9988776;Dbxref=PMID:16847258,PMID:9988776	
+P39685	UniProtKB	Repeat	390	413	.	.	.	Note=1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573	
+P39685	UniProtKB	Repeat	626	650	.	.	.	Note=2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573	
+P39685	UniProtKB	Repeat	732	755	.	.	.	Note=3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573	
+P39685	UniProtKB	Repeat	836	859	.	.	.	Note=4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573	
+P39685	UniProtKB	Repeat	943	966	.	.	.	Note=5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573	
+P39685	UniProtKB	Repeat	1058	1077	.	.	.	Note=6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573	
+P39685	UniProtKB	Repeat	1157	1178	.	.	.	Note=7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573	
+P39685	UniProtKB	Repeat	1253	1276	.	.	.	Note=8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573	
+P39685	UniProtKB	Region	1	175	.	.	.	Note=Pore side;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39685	UniProtKB	Region	196	1337	.	.	.	Note=Cisternal side;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39685	UniProtKB	Region	390	1276	.	.	.	Note=8 X 24 AA approximate repeats	
+P39685	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P39685	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39685	UniProtKB	Glycosylation	280	280	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8138573;Dbxref=PMID:8138573	
+P39685	UniProtKB	Beta strand	722	726	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ	
+P39685	UniProtKB	Beta strand	729	733	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ	
+P39685	UniProtKB	Beta strand	737	746	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ	
+P39685	UniProtKB	Beta strand	748	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ	
+P39685	UniProtKB	Beta strand	766	773	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ	
+P39685	UniProtKB	Beta strand	776	787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ	
+P39685	UniProtKB	Beta strand	790	800	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ	
+P39685	UniProtKB	Turn	801	803	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ	
+P39685	UniProtKB	Beta strand	804	807	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ	
+P39685	UniProtKB	Beta strand	813	817	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ	
+##sequence-region Q05778 1 276
+Q05778	UniProtKB	Chain	1	276	.	.	.	ID=PRO_0000203234;Note=Proteasome chaperone 1	
+Q05778	UniProtKB	Beta strand	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Beta strand	49	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Helix	55	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Turn	63	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Beta strand	124	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Turn	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Helix	144	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Beta strand	164	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Beta strand	178	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Helix	196	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Turn	208	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Beta strand	214	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Beta strand	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Helix	232	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Helix	252	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Helix	265	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Helix	268	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+Q05778	UniProtKB	Beta strand	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+##sequence-region Q12245 1 148
+Q12245	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000238635;Note=Proteasome chaperone 4	
+Q12245	UniProtKB	Sequence conflict	9	9	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12245	UniProtKB	Beta strand	3	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q12245	UniProtKB	Beta strand	21	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q12245	UniProtKB	Beta strand	32	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q12245	UniProtKB	Beta strand	38	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q12245	UniProtKB	Beta strand	55	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q12245	UniProtKB	Beta strand	80	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q12245	UniProtKB	Helix	91	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q12245	UniProtKB	Beta strand	112	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q12245	UniProtKB	Helix	125	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+Q12245	UniProtKB	Helix	131	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B	
+##sequence-region P23594 1 369
+P23594	UniProtKB	Chain	1	369	.	.	.	ID=PRO_0000058873;Note=Serine/threonine-protein phosphatase PP2A-1 catalytic subunit	
+P23594	UniProtKB	Active site	178	178	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23594	UniProtKB	Metal binding	117	117	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23594	UniProtKB	Metal binding	119	119	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23594	UniProtKB	Metal binding	145	145	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23594	UniProtKB	Metal binding	145	145	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23594	UniProtKB	Metal binding	177	177	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23594	UniProtKB	Metal binding	227	227	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23594	UniProtKB	Metal binding	301	301	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23594	UniProtKB	Modified residue	369	369	.	.	.	Note=Leucine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11060018;Dbxref=PMID:11060018	
+P23594	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Reduced interaction with TAP42. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259	
+P23594	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Reduced interaction with TAP42. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259	
+P23594	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Reduced interaction with TAP42. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259	
+##sequence-region P38797 1 343
+P38797	UniProtKB	Transit peptide	1	39	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38797	UniProtKB	Chain	40	343	.	.	.	ID=PRO_0000057779;Note=Protein phosphatase 2C homolog 7%2C mitochondrial	
+P38797	UniProtKB	Domain	76	342	.	.	.	Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082	
+P38797	UniProtKB	Metal binding	109	109	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38797	UniProtKB	Metal binding	109	109	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38797	UniProtKB	Metal binding	110	110	.	.	.	Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38797	UniProtKB	Metal binding	265	265	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P00635 1 467
+P00635	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6093051,ECO:0000269|PubMed:6300772;Dbxref=PMID:6093051,PMID:6300772	
+P00635	UniProtKB	Chain	18	467	.	.	.	ID=PRO_0000023954;Note=Repressible acid phosphatase	
+P00635	UniProtKB	Active site	75	75	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00635	UniProtKB	Active site	338	338	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00635	UniProtKB	Glycosylation	97	97	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Glycosylation	162	162	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Glycosylation	192	192	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Glycosylation	250	250	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Glycosylation	315	315	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Glycosylation	356	356	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Glycosylation	390	390	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Glycosylation	439	439	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Glycosylation	445	445	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Glycosylation	456	456	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Glycosylation	461	461	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P00635	UniProtKB	Sequence conflict	36	36	.	.	.	Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00635	UniProtKB	Sequence conflict	130	130	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00635	UniProtKB	Sequence conflict	294	294	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00635	UniProtKB	Sequence conflict	446	446	.	.	.	Note=S->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00635	UniProtKB	Sequence conflict	462	463	.	.	.	Note=AS->DT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00635	UniProtKB	Sequence conflict	466	466	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40035 1 300
+P40035	UniProtKB	Chain	1	300	.	.	.	ID=PRO_0000090640;Note=Mitochondrial phosphate carrier protein 2	
+P40035	UniProtKB	Transmembrane	22	42	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40035	UniProtKB	Transmembrane	70	89	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40035	UniProtKB	Transmembrane	108	128	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40035	UniProtKB	Transmembrane	171	192	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40035	UniProtKB	Transmembrane	211	231	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40035	UniProtKB	Transmembrane	260	280	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40035	UniProtKB	Repeat	16	100	.	.	.	Note=Solcar 1	
+P40035	UniProtKB	Repeat	107	193	.	.	.	Note=Solcar 2	
+P40035	UniProtKB	Repeat	209	293	.	.	.	Note=Solcar 3	
+P40035	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P38969 1 423
+P38969	UniProtKB	Transmembrane	199	219	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38969	UniProtKB	Sequence conflict	406	423	.	.	.	Note=NISLLKYNSELVATKDIQ->IYHC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40473 1 351
+P40473	UniProtKB	Chain	1	351	.	.	.	ID=PRO_0000202962;Note=Transcriptional activator POG1	
+P40473	UniProtKB	Compositional bias	193	302	.	.	.	Note=Gln-rich	
+P40473	UniProtKB	Modified residue	152	152	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40473	UniProtKB	Modified residue	168	168	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40473	UniProtKB	Modified residue	314	314	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P39008 1 433
+P39008	UniProtKB	Chain	1	433	.	.	.	ID=PRO_0000212849;Note=Poly(A) ribonuclease POP2	
+P39008	UniProtKB	Compositional bias	81	90	.	.	.	Note=Poly-Gln	
+P39008	UniProtKB	Compositional bias	111	125	.	.	.	Note=Poly-Gln	
+P39008	UniProtKB	Compositional bias	363	369	.	.	.	Note=Poly-Gln	
+P39008	UniProtKB	Metal binding	188	188	.	.	.	Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39008	UniProtKB	Metal binding	190	190	.	.	.	Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39008	UniProtKB	Metal binding	310	310	.	.	.	Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39008	UniProtKB	Metal binding	394	394	.	.	.	Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39008	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39008	UniProtKB	Modified residue	97	97	.	.	.	Note=Phosphothreonine%3B by YAK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11358866;Dbxref=PMID:11358866	
+P39008	UniProtKB	Natural variant	41	41	.	.	.	Note=In strain: A364A. K->Q	
+P39008	UniProtKB	Natural variant	91	91	.	.	.	Note=In strain: A364A. Q->QQQQQQQQQQQQQQQQQQ	
+P39008	UniProtKB	Natural variant	118	122	.	.	.	Note=In strain: A364A. Missing	
+P39008	UniProtKB	Natural variant	278	278	.	.	.	Note=In strain: A364A. L->S	
+P39008	UniProtKB	Natural variant	412	412	.	.	.	Note=K->M	
+P39008	UniProtKB	Mutagenesis	97	97	.	.	.	Note=No cell-cycle stop in response to glucose deprivation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11358866;Dbxref=PMID:11358866	
+P39008	UniProtKB	Mutagenesis	188	188	.	.	.	Note=Abolishes poly(A) RNA degradation%3B when associated with A-190. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14618157;Dbxref=PMID:14618157	
+P39008	UniProtKB	Mutagenesis	190	190	.	.	.	Note=Abolishes poly(A) RNA degradation%3B when associated with A-188. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14618157;Dbxref=PMID:14618157	
+P39008	UniProtKB	Helix	155	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Beta strand	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Turn	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Helix	168	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Turn	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Beta strand	184	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Beta strand	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C	
+P39008	UniProtKB	Helix	205	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Beta strand	221	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Beta strand	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Beta strand	242	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Turn	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8A	
+P39008	UniProtKB	Helix	259	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Helix	272	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Helix	282	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Beta strand	292	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8A	
+P39008	UniProtKB	Beta strand	300	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Helix	309	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Helix	327	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Beta strand	339	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Helix	344	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Helix	353	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8A	
+P39008	UniProtKB	Helix	373	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Helix	386	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Helix	391	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Turn	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+P39008	UniProtKB	Helix	419	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC	
+##sequence-region P17157 1 305
+P17157	UniProtKB	Chain	1	305	.	.	.	ID=PRO_0000086521;Note=Cyclin-dependent protein kinase PHO85	
+P17157	UniProtKB	Domain	7	297	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P17157	UniProtKB	Nucleotide binding	13	21	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P17157	UniProtKB	Active site	133	133	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P17157	UniProtKB	Binding site	36	36	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P17157	UniProtKB	Site	166	166	.	.	.	Note=Not phosphorylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490639;Dbxref=PMID:10490639	
+P17157	UniProtKB	Site	167	167	.	.	.	Note=Not phosphorylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490639;Dbxref=PMID:10490639	
+P17157	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10620010;Dbxref=PMID:10620010	
+P17157	UniProtKB	Cross-link	289	289	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P17157	UniProtKB	Mutagenesis	18	18	.	.	.	Note=Reduces kinase activity. Abolishes interaction to PHO80 cyclin%2C but not to PCL1. Y->F	
+P17157	UniProtKB	Mutagenesis	36	36	.	.	.	Note=Loss of kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15057567;Dbxref=PMID:15057567	
+P17157	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Loss of kinase activity. Abolishes interaction to PHO80 and PCL1 cyclins. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10620010;Dbxref=PMID:10620010	
+P17157	UniProtKB	Mutagenesis	82	82	.	.	.	Note=Functional kinase%2C that can be rapidly inhibited by small%2C cell-permeable drugs like 1-Na PP1 (4-amino-1-tert-butyl-3-(1'-naphthyl)pyrazolo[3%2C4-d]pyrimidine). F->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11675494;Dbxref=PMID:11675494	
+P17157	UniProtKB	Sequence conflict	99	99	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17157	UniProtKB	Sequence conflict	99	99	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17157	UniProtKB	Helix	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Beta strand	7	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Beta strand	19	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Turn	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Beta strand	32	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Turn	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	48	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Turn	56	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Beta strand	68	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Beta strand	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	89	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Beta strand	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI	
+P17157	UniProtKB	Helix	107	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Beta strand	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Beta strand	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRC	
+P17157	UniProtKB	Beta strand	156	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	177	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	189	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	214	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Turn	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	234	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Beta strand	244	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRC	
+P17157	UniProtKB	Helix	254	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	268	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	282	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	288	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+P17157	UniProtKB	Helix	295	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD	
+##sequence-region P53191 1 635
+P53191	UniProtKB	Chain	1	635	.	.	.	ID=PRO_0000058425;Note=Phosphatidylinositol 3-phosphate-binding protein 2	
+P53191	UniProtKB	Zinc finger	452	527	.	.	.	Note=FYVE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
+P53191	UniProtKB	Compositional bias	15	18	.	.	.	Note=Poly-Glu	
+P53191	UniProtKB	Compositional bias	195	201	.	.	.	Note=Poly-Asp	
+P53191	UniProtKB	Compositional bias	238	250	.	.	.	Note=Poly-Ser	
+P53191	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53191	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53191	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53191	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53191	UniProtKB	Modified residue	113	113	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53191	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53191	UniProtKB	Modified residue	148	148	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53191	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53191	UniProtKB	Modified residue	174	174	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53191	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53191	UniProtKB	Modified residue	309	309	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53191	UniProtKB	Modified residue	381	381	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53191	UniProtKB	Sequence conflict	152	152	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03760 1 334
+Q03760	UniProtKB	Chain	1	334	.	.	.	ID=PRO_0000203243;Note=Pre-mRNA leakage protein 39	
+Q03760	UniProtKB	Compositional bias	134	137	.	.	.	Note=Poly-Cys	
+##sequence-region P07283 1 254
+P07283	UniProtKB	Chain	1	254	.	.	.	ID=PRO_0000199703;Note=Phosphomannomutase	
+P07283	UniProtKB	Active site	19	19	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07283	UniProtKB	Active site	21	21	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07283	UniProtKB	Binding site	28	28	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07283	UniProtKB	Binding site	130	130	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07283	UniProtKB	Binding site	141	141	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07283	UniProtKB	Binding site	148	148	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07283	UniProtKB	Binding site	186	186	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07283	UniProtKB	Binding site	188	188	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07283	UniProtKB	Modified residue	240	240	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P07283	UniProtKB	Natural variant	234	234	.	.	.	Note=In strain: CLIB 556 haplotype Ha1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P07283	UniProtKB	Natural variant	249	249	.	.	.	Note=In strain: R12 haplotype Ha1. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+##sequence-region P40975 1 43
+P40975	UniProtKB	Propeptide	1	5	.	.	.	ID=PRO_0000022073;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8063750;Dbxref=PMID:8063750	
+P40975	UniProtKB	Chain	6	43	.	.	.	ID=PRO_0000022074;Note=Plasma membrane ATPase proteolipid 2	
+P40975	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40975	UniProtKB	Topological domain	30	43	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36069 1 295
+P36069	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000203152;Note=Probable phosphoglycerate mutase PMU1	
+P36069	UniProtKB	Active site	61	61	.	.	.	Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707	
+P36069	UniProtKB	Active site	170	170	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707	
+P36069	UniProtKB	Site	254	254	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707	
+P36069	UniProtKB	Sequence conflict	44	44	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38218 1 177
+P38218	UniProtKB	Chain	1	177	.	.	.	ID=PRO_0000202470;Note=ADP-ribose 1''-phosphate phosphatase	
+P38218	UniProtKB	Domain	1	177	.	.	.	Note=Macro;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00490	
+P38218	UniProtKB	Region	9	11	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38218	UniProtKB	Region	24	26	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38218	UniProtKB	Region	31	36	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38218	UniProtKB	Region	147	153	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04636 1 552
+Q04636	UniProtKB	Chain	1	552	.	.	.	ID=PRO_0000203250;Note=FACT complex subunit POB3	
+Q04636	UniProtKB	Mutagenesis	20	20	.	.	.	Note=In pob3-11%3B causes severe defects in rate of growth%3B when associated with C-109. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459	
+Q04636	UniProtKB	Mutagenesis	78	78	.	.	.	Note=In pob3-1%3B causes severe defects in rate of growth%3B when associated with K-419 and T-489. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459	
+Q04636	UniProtKB	Mutagenesis	109	109	.	.	.	Note=In pob3-11%3B causes severe defects in rate of growth%3B when associated with H-20. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459	
+Q04636	UniProtKB	Mutagenesis	308	308	.	.	.	Note=No effect. Q->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678108;Dbxref=PMID:16678108	
+Q04636	UniProtKB	Mutagenesis	308	308	.	.	.	Note=Confers sensitivity to HU indicating a disturbed activity in DNA replication%3B confers a SPT- phenotype indicating a disturbed activity in transcription. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678108;Dbxref=PMID:16678108	
+Q04636	UniProtKB	Mutagenesis	308	308	.	.	.	Note=Confers sensitivity to HU indicating a disturbed activity in DNA replication. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678108;Dbxref=PMID:16678108	
+Q04636	UniProtKB	Mutagenesis	311	311	.	.	.	Note=No change of sensitivity to HU%3B confers a SPT- phenotype indicating a disturbed activity in transcription. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678108;Dbxref=PMID:16678108	
+Q04636	UniProtKB	Mutagenesis	419	419	.	.	.	Note=In pob3-1%3B causes severe defects in rate of growth%3B when associated with R-78 and T-489. M->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459	
+Q04636	UniProtKB	Mutagenesis	489	489	.	.	.	Note=In pob3-1%3B causes severe defects in rate of growth%3B when associated with R-78 and K-419. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459	
+Q04636	UniProtKB	Mutagenesis	547	547	.	.	.	Note=In pob3-21%3B causes severe defects in rate of growth. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459	
+Q04636	UniProtKB	Beta strand	1	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Beta strand	17	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Beta strand	25	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Turn	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Helix	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Beta strand	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Helix	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Beta strand	52	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Beta strand	61	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Beta strand	75	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Helix	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Helix	86	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Turn	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R	
+Q04636	UniProtKB	Beta strand	242	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	255	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	263	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	274	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Helix	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	282	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	293	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	311	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	325	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Helix	334	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Turn	341	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	347	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Helix	353	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	384	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	391	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	399	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	410	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Helix	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	417	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	434	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Helix	442	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Beta strand	447	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Helix	455	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+Q04636	UniProtKB	Helix	458	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0	
+##sequence-region P38336 1 279
+P38336	UniProtKB	Chain	1	279	.	.	.	ID=PRO_0000128422;Note=RNases MRP/P 32.9 kDa subunit	
+P38336	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53218 1 158
+P53218	UniProtKB	Chain	1	158	.	.	.	ID=PRO_0000058517;Note=Ribonucleases P/MRP protein subunit POP6	
+P53218	UniProtKB	Coiled coil	51	71	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53218	UniProtKB	Beta strand	5	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Beta strand	10	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Helix	19	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Turn	29	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Beta strand	38	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Helix	55	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Turn	71	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Beta strand	76	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Helix	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Helix	88	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Turn	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Beta strand	110	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Beta strand	133	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P53218	UniProtKB	Beta strand	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+##sequence-region P38291 1 140
+P38291	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000058519;Note=Ribonucleases P/MRP protein subunit POP7	
+P38291	UniProtKB	Modified residue	115	115	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38291	UniProtKB	Sequence conflict	92	92	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38291	UniProtKB	Helix	26	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P38291	UniProtKB	Beta strand	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P38291	UniProtKB	Helix	41	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P38291	UniProtKB	Beta strand	61	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P38291	UniProtKB	Helix	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P38291	UniProtKB	Helix	72	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P38291	UniProtKB	Beta strand	90	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+P38291	UniProtKB	Beta strand	126	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB	
+##sequence-region P23595 1 377
+P23595	UniProtKB	Chain	1	377	.	.	.	ID=PRO_0000058874;Note=Serine/threonine-protein phosphatase PP2A-2 catalytic subunit	
+P23595	UniProtKB	Active site	186	186	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23595	UniProtKB	Metal binding	125	125	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23595	UniProtKB	Metal binding	127	127	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23595	UniProtKB	Metal binding	153	153	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23595	UniProtKB	Metal binding	153	153	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23595	UniProtKB	Metal binding	185	185	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23595	UniProtKB	Metal binding	235	235	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23595	UniProtKB	Metal binding	309	309	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23595	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23595	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23595	UniProtKB	Modified residue	377	377	.	.	.	Note=Leucine methyl ester;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11060018,ECO:0000269|PubMed:11697862;Dbxref=PMID:11060018,PMID:11697862	
+##sequence-region P35182 1 281
+P35182	UniProtKB	Chain	1	281	.	.	.	ID=PRO_0000057774;Note=Protein phosphatase 2C homolog 1	
+P35182	UniProtKB	Domain	20	281	.	.	.	Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082	
+P35182	UniProtKB	Metal binding	58	58	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35182	UniProtKB	Metal binding	58	58	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35182	UniProtKB	Metal binding	59	59	.	.	.	Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35182	UniProtKB	Metal binding	233	233	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35182	UniProtKB	Metal binding	272	272	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35182	UniProtKB	Sequence conflict	53	53	.	.	.	Note=Y->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35182	UniProtKB	Sequence conflict	124	124	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P34221 1 468
+P34221	UniProtKB	Chain	1	468	.	.	.	ID=PRO_0000057776;Note=Protein phosphatase 2C homolog 3	
+P34221	UniProtKB	Domain	23	293	.	.	.	Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082	
+P34221	UniProtKB	Metal binding	62	62	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34221	UniProtKB	Metal binding	62	62	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34221	UniProtKB	Metal binding	63	63	.	.	.	Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34221	UniProtKB	Metal binding	234	234	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34221	UniProtKB	Metal binding	284	284	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34221	UniProtKB	Modified residue	324	324	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34221	UniProtKB	Modified residue	332	332	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P34221	UniProtKB	Sequence conflict	369	369	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P34221	UniProtKB	Sequence conflict	369	369	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40164 1 858
+P40164	UniProtKB	Chain	1	858	.	.	.	ID=PRO_0000203395;Note=Serine/threonine-protein phosphatase 4 regulatory subunit 3	
+##sequence-region P35842 1 467
+P35842	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35842	UniProtKB	Chain	18	467	.	.	.	ID=PRO_0000023956;Note=Acid phosphatase PHO11	
+P35842	UniProtKB	Active site	75	75	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35842	UniProtKB	Active site	338	338	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35842	UniProtKB	Glycosylation	97	97	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35842	UniProtKB	Glycosylation	162	162	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35842	UniProtKB	Glycosylation	192	192	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35842	UniProtKB	Glycosylation	250	250	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35842	UniProtKB	Glycosylation	315	315	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35842	UniProtKB	Glycosylation	356	356	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35842	UniProtKB	Glycosylation	390	390	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35842	UniProtKB	Glycosylation	439	439	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35842	UniProtKB	Glycosylation	445	445	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35842	UniProtKB	Glycosylation	461	461	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35842	UniProtKB	Sequence conflict	17	17	.	.	.	Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35842	UniProtKB	Sequence conflict	82	83	.	.	.	Note=VS->AR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35842	UniProtKB	Sequence conflict	150	150	.	.	.	Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35842	UniProtKB	Sequence conflict	354	354	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35842	UniProtKB	Sequence conflict	423	423	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04705 1 352
+Q04705	UniProtKB	Chain	1	352	.	.	.	ID=PRO_0000203256;Note=Pheromone-regulated membrane protein 6	
+Q04705	UniProtKB	Transmembrane	37	57	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04705	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04705	UniProtKB	Transmembrane	228	248	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39551 1 298
+P39551	UniProtKB	Chain	1	298	.	.	.	ID=PRO_0000207524;Note=Pheromone-regulated membrane protein 9	
+P39551	UniProtKB	Topological domain	1	111	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39551	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39551	UniProtKB	Topological domain	133	137	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39551	UniProtKB	Transmembrane	138	158	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39551	UniProtKB	Topological domain	159	298	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39551	UniProtKB	Region	297	298	.	.	.	Note=COPII binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P32264 1 428
+P32264	UniProtKB	Chain	1	428	.	.	.	ID=PRO_0000109768;Note=Glutamate 5-kinase	
+P32264	UniProtKB	Domain	321	412	.	.	.	Note=PUA	
+P32264	UniProtKB	Nucleotide binding	175	176	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32264	UniProtKB	Nucleotide binding	219	225	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32264	UniProtKB	Binding site	56	56	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32264	UniProtKB	Binding site	143	143	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32264	UniProtKB	Binding site	155	155	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32264	UniProtKB	Sequence conflict	332	332	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53549 1 437
+P53549	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+P53549	UniProtKB	Chain	2	437	.	.	.	ID=PRO_0000084737;Note=26S proteasome subunit RPT4	
+P53549	UniProtKB	Nucleotide binding	222	229	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53549	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+P53549	UniProtKB	Sequence conflict	121	121	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53549	UniProtKB	Sequence conflict	135	135	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q01939 1 405
+Q01939	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+Q01939	UniProtKB	Chain	2	405	.	.	.	ID=PRO_0000084730;Note=26S proteasome regulatory subunit 8 homolog	
+Q01939	UniProtKB	Nucleotide binding	189	196	.	.	.	Note=ATP	
+Q01939	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+Q01939	UniProtKB	Sequence conflict	41	41	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25375 1 712
+P25375	UniProtKB	Chain	1	712	.	.	.	ID=PRO_0000078156;Note=Saccharolysin	
+P25375	UniProtKB	Active site	502	502	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P25375	UniProtKB	Metal binding	501	501	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P25375	UniProtKB	Metal binding	505	505	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P25375	UniProtKB	Metal binding	508	508	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P25375	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25375	UniProtKB	Sequence conflict	384	384	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47032 1 299
+P47032	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47032	UniProtKB	Chain	20	299	.	.	.	ID=PRO_0000006317;Note=Protein PRY1	
+P47032	UniProtKB	Domain	167	281	.	.	.	Note=SCP	
+P47032	UniProtKB	Compositional bias	102	165	.	.	.	Note=Ala/Ser/Thr-rich	
+P47032	UniProtKB	Helix	161	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS	
+P47032	UniProtKB	Helix	187	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS	
+P47032	UniProtKB	Beta strand	212	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS	
+P47032	UniProtKB	Helix	223	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS	
+P47032	UniProtKB	Helix	232	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS	
+P47032	UniProtKB	Turn	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS	
+P47032	UniProtKB	Helix	249	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS	
+P47032	UniProtKB	Beta strand	261	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS	
+P47032	UniProtKB	Turn	271	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS	
+P47032	UniProtKB	Beta strand	275	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS	
+P47032	UniProtKB	Helix	291	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS	
+##sequence-region Q06892 1 414
+Q06892	UniProtKB	Sequence conflict	37	38	.	.	.	Note=KP->EA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06892	UniProtKB	Sequence conflict	180	180	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06892	UniProtKB	Sequence conflict	329	329	.	.	.	Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06892	UniProtKB	Sequence conflict	343	343	.	.	.	Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06892	UniProtKB	Sequence conflict	398	401	.	.	.	Note=LGFN->CRIH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06892	UniProtKB	Beta strand	34	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Helix	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	69	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Helix	79	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Helix	105	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Helix	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	127	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Helix	134	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	142	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Helix	150	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Turn	159	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	168	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Helix	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Helix	187	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	200	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	207	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	220	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	239	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	248	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Helix	264	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Helix	269	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	284	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	300	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	308	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	325	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	332	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	342	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Beta strand	379	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+Q06892	UniProtKB	Helix	389	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO	
+##sequence-region P40506 1 365
+P40506	UniProtKB	Chain	1	365	.	.	.	ID=PRO_0000182042;Note=Phosphopantothenate--cysteine ligase CAB2	
+P40506	UniProtKB	Sequence conflict	338	338	.	.	.	Note=S->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38796 1 400
+P38796	UniProtKB	Chain	1	400	.	.	.	ID=PRO_0000030588;Note=Protein phosphatase methylesterase 1	
+P38796	UniProtKB	Domain	114	365	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38796	UniProtKB	Active site	205	205	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38796	UniProtKB	Active site	233	233	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38796	UniProtKB	Active site	359	359	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38796	UniProtKB	Sequence conflict	36	36	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38796	UniProtKB	Sequence conflict	39	39	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38796	UniProtKB	Sequence conflict	44	44	.	.	.	Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04119 1 674
+Q04119	UniProtKB	Propeptide	1	83	.	.	.	ID=PRO_0000022089;Note=Removed in mature form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15792812;Dbxref=PMID:15792812	
+Q04119	UniProtKB	Chain	84	384	.	.	.	ID=PRO_0000022090;Note=Endopolyphosphatase	
+Q04119	UniProtKB	Propeptide	385	674	.	.	.	ID=PRO_0000022091;Note=Removed in mature form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15792812;Dbxref=PMID:15792812	
+Q04119	UniProtKB	Topological domain	1	21	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04119	UniProtKB	Transmembrane	22	42	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04119	UniProtKB	Topological domain	43	674	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04119	UniProtKB	Glycosylation	58	58	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04119	UniProtKB	Glycosylation	505	505	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04119	UniProtKB	Glycosylation	511	511	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04119	UniProtKB	Cross-link	6	6	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11566881;Dbxref=PMID:11566881	
+Q04119	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Causes accumulation in vacuoles and abolishes sorting into internal vesicles in late endosomes. K->R%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11566881;Dbxref=PMID:11566881	
+Q04119	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Abolishes enzyme activity%3B when associated with A-505 and A-511. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15792812;Dbxref=PMID:15792812	
+Q04119	UniProtKB	Mutagenesis	505	505	.	.	.	Note=Abolishes enzyme activity%3B when associated with A-11 and A-511. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15792812;Dbxref=PMID:15792812	
+Q04119	UniProtKB	Mutagenesis	511	511	.	.	.	Note=Abolishes enzyme activity%3B when associated with A-11 and A-505. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15792812;Dbxref=PMID:15792812	
+##sequence-region P42946 1 383
+P42946	UniProtKB	Chain	1	383	.	.	.	ID=PRO_0000203045;Note=Pheromone-regulated membrane protein 10	
+P42946	UniProtKB	Topological domain	1	65	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Topological domain	87	87	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Topological domain	109	117	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Topological domain	139	141	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Topological domain	163	180	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Transmembrane	181	201	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Topological domain	202	216	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Topological domain	238	241	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Topological domain	263	271	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Transmembrane	272	292	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Topological domain	293	293	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Transmembrane	294	314	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Topological domain	315	352	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Transmembrane	353	373	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Topological domain	374	383	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42946	UniProtKB	Sequence conflict	129	129	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12498 1 284
+Q12498	UniProtKB	Chain	1	284	.	.	.	ID=PRO_0000058579;Note=Pheromone-regulated membrane protein 4	
+Q12498	UniProtKB	Transmembrane	20	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12498	UniProtKB	Domain	157	272	.	.	.	Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686	
+Q12498	UniProtKB	Compositional bias	129	135	.	.	.	Note=Poly-Thr	
+##sequence-region P32524 1 280
+P32524	UniProtKB	Chain	1	280	.	.	.	ID=PRO_0000174322;Note=Pre-mRNA-splicing factor PRP21	
+P32524	UniProtKB	Repeat	11	49	.	.	.	Note=SURP motif 1	
+P32524	UniProtKB	Repeat	95	135	.	.	.	Note=SURP motif 2	
+P32524	UniProtKB	Mutagenesis	168	168	.	.	.	Note=In SPP91-1%3B corrects the PRP9-1 growth defect through partial restoration of splicing and by a complete reversion of the pre-mRNA escape phenotype. T->A	
+P32524	UniProtKB	Sequence conflict	205	205	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32524	UniProtKB	Helix	90	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P32524	UniProtKB	Helix	109	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P32524	UniProtKB	Helix	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P32524	UniProtKB	Helix	132	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P32524	UniProtKB	Helix	157	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P32524	UniProtKB	Turn	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+##sequence-region P20053 1 465
+P20053	UniProtKB	Chain	1	465	.	.	.	ID=PRO_0000051152;Note=U4/U6 small nuclear ribonucleoprotein PRP4	
+P20053	UniProtKB	Repeat	173	212	.	.	.	Note=WD 1	
+P20053	UniProtKB	Repeat	216	256	.	.	.	Note=WD 2	
+P20053	UniProtKB	Repeat	263	302	.	.	.	Note=WD 3	
+P20053	UniProtKB	Repeat	305	344	.	.	.	Note=WD 4	
+P20053	UniProtKB	Repeat	347	386	.	.	.	Note=WD 5	
+P20053	UniProtKB	Repeat	391	432	.	.	.	Note=WD 6	
+P20053	UniProtKB	Repeat	435	464	.	.	.	Note=WD 7	
+##sequence-region Q06449 1 215
+Q06449	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06449	UniProtKB	Chain	2	215	.	.	.	ID=PRO_0000268696;Note=[PSI+] inducibility protein 3	
+Q06449	UniProtKB	Domain	54	113	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+Q06449	UniProtKB	Motif	124	127	.	.	.	Note=PY motif	
+Q06449	UniProtKB	Compositional bias	122	125	.	.	.	Note=Poly-Pro	
+Q06449	UniProtKB	Compositional bias	126	181	.	.	.	Note=Asn/Gln-rich	
+Q06449	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06449	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06449	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06449	UniProtKB	Cross-link	80	80	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q06449	UniProtKB	Mutagenesis	80	80	.	.	.	Note=Abolishes formation of ubiquitinated protein forms. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21777813;Dbxref=PMID:21777813	
+Q06449	UniProtKB	Mutagenesis	91	91	.	.	.	Note=Abolishes interaction with LAS17%2C but not with SUP35. Blocks colocalization with actin%2C aggregation%2C and prion-inducing ability. W->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21777813;Dbxref=PMID:21777813	
+Q06449	UniProtKB	Mutagenesis	124	125	.	.	.	Note=Abolishes RSP5 binding site and consequently ubiquitination. PP->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21777813;Dbxref=PMID:21777813	
+Q06449	UniProtKB	Mutagenesis	174	175	.	.	.	Note=Reduces%2C but does not abolish the ability to promote [PSI+] induction. QQ->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21777813;Dbxref=PMID:21777813	
+Q06449	UniProtKB	Beta strand	58	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6	
+Q06449	UniProtKB	Beta strand	80	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6	
+Q06449	UniProtKB	Beta strand	88	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6	
+Q06449	UniProtKB	Beta strand	99	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6	
+Q06449	UniProtKB	Helix	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6	
+Q06449	UniProtKB	Beta strand	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6	
+##sequence-region P34217 1 668
+P34217	UniProtKB	Chain	1	668	.	.	.	ID=PRO_0000082028;Note=RNA-binding protein PIN4	
+P34217	UniProtKB	Domain	85	163	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P34217	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34217	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34217	UniProtKB	Modified residue	191	191	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34217	UniProtKB	Modified residue	194	194	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34217	UniProtKB	Modified residue	197	197	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P34217	UniProtKB	Modified residue	305	305	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15024067;Dbxref=PMID:15024067	
+P34217	UniProtKB	Modified residue	393	393	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34217	UniProtKB	Modified residue	466	466	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34217	UniProtKB	Modified residue	541	541	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P34217	UniProtKB	Modified residue	636	636	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34217	UniProtKB	Modified residue	638	638	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P34217	UniProtKB	Modified residue	640	640	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34217	UniProtKB	Modified residue	653	653	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P34217	UniProtKB	Modified residue	655	655	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P34217	UniProtKB	Mutagenesis	305	305	.	.	.	Note=No interaction with RAD53. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15024067;Dbxref=PMID:15024067	
+##sequence-region Q12017 1 286
+Q12017	UniProtKB	Chain	1	286	.	.	.	ID=PRO_0000163762;Note=Phosducin-like protein 2	
+Q12017	UniProtKB	Region	96	286	.	.	.	Note=Thioredoxin fold;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12017	UniProtKB	Modified residue	35	35	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+Q12017	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q12008 1 311
+Q12008	UniProtKB	Chain	1	311	.	.	.	ID=PRO_0000179840;Note=Phosphoglycerate mutase 2	
+Q12008	UniProtKB	Region	16	23	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12008	UniProtKB	Region	29	30	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12008	UniProtKB	Region	126	129	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12008	UniProtKB	Region	153	154	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12008	UniProtKB	Region	243	244	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12008	UniProtKB	Active site	17	17	.	.	.	Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12008	UniProtKB	Active site	126	126	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12008	UniProtKB	Binding site	73	73	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12008	UniProtKB	Binding site	137	137	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+Q12008	UniProtKB	Site	242	242	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950	
+##sequence-region P36110 1 329
+P36110	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36110	UniProtKB	Chain	19	329	.	.	.	ID=PRO_0000006318;Note=Protein PRY2	
+P36110	UniProtKB	Domain	197	311	.	.	.	Note=SCP	
+P36110	UniProtKB	Compositional bias	132	195	.	.	.	Note=Ser/Thr-rich	
+##sequence-region P30657 1 266
+P30657	UniProtKB	Propeptide	1	33	.	.	.	ID=PRO_0000331490	
+P30657	UniProtKB	Chain	34	266	.	.	.	ID=PRO_0000148073;Note=Proteasome subunit beta type-7	
+P30657	UniProtKB	Sequence conflict	188	188	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P30657	UniProtKB	Beta strand	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	44	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	52	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	66	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Turn	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	82	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Helix	90	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Turn	112	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Helix	122	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	145	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	158	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP	
+P30657	UniProtKB	Beta strand	173	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Helix	179	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Turn	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GPJ	
+P30657	UniProtKB	Helix	195	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Helix	203	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	226	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Turn	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	238	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Helix	253	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30657	UniProtKB	Beta strand	260	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+##sequence-region Q12161 1 406
+Q12161	UniProtKB	Chain	1	406	.	.	.	ID=PRO_0000235918;Note=RING finger protein PSH1	
+Q12161	UniProtKB	Zinc finger	30	72	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q12161	UniProtKB	Compositional bias	184	325	.	.	.	Note=Glu-rich	
+Q12161	UniProtKB	Modified residue	143	143	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12161	UniProtKB	Modified residue	191	191	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12161	UniProtKB	Modified residue	310	310	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12161	UniProtKB	Modified residue	403	403	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P40555 1 220
+P40555	UniProtKB	Chain	1	220	.	.	.	ID=PRO_0000173856;Note=Probable 26S proteasome regulatory subunit p27	
+P40555	UniProtKB	Domain	119	196	.	.	.	Note=PDZ	
+P40555	UniProtKB	Compositional bias	2	5	.	.	.	Note=Poly-Glu	
+P40555	UniProtKB	Helix	2	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHJ	
+P40555	UniProtKB	Helix	17	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHJ	
+P40555	UniProtKB	Turn	25	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHJ	
+P40555	UniProtKB	Helix	31	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHJ	
+P40555	UniProtKB	Helix	73	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHJ	
+P40555	UniProtKB	Beta strand	135	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06	
+P40555	UniProtKB	Helix	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06	
+P40555	UniProtKB	Beta strand	156	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06	
+P40555	UniProtKB	Turn	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06	
+P40555	UniProtKB	Turn	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06	
+P40555	UniProtKB	Helix	172	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06	
+P40555	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06	
+P40555	UniProtKB	Beta strand	186	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06	
+P40555	UniProtKB	Beta strand	195	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06	
+P40555	UniProtKB	Beta strand	207	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06	
+P40555	UniProtKB	Beta strand	215	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06	
+##sequence-region P08456 1 276
+P08456	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2830250;Dbxref=PMID:2830250	
+P08456	UniProtKB	Chain	2	276	.	.	.	ID=PRO_0000056801;Note=CDP-diacylglycerol--serine O-phosphatidyltransferase	
+P08456	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08456	UniProtKB	Transmembrane	163	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08456	UniProtKB	Transmembrane	210	230	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08456	UniProtKB	Transmembrane	248	268	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08456	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P08456	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P08456	UniProtKB	Modified residue	42	42	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P08456	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P08456	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P08456	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P08456	UniProtKB	Sequence conflict	123	123	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08456	UniProtKB	Sequence conflict	191	191	.	.	.	Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08456	UniProtKB	Sequence conflict	276	276	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36002 1 662
+P36002	UniProtKB	Chain	1	662	.	.	.	ID=PRO_0000086589;Note=Serine/threonine-protein kinase PTK1/STK1	
+P36002	UniProtKB	Domain	196	503	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P36002	UniProtKB	Nucleotide binding	202	210	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P36002	UniProtKB	Compositional bias	4	146	.	.	.	Note=Ser-rich	
+P36002	UniProtKB	Compositional bias	567	624	.	.	.	Note=Pro-rich	
+P36002	UniProtKB	Active site	329	329	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P36002	UniProtKB	Binding site	226	226	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P36002	UniProtKB	Sequence conflict	241	244	.	.	.	Note=KRCS->NAAP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36002	UniProtKB	Sequence conflict	300	300	.	.	.	Note=S->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36002	UniProtKB	Sequence conflict	356	375	.	.	.	Note=TDPHDLSSPVKKCAGMIGSP->HGSTRPVQPCQEVRRDDRLA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36002	UniProtKB	Sequence conflict	637	662	.	.	.	Note=VHHHLNIVNSLVHSSSAASSQVPAST->GASPSEHCQQLGP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40100 1 303
+P40100	UniProtKB	Chain	1	303	.	.	.	ID=PRO_0000202661;Note=Protoporphyrin uptake protein 1	
+P40100	UniProtKB	Topological domain	1	18	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Transmembrane	19	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Topological domain	40	76	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Topological domain	98	111	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Topological domain	133	154	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Transmembrane	155	175	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Topological domain	176	183	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Transmembrane	184	204	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Topological domain	205	226	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Transmembrane	227	247	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Topological domain	248	264	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Transmembrane	265	285	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40100	UniProtKB	Topological domain	286	303	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P28708 1 518
+P28708	UniProtKB	Chain	1	518	.	.	.	ID=PRO_0000086149;Note=Serine/threonine-protein kinase PRR1	
+P28708	UniProtKB	Domain	192	508	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P28708	UniProtKB	Nucleotide binding	198	206	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P28708	UniProtKB	Active site	354	354	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P28708	UniProtKB	Binding site	225	225	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P28708	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P28708	UniProtKB	Modified residue	132	132	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P23639 1 250
+P23639	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000124090;Note=Proteasome subunit alpha type-2	
+P23639	UniProtKB	Cross-link	108	108	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P23639	UniProtKB	Beta strand	7	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65	
+P23639	UniProtKB	Turn	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G0U	
+P23639	UniProtKB	Helix	19	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Beta strand	34	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Beta strand	42	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Beta strand	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Beta strand	63	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Beta strand	71	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Helix	79	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Helix	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Helix	107	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Turn	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Beta strand	132	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Turn	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Beta strand	144	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Beta strand	156	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Helix	168	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Helix	185	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Turn	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Beta strand	209	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Helix	219	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Beta strand	223	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Beta strand	234	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23639	UniProtKB	Helix	240	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+##sequence-region P50109 1 593
+P50109	UniProtKB	Chain	1	593	.	.	.	ID=PRO_0000097069;Note=Protein PSP2	
+P50109	UniProtKB	Compositional bias	408	547	.	.	.	Note=Asn-rich	
+P50109	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P50109	UniProtKB	Modified residue	340	340	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q07949 1 397
+Q07949	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000212577;Note=Probable phosphatase PSR2	
+Q07949	UniProtKB	Domain	223	381	.	.	.	Note=FCP1 homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00336	
+Q07949	UniProtKB	Lipidation	9	9	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255,ECO:0000303;evidence=ECO:0000255,ECO:0000303|PubMed:10777497;Dbxref=PMID:10777497	
+Q07949	UniProtKB	Lipidation	10	10	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255,ECO:0000303;evidence=ECO:0000255,ECO:0000303|PubMed:10777497;Dbxref=PMID:10777497	
+Q07949	UniProtKB	Sequence conflict	59	59	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12335 1 198
+Q12335	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12335	UniProtKB	Chain	22	198	.	.	.	ID=PRO_0000041482;Note=Protoplast secreted protein 2	
+Q12335	UniProtKB	Domain	22	191	.	.	.	Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088	
+##sequence-region P38958 1 111
+P38958	UniProtKB	Transmembrane	18	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P08468 1 800
+P08468	UniProtKB	Sequence conflict	278	278	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08468	UniProtKB	Sequence conflict	709	709	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P10355 1 254
+P10355	UniProtKB	Transit peptide	1	8	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8389363;Dbxref=PMID:8389363	
+P10355	UniProtKB	Chain	9	254	.	.	.	ID=PRO_0000022177;Note=Protein PET122%2C mitochondrial	
+P10355	UniProtKB	Region	185	254	.	.	.	Note=Essential for PET122 function	
+##sequence-region Q12461 1 358
+Q12461	UniProtKB	Chain	1	358	.	.	.	ID=PRO_0000226120;Note=Serine/threonine-protein phosphatase 2A activator 2	
+Q12461	UniProtKB	Turn	10	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	14	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	20	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Turn	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	50	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	84	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	109	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Turn	126	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	133	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	154	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	165	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Beta strand	192	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	199	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Turn	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	216	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	222	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Turn	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	233	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Turn	245	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	250	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	255	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	266	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Turn	281	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Helix	285	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+Q12461	UniProtKB	Beta strand	295	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN	
+##sequence-region P32901 1 601
+P32901	UniProtKB	Chain	1	601	.	.	.	ID=PRO_0000064317;Note=Peptide transporter PTR2	
+P32901	UniProtKB	Topological domain	1	150	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Transmembrane	151	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Topological domain	173	182	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Transmembrane	183	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Topological domain	203	210	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Transmembrane	211	229	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Topological domain	230	267	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Transmembrane	268	287	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Topological domain	288	294	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Transmembrane	295	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Topological domain	317	378	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Transmembrane	379	399	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Topological domain	400	412	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Transmembrane	413	429	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Topological domain	430	448	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Transmembrane	449	466	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Topological domain	467	494	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Transmembrane	495	513	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Topological domain	514	526	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Transmembrane	527	547	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Topological domain	548	554	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Transmembrane	555	577	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Topological domain	578	601	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32901	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32901	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32901	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32901	UniProtKB	Modified residue	594	594	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32901	UniProtKB	Sequence conflict	39	39	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43606 1 678
+P43606	UniProtKB	Chain	1	678	.	.	.	ID=PRO_0000097093;Note=SPS-sensor component PTR3	
+P43606	UniProtKB	Mutagenesis	321	321	.	.	.	Note=No effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17984223;Dbxref=PMID:17984223	
+P43606	UniProtKB	Mutagenesis	435	435	.	.	.	Note=In PTR3-17%3B constitutively active%2C confers increased STP1 processing in the absence of amino acids. T->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15947203,ECO:0000269|PubMed:17984223;Dbxref=PMID:15947203,PMID:17984223	
+P43606	UniProtKB	Mutagenesis	439	439	.	.	.	Note=In PTR3-5%3B constitutively active and hyperphosphorylated%2C confers increased STP1 processing in the absence of amino acids. Q->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15947203,ECO:0000269|PubMed:17984223;Dbxref=PMID:15947203,PMID:17984223	
+P43606	UniProtKB	Mutagenesis	525	525	.	.	.	Note=Loss of function. Abolishes hyperphosphorylation of PTR3 and%2C consequently%2C results in a failure to activate STP1. T->A%2CD%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17984223;Dbxref=PMID:17984223	
+P43606	UniProtKB	Mutagenesis	635	635	.	.	.	Note=No effect. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17984223;Dbxref=PMID:17984223	
+##sequence-region P38089 1 393
+P38089	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000057777;Note=Protein phosphatase 2C homolog 4	
+P38089	UniProtKB	Domain	33	368	.	.	.	Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082	
+P38089	UniProtKB	Metal binding	83	83	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38089	UniProtKB	Metal binding	83	83	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38089	UniProtKB	Metal binding	84	84	.	.	.	Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38089	UniProtKB	Metal binding	310	310	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38089	UniProtKB	Metal binding	359	359	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38193 1 441
+P38193	UniProtKB	Chain	1	441	.	.	.	ID=PRO_0000202458;Note=Serine/threonine-protein phosphatase 4 regulatory subunit 2	
+P38193	UniProtKB	Compositional bias	198	302	.	.	.	Note=Asp-rich	
+P38193	UniProtKB	Modified residue	347	347	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38193	UniProtKB	Sequence conflict	374	374	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38698 1 397
+P38698	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000158601;Note=Exopolyphosphatase	
+P38698	UniProtKB	Metal binding	39	39	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38698	UniProtKB	Metal binding	41	41	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38698	UniProtKB	Metal binding	127	127	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38698	UniProtKB	Metal binding	127	127	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38698	UniProtKB	Metal binding	148	148	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38698	UniProtKB	Metal binding	202	202	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38698	UniProtKB	Sequence conflict	193	193	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38698	UniProtKB	Sequence conflict	284	284	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38698	UniProtKB	Helix	8	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	28	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	40	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	79	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	86	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	105	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	120	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Turn	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	141	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	159	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	169	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	185	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Turn	203	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	212	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	235	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	259	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	267	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	275	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	280	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	291	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	301	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	318	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	331	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	342	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	358	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Beta strand	369	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+P38698	UniProtKB	Helix	381	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7	
+##sequence-region P20457 1 528
+P20457	UniProtKB	Chain	1	528	.	.	.	ID=PRO_0000046776;Note=DNA primase large subunit	
+P20457	UniProtKB	Region	210	239	.	.	.	Note=H-T-H-like motif;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20457	UniProtKB	Metal binding	336	336	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404922;Dbxref=PMID:20404922	
+P20457	UniProtKB	Metal binding	417	417	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404922;Dbxref=PMID:20404922	
+P20457	UniProtKB	Metal binding	434	434	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404922;Dbxref=PMID:20404922	
+P20457	UniProtKB	Metal binding	474	474	.	.	.	Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404922;Dbxref=PMID:20404922	
+P20457	UniProtKB	Mutagenesis	152	152	.	.	.	Note=Temperature-sensitive. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2023935;Dbxref=PMID:2023935	
+P20457	UniProtKB	Mutagenesis	336	336	.	.	.	Note=Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding%3B when associated with S-474. Strong disruption of iron-sulfur-binding%2C leading to destabilization of the protein and preventing its purification%3B when associated with S-417 or S-434. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704817;Dbxref=PMID:17704817	
+P20457	UniProtKB	Mutagenesis	401	401	.	.	.	Note=Lethal. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2023935;Dbxref=PMID:2023935	
+P20457	UniProtKB	Mutagenesis	417	417	.	.	.	Note=Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding%2C leading to destabilization of the protein and preventing its purification%3B when associated with S-336. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704817;Dbxref=PMID:17704817	
+P20457	UniProtKB	Mutagenesis	434	434	.	.	.	Note=Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding%2C leading to destabilization of the protein and preventing its purification%3B when associated with S-336. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704817;Dbxref=PMID:17704817	
+P20457	UniProtKB	Mutagenesis	434	434	.	.	.	Note=Temperature-sensitive. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704817;Dbxref=PMID:17704817	
+P20457	UniProtKB	Mutagenesis	474	474	.	.	.	Note=Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding%3B when associated with S-336. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704817;Dbxref=PMID:17704817	
+P20457	UniProtKB	Helix	323	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	327	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	335	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	352	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	369	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	388	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	396	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	417	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	435	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	441	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	455	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	470	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+P20457	UniProtKB	Helix	500	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB	
+##sequence-region Q12459 1 698
+Q12459	UniProtKB	Chain	1	698	.	.	.	ID=PRO_0000262750;Note=Pheromone-regulated protein PRM7	
+Q12459	UniProtKB	Compositional bias	6	520	.	.	.	Note=Ser-rich	
+Q12459	UniProtKB	Compositional bias	11	372	.	.	.	Note=Thr-rich	
+##sequence-region P38876 1 190
+P38876	UniProtKB	Chain	1	190	.	.	.	ID=PRO_0000187867;Note=Peptidyl-tRNA hydrolase	
+##sequence-region P32857 1 523
+P32857	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Chain	27	523	.	.	.	ID=PRO_0000022180;Note=Membrane protein PTM1	
+P32857	UniProtKB	Topological domain	27	197	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Topological domain	219	230	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Transmembrane	231	251	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Topological domain	252	265	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Transmembrane	266	286	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Topological domain	287	304	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Transmembrane	305	325	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Topological domain	326	333	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Transmembrane	334	354	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Topological domain	355	381	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Transmembrane	382	402	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Topological domain	403	417	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Transmembrane	418	438	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Topological domain	439	523	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32857	UniProtKB	Modified residue	480	480	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32857	UniProtKB	Modified residue	483	483	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32857	UniProtKB	Modified residue	498	498	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32857	UniProtKB	Glycosylation	132	132	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07350 1 266
+Q07350	UniProtKB	Chain	1	266	.	.	.	ID=PRO_0000174317;Note=Pre-mRNA-splicing factor PRP11	
+Q07350	UniProtKB	Zinc finger	66	96	.	.	.	Note=Matrin-type	
+Q07350	UniProtKB	Compositional bias	12	15	.	.	.	Note=Poly-Gly	
+Q07350	UniProtKB	Beta strand	153	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+Q07350	UniProtKB	Beta strand	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+Q07350	UniProtKB	Beta strand	179	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+Q07350	UniProtKB	Beta strand	197	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+Q07350	UniProtKB	Beta strand	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+Q07350	UniProtKB	Helix	235	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+Q07350	UniProtKB	Beta strand	241	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+Q07350	UniProtKB	Turn	245	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+Q07350	UniProtKB	Beta strand	249	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+##sequence-region P40968 1 455
+P40968	UniProtKB	Chain	1	455	.	.	.	ID=PRO_0000051144;Note=Pre-mRNA-processing factor 17	
+P40968	UniProtKB	Repeat	160	200	.	.	.	Note=WD 1	
+P40968	UniProtKB	Repeat	204	243	.	.	.	Note=WD 2	
+P40968	UniProtKB	Repeat	291	330	.	.	.	Note=WD 3	
+P40968	UniProtKB	Repeat	334	373	.	.	.	Note=WD 4	
+P40968	UniProtKB	Repeat	379	422	.	.	.	Note=WD 5	
+P40968	UniProtKB	Repeat	424	454	.	.	.	Note=WD 6	
+P40968	UniProtKB	Sequence conflict	390	390	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40968	UniProtKB	Helix	53	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Turn	66	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	153	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Turn	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	177	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	188	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	198	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	211	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	216	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	226	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	230	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Turn	235	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	239	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Turn	258	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	262	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	270	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	287	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	296	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	303	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	308	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	317	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Turn	322	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	326	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	342	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	352	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	361	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	381	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	387	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	394	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Turn	403	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	408	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Helix	424	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	429	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	442	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Turn	447	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40968	UniProtKB	Beta strand	450	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P23394 1 588
+P23394	UniProtKB	Chain	1	588	.	.	.	ID=PRO_0000055127;Note=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28	
+P23394	UniProtKB	Domain	208	399	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P23394	UniProtKB	Domain	427	579	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P23394	UniProtKB	Nucleotide binding	221	228	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P23394	UniProtKB	Motif	172	202	.	.	.	Note=Q motif	
+P23394	UniProtKB	Motif	341	344	.	.	.	Note=DEAD box	
+P23394	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23394	UniProtKB	Mutagenesis	221	221	.	.	.	Note=In PRP28-103%3B no growth at 15 and 37 degrees Celsius. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	223	223	.	.	.	Note=In PRP28-117%3B no growth at 15 degrees Celsius. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	264	264	.	.	.	Note=Lethal. R->D%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	265	265	.	.	.	Note=In PRP28-99%3B no growth at 15 and 37 degrees Celsius. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	297	297	.	.	.	Note=In PRP28-1%3B no growth at 15 degrees Celsius. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2010088;Dbxref=PMID:2010088	
+P23394	UniProtKB	Mutagenesis	317	317	.	.	.	Note=In PRP28-36%3B slow growth at 30 degrees Celsius%2C and no growth at 15 and 37 degrees Celsius. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	317	317	.	.	.	Note=Lethal. T->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	319	319	.	.	.	Note=No growth at 15 and 37 degrees Celsius. G->E%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	376	376	.	.	.	Note=In PRP28-32%3B no growth at 15 degrees Celsius. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	379	379	.	.	.	Note=In PRP28-102%3B no growth at 25 degrees Celsius or lower. A->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	438	438	.	.	.	Note=In PRP28-61%3B no growth at 37 degrees Celsius%3B when associated with L-468 and D-486. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	440	440	.	.	.	Note=In PRP28-56%3B no growth at 37 degrees Celsius%3B when associated with S-546 and E-584. I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	442	442	.	.	.	Note=In PRP28-101%3B no growth at 15 and 37 degrees Celsius. F->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	442	442	.	.	.	Note=In PRP28-55%3B no growth at 37 degrees Celsius. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	449	449	.	.	.	Note=In PRP28-66%3B no growth at 37 degrees Celsius%3B when associated with A-541%3B V-549%3B N-580 and V-586. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	468	468	.	.	.	Note=In PRP28-61%3B no growth at 37 degrees Celsius%3B when associated with L-438 and D-486. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	486	486	.	.	.	Note=In PRP28-61%3B no growth at 37 degrees Celsius%3B when associated with L-438 and L-468. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	491	491	.	.	.	Note=In PRP28-52%3B no growth at 37 degrees Celsius. M->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	499	499	.	.	.	Note=In PRP28-86%3B lethal. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	499	499	.	.	.	Note=No growth at 15 degrees Celsius. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	502	502	.	.	.	Note=Lethal. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	521	521	.	.	.	Note=In PRP28-37%3B no growth at 37 degrees Celsius. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	527	527	.	.	.	Note=Lethal. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	541	541	.	.	.	Note=In PRP28-66%3B no growth at 37 degrees Celsius%3B when associated with T-449%3B V-549%3B N-580 and V-586. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	546	546	.	.	.	Note=In PRP28-56%3B no growth at 37 degrees Celsius%3B when associated with F-440 and E-584. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	549	549	.	.	.	Note=In PRP28-66%3B no growth at 37 degrees Celsius%3B when associated with T-449%3B A-541%3B N-580 and V-586. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	580	580	.	.	.	Note=In PRP28-66%3B no growth at 37 degrees Celsius%3B when associated with T-449%3B A-541%3B V-549 and V-586. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	584	584	.	.	.	Note=In PRP28-56%3B no growth at 37 degrees Celsius%3B when associated with F-440 and S-546. N->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Mutagenesis	586	586	.	.	.	Note=In PRP28-66%3B no growth at 37 degrees Celsius%3B when associated with T-449%3B A-541%3B V-549 and N-580. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812	
+P23394	UniProtKB	Sequence conflict	493	493	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23394	UniProtKB	Helix	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	148	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	160	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	172	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	182	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	199	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	217	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	227	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	247	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	256	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	264	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	284	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	291	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	300	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	312	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	318	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	337	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	343	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	352	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	373	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	383	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	397	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	410	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	421	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	439	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	446	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	464	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	473	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	487	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Turn	495	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	506	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	518	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Beta strand	534	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	547	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+P23394	UniProtKB	Helix	570	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S	
+##sequence-region P25043 1 261
+P25043	UniProtKB	Propeptide	1	29	.	.	.	ID=PRO_0000026657;Note=Removed in mature form	
+P25043	UniProtKB	Chain	30	261	.	.	.	ID=PRO_0000026658;Note=Proteasome subunit beta type-2	
+P25043	UniProtKB	Active site	30	30	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9087403;Dbxref=PMID:9087403	
+P25043	UniProtKB	Beta strand	23	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FGI	
+P25043	UniProtKB	Beta strand	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Beta strand	40	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Beta strand	54	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Beta strand	63	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Beta strand	70	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Helix	78	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Helix	105	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Turn	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Beta strand	125	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Beta strand	136	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Turn	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G0U	
+P25043	UniProtKB	Beta strand	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Beta strand	152	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Helix	160	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Helix	177	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Beta strand	202	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Beta strand	213	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25043	UniProtKB	Beta strand	241	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+##sequence-region P22141 1 198
+P22141	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000148055;Note=Proteasome subunit beta type-4	
+P22141	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P22141	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22141	UniProtKB	Sequence conflict	183	183	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22141	UniProtKB	Sequence conflict	188	188	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22141	UniProtKB	Beta strand	4	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Beta strand	13	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Beta strand	26	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Beta strand	35	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Beta strand	42	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Helix	50	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Helix	77	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Beta strand	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Beta strand	100	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Turn	109	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Beta strand	113	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Turn	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65	
+P22141	UniProtKB	Beta strand	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Beta strand	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Helix	136	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Helix	154	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Beta strand	179	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Beta strand	188	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P22141	UniProtKB	Turn	194	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNP	
+##sequence-region P30656 1 287
+P30656	UniProtKB	Propeptide	1	75	.	.	.	ID=PRO_0000026611;Note=Removed in mature form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7781614;Dbxref=PMID:7781614	
+P30656	UniProtKB	Chain	76	287	.	.	.	ID=PRO_0000026612;Note=Proteasome subunit beta type-5	
+P30656	UniProtKB	Active site	76	76	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9087403;Dbxref=PMID:9087403	
+P30656	UniProtKB	Binding site	124	124	.	.	.	Note=Bortezomib%3B via amide nitrogen	
+P30656	UniProtKB	Mutagenesis	126	126	.	.	.	Note=In DOA3-1%3B decrease in activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7781614;Dbxref=PMID:7781614	
+P30656	UniProtKB	Sequence conflict	282	287	.	.	.	Note=FNNVIG->STTLLAK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P30656	UniProtKB	Beta strand	78	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Beta strand	86	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Beta strand	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Beta strand	100	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Beta strand	109	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Beta strand	116	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Beta strand	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GPJ	
+P30656	UniProtKB	Helix	124	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Helix	151	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Turn	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Beta strand	172	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Beta strand	184	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Turn	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G0U	
+P30656	UniProtKB	Beta strand	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Beta strand	200	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Helix	208	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Helix	225	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Beta strand	243	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EU2	
+P30656	UniProtKB	Beta strand	248	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Beta strand	259	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P30656	UniProtKB	Helix	268	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+##sequence-region P23724 1 241
+P23724	UniProtKB	Propeptide	1	19	.	.	.	ID=PRO_0000331489	
+P23724	UniProtKB	Chain	20	241	.	.	.	ID=PRO_0000148042;Note=Proteasome subunit beta type-6	
+P23724	UniProtKB	Beta strand	30	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Beta strand	40	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Beta strand	53	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R18	
+P23724	UniProtKB	Beta strand	70	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Helix	77	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Turn	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Helix	105	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Turn	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Beta strand	126	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Beta strand	139	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Beta strand	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MG0	
+P23724	UniProtKB	Beta strand	150	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Helix	162	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP	
+P23724	UniProtKB	Beta strand	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R17	
+P23724	UniProtKB	Helix	196	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Beta strand	214	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65	
+P23724	UniProtKB	Beta strand	219	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23724	UniProtKB	Beta strand	230	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+##sequence-region P53043 1 513
+P53043	UniProtKB	Chain	1	513	.	.	.	ID=PRO_0000058898;Note=Serine/threonine-protein phosphatase T	
+P53043	UniProtKB	Repeat	12	45	.	.	.	Note=TPR 1	
+P53043	UniProtKB	Repeat	46	79	.	.	.	Note=TPR 2	
+P53043	UniProtKB	Repeat	80	113	.	.	.	Note=TPR 3	
+P53043	UniProtKB	Region	188	513	.	.	.	Note=Catalytic	
+P53043	UniProtKB	Active site	311	311	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53043	UniProtKB	Metal binding	249	249	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53043	UniProtKB	Metal binding	251	251	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53043	UniProtKB	Metal binding	278	278	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53043	UniProtKB	Metal binding	278	278	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53043	UniProtKB	Metal binding	310	310	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53043	UniProtKB	Metal binding	359	359	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53043	UniProtKB	Metal binding	434	434	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53043	UniProtKB	Mutagenesis	311	311	.	.	.	Note=Loss of phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407978;Dbxref=PMID:16407978	
+P53043	UniProtKB	Helix	192	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	211	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	230	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	243	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	254	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	271	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	280	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	286	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Turn	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	304	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	314	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	322	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	332	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	347	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Turn	352	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	355	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	370	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	384	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	387	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	398	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	411	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	415	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	428	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	439	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	445	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	449	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Helix	458	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	465	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Turn	480	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Beta strand	488	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+P53043	UniProtKB	Turn	503	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF	
+##sequence-region P33329 1 710
+P33329	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33329	UniProtKB	Chain	2	710	.	.	.	ID=PRO_0000058892;Note=Serine/threonine-protein phosphatase PP-Z2	
+P33329	UniProtKB	Compositional bias	346	353	.	.	.	Note=Poly-Ser	
+P33329	UniProtKB	Active site	515	515	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33329	UniProtKB	Metal binding	454	454	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33329	UniProtKB	Metal binding	456	456	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33329	UniProtKB	Metal binding	482	482	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33329	UniProtKB	Metal binding	482	482	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33329	UniProtKB	Metal binding	514	514	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33329	UniProtKB	Metal binding	563	563	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33329	UniProtKB	Metal binding	638	638	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33329	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26570	
+P33329	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33329	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26570	
+P33329	UniProtKB	Modified residue	203	203	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P33329	UniProtKB	Modified residue	224	224	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33329	UniProtKB	Modified residue	271	271	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26570	
+P33329	UniProtKB	Modified residue	275	275	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26570	
+P33329	UniProtKB	Modified residue	310	310	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33329	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33329	UniProtKB	Sequence conflict	231	231	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P10363 1 409
+P10363	UniProtKB	Chain	1	409	.	.	.	ID=PRO_0000046736;Note=DNA primase small subunit	
+P10363	UniProtKB	Motif	123	133	.	.	.	Note=Zinc knuckle motif	
+P10363	UniProtKB	Active site	46	46	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10363	UniProtKB	Active site	111	111	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10363	UniProtKB	Active site	113	113	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10363	UniProtKB	Mutagenesis	184	184	.	.	.	Note=Temperature-sensitive. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2023935;Dbxref=PMID:2023935	
+P10363	UniProtKB	Mutagenesis	316	316	.	.	.	Note=Cold-sensitive. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2023935;Dbxref=PMID:2023935	
+P10363	UniProtKB	Sequence conflict	231	232	.	.	.	Note=EQ->DE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10363	UniProtKB	Helix	12	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	25	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Beta strand	34	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	40	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Beta strand	45	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Beta strand	56	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	65	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Beta strand	78	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Beta strand	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Beta strand	108	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	114	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Turn	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	131	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Beta strand	157	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Beta strand	163	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	181	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Beta strand	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	211	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	224	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	228	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	238	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	252	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	270	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Beta strand	287	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	290	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	315	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Turn	333	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	348	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	354	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+P10363	UniProtKB	Helix	367	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LIM	
+P10363	UniProtKB	Helix	373	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2	
+##sequence-region P40494 1 810
+P40494	UniProtKB	Chain	1	810	.	.	.	ID=PRO_0000086581;Note=Actin-regulating kinase PRK1	
+P40494	UniProtKB	Domain	22	298	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P40494	UniProtKB	Nucleotide binding	28	36	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P40494	UniProtKB	Region	743	756	.	.	.	Note=Interaction with SH3 domain of ABP1	
+P40494	UniProtKB	Active site	158	158	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P40494	UniProtKB	Binding site	56	56	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P40494	UniProtKB	Modified residue	402	402	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40494	UniProtKB	Modified residue	428	428	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40494	UniProtKB	Modified residue	484	484	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40494	UniProtKB	Modified residue	553	553	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40494	UniProtKB	Modified residue	556	556	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40494	UniProtKB	Mutagenesis	56	56	.	.	.	Note=Abolishes protein kinase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10087264;Dbxref=PMID:10087264	
+P40494	UniProtKB	Sequence conflict	786	786	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53835 1 661
+P53835	UniProtKB	Chain	1	661	.	.	.	ID=PRO_0000203377;Note=Plasma membrane fusion protein PRM1	
+P53835	UniProtKB	Topological domain	1	16	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Topological domain	38	105	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Topological domain	127	296	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Transmembrane	297	317	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Topological domain	318	424	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Transmembrane	425	445	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Topological domain	446	629	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Transmembrane	630	650	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Topological domain	651	661	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	135	135	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	145	145	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	188	188	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	197	197	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	231	231	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	252	252	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	272	272	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	280	280	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	490	490	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	505	505	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	512	512	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	531	531	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	573	573	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53835	UniProtKB	Glycosylation	587	587	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P49704 1 494
+P49704	UniProtKB	Chain	1	494	.	.	.	ID=PRO_0000058589;Note=Pre-mRNA-processing factor 31	
+P49704	UniProtKB	Domain	225	346	.	.	.	Note=Nop;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00690	
+P49704	UniProtKB	Coiled coil	88	122	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49704	UniProtKB	Coiled coil	191	225	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49704	UniProtKB	Site	257	257	.	.	.	Note=Interaction with U4 snRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P49704	UniProtKB	Sequence conflict	31	31	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P28004 1 379
+P28004	UniProtKB	Chain	1	379	.	.	.	ID=PRO_0000084825;Note=Pre-mRNA-processing protein 45	
+P28004	UniProtKB	Helix	31	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28004	UniProtKB	Turn	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28004	UniProtKB	Helix	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28004	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28004	UniProtKB	Helix	63	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28004	UniProtKB	Helix	90	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28004	UniProtKB	Beta strand	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28004	UniProtKB	Beta strand	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28004	UniProtKB	Helix	159	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28004	UniProtKB	Helix	182	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P28004	UniProtKB	Helix	199	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P19735 1 899
+P19735	UniProtKB	Chain	1	899	.	.	.	ID=PRO_0000205756;Note=Pre-mRNA-splicing factor 6	
+P19735	UniProtKB	Repeat	221	253	.	.	.	Note=HAT 1	
+P19735	UniProtKB	Repeat	255	287	.	.	.	Note=HAT 2	
+P19735	UniProtKB	Repeat	289	318	.	.	.	Note=HAT 3	
+P19735	UniProtKB	Repeat	319	350	.	.	.	Note=HAT 4	
+P19735	UniProtKB	Repeat	352	381	.	.	.	Note=HAT 5	
+P19735	UniProtKB	Repeat	383	414	.	.	.	Note=HAT 6	
+P19735	UniProtKB	Repeat	493	525	.	.	.	Note=HAT 7	
+P19735	UniProtKB	Repeat	545	578	.	.	.	Note=HAT 8	
+P19735	UniProtKB	Repeat	608	645	.	.	.	Note=HAT 9	
+P19735	UniProtKB	Repeat	648	680	.	.	.	Note=HAT 10	
+P19735	UniProtKB	Repeat	682	714	.	.	.	Note=HAT 11	
+P19735	UniProtKB	Repeat	751	783	.	.	.	Note=HAT 12	
+P19735	UniProtKB	Repeat	819	851	.	.	.	Note=HAT 13	
+##sequence-region P33334 1 2413
+P33334	UniProtKB	Chain	1	2413	.	.	.	ID=PRO_0000097042;Note=Pre-mRNA-splicing factor 8	
+P33334	UniProtKB	Domain	2182	2311	.	.	.	Note=MPN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+P33334	UniProtKB	Region	253	543	.	.	.	Note=SNU114/CWC21 interacting domain (SCwid)	
+P33334	UniProtKB	Region	885	1375	.	.	.	Note=Reverse transcriptase homology domain	
+P33334	UniProtKB	Region	1376	1649	.	.	.	Note=Linker	
+P33334	UniProtKB	Region	1585	1598	.	.	.	Note=Important for branch point selection	
+P33334	UniProtKB	Region	1653	1824	.	.	.	Note=Restriction endonuclease homology domain	
+P33334	UniProtKB	Region	1839	2092	.	.	.	Note=RNase H homology domain	
+P33334	UniProtKB	Compositional bias	5	9	.	.	.	Note=Poly-Pro	
+P33334	UniProtKB	Compositional bias	20	27	.	.	.	Note=Poly-Pro	
+P33334	UniProtKB	Compositional bias	50	56	.	.	.	Note=Poly-Pro	
+P33334	UniProtKB	Compositional bias	72	78	.	.	.	Note=Poly-Pro	
+P33334	UniProtKB	Mutagenesis	1658	1658	.	.	.	Note=No effect on viability. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23354046;Dbxref=PMID:23354046	
+P33334	UniProtKB	Mutagenesis	1684	1684	.	.	.	Note=No effect on viability. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23354046;Dbxref=PMID:23354046	
+P33334	UniProtKB	Mutagenesis	1687	1687	.	.	.	Note=No effect on viability. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23354046;Dbxref=PMID:23354046	
+P33334	UniProtKB	Mutagenesis	1700	1700	.	.	.	Note=No effect on viability. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23354046;Dbxref=PMID:23354046	
+P33334	UniProtKB	Mutagenesis	1735	1735	.	.	.	Note=No effect on viability. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23354046;Dbxref=PMID:23354046	
+P33334	UniProtKB	Mutagenesis	1853	1853	.	.	.	Note=Alters protein folding. Severely impaired growth. Strongly reduced growth at 35 degrees Celsius%3B when associated with A-1854. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18779563,ECO:0000269|PubMed:18836455,ECO:0000269|PubMed:18843295;Dbxref=PMID:18779563,PMID:18836455,PMID:18843295	
+P33334	UniProtKB	Mutagenesis	1853	1853	.	.	.	Note=Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. D->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18779563,ECO:0000269|PubMed:18836455,ECO:0000269|PubMed:18843295;Dbxref=PMID:18779563,PMID:18836455,PMID:18843295	
+P33334	UniProtKB	Mutagenesis	1854	1854	.	.	.	Note=Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. Strongly reduced growth at 35 degrees Celsius%3B when associated with A-1853. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18836455,ECO:0000269|PubMed:18843295;Dbxref=PMID:18836455,PMID:18843295	
+P33334	UniProtKB	Mutagenesis	1854	1854	.	.	.	Note=Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18836455,ECO:0000269|PubMed:18843295;Dbxref=PMID:18836455,PMID:18843295	
+P33334	UniProtKB	Mutagenesis	1855	1855	.	.	.	Note=Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18843295;Dbxref=PMID:18843295	
+P33334	UniProtKB	Mutagenesis	1936	1936	.	.	.	Note=Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18843295;Dbxref=PMID:18843295	
+P33334	UniProtKB	Mutagenesis	1937	1937	.	.	.	Note=Severely impaired growth. Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18843295;Dbxref=PMID:18843295	
+P33334	UniProtKB	Sequence conflict	388	420	.	.	.	Note=PHLYNSRPRSVRIPWYNNPVSCIIQNDEEYDTP->LIYIIPGPVQCAYHGIIIQCRVLSRTMRSTTRL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33334	UniProtKB	Sequence conflict	1132	1132	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33334	UniProtKB	Sequence conflict	1575	1575	.	.	.	Note=W->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33334	UniProtKB	Helix	136	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	155	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	168	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	188	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	210	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	239	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Turn	251	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Turn	272	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	282	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	290	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	305	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	316	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	333	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	370	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	381	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	388	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	392	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	417	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Turn	461	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	473	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	484	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	496	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	503	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	512	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	516	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Turn	541	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	547	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	557	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	564	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	590	593	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	599	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	607	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	617	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	647	663	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	666	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	671	673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	674	689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	697	699	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	705	735	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Turn	747	749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	750	769	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	776	794	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	806	835	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	842	870	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	885	892	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	908	924	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	931	945	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	947	960	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	967	969	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	975	979	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	986	1005	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1013	1015	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1021	1033	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1036	1039	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1042	1044	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	1046	1053	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1056	1060	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1063	1071	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1076	1085	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1087	1092	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1095	1098	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1110	1135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1138	1140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZEF	
+P33334	UniProtKB	Helix	1150	1154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1156	1164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1167	1174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1176	1189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1197	1200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1205	1207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	1209	1211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1217	1231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1236	1238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1243	1245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1246	1252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1258	1262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1265	1271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1272	1274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1283	1289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1291	1293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1295	1304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1306	1320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1328	1346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1348	1351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1354	1375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1380	1382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	1385	1389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1392	1394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1409	1412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1414	1417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1422	1425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1427	1429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1434	1436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZEF	
+P33334	UniProtKB	Helix	1440	1443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1447	1470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1477	1479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1480	1482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1487	1490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1491	1495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1499	1502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1508	1514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1515	1517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1530	1533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1540	1549	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1552	1558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1559	1561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Helix	1563	1565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1603	1614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1617	1619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1624	1626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	1628	1630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P33334	UniProtKB	Beta strand	1633	1636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1641	1648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1649	1652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1653	1670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1671	1677	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1678	1683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1690	1692	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1700	1711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1726	1739	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1743	1745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1748	1759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1763	1766	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1768	1778	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1779	1782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Beta strand	1783	1788	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1794	1808	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1810	1822	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Turn	1837	1839	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1840	1844	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Beta strand	1845	1847	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Beta strand	1849	1853	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Beta strand	1857	1864	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Beta strand	1866	1868	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ILG	
+P33334	UniProtKB	Beta strand	1870	1875	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Beta strand	1877	1882	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Turn	1884	1886	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Beta strand	1888	1894	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Helix	1896	1899	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Helix	1905	1923	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Helix	1926	1928	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Beta strand	1931	1937	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Helix	1938	1940	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Helix	1941	1947	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Turn	1948	1950	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Beta strand	1954	1957	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Beta strand	1959	1961	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	1965	1970	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Helix	1972	1980	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Beta strand	1985	1990	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Turn	1991	1994	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Helix	1995	1997	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Helix	2001	2017	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Helix	2019	2026	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Beta strand	2030	2032	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9P	
+P33334	UniProtKB	Beta strand	2039	2041	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ILH	
+P33334	UniProtKB	Helix	2045	2067	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Helix	2071	2073	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ILH	
+P33334	UniProtKB	Helix	2076	2084	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT	
+P33334	UniProtKB	Helix	2149	2159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Helix	2160	2167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2168	2171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2178	2180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P33334	UniProtKB	Beta strand	2182	2186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Helix	2187	2195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2199	2201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2204	2211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2218	2225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2229	2231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2236	2238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2245	2247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZEF	
+P33334	UniProtKB	Beta strand	2254	2264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Helix	2271	2281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Turn	2282	2284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2289	2296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2299	2307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Helix	2309	2316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Turn	2317	2320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBG	
+P33334	UniProtKB	Turn	2323	2325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD	
+P33334	UniProtKB	Helix	2331	2333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2334	2345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2348	2352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Helix	2360	2362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43	
+P33334	UniProtKB	Helix	2363	2365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Beta strand	2374	2376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Helix	2385	2387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4	
+P33334	UniProtKB	Helix	2389	2396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA	
+P33334	UniProtKB	Turn	2406	2408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52	
+##sequence-region P21243 1 252
+P21243	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P21243	UniProtKB	Chain	2	252	.	.	.	ID=PRO_0000124141;Note=Proteasome subunit alpha type-1	
+P21243	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P21243	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P21243	UniProtKB	Cross-link	232	232	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P21243	UniProtKB	Helix	11	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Turn	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD2	
+P21243	UniProtKB	Helix	26	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Turn	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	42	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	48	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D29	
+P21243	UniProtKB	Helix	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	71	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	80	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Helix	87	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Helix	114	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP	
+P21243	UniProtKB	Beta strand	140	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Turn	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	151	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G0U	
+P21243	UniProtKB	Beta strand	163	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Helix	175	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	191	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Helix	199	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	222	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Beta strand	232	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Helix	238	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21243	UniProtKB	Turn	249	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65	
+##sequence-region P21242 1 288
+P21242	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1697860;Dbxref=PMID:22814378,PMID:1697860	
+P21242	UniProtKB	Chain	2	288	.	.	.	ID=PRO_0000124102;Note=Probable proteasome subunit alpha type-7	
+P21242	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P21242	UniProtKB	Helix	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R18	
+P21242	UniProtKB	Beta strand	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4INU	
+P21242	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QLV	
+P21242	UniProtKB	Helix	22	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Beta strand	37	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Beta strand	45	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Turn	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Beta strand	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Turn	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Beta strand	74	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Helix	82	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Helix	109	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Turn	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FZC	
+P21242	UniProtKB	Beta strand	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GPT	
+P21242	UniProtKB	Beta strand	134	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Beta strand	145	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Turn	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD2	
+P21242	UniProtKB	Beta strand	157	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Helix	169	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Helix	189	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Helix	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Beta strand	212	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Turn	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Beta strand	227	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P21242	UniProtKB	Helix	234	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+##sequence-region P07272 1 904
+P07272	UniProtKB	Chain	1	904	.	.	.	ID=PRO_0000114965;Note=Pyrimidine pathway regulatory protein 1	
+P07272	UniProtKB	DNA binding	34	61	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P07272	UniProtKB	Metal binding	34	34	.	.	.	Note=Zinc 1	
+P07272	UniProtKB	Metal binding	34	34	.	.	.	Note=Zinc 2	
+P07272	UniProtKB	Metal binding	37	37	.	.	.	Note=Zinc 1	
+P07272	UniProtKB	Metal binding	44	44	.	.	.	Note=Zinc 1	
+P07272	UniProtKB	Metal binding	51	51	.	.	.	Note=Zinc 1	
+P07272	UniProtKB	Metal binding	51	51	.	.	.	Note=Zinc 2	
+P07272	UniProtKB	Metal binding	54	54	.	.	.	Note=Zinc 2	
+P07272	UniProtKB	Metal binding	61	61	.	.	.	Note=Zinc 2	
+P07272	UniProtKB	Helix	35	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI	
+P07272	UniProtKB	Helix	52	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI	
+P07272	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI	
+P07272	UniProtKB	Turn	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI	
+P07272	UniProtKB	Beta strand	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI	
+P07272	UniProtKB	Helix	74	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI	
+P07272	UniProtKB	Turn	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI	
+##sequence-region P38148 1 807
+P38148	UniProtKB	Chain	1	807	.	.	.	ID=PRO_0000094921;Note=Dual specificity protein phosphatase PPS1	
+P38148	UniProtKB	Region	593	807	.	.	.	Note=Catalytic	
+P38148	UniProtKB	Active site	725	725	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10044	
+##sequence-region P26570 1 692
+P26570	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P26570	UniProtKB	Chain	2	692	.	.	.	ID=PRO_0000058891;Note=Serine/threonine-protein phosphatase PP-Z1	
+P26570	UniProtKB	Compositional bias	2	319	.	.	.	Note=Ser-rich	
+P26570	UniProtKB	Active site	480	480	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26570	UniProtKB	Metal binding	419	419	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26570	UniProtKB	Metal binding	421	421	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26570	UniProtKB	Metal binding	447	447	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26570	UniProtKB	Metal binding	447	447	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26570	UniProtKB	Metal binding	479	479	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26570	UniProtKB	Metal binding	528	528	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26570	UniProtKB	Metal binding	603	603	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26570	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P26570	UniProtKB	Modified residue	171	171	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P26570	UniProtKB	Modified residue	209	209	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33329	
+P26570	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P26570	UniProtKB	Modified residue	261	261	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P26570	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P26570	UniProtKB	Modified residue	690	690	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P26570	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P26570	UniProtKB	Sequence conflict	340	340	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P26570	UniProtKB	Sequence conflict	440	440	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P26570	UniProtKB	Sequence conflict	649	649	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P49960 1 444
+P49960	UniProtKB	Chain	1	444	.	.	.	ID=PRO_0000081736;Note=U4/U6 snRNA-associated-splicing factor PRP24	
+P49960	UniProtKB	Domain	41	116	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P49960	UniProtKB	Domain	117	195	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P49960	UniProtKB	Domain	210	289	.	.	.	Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P49960	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P49960	UniProtKB	Sequence conflict	197	197	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P49960	UniProtKB	Helix	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	42	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GO9	
+P49960	UniProtKB	Helix	54	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	67	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	78	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	90	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Turn	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	118	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	130	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Turn	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KH9	
+P49960	UniProtKB	Beta strand	144	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GHP	
+P49960	UniProtKB	Beta strand	160	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	168	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	189	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Turn	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GHP	
+P49960	UniProtKB	Beta strand	211	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	219	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	224	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	232	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	237	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Turn	244	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	252	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	263	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	270	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	275	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TF6	
+P49960	UniProtKB	Beta strand	283	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	290	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	307	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	313	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	325	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	343	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	350	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	354	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	362	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Beta strand	373	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9W	
+P49960	UniProtKB	Beta strand	383	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+P49960	UniProtKB	Helix	387	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T	
+##sequence-region P39682 1 629
+P39682	UniProtKB	Chain	1	629	.	.	.	ID=PRO_0000205758;Note=Pre-mRNA-processing factor 39	
+P39682	UniProtKB	Repeat	68	100	.	.	.	Note=HAT 1	
+P39682	UniProtKB	Repeat	102	134	.	.	.	Note=HAT 2	
+P39682	UniProtKB	Repeat	138	173	.	.	.	Note=HAT 3	
+P39682	UniProtKB	Repeat	175	208	.	.	.	Note=HAT 4	
+P39682	UniProtKB	Repeat	233	265	.	.	.	Note=HAT 5	
+P39682	UniProtKB	Repeat	270	302	.	.	.	Note=HAT 6	
+P39682	UniProtKB	Repeat	446	480	.	.	.	Note=HAT 7	
+P39682	UniProtKB	Sequence conflict	615	615	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33203 1 583
+P33203	UniProtKB	Chain	1	583	.	.	.	ID=PRO_0000076084;Note=Pre-mRNA-processing protein PRP40	
+P33203	UniProtKB	Domain	1	31	.	.	.	Note=WW 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224	
+P33203	UniProtKB	Domain	42	72	.	.	.	Note=WW 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224	
+P33203	UniProtKB	Domain	132	188	.	.	.	Note=FF 1	
+P33203	UniProtKB	Domain	201	257	.	.	.	Note=FF 2	
+P33203	UniProtKB	Domain	262	332	.	.	.	Note=FF 3	
+P33203	UniProtKB	Domain	354	413	.	.	.	Note=FF 4	
+P33203	UniProtKB	Domain	427	488	.	.	.	Note=FF 5	
+P33203	UniProtKB	Domain	491	552	.	.	.	Note=FF 6	
+P33203	UniProtKB	Modified residue	576	576	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33203	UniProtKB	Mutagenesis	240	240	.	.	.	Note=In PRP40-1 suppressor%3B affects SAR1 mRNA accumulation in U1-U4 mutant at 18 degrees Celsius. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8622699;Dbxref=PMID:8622699	
+P33203	UniProtKB	Mutagenesis	274	274	.	.	.	Note=Temperature sensitive growth at 36 degrees Celsius. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406	
+P33203	UniProtKB	Mutagenesis	277	277	.	.	.	Note=Temperature sensitive growth at 36 degrees Celsius. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406	
+P33203	UniProtKB	Mutagenesis	281	281	.	.	.	Note=Temperature sensitive growth at 36 degrees Celsius. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406	
+P33203	UniProtKB	Mutagenesis	340	340	.	.	.	Note=Wild-type growth at 36 degrees Celsius. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406	
+P33203	UniProtKB	Mutagenesis	344	344	.	.	.	Note=Wild-type growth at 36 degrees Celsius. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406	
+P33203	UniProtKB	Mutagenesis	347	347	.	.	.	Note=Wild-type growth at 36 degrees Celsius. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406	
+P33203	UniProtKB	Beta strand	4	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W	
+P33203	UniProtKB	Beta strand	14	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W	
+P33203	UniProtKB	Turn	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W	
+P33203	UniProtKB	Beta strand	23	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W	
+P33203	UniProtKB	Helix	30	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W	
+P33203	UniProtKB	Beta strand	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W	
+P33203	UniProtKB	Beta strand	55	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W	
+P33203	UniProtKB	Turn	60	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W	
+P33203	UniProtKB	Beta strand	64	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W	
+P33203	UniProtKB	Helix	134	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7E	
+P33203	UniProtKB	Helix	154	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7E	
+P33203	UniProtKB	Helix	167	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7E	
+P33203	UniProtKB	Helix	175	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7E	
+P33203	UniProtKB	Helix	489	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KFD	
+P33203	UniProtKB	Beta strand	510	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KFD	
+P33203	UniProtKB	Helix	519	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KFD	
+P33203	UniProtKB	Helix	533	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KFD	
+P33203	UniProtKB	Helix	539	549	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KFD	
+##sequence-region P40303 1 254
+P40303	UniProtKB	Chain	1	254	.	.	.	ID=PRO_0000124165;Note=Proteasome subunit alpha type-4	
+P40303	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P40303	UniProtKB	Beta strand	7	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FNT	
+P40303	UniProtKB	Turn	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Helix	18	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Beta strand	33	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Beta strand	42	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Turn	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Beta strand	63	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Beta strand	71	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Helix	79	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Helix	106	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Turn	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P40303	UniProtKB	Beta strand	123	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FNT	
+P40303	UniProtKB	Beta strand	130	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Beta strand	146	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Turn	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FNT	
+P40303	UniProtKB	Beta strand	156	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Helix	168	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Beta strand	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP	
+P40303	UniProtKB	Helix	188	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Beta strand	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R17	
+P40303	UniProtKB	Beta strand	210	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Turn	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Beta strand	220	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Helix	226	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40303	UniProtKB	Helix	238	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+##sequence-region P38624 1 215
+P38624	UniProtKB	Propeptide	1	19	.	.	.	ID=PRO_0000026643;Note=Removed in mature form	
+P38624	UniProtKB	Chain	20	215	.	.	.	ID=PRO_0000026644;Note=Proteasome subunit beta type-1	
+P38624	UniProtKB	Active site	20	20	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9087403;Dbxref=PMID:9087403	
+P38624	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38624	UniProtKB	Helix	6	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FGI	
+P38624	UniProtKB	Beta strand	22	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Beta strand	30	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Beta strand	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Beta strand	44	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Beta strand	53	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Beta strand	60	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Helix	68	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Helix	94	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Turn	108	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Beta strand	114	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Turn	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Beta strand	126	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Turn	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD2	
+P38624	UniProtKB	Beta strand	139	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Helix	148	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Helix	154	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Helix	167	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Beta strand	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SDK	
+P38624	UniProtKB	Beta strand	192	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Beta strand	201	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P38624	UniProtKB	Helix	209	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+##sequence-region P25451 1 205
+P25451	UniProtKB	Chain	1	205	.	.	.	ID=PRO_0000148070;Note=Proteasome subunit beta type-3	
+P25451	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25451	UniProtKB	Cross-link	70	70	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25451	UniProtKB	Helix	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Beta strand	11	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Beta strand	18	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Beta strand	34	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Beta strand	43	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Beta strand	49	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Helix	57	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Helix	84	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Turn	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Beta strand	105	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Turn	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Beta strand	119	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Beta strand	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65	
+P25451	UniProtKB	Beta strand	134	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Helix	143	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Helix	160	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Beta strand	178	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNN	
+P25451	UniProtKB	Beta strand	185	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P25451	UniProtKB	Beta strand	195	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+##sequence-region P40359 1 213
+P40359	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000194822;Note=DNA replication complex GINS protein PSF2	
+##sequence-region Q08217 1 1101
+Q08217	UniProtKB	Chain	1	1101	.	.	.	ID=PRO_0000086156;Note=Serine/threonine-protein kinase PSK2	
+Q08217	UniProtKB	Domain	841	1099	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q08217	UniProtKB	Nucleotide binding	847	855	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q08217	UniProtKB	Active site	975	975	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q08217	UniProtKB	Binding site	870	870	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q08217	UniProtKB	Modified residue	118	118	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P14747 1 604
+P14747	UniProtKB	Chain	1	604	.	.	.	ID=PRO_0000058837;Note=Serine/threonine-protein phosphatase 2B catalytic subunit A2	
+P14747	UniProtKB	Region	501	523	.	.	.	Note=Calmodulin-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14747	UniProtKB	Active site	205	205	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14747	UniProtKB	Metal binding	144	144	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14747	UniProtKB	Metal binding	146	146	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14747	UniProtKB	Metal binding	172	172	.	.	.	Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14747	UniProtKB	Metal binding	172	172	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14747	UniProtKB	Metal binding	204	204	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14747	UniProtKB	Metal binding	253	253	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14747	UniProtKB	Metal binding	359	359	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P14747	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14747	UniProtKB	Modified residue	489	489	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14747	UniProtKB	Modified residue	520	520	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14747	UniProtKB	Sequence conflict	87	88	.	.	.	Note=EL->DV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14747	UniProtKB	Sequence conflict	581	581	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P24031 1 467
+P24031	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Chain	18	467	.	.	.	ID=PRO_0000023953;Note=Constitutive acid phosphatase	
+P24031	UniProtKB	Active site	75	75	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P24031	UniProtKB	Active site	338	338	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P24031	UniProtKB	Glycosylation	97	97	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Glycosylation	162	162	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Glycosylation	192	192	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Glycosylation	250	250	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Glycosylation	315	315	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Glycosylation	356	356	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Glycosylation	390	390	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Glycosylation	439	439	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Glycosylation	445	445	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Glycosylation	456	456	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Glycosylation	461	461	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P24031	UniProtKB	Sequence conflict	219	221	.	.	.	Note=DED->MKT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P52290 1 468
+P52290	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52290	UniProtKB	Chain	21	468	.	.	.	ID=PRO_0000023958;Note=Probable acid phosphatase DIA3	
+P52290	UniProtKB	Active site	76	76	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52290	UniProtKB	Active site	339	339	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52290	UniProtKB	Glycosylation	98	98	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52290	UniProtKB	Glycosylation	163	163	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52290	UniProtKB	Glycosylation	193	193	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52290	UniProtKB	Glycosylation	202	202	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52290	UniProtKB	Glycosylation	238	238	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52290	UniProtKB	Glycosylation	251	251	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52290	UniProtKB	Glycosylation	316	316	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52290	UniProtKB	Glycosylation	357	357	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52290	UniProtKB	Glycosylation	391	391	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52290	UniProtKB	Glycosylation	457	457	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52290	UniProtKB	Glycosylation	462	462	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40347 1 161
+P40347	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000046565;Note=Low molecular weight phosphotyrosine protein phosphatase	
+P40347	UniProtKB	Active site	14	14	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40347	UniProtKB	Active site	20	20	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40347	UniProtKB	Active site	133	133	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40347	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40347	UniProtKB	Beta strand	8	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+P40347	UniProtKB	Helix	20	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+P40347	UniProtKB	Helix	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+P40347	UniProtKB	Beta strand	41	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+P40347	UniProtKB	Turn	52	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1P	
+P40347	UniProtKB	Helix	60	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+P40347	UniProtKB	Helix	82	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+P40347	UniProtKB	Beta strand	89	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+P40347	UniProtKB	Helix	96	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+P40347	UniProtKB	Beta strand	113	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+P40347	UniProtKB	Helix	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+P40347	UniProtKB	Beta strand	124	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+P40347	UniProtKB	Helix	139	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q	
+##sequence-region P40012 1 539
+P40012	UniProtKB	Chain	1	539	.	.	.	ID=PRO_0000135274;Note=Protoporphyrinogen oxidase	
+P40012	UniProtKB	Nucleotide binding	18	23	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40012	UniProtKB	Nucleotide binding	43	44	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40012	UniProtKB	Nucleotide binding	70	73	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40012	UniProtKB	Nucleotide binding	521	523	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40012	UniProtKB	Binding site	51	51	.	.	.	Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40012	UniProtKB	Binding site	300	300	.	.	.	Note=FAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40012	UniProtKB	Mutagenesis	422	422	.	.	.	Note=In HEM14-1%3B loss of activity. L->P	
+P40012	UniProtKB	Mutagenesis	424	424	.	.	.	Note=In HEM14-1%3B loss of activity. K->E	
+##sequence-region P32945 1 549
+P32945	UniProtKB	Chain	1	549	.	.	.	ID=PRO_0000058893;Note=Serine/threonine-protein phosphatase PPQ	
+P32945	UniProtKB	Compositional bias	113	219	.	.	.	Note=Ser-rich	
+P32945	UniProtKB	Active site	362	362	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32945	UniProtKB	Metal binding	301	301	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32945	UniProtKB	Metal binding	303	303	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32945	UniProtKB	Metal binding	329	329	.	.	.	Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32945	UniProtKB	Metal binding	329	329	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32945	UniProtKB	Metal binding	361	361	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32945	UniProtKB	Metal binding	410	410	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32945	UniProtKB	Metal binding	485	485	.	.	.	Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12036 1 173
+Q12036	UniProtKB	Chain	1	173	.	.	.	ID=PRO_0000175745;Note=Mitochondrial holo-[acyl-carrier-protein] synthase	
+##sequence-region P40534 1 656
+P40534	UniProtKB	Chain	1	656	.	.	.	ID=PRO_0000202994;Note=Pheromone-regulated membrane protein 2	
+P40534	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40534	UniProtKB	Transmembrane	320	340	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40534	UniProtKB	Transmembrane	422	442	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40534	UniProtKB	Transmembrane	634	654	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08931 1 133
+Q08931	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000262749;Note=Pheromone-regulated membrane protein 3	
+Q08931	UniProtKB	Topological domain	1	104	.	.	.	Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08931	UniProtKB	Transmembrane	105	127	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08931	UniProtKB	Topological domain	128	133	.	.	.	Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08931	UniProtKB	Motif	69	75	.	.	.	Note=Bipartite nuclear localization signal	
+Q08931	UniProtKB	Mutagenesis	106	106	.	.	.	Note=In pmr3-7%3B leads to mislocalization and decreases nuclear fusion efficiency when temperature rises. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527	
+Q08931	UniProtKB	Mutagenesis	108	108	.	.	.	Note=In pmr3-1%3B decreases nuclear fusion efficiency. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527	
+Q08931	UniProtKB	Mutagenesis	112	112	.	.	.	Note=In pmr3-8%3B leads to mislocalization and decreases nuclear fusion efficiency. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527	
+Q08931	UniProtKB	Mutagenesis	114	114	.	.	.	Note=In pmr3-3%3B leads to mislocalization and decreases nuclear fusion efficiency. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527	
+Q08931	UniProtKB	Mutagenesis	115	115	.	.	.	Note=In pmr3-5%3B leads to mislocalization and decreases nuclear fusion efficiency. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527	
+Q08931	UniProtKB	Mutagenesis	121	121	.	.	.	Note=In pmr3-6%3B leads to mislocalization. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527	
+Q08931	UniProtKB	Mutagenesis	122	122	.	.	.	Note=In pmr3-2%3B leads to mislocalization and decreases nuclear fusion efficiency. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527	
+##sequence-region P40476 1 318
+P40476	UniProtKB	Chain	1	318	.	.	.	ID=PRO_0000202963;Note=Pheromone-regulated membrane protein 5	
+P40476	UniProtKB	Transmembrane	75	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40476	UniProtKB	Compositional bias	17	54	.	.	.	Note=Ser-rich	
+P40476	UniProtKB	Compositional bias	240	246	.	.	.	Note=Poly-Ser	
+P40476	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40476	UniProtKB	Modified residue	279	279	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40476	UniProtKB	Modified residue	282	282	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40476	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40476	UniProtKB	Cross-link	314	314	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P53174 1 237
+P53174	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000207523;Note=Pheromone-regulated membrane protein 8	
+P53174	UniProtKB	Topological domain	1	47	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53174	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53174	UniProtKB	Topological domain	69	74	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53174	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53174	UniProtKB	Topological domain	96	237	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53174	UniProtKB	Region	236	237	.	.	.	Note=COPII binding	
+##sequence-region P07274 1 126
+P07274	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000199608;Note=Profilin	
+P07274	UniProtKB	Helix	3	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR	
+P07274	UniProtKB	Beta strand	17	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR	
+P07274	UniProtKB	Beta strand	29	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR	
+P07274	UniProtKB	Helix	40	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR	
+P07274	UniProtKB	Helix	54	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR	
+P07274	UniProtKB	Beta strand	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR	
+P07274	UniProtKB	Beta strand	66	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR	
+P07274	UniProtKB	Beta strand	75	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR	
+P07274	UniProtKB	Beta strand	85	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR	
+P07274	UniProtKB	Beta strand	93	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR	
+P07274	UniProtKB	Helix	107	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR	
+##sequence-region P15938 1 1071
+P15938	UniProtKB	Chain	1	1071	.	.	.	ID=PRO_0000055150;Note=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16	
+P15938	UniProtKB	Domain	360	526	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P15938	UniProtKB	Domain	540	735	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P15938	UniProtKB	Nucleotide binding	373	380	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P15938	UniProtKB	Motif	473	476	.	.	.	Note=DEAH box	
+P15938	UniProtKB	Mutagenesis	386	386	.	.	.	Note=Suppressor phenotype. Y->D	
+P15938	UniProtKB	Sequence conflict	698	698	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33411 1 251
+P33411	UniProtKB	Chain	1	251	.	.	.	ID=PRO_0000058586;Note=Pre-mRNA-splicing factor 18	
+P33411	UniProtKB	Sequence conflict	194	249	.	.	.	Note=PIGVTSVGIHARSAHSKIQGGRNAANIMIDERTRLWITSIKRLITFEEWYTSNHDS->LLVL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33411	UniProtKB	Sequence conflict	201	251	.	.	.	Note=GIHARSAHSKIQGGRNAANIMIDERTRLWITSIKRLITFEEWYTSNHDSLA->AFMLVVHIRKFKEAGMLLT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33411	UniProtKB	Helix	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK	
+P33411	UniProtKB	Helix	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK	
+P33411	UniProtKB	Helix	106	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK	
+P33411	UniProtKB	Helix	127	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK	
+P33411	UniProtKB	Turn	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK	
+P33411	UniProtKB	Helix	136	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK	
+P33411	UniProtKB	Helix	157	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK	
+P33411	UniProtKB	Helix	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK	
+P33411	UniProtKB	Helix	176	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK	
+P33411	UniProtKB	Helix	224	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK	
+##sequence-region Q00723 1 242
+Q00723	UniProtKB	Chain	1	242	.	.	.	ID=PRO_0000058590;Note=Pre-mRNA-splicing factor 38	
+Q00723	UniProtKB	Compositional bias	217	242	.	.	.	Note=Ser-rich	
+Q00723	UniProtKB	Mutagenesis	87	87	.	.	.	Note=In PRP83-2%3B temperature-sensitive%3B blocks splicing of RPS17A after a 2 hour shift to the restrictive temperature of 37 degrees Celsius%3B spliceosome assembly arrested at the complex I stage. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9582287;Dbxref=PMID:9582287	
+##sequence-region Q03776 1 544
+Q03776	UniProtKB	Chain	1	544	.	.	.	ID=PRO_0000262751;Note=U1 small nuclear ribonucleoprotein component PRP42	
+Q03776	UniProtKB	Repeat	7	39	.	.	.	Note=HAT 1	
+Q03776	UniProtKB	Repeat	51	83	.	.	.	Note=HAT 2	
+Q03776	UniProtKB	Repeat	85	118	.	.	.	Note=HAT 3	
+Q03776	UniProtKB	Repeat	121	156	.	.	.	Note=HAT 4	
+Q03776	UniProtKB	Repeat	163	195	.	.	.	Note=HAT 5	
+Q03776	UniProtKB	Repeat	255	288	.	.	.	Note=HAT 6	
+Q03776	UniProtKB	Repeat	290	322	.	.	.	Note=HAT 7	
+Q03776	UniProtKB	Repeat	366	397	.	.	.	Note=HAT 8	
+Q03776	UniProtKB	Repeat	456	488	.	.	.	Note=HAT 9	
+Q03776	UniProtKB	Motif	230	235	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53131 1 767
+P53131	UniProtKB	Chain	1	767	.	.	.	ID=PRO_0000055145;Note=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43	
+P53131	UniProtKB	Domain	103	268	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53131	UniProtKB	Domain	293	473	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P53131	UniProtKB	Nucleotide binding	116	123	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53131	UniProtKB	Motif	215	218	.	.	.	Note=DEAH box	
+P53131	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53131	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53131	UniProtKB	Mutagenesis	194	194	.	.	.	Note=In PRP43-DN1%3B dominant-negative phenotype. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9342317;Dbxref=PMID:9342317	
+P53131	UniProtKB	Mutagenesis	247	247	.	.	.	Note=In PRP43-DN2%3B dominant-negative phenotype. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9342317;Dbxref=PMID:9342317	
+P53131	UniProtKB	Mutagenesis	395	395	.	.	.	Note=In PRP43-1%3B temperature-sensitive. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9342317;Dbxref=PMID:9342317	
+P53131	UniProtKB	Beta strand	9	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Turn	14	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	19	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Turn	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	60	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Turn	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JPT	
+P53131	UniProtKB	Helix	81	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	94	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	99	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	110	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	122	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	136	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	142	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	150	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Turn	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	172	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	187	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	193	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	209	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	222	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	242	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	253	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	264	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	274	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	286	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	305	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	313	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	339	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	350	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	354	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	364	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	370	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	378	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	388	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	395	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Turn	404	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	408	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	418	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	430	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	442	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	456	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	463	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	477	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	488	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	512	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	520	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	524	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	533	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	539	549	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	559	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JPT	
+P53131	UniProtKB	Helix	562	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	578	589	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	592	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	599	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	610	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	644	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	659	663	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Turn	665	667	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KX2	
+P53131	UniProtKB	Beta strand	670	672	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Turn	673	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	678	681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Beta strand	692	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	715	721	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Turn	723	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	728	730	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+P53131	UniProtKB	Helix	735	748	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU	
+##sequence-region P21372 1 849
+P21372	UniProtKB	Chain	1	849	.	.	.	ID=PRO_0000055126;Note=Pre-mRNA-processing ATP-dependent RNA helicase PRP5	
+P21372	UniProtKB	Domain	287	467	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P21372	UniProtKB	Domain	502	661	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P21372	UniProtKB	Nucleotide binding	300	307	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P21372	UniProtKB	Coiled coil	13	81	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21372	UniProtKB	Motif	90	96	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21372	UniProtKB	Motif	255	284	.	.	.	Note=Q motif	
+P21372	UniProtKB	Motif	415	418	.	.	.	Note=DEAD box	
+P21372	UniProtKB	Mutagenesis	293	293	.	.	.	Note=In PRP5-1%3B no growth at 37 degrees Celsius and impairs pre-spliceosome formation in vitro. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11927574,ECO:0000269|PubMed:8405998;Dbxref=PMID:11927574,PMID:8405998	
+P21372	UniProtKB	Helix	223	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	230	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	243	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	257	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	264	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	281	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	296	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	306	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	332	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	340	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	362	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	372	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	383	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	389	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	398	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	411	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	417	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	426	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	441	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	451	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	461	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	465	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	479	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	489	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	528	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	535	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	553	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	561	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	578	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	583	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	595	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	606	613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	614	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	619	621	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Beta strand	624	630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	634	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	646	650	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+P21372	UniProtKB	Helix	654	672	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY	
+##sequence-region P19736 1 530
+P19736	UniProtKB	Chain	1	530	.	.	.	ID=PRO_0000174321;Note=Pre-mRNA-splicing factor PRP9	
+P19736	UniProtKB	Zinc finger	280	310	.	.	.	Note=Matrin-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00130	
+P19736	UniProtKB	Zinc finger	421	452	.	.	.	Note=Matrin-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00130	
+P19736	UniProtKB	Helix	3	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	30	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	51	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Beta strand	58	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	69	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	113	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	137	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Beta strand	149	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Turn	172	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	183	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	200	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Beta strand	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	215	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	227	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	253	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	268	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Turn	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Turn	283	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Beta strand	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	292	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Beta strand	299	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	302	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	312	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	329	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+P19736	UniProtKB	Helix	347	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW	
+##sequence-region Q12310 1 699
+Q12310	UniProtKB	Chain	1	699	.	.	.	ID=PRO_0000262752;Note=Serine/threonine-protein kinase PRR2	
+Q12310	UniProtKB	Domain	361	653	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12310	UniProtKB	Nucleotide binding	367	375	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12310	UniProtKB	Active site	484	484	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q12310	UniProtKB	Binding site	390	390	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12310	UniProtKB	Mutagenesis	390	390	.	.	.	Note=Abolishes kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337509;Dbxref=PMID:11337509	
+##sequence-region P40327 1 437
+P40327	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+P40327	UniProtKB	Chain	2	437	.	.	.	ID=PRO_0000084685;Note=26S proteasome regulatory subunit 4 homolog	
+P40327	UniProtKB	Nucleotide binding	223	230	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40327	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+P40327	UniProtKB	Cross-link	234	234	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40327	UniProtKB	Cross-link	255	255	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40327	UniProtKB	Cross-link	290	290	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40327	UniProtKB	Mutagenesis	229	229	.	.	.	Note=73%25 loss of ATPase activity. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7721833;Dbxref=PMID:7721833	
+P40327	UniProtKB	Sequence conflict	347	347	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33297 1 434
+P33297	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901	
+P33297	UniProtKB	Chain	2	434	.	.	.	ID=PRO_0000084708;Note=26S proteasome regulatory subunit 6A	
+P33297	UniProtKB	Nucleotide binding	222	229	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33297	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901	
+P33297	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33297	UniProtKB	Helix	356	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK	
+P33297	UniProtKB	Helix	376	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK	
+P33297	UniProtKB	Turn	382	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK	
+P33297	UniProtKB	Helix	388	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK	
+P33297	UniProtKB	Beta strand	408	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK	
+P33297	UniProtKB	Helix	412	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK	
+##sequence-region P33298 1 428
+P33298	UniProtKB	Chain	1	428	.	.	.	ID=PRO_0000084697;Note=26S proteasome regulatory subunit 6B homolog	
+P33298	UniProtKB	Nucleotide binding	213	220	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33298	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+P33298	UniProtKB	Cross-link	280	280	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P33298	UniProtKB	Sequence conflict	342	342	.	.	.	Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33298	UniProtKB	Sequence conflict	342	342	.	.	.	Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33298	UniProtKB	Helix	351	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P33298	UniProtKB	Helix	368	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZO	
+P33298	UniProtKB	Helix	380	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P33298	UniProtKB	Beta strand	400	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+P33298	UniProtKB	Helix	404	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN	
+##sequence-region P09232 1 635
+P09232	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P09232	UniProtKB	Propeptide	20	280	.	.	.	ID=PRO_0000027136;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3325823;Dbxref=PMID:3325823	
+P09232	UniProtKB	Chain	281	574	.	.	.	ID=PRO_0000027137;Note=Cerevisin	
+P09232	UniProtKB	Propeptide	575	635	.	.	.	ID=PRO_0000417567	
+P09232	UniProtKB	Domain	322	568	.	.	.	Note=Peptidase S8	
+P09232	UniProtKB	Compositional bias	63	154	.	.	.	Note=Lys-rich	
+P09232	UniProtKB	Active site	325	325	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09232	UniProtKB	Active site	357	357	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09232	UniProtKB	Active site	519	519	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09232	UniProtKB	Glycosylation	594	594	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09232	UniProtKB	Disulfide bond	460	491	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P09232	UniProtKB	Sequence conflict	622	622	.	.	.	Note=F->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09232	UniProtKB	Sequence conflict	622	622	.	.	.	Note=F->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P23638 1 258
+P23638	UniProtKB	Chain	1	258	.	.	.	ID=PRO_0000124116;Note=Proteasome subunit alpha type-3	
+P23638	UniProtKB	Cross-link	100	100	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P23638	UniProtKB	Cross-link	199	199	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P23638	UniProtKB	Cross-link	231	231	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P23638	UniProtKB	Helix	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Helix	20	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Beta strand	35	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Beta strand	43	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Beta strand	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Helix	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CZ4	
+P23638	UniProtKB	Beta strand	64	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Helix	81	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Helix	108	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Beta strand	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Beta strand	133	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Turn	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Beta strand	145	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Beta strand	157	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Helix	169	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Helix	186	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Beta strand	202	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Helix	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Beta strand	211	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Beta strand	220	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Beta strand	226	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Helix	232	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P23638	UniProtKB	Turn	242	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BDM	
+##sequence-region P53633 1 176
+P53633	UniProtKB	Chain	1	176	.	.	.	ID=PRO_0000220887;Note=Prenylated Rab acceptor 1	
+P53633	UniProtKB	Transmembrane	84	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53633	UniProtKB	Transmembrane	129	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53633	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53633	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53633	UniProtKB	Sequence conflict	29	29	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53633	UniProtKB	Sequence conflict	29	29	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P54885 1 456
+P54885	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P54885	UniProtKB	Chain	2	456	.	.	.	ID=PRO_0000189824;Note=Gamma-glutamyl phosphate reductase	
+P54885	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P54885	UniProtKB	Helix	3	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	23	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	41	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	62	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	75	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	96	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	106	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	117	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	127	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	142	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	149	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	152	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	179	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	190	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Turn	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	201	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	208	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	230	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	240	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	262	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	273	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	288	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	292	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	310	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	335	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	342	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	357	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	365	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	378	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	386	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Helix	416	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+P54885	UniProtKB	Beta strand	419	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU	
+##sequence-region P32523 1 503
+P32523	UniProtKB	Chain	1	503	.	.	.	ID=PRO_0000058587;Note=Pre-mRNA-processing factor 19	
+P32523	UniProtKB	Domain	1	71	.	.	.	Note=U-box	
+P32523	UniProtKB	Repeat	328	367	.	.	.	Note=WD 1	
+P32523	UniProtKB	Repeat	372	410	.	.	.	Note=WD 2	
+P32523	UniProtKB	Repeat	418	458	.	.	.	Note=WD 3	
+P32523	UniProtKB	Region	57	144	.	.	.	Note=Required for self-association	
+P32523	UniProtKB	Region	76	134	.	.	.	Note=Interaction with CEF1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15601865;Dbxref=PMID:15601865	
+P32523	UniProtKB	Sequence conflict	239	239	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32523	UniProtKB	Turn	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY	
+P32523	UniProtKB	Beta strand	11	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY	
+P32523	UniProtKB	Turn	17	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY	
+P32523	UniProtKB	Beta strand	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY	
+P32523	UniProtKB	Helix	25	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY	
+P32523	UniProtKB	Turn	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY	
+P32523	UniProtKB	Helix	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY	
+P32523	UniProtKB	Beta strand	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P32523	UniProtKB	Helix	78	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P32523	UniProtKB	Helix	149	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P32523	UniProtKB	Beta strand	179	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	204	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	219	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	232	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Helix	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	247	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Turn	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	256	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Turn	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	265	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Turn	271	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	275	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	288	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	295	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	301	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	311	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	321	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Turn	327	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P32523	UniProtKB	Beta strand	335	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	342	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	354	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Turn	359	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P32523	UniProtKB	Beta strand	363	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P32523	UniProtKB	Beta strand	377	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	386	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Turn	402	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P32523	UniProtKB	Beta strand	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	424	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	432	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Turn	440	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	444	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Turn	452	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	456	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	462	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P32523	UniProtKB	Beta strand	466	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P32523	UniProtKB	Helix	473	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P32523	UniProtKB	Beta strand	476	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	485	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+P32523	UniProtKB	Beta strand	493	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4	
+##sequence-region P24384 1 1145
+P24384	UniProtKB	Chain	1	1145	.	.	.	ID=PRO_0000055135;Note=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22	
+P24384	UniProtKB	Domain	178	250	.	.	.	Note=S1 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+P24384	UniProtKB	Domain	493	656	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P24384	UniProtKB	Domain	678	854	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P24384	UniProtKB	Nucleotide binding	506	513	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P24384	UniProtKB	Motif	603	606	.	.	.	Note=DEAH box	
+##sequence-region P20095 1 876
+P20095	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P20095	UniProtKB	Chain	2	876	.	.	.	ID=PRO_0000055130;Note=Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein PRP2	
+P20095	UniProtKB	Domain	233	399	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P20095	UniProtKB	Domain	424	598	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P20095	UniProtKB	Nucleotide binding	246	253	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P20095	UniProtKB	Motif	346	349	.	.	.	Note=DEAH box	
+P20095	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P20095	UniProtKB	Mutagenesis	6	206	.	.	.	Note=No affect on activity. Missing	
+P20095	UniProtKB	Mutagenesis	89	552	.	.	.	Note=Loss of ATPase and splicing activity. Missing	
+P20095	UniProtKB	Mutagenesis	89	206	.	.	.	Note=Wild-type RNA-dependent ATPase activity%3B bound tightly to the spliceosome and after addition of ATP released from the spliceosome. Missing	
+P20095	UniProtKB	Mutagenesis	349	349	.	.	.	Note=Fails to release from the spliceosome%3B when associated with H-548. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730020;Dbxref=PMID:14730020	
+P20095	UniProtKB	Mutagenesis	378	378	.	.	.	Note=In PRP2-dn1%3B 40%25 of wild-type RNA-stimulated ATPase activity%3B splicing activity abolished%3B accumulates stalled splicing complexes. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8112301;Dbxref=PMID:8112301	
+P20095	UniProtKB	Mutagenesis	548	548	.	.	.	Note=Fails to release from the spliceosome%3B when associated with D-349. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730020;Dbxref=PMID:14730020	
+P20095	UniProtKB	Mutagenesis	551	551	.	.	.	Note=Fails to release from the spliceosome. G->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730020;Dbxref=PMID:14730020	
+P20095	UniProtKB	Mutagenesis	554	876	.	.	.	Note=Has small amount of ATPase activity%2C but no splicing activity. Missing	
+P20095	UniProtKB	Mutagenesis	615	876	.	.	.	Note=Loss of activity. Missing	
+P20095	UniProtKB	Mutagenesis	824	876	.	.	.	Note=Spliceosome binding mutant%3B not active in splicing%3B when associated with N-551. Missing	
+P20095	UniProtKB	Mutagenesis	833	876	.	.	.	Note=Spliceosome binding mutant%3B not active in splicing%3B when associated with N-551. Missing	
+P20095	UniProtKB	Mutagenesis	834	876	.	.	.	Note=Spliceosome binding mutant%3B not active in splicing%3B when associated with N-551. Almost wild-type RNA-dependent ATPase activity. Missing	
+P20095	UniProtKB	Mutagenesis	845	846	.	.	.	Note=Spliceosome binding mutant%3B not active in splicing%3B when associated with N-551%2C or D-349 and H-548. Loss of interaction with SPP2. DC->NY;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14730020,ECO:0000269|PubMed:15542821;Dbxref=PMID:14730020,PMID:15542821	
+P20095	UniProtKB	Mutagenesis	845	845	.	.	.	Note=Temperature-sensitive%3B decreased interaction with SPP2%2C decreased cell growth on benomyl and decreased splicing at elevated temperatures%3B when associated with D-349 and H-548. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542821;Dbxref=PMID:15542821	
+P20095	UniProtKB	Mutagenesis	854	855	.	.	.	Note=Loss of interaction with SPP2. WL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542821;Dbxref=PMID:15542821	
+##sequence-region Q03338 1 469
+Q03338	UniProtKB	Chain	1	469	.	.	.	ID=PRO_0000097037;Note=U4/U6 small nuclear ribonucleoprotein PRP3	
+Q03338	UniProtKB	Beta strand	337	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV	
+Q03338	UniProtKB	Helix	350	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV	
+Q03338	UniProtKB	Beta strand	366	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV	
+Q03338	UniProtKB	Beta strand	378	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV	
+Q03338	UniProtKB	Helix	386	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV	
+Q03338	UniProtKB	Beta strand	406	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV	
+Q03338	UniProtKB	Beta strand	414	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV	
+Q03338	UniProtKB	Beta strand	424	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV	
+Q03338	UniProtKB	Beta strand	439	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV	
+Q03338	UniProtKB	Helix	448	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV	
+Q03338	UniProtKB	Helix	461	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV	
+##sequence-region Q12417 1 451
+Q12417	UniProtKB	Chain	1	451	.	.	.	ID=PRO_0000051169;Note=Pre-mRNA-splicing factor PRP46	
+Q12417	UniProtKB	Repeat	137	168	.	.	.	Note=WD 1	
+Q12417	UniProtKB	Repeat	180	210	.	.	.	Note=WD 2	
+Q12417	UniProtKB	Repeat	222	252	.	.	.	Note=WD 3	
+Q12417	UniProtKB	Repeat	264	294	.	.	.	Note=WD 4	
+Q12417	UniProtKB	Repeat	306	335	.	.	.	Note=WD 5	
+Q12417	UniProtKB	Repeat	348	377	.	.	.	Note=WD 6	
+Q12417	UniProtKB	Repeat	397	427	.	.	.	Note=WD 7	
+Q12417	UniProtKB	Helix	112	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	129	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Turn	149	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	154	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Turn	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	187	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	192	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	206	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Turn	211	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	215	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	229	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Turn	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	238	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	246	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Turn	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	269	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	276	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	281	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	290	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Turn	295	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	299	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	314	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Turn	318	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	321	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	332	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	353	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	362	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Turn	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	383	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Helix	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	402	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	409	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Turn	419	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12417	UniProtKB	Beta strand	422	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region Q12428 1 516
+Q12428	UniProtKB	Chain	1	516	.	.	.	ID=PRO_0000215027;Note=Probable 2-methylcitrate dehydratase	
+##sequence-region P33299 1 467
+P33299	UniProtKB	Chain	1	467	.	.	.	ID=PRO_0000084719;Note=26S proteasome regulatory subunit 7 homolog	
+P33299	UniProtKB	Nucleotide binding	250	257	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33299	UniProtKB	Modified residue	164	164	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P33299	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P34227 1 261
+P34227	UniProtKB	Transit peptide	1	13	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34227	UniProtKB	Chain	14	261	.	.	.	ID=PRO_0000135151;Note=Peroxiredoxin PRX1%2C mitochondrial	
+P34227	UniProtKB	Domain	49	212	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P34227	UniProtKB	Active site	91	91	.	.	.	Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10681558;Dbxref=PMID:10681558	
+P34227	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P34227	UniProtKB	Disulfide bond	38	38	.	.	.	Note=Interchain;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10821871;Dbxref=PMID:10821871	
+P34227	UniProtKB	Mutagenesis	38	38	.	.	.	Note=Impairs dimer formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10821871;Dbxref=PMID:10821871	
+P34227	UniProtKB	Mutagenesis	91	91	.	.	.	Note=No activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10681558;Dbxref=PMID:10681558	
+##sequence-region P47033 1 881
+P47033	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47033	UniProtKB	Chain	19	853	.	.	.	ID=PRO_0000211549;Note=Cell wall protein PRY3	
+P47033	UniProtKB	Propeptide	854	881	.	.	.	ID=PRO_0000372447;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47033	UniProtKB	Domain	30	144	.	.	.	Note=SCP	
+P47033	UniProtKB	Compositional bias	163	845	.	.	.	Note=Ser/Thr-rich	
+P47033	UniProtKB	Lipidation	853	853	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47033	UniProtKB	Glycosylation	101	101	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23038983;Dbxref=PMID:23038983	
+P47033	UniProtKB	Glycosylation	360	360	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47033	UniProtKB	Glycosylation	488	488	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47033	UniProtKB	Glycosylation	535	535	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47033	UniProtKB	Glycosylation	547	547	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47033	UniProtKB	Glycosylation	569	569	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47033	UniProtKB	Glycosylation	625	625	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32379 1 260
+P32379	UniProtKB	Chain	1	260	.	.	.	ID=PRO_0000124129;Note=Proteasome subunit alpha type-5	
+P32379	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32379	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32379	UniProtKB	Modified residue	251	251	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32379	UniProtKB	Mutagenesis	49	49	.	.	.	Note=In DOA5-1%3B slight decrease in activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7781614;Dbxref=PMID:7781614	
+P32379	UniProtKB	Sequence conflict	192	192	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32379	UniProtKB	Beta strand	19	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QBY	
+P32379	UniProtKB	Helix	22	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Beta strand	37	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Beta strand	46	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Beta strand	55	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65	
+P32379	UniProtKB	Helix	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Beta strand	67	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Beta strand	74	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Helix	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Helix	85	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Helix	109	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Turn	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Beta strand	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LTC	
+P32379	UniProtKB	Beta strand	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Beta strand	139	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Turn	149	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Beta strand	152	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Turn	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S	
+P32379	UniProtKB	Beta strand	164	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Helix	176	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Helix	193	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Beta strand	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FNT	
+P32379	UniProtKB	Beta strand	216	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Turn	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Beta strand	227	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P32379	UniProtKB	Helix	233	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+##sequence-region P40302 1 234
+P40302	UniProtKB	Chain	1	234	.	.	.	ID=PRO_0000124076;Note=Proteasome subunit alpha type-6	
+P40302	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40302	UniProtKB	Cross-link	191	191	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P40302	UniProtKB	Helix	3	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Beta strand	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FZC	
+P40302	UniProtKB	Helix	20	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Beta strand	35	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Beta strand	41	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Beta strand	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R17	
+P40302	UniProtKB	Beta strand	63	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Beta strand	70	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Helix	78	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Helix	105	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Beta strand	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP	
+P40302	UniProtKB	Beta strand	130	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Beta strand	141	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Turn	149	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G0U	
+P40302	UniProtKB	Beta strand	153	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Turn	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Helix	166	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Helix	186	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Helix	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP	
+P40302	UniProtKB	Beta strand	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EU2	
+P40302	UniProtKB	Turn	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Beta strand	211	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Beta strand	220	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+P40302	UniProtKB	Helix	227	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP	
+##sequence-region Q12146 1 194
+Q12146	UniProtKB	Chain	1	194	.	.	.	ID=PRO_0000132325;Note=DNA replication complex GINS protein PSF3	
+##sequence-region Q07800 1 427
+Q07800	UniProtKB	Chain	1	427	.	.	.	ID=PRO_0000212576;Note=Phosphatase PSR1	
+Q07800	UniProtKB	Domain	253	411	.	.	.	Note=FCP1 homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00336	
+Q07800	UniProtKB	Compositional bias	152	189	.	.	.	Note=Gln-rich	
+Q07800	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+Q07800	UniProtKB	Lipidation	9	9	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255,ECO:0000303;evidence=ECO:0000255,ECO:0000303|PubMed:10777497;Dbxref=PMID:10777497	
+Q07800	UniProtKB	Lipidation	10	10	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255,ECO:0000303;evidence=ECO:0000255,ECO:0000303|PubMed:10777497;Dbxref=PMID:10777497	
+Q07800	UniProtKB	Cross-link	154	154	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q07800	UniProtKB	Mutagenesis	2	2	.	.	.	Note=No effect on membrane association. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10777497;Dbxref=PMID:10777497	
+Q07800	UniProtKB	Mutagenesis	9	10	.	.	.	Note=Impairs membrane association. CC->GG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10777497;Dbxref=PMID:10777497	
+Q07800	UniProtKB	Mutagenesis	263	263	.	.	.	Note=Low residual phosphatase activity. Loss of stress response functions. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10777497;Dbxref=PMID:10777497	
+Q07800	UniProtKB	Mutagenesis	265	265	.	.	.	Note=Low residual phosphatase activity. Loss of stress response functions. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10777497;Dbxref=PMID:10777497	
+##sequence-region Q12211 1 544
+Q12211	UniProtKB	Chain	1	544	.	.	.	ID=PRO_0000057530;Note=tRNA pseudouridine synthase 1	
+Q12211	UniProtKB	Active site	134	134	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12211	UniProtKB	Binding site	190	190	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P48567 1 403
+P48567	UniProtKB	Chain	1	403	.	.	.	ID=PRO_0000121976;Note=tRNA pseudouridine synthase 4	
+P48567	UniProtKB	Active site	75	75	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P07275 1 575
+P07275	UniProtKB	Nucleotide binding	297	302	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07275	UniProtKB	Active site	317	317	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P07275	UniProtKB	Active site	351	351	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008	
+P07275	UniProtKB	Site	212	212	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07275	UniProtKB	Sequence conflict	187	188	.	.	.	Note=ES->SR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07275	UniProtKB	Sequence conflict	264	264	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07275	UniProtKB	Sequence conflict	541	541	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07275	UniProtKB	Sequence conflict	561	561	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07275	UniProtKB	Helix	44	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Turn	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	78	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	86	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	99	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	121	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Turn	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	140	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	155	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	164	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	193	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	202	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	214	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	231	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	240	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	259	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	267	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	280	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	289	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	313	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	322	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	332	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	345	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	354	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	361	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	405	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	424	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	435	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	443	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	453	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	461	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	471	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	474	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	489	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	498	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Turn	508	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	513	519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Helix	548	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+P07275	UniProtKB	Beta strand	553	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6	
+##sequence-region P15380 1 627
+P15380	UniProtKB	Chain	1	627	.	.	.	ID=PRO_0000054158;Note=Proline-specific permease	
+P15380	UniProtKB	Transmembrane	115	136	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Transmembrane	191	210	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Transmembrane	229	247	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Transmembrane	262	281	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Transmembrane	306	326	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Transmembrane	351	370	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Transmembrane	408	427	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Transmembrane	455	473	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Transmembrane	483	503	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Transmembrane	522	542	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Transmembrane	558	578	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Glycosylation	72	72	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Glycosylation	78	78	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15380	UniProtKB	Sequence conflict	38	38	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07259 1 2214
+P07259	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07259	UniProtKB	Chain	2	2214	.	.	.	ID=PRO_0000199511;Note=Protein URA2	
+P07259	UniProtKB	Domain	228	413	.	.	.	Note=Glutamine amidotransferase type-1	
+P07259	UniProtKB	Domain	562	754	.	.	.	Note=ATP-grasp 1	
+P07259	UniProtKB	Domain	1099	1290	.	.	.	Note=ATP-grasp 2	
+P07259	UniProtKB	Region	2	400	.	.	.	Note=GATase (Glutamine amidotransferase)	
+P07259	UniProtKB	Region	401	440	.	.	.	Note=Linker	
+P07259	UniProtKB	Region	441	1482	.	.	.	Note=CPSase (Carbamoyl-phosphate synthase)	
+P07259	UniProtKB	Region	1483	1492	.	.	.	Note=Linker	
+P07259	UniProtKB	Region	1493	1821	.	.	.	Note=Defective DHOase domain	
+P07259	UniProtKB	Region	1822	1909	.	.	.	Note=Linker	
+P07259	UniProtKB	Region	1910	2214	.	.	.	Note=ATCase (Aspartate transcarbamylase)	
+P07259	UniProtKB	Active site	302	302	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07259	UniProtKB	Active site	386	386	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07259	UniProtKB	Active site	388	388	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07259	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P07259	UniProtKB	Modified residue	1857	1857	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:1977585;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198,PMID:1977585	
+P07259	UniProtKB	Cross-link	1853	1853	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P07259	UniProtKB	Sequence conflict	86	86	.	.	.	Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	123	123	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	250	257	.	.	.	Note=ELKVVPWN->RIESCSMD;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	270	270	.	.	.	Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	313	314	.	.	.	Note=GA->VQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	372	373	.	.	.	Note=GI->RF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	394	402	.	.	.	Note=RDTEFLFDV->EIQNSCLT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	431	433	.	.	.	Note=KAH->QGT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	482	482	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	485	485	.	.	.	Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	492	492	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	501	510	.	.	.	Note=TAEFVRKVIL->NAAKQRDVDR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	1411	1412	.	.	.	Note=EV->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	1582	1582	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	1588	1588	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	1592	1592	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	1595	1595	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	1872	1872	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	1937	1937	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	1937	1937	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	1997	1997	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	2039	2039	.	.	.	Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07259	UniProtKB	Sequence conflict	2158	2165	.	.	.	Note=KILAHAKE->VRSWHTQQK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q9ZZX8 1 53
+Q9ZZX8	UniProtKB	Chain	1	53	.	.	.	ID=PRO_0000299679;Note=Putative uncharacterized protein Q0017%2C mitochondrial	
+##sequence-region P22289 1 66
+P22289	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2174427;Dbxref=PMID:2174427	
+P22289	UniProtKB	Chain	2	66	.	.	.	ID=PRO_0000193558;Note=Cytochrome b-c1 complex subunit 9	
+P22289	UniProtKB	Transmembrane	16	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22289	UniProtKB	Helix	4	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P22289	UniProtKB	Helix	18	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P22289	UniProtKB	Turn	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P22289	UniProtKB	Helix	49	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+##sequence-region P32849 1 1169
+P32849	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32849	UniProtKB	Chain	2	1169	.	.	.	ID=PRO_0000056130;Note=DNA repair protein RAD5	
+P32849	UniProtKB	Domain	519	730	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32849	UniProtKB	Domain	995	1165	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P32849	UniProtKB	Nucleotide binding	532	539	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32849	UniProtKB	Zinc finger	914	961	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P32849	UniProtKB	Motif	681	684	.	.	.	Note=DEGH box	
+P32849	UniProtKB	Compositional bias	42	60	.	.	.	Note=Asp/Glu-rich (acidic)	
+P32849	UniProtKB	Compositional bias	303	315	.	.	.	Note=Arg/Lys-rich (basic)	
+P32849	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32849	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32849	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32849	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32849	UniProtKB	Modified residue	130	130	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32849	UniProtKB	Mutagenesis	538	539	.	.	.	Note=Increased sensitivity toward ionizing radiation. KT->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16224103;Dbxref=PMID:16224103	
+P32849	UniProtKB	Mutagenesis	914	914	.	.	.	Note=Abolishes interaction with UBC13. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10880451,ECO:0000269|PubMed:12496280;Dbxref=PMID:10880451,PMID:12496280	
+P32849	UniProtKB	Mutagenesis	916	916	.	.	.	Note=Abolishes interaction with UBC13. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496280;Dbxref=PMID:12496280	
+P32849	UniProtKB	Mutagenesis	944	944	.	.	.	Note=Abolishes interaction with UBC13. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496280;Dbxref=PMID:12496280	
+P32849	UniProtKB	Mutagenesis	959	959	.	.	.	Note=Abolishes interaction with UBC13. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496280;Dbxref=PMID:12496280	
+P32849	UniProtKB	Sequence conflict	478	478	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32849	UniProtKB	Sequence conflict	635	635	.	.	.	Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32849	UniProtKB	Sequence conflict	846	846	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32849	UniProtKB	Sequence conflict	898	898	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32849	UniProtKB	Sequence conflict	973	973	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32849	UniProtKB	Sequence conflict	1063	1063	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P14737 1 1309
+P14737	UniProtKB	Chain	1	1309	.	.	.	ID=PRO_0000097158;Note=DNA repair protein RAD9	
+P14737	UniProtKB	Domain	994	1122	.	.	.	Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P14737	UniProtKB	Modified residue	26	26	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14737	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14737	UniProtKB	Modified residue	205	205	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14737	UniProtKB	Modified residue	218	218	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14737	UniProtKB	Modified residue	248	248	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14737	UniProtKB	Modified residue	312	312	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14737	UniProtKB	Modified residue	315	315	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14737	UniProtKB	Modified residue	462	462	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14737	UniProtKB	Modified residue	471	471	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14737	UniProtKB	Modified residue	474	474	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14737	UniProtKB	Modified residue	568	568	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14737	UniProtKB	Modified residue	729	729	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14737	UniProtKB	Sequence conflict	433	433	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14737	UniProtKB	Sequence conflict	433	433	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14737	UniProtKB	Beta strand	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K3Q	
+##sequence-region P20051 1 364
+P20051	UniProtKB	Chain	1	364	.	.	.	ID=PRO_0000147292;Note=Dihydroorotase	
+P20051	UniProtKB	Metal binding	14	14	.	.	.	Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020	
+P20051	UniProtKB	Metal binding	16	16	.	.	.	Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020	
+P20051	UniProtKB	Metal binding	98	98	.	.	.	Note=Zinc 1%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020	
+P20051	UniProtKB	Metal binding	98	98	.	.	.	Note=Zinc 2%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020	
+P20051	UniProtKB	Metal binding	137	137	.	.	.	Note=Zinc 2%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020	
+P20051	UniProtKB	Metal binding	180	180	.	.	.	Note=Zinc 2%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020	
+P20051	UniProtKB	Metal binding	258	258	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020	
+P20051	UniProtKB	Modified residue	98	98	.	.	.	Note=N6-carboxylysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020	
+P20051	UniProtKB	Sequence conflict	107	119	.	.	.	Note=NSAAGVDPNDFSA->IRLLGWIQMTSAH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20051	UniProtKB	Sequence conflict	156	156	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20051	UniProtKB	Sequence conflict	240	240	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20051	UniProtKB	Sequence conflict	269	269	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20051	UniProtKB	Sequence conflict	319	319	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07257 1 368
+P07257	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion	
+P07257	UniProtKB	Chain	17	368	.	.	.	ID=PRO_0000026801;Note=Cytochrome b-c1 complex subunit 2%2C mitochondrial	
+P07257	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P07257	UniProtKB	Modified residue	168	168	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07257	UniProtKB	Beta strand	18	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	27	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	47	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	64	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	77	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	87	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	98	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	116	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	123	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	138	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Turn	152	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	169	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	182	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	185	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	194	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Turn	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	228	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	234	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Turn	247	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	250	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P84	
+P07257	UniProtKB	Helix	268	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	272	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	282	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	294	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	315	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	318	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	329	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KB9	
+P07257	UniProtKB	Helix	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Beta strand	352	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	359	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P07257	UniProtKB	Helix	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+##sequence-region P00128 1 127
+P00128	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000193539;Note=Cytochrome b-c1 complex subunit 7	
+P00128	UniProtKB	Sequence conflict	92	92	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00128	UniProtKB	Helix	5	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00128	UniProtKB	Helix	19	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00128	UniProtKB	Helix	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00128	UniProtKB	Helix	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00128	UniProtKB	Helix	54	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00128	UniProtKB	Helix	65	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00128	UniProtKB	Helix	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00128	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00128	UniProtKB	Helix	104	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+##sequence-region P40475 1 563
+P40475	UniProtKB	Chain	1	563	.	.	.	ID=PRO_0000173441;Note=Quinidine resistance protein 1	
+P40475	UniProtKB	Topological domain	1	75	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	97	108	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	130	135	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	157	165	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	166	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	187	195	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	196	216	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	217	224	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	225	245	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	246	296	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	297	317	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	318	341	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	342	362	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	363	421	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	422	442	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	443	445	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	446	466	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	467	481	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	482	502	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	503	511	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Transmembrane	512	532	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40475	UniProtKB	Topological domain	533	563	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40474 1 542
+P40474	UniProtKB	Chain	1	542	.	.	.	ID=PRO_0000173442;Note=Quinidine resistance protein 2	
+P40474	UniProtKB	Topological domain	1	67	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	89	100	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	122	127	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	149	149	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	171	187	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	209	216	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	238	300	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	301	321	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	322	333	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	334	354	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	355	413	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	414	434	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	435	437	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	438	458	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	459	472	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	473	493	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	494	503	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Transmembrane	504	524	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Topological domain	525	542	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40474	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40474	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40474	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38227 1 689
+P38227	UniProtKB	Chain	1	689	.	.	.	ID=PRO_0000173437;Note=Quinidine resistance protein 3	
+P38227	UniProtKB	Topological domain	1	108	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Transmembrane	109	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Topological domain	132	139	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Transmembrane	140	163	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Topological domain	164	175	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Transmembrane	176	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Topological domain	194	235	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Transmembrane	236	256	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Topological domain	257	265	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Transmembrane	266	283	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Topological domain	284	475	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Transmembrane	476	493	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Topological domain	494	510	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Transmembrane	511	532	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Topological domain	533	558	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Transmembrane	559	577	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Topological domain	578	586	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Transmembrane	587	609	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Topological domain	610	624	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Transmembrane	625	642	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Topological domain	643	648	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Transmembrane	649	668	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Topological domain	669	689	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38227	UniProtKB	Modified residue	436	436	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38227	UniProtKB	Sequence conflict	37	37	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P48581 1 401
+P48581	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000097150;Note=DNA damage checkpoint control protein RAD17	
+P48581	UniProtKB	Modified residue	383	383	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P48581	UniProtKB	Mutagenesis	128	128	.	.	.	Note=In RAD17-1%3B UV-sensitive. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8649984;Dbxref=PMID:8649984	
+##sequence-region P40352 1 1085
+P40352	UniProtKB	Chain	1	1085	.	.	.	ID=PRO_0000074336;Note=DNA repair and recombination protein RAD26	
+P40352	UniProtKB	Domain	309	518	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P40352	UniProtKB	Domain	655	818	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P40352	UniProtKB	Nucleotide binding	322	329	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P40352	UniProtKB	Motif	469	472	.	.	.	Note=DEGH box	
+P40352	UniProtKB	Compositional bias	173	228	.	.	.	Note=Asp/Glu-rich (acidic)	
+P40352	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40352	UniProtKB	Sequence conflict	366	366	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40352	UniProtKB	Sequence conflict	963	963	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12223 1 238
+Q12223	UniProtKB	Chain	1	238	.	.	.	ID=PRO_0000173897;Note=DNA repair protein RAD59	
+##sequence-region P21827 1 482
+P21827	UniProtKB	Chain	1	482	.	.	.	ID=PRO_0000206634;Note=Guanine nucleotide exchange factor SRM1	
+P21827	UniProtKB	Repeat	45	101	.	.	.	Note=RCC1 1	
+P21827	UniProtKB	Repeat	103	152	.	.	.	Note=RCC1 2	
+P21827	UniProtKB	Repeat	183	238	.	.	.	Note=RCC1 3	
+P21827	UniProtKB	Repeat	239	291	.	.	.	Note=RCC1 4	
+P21827	UniProtKB	Repeat	292	347	.	.	.	Note=RCC1 5	
+P21827	UniProtKB	Repeat	349	411	.	.	.	Note=RCC1 6	
+P21827	UniProtKB	Repeat	412	466	.	.	.	Note=RCC1 7	
+P21827	UniProtKB	Motif	15	26	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11523802;Dbxref=PMID:11523802	
+P21827	UniProtKB	Modified residue	135	135	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P21827	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P21827	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Impairs correct nuclear localization%3B when associated with T-20 and T-23. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11523802;Dbxref=PMID:11523802	
+P21827	UniProtKB	Mutagenesis	20	20	.	.	.	Note=Impairs activity. K->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11523802;Dbxref=PMID:11523802	
+P21827	UniProtKB	Mutagenesis	20	20	.	.	.	Note=Impairs correct nuclear localization%3B when associated with T-19 and T-23. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11523802;Dbxref=PMID:11523802	
+P21827	UniProtKB	Mutagenesis	23	23	.	.	.	Note=Impairs correct nuclear localization%3B when associated with T-19 and T-20. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11523802;Dbxref=PMID:11523802	
+P21827	UniProtKB	Mutagenesis	282	282	.	.	.	Note=Leads to temperature-dependent mislocalization of nucleoporins (nups) and the pore-membrane protein POM152. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654904;Dbxref=PMID:12654904	
+P21827	UniProtKB	Helix	33	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Helix	37	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	47	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Helix	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	69	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Turn	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	86	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	93	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	105	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Helix	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Helix	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Helix	159	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	167	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	174	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	186	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	197	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Turn	203	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	209	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	223	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	230	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	242	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Helix	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Turn	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	275	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	283	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	295	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	317	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	332	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	339	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	351	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Helix	366	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	381	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	396	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	403	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	415	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	435	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Turn	444	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	449	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Beta strand	458	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+P21827	UniProtKB	Helix	470	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7	
+##sequence-region P53972 1 490
+P53972	UniProtKB	Chain	1	490	.	.	.	ID=PRO_0000203461;Note=25S rRNA (cytosine(2278)-C(5))-methyltransferase	
+P53972	UniProtKB	Region	250	256	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P53972	UniProtKB	Active site	404	404	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P53972	UniProtKB	Binding site	280	280	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P53972	UniProtKB	Binding site	308	308	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P53972	UniProtKB	Binding site	327	327	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023	
+P53972	UniProtKB	Mutagenesis	330	330	.	.	.	Note=Lethal. Blocks the separation of the enzyme from its RNA substrate. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23913415;Dbxref=PMID:23913415	
+P53972	UniProtKB	Mutagenesis	404	404	.	.	.	Note=Fails to ctalyze the C-5 methylation of the C2278 residue. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23913415;Dbxref=PMID:23913415	
+##sequence-region P30402 1 227
+P30402	UniProtKB	Chain	1	227	.	.	.	ID=PRO_0000110805;Note=Orotate phosphoribosyltransferase 2	
+P30402	UniProtKB	Region	41	42	.	.	.	Note=Orotate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30402	UniProtKB	Region	79	80	.	.	.	Note=5-phosphoribose 1-diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30402	UniProtKB	Region	135	143	.	.	.	Note=5-phosphoribose 1-diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30402	UniProtKB	Binding site	109	109	.	.	.	Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30402	UniProtKB	Binding site	110	110	.	.	.	Note=5-phosphoribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30402	UniProtKB	Binding site	113	113	.	.	.	Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30402	UniProtKB	Binding site	115	115	.	.	.	Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30402	UniProtKB	Binding site	139	139	.	.	.	Note=Orotate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30402	UniProtKB	Binding site	167	167	.	.	.	Note=Orotate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P30402	UniProtKB	Sequence conflict	143	143	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P30402	UniProtKB	Sequence conflict	158	158	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q9ZZX7 1 96
+Q9ZZX7	UniProtKB	Chain	1	96	.	.	.	ID=PRO_0000299680;Note=Putative uncharacterized protein Q0032%2C mitochondrial	
+##sequence-region Q9ZZW3 1 50
+Q9ZZW3	UniProtKB	Chain	1	50	.	.	.	ID=PRO_0000299683;Note=Putative uncharacterized protein Q0143%2C mitochondrial	
+##sequence-region P00127 1 147
+P00127	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000193542;Note=Cytochrome b-c1 complex subunit 6	
+P00127	UniProtKB	Compositional bias	26	80	.	.	.	Note=Asp/Glu-rich (acidic)	
+P00127	UniProtKB	Disulfide bond	101	123	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11726495,ECO:0000269|PubMed:11880631,ECO:0000269|PubMed:12782631,ECO:0000269|PubMed:17337272,ECO:0000269|PubMed:18390544;Dbxref=PMID:10873857,PMID:11726495,PMID:11880631,PMID:12782631,PMID:17337272,PMID:18390544	
+P00127	UniProtKB	Sequence conflict	2	2	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00127	UniProtKB	Helix	77	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00127	UniProtKB	Helix	89	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00127	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00127	UniProtKB	Helix	124	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+P00127	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5	
+##sequence-region P07276 1 1031
+P07276	UniProtKB	Chain	1	1031	.	.	.	ID=PRO_0000154035;Note=DNA repair protein RAD2	
+P07276	UniProtKB	Region	1	95	.	.	.	Note=N-domain	
+P07276	UniProtKB	Region	756	884	.	.	.	Note=I-domain	
+P07276	UniProtKB	Metal binding	30	30	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07276	UniProtKB	Metal binding	77	77	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07276	UniProtKB	Metal binding	792	792	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07276	UniProtKB	Metal binding	794	794	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07276	UniProtKB	Metal binding	813	813	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07276	UniProtKB	Metal binding	815	815	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07276	UniProtKB	Metal binding	864	864	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07276	UniProtKB	Modified residue	118	118	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07276	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P07276	UniProtKB	Modified residue	583	583	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07276	UniProtKB	Sequence conflict	782	782	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07276	UniProtKB	Helix	6	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Beta strand	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Beta strand	26	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	34	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Beta strand	45	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0Z	
+P07276	UniProtKB	Helix	53	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Beta strand	71	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	82	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Beta strand	667	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LOX	
+P07276	UniProtKB	Helix	769	781	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Beta strand	786	788	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	793	802	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Beta strand	807	810	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	815	818	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Beta strand	823	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Beta strand	830	839	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	840	847	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	851	861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	874	884	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	887	899	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	901	904	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	909	920	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	932	939	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	957	968	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+P07276	UniProtKB	Helix	972	982	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W	
+##sequence-region Q12465 1 1220
+Q12465	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Chain	21	1220	.	.	.	ID=PRO_0000262737;Note=Bud site selection protein RAX2	
+Q12465	UniProtKB	Topological domain	21	1162	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Transmembrane	1163	1183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Topological domain	1184	1220	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Compositional bias	1149	1156	.	.	.	Note=Poly-Lys	
+Q12465	UniProtKB	Glycosylation	41	41	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	45	45	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	69	69	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	88	88	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	124	124	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	134	134	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	145	145	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	158	158	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	166	166	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	171	171	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	187	187	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	200	200	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	235	235	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	238	238	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	244	244	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	333	333	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	365	365	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	379	379	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	432	432	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	445	445	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	516	516	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	524	524	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	613	613	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	620	620	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	626	626	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	640	640	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	677	677	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	705	705	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	713	713	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	721	721	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	731	731	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	749	749	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	758	758	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	792	792	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	821	821	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	848	848	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	861	861	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	884	884	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	890	890	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	908	908	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	923	923	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	942	942	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	956	956	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	980	980	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	983	983	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	1011	1011	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	1024	1024	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	1031	1031	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	1060	1060	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	1071	1071	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	1098	1098	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12465	UniProtKB	Glycosylation	1126	1126	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A0B7P221 1 28
+A0A0B7P221	UniProtKB	Chain	1	28	.	.	.	ID=PRO_0000434005;Note=Uncharacterized protein RDT1	
+##sequence-region P21651 1 314
+P21651	UniProtKB	Chain	1	314	.	.	.	ID=PRO_0000096421;Note=Recombination protein 107	
+P21651	UniProtKB	Sequence conflict	279	279	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21651	UniProtKB	Sequence conflict	279	279	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21651	UniProtKB	Sequence conflict	284	314	.	.	.	Note=DNDDASHRLKRAARTIIPWEELRPDTLESEL->TMMTLAIG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21651	UniProtKB	Sequence conflict	284	314	.	.	.	Note=DNDDASHRLKRAARTIIPWEELRPDTLESEL->TMMTLAIG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P31244 1 790
+P31244	UniProtKB	Chain	1	790	.	.	.	ID=PRO_0000056132;Note=DNA repair protein RAD16	
+P31244	UniProtKB	Domain	197	371	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P31244	UniProtKB	Domain	623	777	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P31244	UniProtKB	Nucleotide binding	210	217	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P31244	UniProtKB	Zinc finger	537	581	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P31244	UniProtKB	Motif	322	325	.	.	.	Note=DEAH box	
+P31244	UniProtKB	Compositional bias	8	13	.	.	.	Note=Poly-Arg	
+P31244	UniProtKB	Compositional bias	65	70	.	.	.	Note=Poly-Asp	
+P31244	UniProtKB	Compositional bias	125	129	.	.	.	Note=Poly-Lys	
+P31244	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P31244	UniProtKB	Modified residue	109	109	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P25301 1 460
+P25301	UniProtKB	Chain	1	460	.	.	.	ID=PRO_0000122956;Note=DNA repair protein RAD57	
+P25301	UniProtKB	Nucleotide binding	125	132	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q99359 1 647
+Q99359	UniProtKB	Chain	1	647	.	.	.	ID=PRO_0000255971;Note=Protein RAD61	
+##sequence-region P11938 1 827
+P11938	UniProtKB	Chain	1	827	.	.	.	ID=PRO_0000197112;Note=DNA-binding protein RAP1	
+P11938	UniProtKB	Domain	121	208	.	.	.	Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P11938	UniProtKB	Domain	355	415	.	.	.	Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P11938	UniProtKB	DNA binding	388	411	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P11938	UniProtKB	Region	630	695	.	.	.	Note=Activation domain	
+P11938	UniProtKB	Compositional bias	71	74	.	.	.	Note=Poly-Asp	
+P11938	UniProtKB	Compositional bias	81	84	.	.	.	Note=Poly-Thr	
+P11938	UniProtKB	Compositional bias	313	320	.	.	.	Note=Poly-Asn	
+P11938	UniProtKB	Compositional bias	614	627	.	.	.	Note=Poly-Ala	
+P11938	UniProtKB	Modified residue	486	486	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P11938	UniProtKB	Modified residue	731	731	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P11938	UniProtKB	Sequence conflict	672	672	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11938	UniProtKB	Helix	365	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Helix	379	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Helix	386	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Turn	392	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Helix	400	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Helix	412	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Beta strand	437	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Helix	451	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Beta strand	474	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Beta strand	509	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UKG	
+P11938	UniProtKB	Helix	525	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Turn	533	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Helix	538	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Helix	549	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Helix	554	562	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN	
+P11938	UniProtKB	Turn	595	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UKG	
+P11938	UniProtKB	Helix	681	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Helix	688	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Turn	700	702	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Helix	705	708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Helix	713	724	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Turn	730	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6	
+P11938	UniProtKB	Helix	733	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Helix	748	757	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Turn	758	760	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Helix	762	764	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Helix	765	775	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Beta strand	781	783	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6	
+P11938	UniProtKB	Helix	789	796	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Helix	800	810	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+P11938	UniProtKB	Helix	812	823	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT	
+##sequence-region P53295 1 368
+P53295	UniProtKB	Chain	1	368	.	.	.	ID=PRO_0000205450;Note=Ribosome-interacting GTPase 2	
+P53295	UniProtKB	Domain	64	292	.	.	.	Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P53295	UniProtKB	Nucleotide binding	70	77	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P53295	UniProtKB	Nucleotide binding	116	120	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P53295	UniProtKB	Nucleotide binding	250	253	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P53295	UniProtKB	Modified residue	364	364	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q06835 1 107
+Q06835	UniProtKB	Chain	1	107	.	.	.	ID=PRO_0000218722;Note=Pre-mRNA-splicing factor RDS3	
+Q06835	UniProtKB	Beta strand	15	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A	
+Q06835	UniProtKB	Helix	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A	
+Q06835	UniProtKB	Turn	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A	
+Q06835	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A	
+Q06835	UniProtKB	Helix	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A	
+Q06835	UniProtKB	Turn	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A	
+Q06835	UniProtKB	Beta strand	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A	
+Q06835	UniProtKB	Helix	74	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A	
+##sequence-region Q08096 1 367
+Q08096	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08096	UniProtKB	Chain	2	367	.	.	.	ID=PRO_0000156444;Note=RNA 3'-terminal phosphate cyclase-like protein	
+Q08096	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08096	UniProtKB	Beta strand	9	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	17	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	31	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Turn	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	47	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	84	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	96	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	114	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	130	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	137	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	150	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	164	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	190	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	203	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	219	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	240	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Turn	250	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	254	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	268	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	287	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Turn	291	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	294	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	306	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	315	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Helix	320	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	338	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+Q08096	UniProtKB	Beta strand	350	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ	
+##sequence-region Q03446 1 210
+Q03446	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000097205;Note=Protein RCR2	
+Q03446	UniProtKB	Transmembrane	41	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03446	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03446	UniProtKB	Modified residue	191	191	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P39531 1 840
+P39531	UniProtKB	Chain	1	840	.	.	.	ID=PRO_0000119953;Note=Recyclin-1	
+P39531	UniProtKB	Domain	1	48	.	.	.	Note=F-box	
+P39531	UniProtKB	Modified residue	409	409	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q08904 1 546
+Q08904	UniProtKB	Chain	1	546	.	.	.	ID=PRO_0000114972;Note=Protein RDR1	
+Q08904	UniProtKB	DNA binding	20	46	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P03872 1 296
+P03872	UniProtKB	Chain	1	296	.	.	.	ID=PRO_0000150898;Note=Partitioning protein REP2	
+P03872	UniProtKB	Region	1	57	.	.	.	Note=Interaction with REP1	
+P03872	UniProtKB	Region	58	296	.	.	.	Note=DNA-binding%2C and self-association	
+P03872	UniProtKB	Region	276	296	.	.	.	Note=Nuclear localization	
+P03872	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P25560 1 188
+P25560	UniProtKB	Chain	1	188	.	.	.	ID=PRO_0000207593;Note=Protein RER1	
+P25560	UniProtKB	Topological domain	1	61	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25560	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25560	UniProtKB	Topological domain	83	138	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25560	UniProtKB	Transmembrane	139	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25560	UniProtKB	Topological domain	162	188	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25560	UniProtKB	Sequence conflict	109	125	.	.	.	Note=RPFIRRLPEFKFWYNSI->LSIHQKTYQSSNSGITAF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25560	UniProtKB	Sequence conflict	136	136	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25560	UniProtKB	Sequence conflict	141	141	.	.	.	Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25560	UniProtKB	Sequence conflict	145	188	.	.	.	Note=FWPILLMYFILLFFLTMRRQIQHMIKYRYIPLDIGKKKYSHSSN->IFAHSLFDCYFHYYCFF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43556 1 714
+P43556	UniProtKB	Chain	1	714	.	.	.	ID=PRO_0000097318;Note=Rho-GTPase-activating protein RGD2	
+P43556	UniProtKB	Domain	2	441	.	.	.	Note=F-BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01077	
+P43556	UniProtKB	Domain	218	298	.	.	.	Note=DEP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00066	
+P43556	UniProtKB	Domain	475	704	.	.	.	Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172	
+##sequence-region P06780 1 209
+P06780	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378	
+P06780	UniProtKB	Chain	2	206	.	.	.	ID=PRO_0000198945;Note=GTP-binding protein RHO1	
+P06780	UniProtKB	Propeptide	207	209	.	.	.	ID=PRO_0000281275;Note=Removed in mature form	
+P06780	UniProtKB	Nucleotide binding	17	24	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06780	UniProtKB	Nucleotide binding	64	68	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06780	UniProtKB	Nucleotide binding	122	125	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06780	UniProtKB	Motif	39	47	.	.	.	Note=Effector region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06780	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378	
+P06780	UniProtKB	Modified residue	206	206	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06780	UniProtKB	Lipidation	206	206	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06780	UniProtKB	Mutagenesis	22	22	.	.	.	Note=Abolishes GTP-binding. G->A	
+P06780	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Abolishes GTP-binding. T->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8947028;Dbxref=PMID:8947028	
+P06780	UniProtKB	Mutagenesis	42	42	.	.	.	Note=Impairs interaction with targets. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8947028;Dbxref=PMID:8947028	
+P06780	UniProtKB	Mutagenesis	43	43	.	.	.	Note=Temperature sensitive growth defect. V->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8846785;Dbxref=PMID:8846785	
+P06780	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Temperature sensitive growth defect. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8846785;Dbxref=PMID:8846785	
+P06780	UniProtKB	Mutagenesis	45	45	.	.	.	Note=Temperature sensitive growth defect. E->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11574532,ECO:0000269|PubMed:8846785;Dbxref=PMID:11574532,PMID:8846785	
+P06780	UniProtKB	Mutagenesis	45	45	.	.	.	Note=In RHO1-2%3B temperature sensitive%2C fails to activate PKC1. E->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11574532,ECO:0000269|PubMed:8846785;Dbxref=PMID:11574532,PMID:8846785	
+P06780	UniProtKB	Mutagenesis	60	60	.	.	.	Note=In RHO1-3%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532	
+P06780	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Locks RHO1 in the GTP-bound form by abolishing GTP hydrolysis. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3543936;Dbxref=PMID:3543936	
+P06780	UniProtKB	Mutagenesis	70	70	.	.	.	Note=In RHO1-10%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation%3B when associated with P-165. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532	
+P06780	UniProtKB	Mutagenesis	102	102	.	.	.	Note=In RHO1-11%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation%3B when associated with E-166. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532	
+P06780	UniProtKB	Mutagenesis	104	104	.	.	.	Note=In RHO1-4%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532	
+P06780	UniProtKB	Mutagenesis	121	121	.	.	.	Note=In RHO1-5%3B temperature sensitive%2C fails to activate PCK1. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532	
+P06780	UniProtKB	Mutagenesis	165	165	.	.	.	Note=In RHO1-10%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation%3B when associated with G-69. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532	
+P06780	UniProtKB	Mutagenesis	167	167	.	.	.	Note=In RHO1-11%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation%3B when associated with K-101. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532	
+P06780	UniProtKB	Beta strand	9	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Helix	23	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Beta strand	45	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Beta strand	56	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Helix	69	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Beta strand	83	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Helix	94	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Helix	104	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Beta strand	117	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Helix	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Helix	130	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Helix	146	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Beta strand	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Turn	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P06780	UniProtKB	Helix	172	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+##sequence-region Q06665 1 692
+Q06665	UniProtKB	Chain	1	692	.	.	.	ID=PRO_0000253814;Note=DNA repair protein RAD34	
+##sequence-region P25454 1 400
+P25454	UniProtKB	Chain	1	400	.	.	.	ID=PRO_0000122925;Note=DNA repair protein RAD51	
+P25454	UniProtKB	Nucleotide binding	185	192	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25454	UniProtKB	Helix	83	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	93	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	107	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	115	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	126	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	147	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	165	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Turn	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Beta strand	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Beta strand	179	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	191	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Beta strand	212	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	226	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	240	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Beta strand	247	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	255	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Beta strand	274	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	282	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	296	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Beta strand	320	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Helix	349	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Beta strand	355	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Beta strand	367	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Beta strand	376	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Beta strand	382	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+P25454	UniProtKB	Beta strand	391	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA	
+##sequence-region Q03956 1 351
+Q03956	UniProtKB	Chain	1	351	.	.	.	ID=PRO_0000097175;Note=Regulator of V-ATPase in vacuolar membrane protein 2	
+##sequence-region Q05672 1 457
+Q05672	UniProtKB	Chain	1	457	.	.	.	ID=PRO_0000076298;Note=RNA-binding suppressor of PAS kinase protein 1	
+Q05672	UniProtKB	Domain	26	88	.	.	.	Note=R3H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00382	
+Q05672	UniProtKB	Compositional bias	234	239	.	.	.	Note=Poly-Ser	
+Q05672	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q05672	UniProtKB	Modified residue	435	435	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+Q05672	UniProtKB	Modified residue	439	439	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+Q05672	UniProtKB	Modified residue	447	447	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05672	UniProtKB	Sequence conflict	1	3	.	.	.	Note=MTA->MRVSLSVSSFFHIQLDKFWRRQLSHIVPASRGDT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q05672	UniProtKB	Sequence conflict	43	43	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q05672	UniProtKB	Sequence conflict	81	81	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25332 1 333
+P25332	UniProtKB	Chain	1	333	.	.	.	ID=PRO_0000080094;Note=Ribokinase	
+P25332	UniProtKB	Nucleotide binding	248	253	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Nucleotide binding	282	283	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Region	10	12	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Region	38	42	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Active site	283	283	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Metal binding	277	277	.	.	.	Note=Potassium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Metal binding	279	279	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Metal binding	313	313	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Metal binding	316	316	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Metal binding	318	318	.	.	.	Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Metal binding	322	322	.	.	.	Note=Potassium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Binding site	149	149	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Binding site	193	193	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Binding site	283	283	.	.	.	Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215	
+P25332	UniProtKB	Sequence conflict	178	178	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25332	UniProtKB	Sequence conflict	301	301	.	.	.	Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08273 1 121
+Q08273	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000056022;Note=RING-box protein HRT1	
+Q08273	UniProtKB	Zinc finger	55	111	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q08273	UniProtKB	Metal binding	55	55	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878	
+Q08273	UniProtKB	Metal binding	58	58	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878	
+Q08273	UniProtKB	Metal binding	66	66	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878	
+Q08273	UniProtKB	Metal binding	69	69	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878	
+Q08273	UniProtKB	Metal binding	81	81	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878	
+Q08273	UniProtKB	Metal binding	88	88	.	.	.	Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878	
+Q08273	UniProtKB	Metal binding	90	90	.	.	.	Note=Zinc 3%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878	
+Q08273	UniProtKB	Metal binding	93	93	.	.	.	Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878	
+Q08273	UniProtKB	Metal binding	95	95	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878	
+Q08273	UniProtKB	Metal binding	107	107	.	.	.	Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878	
+Q08273	UniProtKB	Metal binding	110	110	.	.	.	Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878	
+Q08273	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08273	UniProtKB	Mutagenesis	72	72	.	.	.	Note=In RBX1-1%3B temperature-sensitive allele. At 38 degrees Celsius induces defects in ubiquitin ligase activity%3B when associated with R-81. K->R	
+Q08273	UniProtKB	Mutagenesis	81	81	.	.	.	Note=In RBX1-1%3B temperature-sensitive allele. At 38 degrees Celsius induces defects in ubiquitin ligase activity%3B when associated with R-72. C->R	
+Q08273	UniProtKB	Mutagenesis	81	81	.	.	.	Note=In HRT1-C81Y%3B defects in ubiquitin ligase activity. C->Y	
+##sequence-region Q03530 1 315
+Q03530	UniProtKB	Chain	1	315	.	.	.	ID=PRO_0000194834;Note=CAAX prenyl protease 2	
+Q03530	UniProtKB	Topological domain	1	3	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Transmembrane	4	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Topological domain	24	44	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Topological domain	66	74	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Transmembrane	75	95	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Topological domain	96	105	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Transmembrane	106	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Topological domain	127	148	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Transmembrane	149	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Topological domain	170	208	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Topological domain	230	237	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Transmembrane	238	258	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Topological domain	259	275	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Transmembrane	276	296	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Topological domain	297	315	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03530	UniProtKB	Active site	156	156	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6LZY8	
+Q03530	UniProtKB	Active site	194	194	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6LZY8	
+Q03530	UniProtKB	Site	248	248	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6LZY8	
+Q03530	UniProtKB	Site	252	252	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6LZY8	
+##sequence-region P38622 1 512
+P38622	UniProtKB	Chain	1	512	.	.	.	ID=PRO_0000086603;Note=Serine/threonine-protein kinase RCK1	
+P38622	UniProtKB	Domain	121	414	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38622	UniProtKB	Nucleotide binding	127	135	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38622	UniProtKB	Region	502	512	.	.	.	Note=Calmodulin-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38622	UniProtKB	Active site	259	259	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P38622	UniProtKB	Binding site	152	152	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region P32841 1 428
+P32841	UniProtKB	Chain	1	428	.	.	.	ID=PRO_0000097219;Note=Meiotic recombination protein REC114	
+P32841	UniProtKB	Sequence conflict	96	97	.	.	.	Note=KY->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32841	UniProtKB	Sequence conflict	100	103	.	.	.	Note=EEFG->RRIR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32841	UniProtKB	Sequence conflict	377	377	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P21538 1 810
+P21538	UniProtKB	Chain	1	810	.	.	.	ID=PRO_0000197089;Note=DNA-binding protein REB1	
+P21538	UniProtKB	Domain	470	523	.	.	.	Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P21538	UniProtKB	Domain	692	717	.	.	.	Note=Myb-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133	
+P21538	UniProtKB	DNA binding	497	519	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P21538	UniProtKB	Modified residue	355	355	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P21538	UniProtKB	Cross-link	807	807	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542864;Dbxref=PMID:15542864	
+P21538	UniProtKB	Sequence conflict	56	56	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21538	UniProtKB	Sequence conflict	592	618	.	.	.	Note=AAAAIQEQQQLLQQKQQDDDDAIAAAA->RAVVFKNNNNFFNKSSKMMTMLLRSC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21538	UniProtKB	Sequence conflict	627	627	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21538	UniProtKB	Sequence conflict	636	636	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P42073 1 533
+P42073	UniProtKB	Chain	1	533	.	.	.	ID=PRO_0000097239;Note=RNA end formation protein 2	
+P42073	UniProtKB	Compositional bias	321	331	.	.	.	Note=Ser/Thr-rich	
+##sequence-region P28519 1 371
+P28519	UniProtKB	Chain	1	371	.	.	.	ID=PRO_0000208654;Note=DNA repair protein RAD14	
+P28519	UniProtKB	Zinc finger	191	216	.	.	.	.	
+P28519	UniProtKB	Mutagenesis	207	207	.	.	.	Note=In RAD14-2%3B loss of recognition of cyclobutane pyrimidine dimers. V->M	
+P28519	UniProtKB	Mutagenesis	216	216	.	.	.	Note=In RAD14-2%3B loss of recognition of cyclobutane pyrimidine dimers. C->Y	
+P28519	UniProtKB	Turn	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+P28519	UniProtKB	Helix	202	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+P28519	UniProtKB	Helix	214	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+P28519	UniProtKB	Helix	221	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+P28519	UniProtKB	Beta strand	226	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+P28519	UniProtKB	Helix	229	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+P28519	UniProtKB	Helix	240	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+P28519	UniProtKB	Turn	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+P28519	UniProtKB	Beta strand	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+P28519	UniProtKB	Beta strand	265	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+P28519	UniProtKB	Helix	270	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+P28519	UniProtKB	Helix	283	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D	
+##sequence-region P10862 1 487
+P10862	UniProtKB	Chain	1	487	.	.	.	ID=PRO_0000056161;Note=Postreplication repair E3 ubiquitin-protein ligase RAD18	
+P10862	UniProtKB	Domain	278	312	.	.	.	Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186	
+P10862	UniProtKB	Zinc finger	28	66	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P10862	UniProtKB	Zinc finger	190	210	.	.	.	Note=UBZ-type	
+P10862	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P10862	UniProtKB	Modified residue	174	174	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P10862	UniProtKB	Cross-link	204	204	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q12021 1 506
+Q12021	UniProtKB	Chain	1	506	.	.	.	ID=PRO_0000268697;Note=Radiation-sensitive protein 28	
+Q12021	UniProtKB	Repeat	55	94	.	.	.	Note=WD 1	
+Q12021	UniProtKB	Repeat	193	233	.	.	.	Note=WD 2	
+Q12021	UniProtKB	Repeat	285	325	.	.	.	Note=WD 3	
+Q12021	UniProtKB	Repeat	357	396	.	.	.	Note=WD 4	
+Q12021	UniProtKB	Repeat	404	451	.	.	.	Note=WD 5	
+##sequence-region P12753 1 1312
+P12753	UniProtKB	Chain	1	1312	.	.	.	ID=PRO_0000138648;Note=DNA repair protein RAD50	
+P12753	UniProtKB	Domain	640	741	.	.	.	Note=Zinc-hook;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00471	
+P12753	UniProtKB	Nucleotide binding	34	41	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12753	UniProtKB	Coiled coil	185	347	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12753	UniProtKB	Coiled coil	403	558	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12753	UniProtKB	Coiled coil	640	678	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12753	UniProtKB	Coiled coil	712	741	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12753	UniProtKB	Coiled coil	787	1108	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12753	UniProtKB	Compositional bias	1204	1241	.	.	.	Note=Ala/Asp-rich (DA-box)	
+P12753	UniProtKB	Metal binding	687	687	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00471	
+P12753	UniProtKB	Metal binding	690	690	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00471	
+P12753	UniProtKB	Modified residue	469	469	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P12753	UniProtKB	Modified residue	568	568	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32863 1 898
+P32863	UniProtKB	Chain	1	898	.	.	.	ID=PRO_0000074344;Note=DNA repair and recombination protein RAD54	
+P32863	UniProtKB	Domain	322	504	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32863	UniProtKB	Domain	659	812	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P32863	UniProtKB	Nucleotide binding	335	342	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32863	UniProtKB	Motif	21	25	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32863	UniProtKB	Motif	41	45	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32863	UniProtKB	Motif	455	458	.	.	.	Note=DEGH box	
+##sequence-region Q08760 1 435
+Q08760	UniProtKB	Chain	1	435	.	.	.	ID=PRO_0000262736;Note=Bud site selection protein RAX1	
+Q08760	UniProtKB	Topological domain	1	297	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08760	UniProtKB	Transmembrane	298	318	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08760	UniProtKB	Topological domain	319	325	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08760	UniProtKB	Transmembrane	326	346	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08760	UniProtKB	Topological domain	347	409	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08760	UniProtKB	Transmembrane	410	430	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08760	UniProtKB	Topological domain	431	435	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08760	UniProtKB	Domain	126	257	.	.	.	Note=RGS	
+Q08760	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q03713 1 159
+Q03713	UniProtKB	Chain	1	159	.	.	.	ID=PRO_0000215779;Note=Respiratory supercomplex factor 1%2C mitochondrial	
+Q03713	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836	
+Q03713	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836	
+Q03713	UniProtKB	Domain	5	96	.	.	.	Note=HIG1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836	
+Q03713	UniProtKB	Coiled coil	88	159	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12044 1 265
+Q12044	UniProtKB	Chain	1	265	.	.	.	ID=PRO_0000237641;Note=Regulator of calcineurin 2	
+Q12044	UniProtKB	Compositional bias	141	204	.	.	.	Note=Ser-rich	
+Q12044	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12044	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12044	UniProtKB	Modified residue	132	132	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12044	UniProtKB	Modified residue	152	152	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12044	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12044	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12044	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+Q12044	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12044	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12044	UniProtKB	Modified residue	201	201	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12044	UniProtKB	Modified residue	255	255	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q04779 1 684
+Q04779	UniProtKB	Chain	1	684	.	.	.	ID=PRO_0000203282;Note=Transcriptional regulatory protein RCO1	
+Q04779	UniProtKB	Zinc finger	260	309	.	.	.	Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+Q04779	UniProtKB	Zinc finger	414	472	.	.	.	Note=PHD-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+Q04779	UniProtKB	Compositional bias	15	30	.	.	.	Note=Poly-Ser	
+Q04779	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04779	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04779	UniProtKB	Modified residue	683	683	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P38212 1 213
+P38212	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000202466;Note=Protein RCR1	
+P38212	UniProtKB	Topological domain	1	39	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38212	UniProtKB	Transmembrane	40	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38212	UniProtKB	Topological domain	63	213	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38212	UniProtKB	Motif	104	107	.	.	.	Note=PY motif	
+P38212	UniProtKB	Mutagenesis	82	83	.	.	.	Note=Reduced interaction with WW domain of RSP5. No interaction with WW domain of RSP5%3B when in association with A-105. PP->QA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17213653;Dbxref=PMID:17213653	
+P38212	UniProtKB	Mutagenesis	105	105	.	.	.	Note=Reduced interaction with WW domain of RSP5. No interaction with WW domain of RSP5%3B when in association with 82-QA-83. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17213653;Dbxref=PMID:17213653	
+P38212	UniProtKB	Mutagenesis	130	130	.	.	.	Note=No effect in conferring Congo red resistance%3B when associated with A-208. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17213653;Dbxref=PMID:17213653	
+P38212	UniProtKB	Mutagenesis	208	208	.	.	.	Note=No effect in conferring Congo red resistance%3B when associated with A-130. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17213653;Dbxref=PMID:17213653	
+##sequence-region P25611 1 832
+P25611	UniProtKB	Chain	1	832	.	.	.	ID=PRO_0000114994;Note=Regulator of drug sensitivity 1	
+P25611	UniProtKB	DNA binding	15	42	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P19541 1 446
+P19541	UniProtKB	Chain	1	446	.	.	.	ID=PRO_0000115006;Note=Regulator of drug sensitivity 2	
+P19541	UniProtKB	DNA binding	15	45	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P19541	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P19541	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P14291 1 827
+P14291	UniProtKB	Chain	1	827	.	.	.	ID=PRO_0000097234;Note=Protein RED1	
+##sequence-region P40893 1 198
+P40893	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000203011;Note=Regulation of enolase protein 1	
+P40893	UniProtKB	Helix	9	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	13	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	19	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	27	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Turn	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	60	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	78	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	89	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	101	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	126	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	137	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	151	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	164	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+P40893	UniProtKB	Beta strand	178	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12	
+##sequence-region Q00816 1 1014
+Q00816	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q00816	UniProtKB	Chain	2	1014	.	.	.	ID=PRO_0000083953;Note=Resistance to glucose repression protein 1	
+Q00816	UniProtKB	Motif	277	283	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q00816	UniProtKB	Motif	595	599	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q00816	UniProtKB	Motif	873	879	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q00816	UniProtKB	Compositional bias	543	552	.	.	.	Note=Ser-rich	
+Q00816	UniProtKB	Compositional bias	742	760	.	.	.	Note=Asp/Glu-rich (acidic)	
+Q00816	UniProtKB	Compositional bias	834	844	.	.	.	Note=Asp/Glu-rich (acidic)	
+Q00816	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q00816	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q00816	UniProtKB	Modified residue	75	75	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+Q00816	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00816	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q00816	UniProtKB	Modified residue	311	311	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q00816	UniProtKB	Modified residue	421	421	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q00816	UniProtKB	Modified residue	480	480	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q00816	UniProtKB	Modified residue	490	490	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q00816	UniProtKB	Modified residue	570	570	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00816	UniProtKB	Modified residue	572	572	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q00816	UniProtKB	Modified residue	576	576	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q00816	UniProtKB	Modified residue	610	610	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00816	UniProtKB	Modified residue	614	614	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00816	UniProtKB	Modified residue	680	680	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q00816	UniProtKB	Modified residue	896	896	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00816	UniProtKB	Modified residue	898	898	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00816	UniProtKB	Modified residue	980	980	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00816	UniProtKB	Sequence conflict	376	377	.	.	.	Note=DK->EE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00816	UniProtKB	Sequence conflict	534	534	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00816	UniProtKB	Sequence conflict	657	657	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00816	UniProtKB	Sequence conflict	889	889	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00816	UniProtKB	Sequence conflict	988	1014	.	.	.	Note=ARGMASKYLHSWKKSDVKPQENGNDSS->QEVWQASTCTLGKRVTSSHKKMEMTAVRRKNFEVNMKRK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06709 1 432
+Q06709	UniProtKB	Chain	1	432	.	.	.	ID=PRO_0000268700;Note=Cytoplasmic 60S subunit biogenesis factor REH1	
+Q06709	UniProtKB	Zinc finger	6	30	.	.	.	Note=C2H2-type 1	
+Q06709	UniProtKB	Zinc finger	186	209	.	.	.	Note=C2H2-type 2	
+Q06709	UniProtKB	Zinc finger	237	261	.	.	.	Note=C2H2-type 3	
+##sequence-region P38344 1 393
+P38344	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000202529;Note=Cytoplasmic 60S subunit biogenesis factor REI1	
+P38344	UniProtKB	Zinc finger	7	31	.	.	.	Note=C2H2-type 1	
+P38344	UniProtKB	Zinc finger	162	187	.	.	.	Note=C2H2-type 2	
+P38344	UniProtKB	Zinc finger	215	239	.	.	.	Note=C2H2-type 3	
+P38344	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38344	UniProtKB	Sequence conflict	152	153	.	.	.	Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38344	UniProtKB	Sequence conflict	152	153	.	.	.	Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12090 1 404
+Q12090	UniProtKB	Chain	1	404	.	.	.	ID=PRO_0000120937;Note=RNA exonuclease 3	
+Q12090	UniProtKB	Domain	243	389	.	.	.	Note=Exonuclease	
+##sequence-region Q04418 1 439
+Q04418	UniProtKB	Chain	1	439	.	.	.	ID=PRO_0000255972;Note=RNA polymerase II-associated protein RBA50	
+Q04418	UniProtKB	Sequence conflict	192	194	.	.	.	Note=EEA->GEG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39729 1 369
+P39729	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39729	UniProtKB	Chain	2	369	.	.	.	ID=PRO_0000205449;Note=Ribosome-interacting GTPase 1	
+P39729	UniProtKB	Domain	66	292	.	.	.	Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P39729	UniProtKB	Nucleotide binding	72	79	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P39729	UniProtKB	Nucleotide binding	118	122	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P39729	UniProtKB	Nucleotide binding	250	253	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047	
+P39729	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39729	UniProtKB	Helix	3	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Turn	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	25	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Turn	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	64	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	76	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	102	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	112	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	132	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	144	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	155	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	180	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	190	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	203	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	217	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	228	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Turn	236	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	245	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	257	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	269	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Turn	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	280	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	294	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	311	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	320	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Helix	329	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	335	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	345	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+P39729	UniProtKB	Beta strand	363	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A	
+##sequence-region P53721 1 224
+P53721	UniProtKB	Chain	1	224	.	.	.	ID=PRO_0000215780;Note=Respiratory supercomplex factor 2%2C mitochondrial	
+P53721	UniProtKB	Transmembrane	19	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836	
+P53721	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836	
+P53721	UniProtKB	Transmembrane	152	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836	
+P53721	UniProtKB	Domain	89	180	.	.	.	Note=HIG1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836	
+P53721	UniProtKB	Compositional bias	196	199	.	.	.	Note=Poly-Glu	
+##sequence-region P38623 1 610
+P38623	UniProtKB	Chain	1	610	.	.	.	ID=PRO_0000086604;Note=Serine/threonine-protein kinase RCK2	
+P38623	UniProtKB	Domain	163	478	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38623	UniProtKB	Nucleotide binding	169	177	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38623	UniProtKB	Region	493	506	.	.	.	Note=Calmodulin-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38623	UniProtKB	Active site	313	313	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P38623	UniProtKB	Binding site	201	201	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38623	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38623	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38623	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38623	UniProtKB	Modified residue	350	350	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38623	UniProtKB	Modified residue	520	520	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10805732;Dbxref=PMID:10805732	
+P38623	UniProtKB	Sequence conflict	109	109	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38623	UniProtKB	Sequence conflict	109	109	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38623	UniProtKB	Sequence conflict	188	188	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38623	UniProtKB	Sequence conflict	188	188	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38623	UniProtKB	Sequence conflict	233	233	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38623	UniProtKB	Sequence conflict	233	233	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38623	UniProtKB	Sequence conflict	328	328	.	.	.	Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38623	UniProtKB	Sequence conflict	328	328	.	.	.	Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38623	UniProtKB	Sequence conflict	456	456	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38623	UniProtKB	Sequence conflict	456	456	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36054 1 211
+P36054	UniProtKB	Chain	1	211	.	.	.	ID=PRO_0000211424;Note=Calcipressin-like protein	
+P36054	UniProtKB	Modified residue	113	113	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36054	UniProtKB	Modified residue	117	117	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P36054	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38086 1 958
+P38086	UniProtKB	Chain	1	958	.	.	.	ID=PRO_0000074346;Note=DNA repair and recombination protein RDH54	
+P38086	UniProtKB	Domain	333	521	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P38086	UniProtKB	Domain	665	824	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P38086	UniProtKB	Nucleotide binding	380	387	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P38086	UniProtKB	Motif	506	509	.	.	.	Note=DEGH box	
+P38086	UniProtKB	Cross-link	649	649	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38086	UniProtKB	Mutagenesis	352	352	.	.	.	Note=1%25-2%25 of the ATPase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10970884;Dbxref=PMID:10970884	
+P38086	UniProtKB	Sequence conflict	752	752	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38086	UniProtKB	Sequence conflict	752	752	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08742 1 149
+Q08742	UniProtKB	Transit peptide	1	25	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08742	UniProtKB	Chain	26	149	.	.	.	ID=PRO_0000245268;Note=Thiosulfate sulfurtransferase RDL2%2C mitochondrial	
+Q08742	UniProtKB	Domain	45	146	.	.	.	Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+Q08742	UniProtKB	Active site	106	106	.	.	.	Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+##sequence-region P33323 1 182
+P33323	UniProtKB	Chain	1	182	.	.	.	ID=PRO_0000097216;Note=Meiotic recombination protein REC104	
+##sequence-region Q12188 1 680
+Q12188	UniProtKB	Chain	1	680	.	.	.	ID=PRO_0000268699;Note=Meiotic recombination protein REC8	
+Q12188	UniProtKB	Site	431	432	.	.	.	Note=Cleavage%3B by ESP1	
+Q12188	UniProtKB	Site	453	454	.	.	.	Note=Cleavage%3B by ESP1	
+Q12188	UniProtKB	Mutagenesis	428	428	.	.	.	Note=Abolishes cleavage by ESP1 at position R-431%3B when associated with E-431. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11081626;Dbxref=PMID:11081626	
+Q12188	UniProtKB	Mutagenesis	431	431	.	.	.	Note=Reduces cleavage by ESP1 at position R-431. Abolishes cleavage by ESP1 at position R-431%3B when associated with R-428. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11081626;Dbxref=PMID:11081626	
+Q12188	UniProtKB	Mutagenesis	453	453	.	.	.	Note=Abolishes cleavage by ESP1 at position R-453. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11081626;Dbxref=PMID:11081626	
+##sequence-region P38232 1 338
+P38232	UniProtKB	Chain	1	338	.	.	.	ID=PRO_0000071523;Note=Protein REG2	
+##sequence-region P01119 1 309
+P01119	UniProtKB	Chain	1	306	.	.	.	ID=PRO_0000030193;Note=Ras-like protein 1	
+P01119	UniProtKB	Propeptide	307	309	.	.	.	ID=PRO_0000030194;Note=Removed in mature form	
+P01119	UniProtKB	Nucleotide binding	17	24	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P01119	UniProtKB	Nucleotide binding	64	68	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P01119	UniProtKB	Nucleotide binding	123	126	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P01119	UniProtKB	Motif	39	47	.	.	.	Note=Effector region	
+P01119	UniProtKB	Modified residue	306	306	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2050108;Dbxref=PMID:2050108	
+P01119	UniProtKB	Lipidation	305	305	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3513173;Dbxref=PMID:3513173	
+P01119	UniProtKB	Lipidation	306	306	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1763050;Dbxref=PMID:1763050	
+P01119	UniProtKB	Mutagenesis	66	66	.	.	.	Note=Impaired GTPase activity%2C autophosphorylating activity. A->T	
+P01119	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Impaired GTPase activity. Q->L	
+P01119	UniProtKB	Sequence conflict	204	204	.	.	.	Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P01120 1 322
+P01120	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406252;Dbxref=PMID:2406252	
+P01120	UniProtKB	Chain	2	319	.	.	.	ID=PRO_0000030195;Note=Ras-like protein 2	
+P01120	UniProtKB	Propeptide	320	322	.	.	.	ID=PRO_0000030196;Note=Removed in mature form	
+P01120	UniProtKB	Nucleotide binding	17	24	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P01120	UniProtKB	Nucleotide binding	64	68	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P01120	UniProtKB	Nucleotide binding	123	126	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P01120	UniProtKB	Motif	39	47	.	.	.	Note=Effector region	
+P01120	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P01120	UniProtKB	Modified residue	202	202	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P01120	UniProtKB	Modified residue	207	207	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P01120	UniProtKB	Modified residue	214	214	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P01120	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+P01120	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P01120	UniProtKB	Modified residue	319	319	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2050108,ECO:0000269|PubMed:2663844;Dbxref=PMID:2050108,PMID:2663844	
+P01120	UniProtKB	Lipidation	318	318	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406252;Dbxref=PMID:2406252	
+P01120	UniProtKB	Lipidation	319	319	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1763050;Dbxref=PMID:1763050	
+P01120	UniProtKB	Cross-link	131	131	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P01120	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Low sporulation efficiency. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6327067;Dbxref=PMID:6327067	
+P01120	UniProtKB	Mutagenesis	70	70	.	.	.	Note=In GLC5-1%3B low glycogen accumulation and sporulation deficiency. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8150278;Dbxref=PMID:8150278	
+P01120	UniProtKB	Sequence conflict	108	108	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P01120	UniProtKB	Sequence conflict	210	210	.	.	.	Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P01120	UniProtKB	Sequence conflict	255	255	.	.	.	Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P01120	UniProtKB	Sequence conflict	298	299	.	.	.	Note=KQ->SK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47104 1 1357
+P47104	UniProtKB	Chain	1	1357	.	.	.	ID=PRO_0000051183;Note=Regulator of V-ATPase in vacuolar membrane protein 1	
+P47104	UniProtKB	Repeat	98	134	.	.	.	Note=WD 1	
+P47104	UniProtKB	Repeat	142	182	.	.	.	Note=WD 2	
+P47104	UniProtKB	Repeat	190	239	.	.	.	Note=WD 3	
+P47104	UniProtKB	Repeat	384	423	.	.	.	Note=WD 4	
+P47104	UniProtKB	Repeat	431	470	.	.	.	Note=WD 5	
+P47104	UniProtKB	Repeat	595	636	.	.	.	Note=WD 6	
+P47104	UniProtKB	Repeat	638	679	.	.	.	Note=WD 7	
+P47104	UniProtKB	Repeat	898	939	.	.	.	Note=WD 8	
+P47104	UniProtKB	Modified residue	1244	1244	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198	
+P47104	UniProtKB	Modified residue	1248	1248	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q12192 1 310
+Q12192	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000097309;Note=Repression factor of MSEs protein 1	
+Q12192	UniProtKB	Compositional bias	95	100	.	.	.	Note=Poly-Ser	
+Q12192	UniProtKB	Compositional bias	128	135	.	.	.	Note=Poly-Arg	
+Q12192	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P40043 1 161
+P40043	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000202633;Note=Respiratory growth induced protein 1	
+P40043	UniProtKB	Cross-link	68	68	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P40043	UniProtKB	Beta strand	17	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+P40043	UniProtKB	Helix	28	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+P40043	UniProtKB	Beta strand	48	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+P40043	UniProtKB	Helix	56	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+P40043	UniProtKB	Turn	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+P40043	UniProtKB	Helix	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+P40043	UniProtKB	Helix	78	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+P40043	UniProtKB	Helix	92	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+P40043	UniProtKB	Beta strand	108	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+P40043	UniProtKB	Beta strand	116	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+P40043	UniProtKB	Beta strand	132	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+P40043	UniProtKB	Beta strand	149	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY	
+##sequence-region P32862 1 1170
+P32862	UniProtKB	Chain	1	1170	.	.	.	ID=PRO_0000115001;Note=Glucose transport transcription regulator RGT1	
+P32862	UniProtKB	DNA binding	47	76	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P32862	UniProtKB	Modified residue	202	202	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P32862	UniProtKB	Modified residue	205	205	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32862	UniProtKB	Modified residue	208	208	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32862	UniProtKB	Modified residue	229	229	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198	
+P32862	UniProtKB	Modified residue	283	283	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32862	UniProtKB	Modified residue	284	284	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32862	UniProtKB	Modified residue	410	410	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32862	UniProtKB	Modified residue	414	414	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32862	UniProtKB	Modified residue	1130	1130	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P25378 1 209
+P25378	UniProtKB	Chain	1	206	.	.	.	ID=PRO_0000082713;Note=Rheb-like protein RHB1	
+P25378	UniProtKB	Propeptide	207	209	.	.	.	ID=PRO_0000281370;Note=Removed in mature form	
+P25378	UniProtKB	Nucleotide binding	23	30	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25378	UniProtKB	Nucleotide binding	70	74	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25378	UniProtKB	Nucleotide binding	129	132	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25378	UniProtKB	Motif	45	53	.	.	.	Note=Effector region	
+P25378	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25378	UniProtKB	Modified residue	206	206	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25378	UniProtKB	Lipidation	206	206	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10753927;Dbxref=PMID:10753927	
+##sequence-region Q12305 1 139
+Q12305	UniProtKB	Chain	1	139	.	.	.	ID=PRO_0000245269;Note=Thiosulfate sulfurtransferase RDL1%2C mitochondrial	
+Q12305	UniProtKB	Domain	37	138	.	.	.	Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+Q12305	UniProtKB	Active site	98	98	.	.	.	Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173	
+Q12305	UniProtKB	Modified residue	26	26	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12305	UniProtKB	Helix	27	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Beta strand	41	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Helix	49	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Turn	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Helix	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Helix	76	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Beta strand	92	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Beta strand	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Helix	102	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Turn	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Beta strand	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Helix	125	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+Q12305	UniProtKB	Helix	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P	
+##sequence-region P53331 1 553
+P53331	UniProtKB	Chain	1	553	.	.	.	ID=PRO_0000202869;Note=RNA exonuclease 1	
+P53331	UniProtKB	Domain	225	373	.	.	.	Note=Exonuclease	
+P53331	UniProtKB	Coiled coil	167	194	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53331	UniProtKB	Coiled coil	509	533	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53331	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53331	UniProtKB	Mutagenesis	305	305	.	.	.	Note=In REX1-1%3B impairs 5S rRNA maturation. L->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16100378;Dbxref=PMID:16100378	
+##sequence-region Q08237 1 289
+Q08237	UniProtKB	Chain	1	289	.	.	.	ID=PRO_0000131702;Note=RNA exonuclease 4	
+Q08237	UniProtKB	Domain	121	273	.	.	.	Note=Exonuclease	
+##sequence-region P38630 1 861
+P38630	UniProtKB	Chain	1	861	.	.	.	ID=PRO_0000121776;Note=Replication factor C subunit 1	
+P38630	UniProtKB	Domain	153	243	.	.	.	Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P38630	UniProtKB	Nucleotide binding	353	361	.	.	.	Note=ATP	
+P38630	UniProtKB	Motif	830	834	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38630	UniProtKB	Motif	855	860	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38630	UniProtKB	Binding site	299	299	.	.	.	Note=ATP%3B via carbonyl oxygen	
+P38630	UniProtKB	Binding site	311	311	.	.	.	Note=ATP%3B via amide nitrogen and carbonyl oxygen	
+P38630	UniProtKB	Binding site	456	456	.	.	.	Note=ATP	
+P38630	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38630	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38630	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38630	UniProtKB	Mutagenesis	427	427	.	.	.	Note=In cs mutant CDC44-2%3B causes cell cycle arrest. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8264593;Dbxref=PMID:8264593	
+P38630	UniProtKB	Mutagenesis	436	436	.	.	.	Note=In cs mutant CDC44-3/4%3B causes cell cycle arrest. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8264593;Dbxref=PMID:8264593	
+P38630	UniProtKB	Mutagenesis	512	512	.	.	.	Note=In cs mutant CDC44-9%3B no effect. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8264593;Dbxref=PMID:8264593	
+P38630	UniProtKB	Mutagenesis	513	513	.	.	.	Note=In cs mutants CDC44-1/5/8 and CDC44-9%3B causes cell cycle arrest. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8264593;Dbxref=PMID:8264593	
+P38630	UniProtKB	Helix	298	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	314	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	327	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Turn	333	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Beta strand	347	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	359	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Beta strand	373	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	385	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	392	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Turn	402	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Beta strand	418	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	426	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	436	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Beta strand	451	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	464	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Turn	467	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Beta strand	470	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	480	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	502	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Turn	510	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	514	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	523	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	535	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Turn	545	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	550	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	561	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	568	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	574	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Turn	585	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	588	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Beta strand	596	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	610	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	638	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	641	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	650	654	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	669	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Turn	688	692	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	699	703	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Turn	704	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	707	714	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	725	730	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Turn	731	733	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38630	UniProtKB	Helix	737	746	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+##sequence-region P38629 1 340
+P38629	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38629	UniProtKB	Chain	2	340	.	.	.	ID=PRO_0000121756;Note=Replication factor C subunit 3	
+P38629	UniProtKB	Nucleotide binding	16	19	.	.	.	Note=ATP	
+P38629	UniProtKB	Nucleotide binding	53	61	.	.	.	Note=ATP	
+P38629	UniProtKB	Binding site	20	20	.	.	.	Note=ATP	
+P38629	UniProtKB	Binding site	28	28	.	.	.	Note=ATP%3B via amide nitrogen and carbonyl oxygen	
+P38629	UniProtKB	Binding site	148	148	.	.	.	Note=ATP	
+P38629	UniProtKB	Binding site	206	206	.	.	.	Note=ATP	
+P38629	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38629	UniProtKB	Helix	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	31	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Beta strand	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Beta strand	54	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	59	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Beta strand	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	90	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	96	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Beta strand	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Beta strand	112	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	124	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Turn	137	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Beta strand	141	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	155	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Beta strand	161	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	171	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Turn	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	191	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	205	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Turn	212	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Beta strand	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	229	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	241	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	256	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Turn	269	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	274	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	293	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38629	UniProtKB	Helix	316	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+##sequence-region Q99188 1 309
+Q99188	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000268701;Note=Regulator of G-protein signaling 2	
+Q99188	UniProtKB	Domain	37	161	.	.	.	Note=RGS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00171	
+Q99188	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Decreases the ability to suppress glucose-induced cAMP signaling when overexpressed. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523302;Dbxref=PMID:10523302	
+Q99188	UniProtKB	Mutagenesis	144	144	.	.	.	Note=Abolishes the ability to suppress glucose-induced cAMP signaling when overexpressed. L->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523302;Dbxref=PMID:10523302	
+##sequence-region Q06624 1 347
+Q06624	UniProtKB	Chain	1	347	.	.	.	ID=PRO_0000194975;Note=DNA damage tolerance protein RHC31	
+Q06624	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06624	UniProtKB	Cross-link	35	35	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219	
+##sequence-region P40395 1 1056
+P40395	UniProtKB	Chain	1	1056	.	.	.	ID=PRO_0000097332;Note=Guanine nucleotide exchange factor subunit RIC1	
+##sequence-region P43565 1 1770
+P43565	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000086605;Note=Serine/threonine-protein kinase RIM15	
+P43565	UniProtKB	Domain	794	1254	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P43565	UniProtKB	Domain	1255	1320	.	.	.	Note=AGC-kinase C-terminal	
+P43565	UniProtKB	Domain	1636	1750	.	.	.	Note=Response regulatory;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00169	
+P43565	UniProtKB	Nucleotide binding	800	808	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P43565	UniProtKB	Compositional bias	343	358	.	.	.	Note=Poly-Asn	
+P43565	UniProtKB	Compositional bias	620	624	.	.	.	Note=Poly-Ser	
+P43565	UniProtKB	Compositional bias	975	980	.	.	.	Note=Poly-Asn	
+P43565	UniProtKB	Compositional bias	1213	1218	.	.	.	Note=Poly-Glu	
+P43565	UniProtKB	Compositional bias	1386	1391	.	.	.	Note=Poly-Thr	
+P43565	UniProtKB	Active site	918	918	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P43565	UniProtKB	Binding site	823	823	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P43565	UniProtKB	Modified residue	380	380	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43565	UniProtKB	Modified residue	476	476	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43565	UniProtKB	Modified residue	704	704	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P43565	UniProtKB	Modified residue	709	709	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43565	UniProtKB	Modified residue	733	733	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P43565	UniProtKB	Modified residue	736	736	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43565	UniProtKB	Modified residue	737	737	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43565	UniProtKB	Modified residue	747	747	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43565	UniProtKB	Modified residue	1044	1044	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43565	UniProtKB	Modified residue	1048	1048	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43565	UniProtKB	Modified residue	1064	1064	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43565	UniProtKB	Modified residue	1075	1075	.	.	.	Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16308562;Dbxref=PMID:16308562	
+P43565	UniProtKB	Modified residue	1421	1421	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43565	UniProtKB	Modified residue	1531	1531	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43565	UniProtKB	Modified residue	1538	1538	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43565	UniProtKB	Modified residue	1542	1542	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43565	UniProtKB	Modified residue	1565	1565	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43565	UniProtKB	Modified residue	1764	1764	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P43565	UniProtKB	Mutagenesis	823	823	.	.	.	Note=Loss of kinase activity. K->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9744870;Dbxref=PMID:9744870	
+##sequence-region Q08003 1 200
+Q08003	UniProtKB	Chain	1	200	.	.	.	ID=PRO_0000247248;Note=Regulator of free ubiquitin chains 1	
+Q08003	UniProtKB	Compositional bias	75	81	.	.	.	Note=Poly-Ser	
+##sequence-region P39083 1 1007
+P39083	UniProtKB	Chain	1	1007	.	.	.	ID=PRO_0000075899;Note=Rho-type GTPase-activating protein 1	
+P39083	UniProtKB	Domain	13	66	.	.	.	Note=LIM zinc-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125	
+P39083	UniProtKB	Domain	70	122	.	.	.	Note=LIM zinc-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125	
+P39083	UniProtKB	Domain	791	1006	.	.	.	Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172	
+P39083	UniProtKB	Modified residue	278	278	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39083	UniProtKB	Modified residue	291	291	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39083	UniProtKB	Modified residue	532	532	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39083	UniProtKB	Natural variant	866	866	.	.	.	Note=V->A	
+P39083	UniProtKB	Natural variant	898	898	.	.	.	Note=K->R	
+P39083	UniProtKB	Natural variant	926	926	.	.	.	Note=S->G	
+P39083	UniProtKB	Mutagenesis	37	37	.	.	.	Note=Bipolar budding. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8657111;Dbxref=PMID:8657111	
+P39083	UniProtKB	Mutagenesis	40	40	.	.	.	Note=Bipolar budding. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8657111;Dbxref=PMID:8657111	
+P39083	UniProtKB	Mutagenesis	98	98	.	.	.	Note=Bipolar budding. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8657111;Dbxref=PMID:8657111	
+P39083	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Bipolar budding. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8657111;Dbxref=PMID:8657111	
+P39083	UniProtKB	Sequence conflict	457	457	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39083	UniProtKB	Sequence conflict	507	507	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06108 1 1083
+Q06108	UniProtKB	Chain	1	1083	.	.	.	ID=PRO_0000242488;Note=Regulator of the glycerol channel 1	
+Q06108	UniProtKB	Domain	495	606	.	.	.	Note=PH	
+Q06108	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	249	249	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	252	252	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	481	481	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06108	UniProtKB	Modified residue	537	537	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	652	652	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06108	UniProtKB	Modified residue	765	765	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	813	813	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	817	817	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06108	UniProtKB	Modified residue	857	857	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	866	866	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06108	UniProtKB	Modified residue	879	879	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	918	918	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06108	UniProtKB	Modified residue	966	966	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	969	969	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	975	975	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	1059	1059	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06108	UniProtKB	Modified residue	1081	1081	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06108	UniProtKB	Modified residue	1082	1082	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P16664 1 663
+P16664	UniProtKB	Chain	1	663	.	.	.	ID=PRO_0000097319;Note=Guanine nucleotide exchange factor subunit RGP1	
+P16664	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P16664	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P16664	UniProtKB	Modified residue	357	357	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P16664	UniProtKB	Modified residue	363	363	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P16664	UniProtKB	Modified residue	364	364	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P16664	UniProtKB	Modified residue	370	370	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P16664	UniProtKB	Sequence conflict	52	56	.	.	.	Note=EKLLT->KAS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12300 1 763
+Q12300	UniProtKB	Chain	1	763	.	.	.	ID=PRO_0000050389;Note=High-affinity glucose transporter RGT2	
+Q12300	UniProtKB	Topological domain	1	99	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	121	144	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	145	165	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	166	175	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	176	196	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	197	197	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	219	231	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	232	252	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	253	266	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	288	357	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	358	378	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	379	393	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	394	414	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	415	421	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	422	442	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	443	452	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	453	473	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	474	491	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	492	512	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	513	524	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Transmembrane	525	545	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Topological domain	546	763	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Glycosylation	136	136	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Glycosylation	385	385	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12300	UniProtKB	Mutagenesis	231	231	.	.	.	Note=In RGT2-1%3B constitutively signaling glucose receptor. R->K	
+##sequence-region P21524 1 888
+P21524	UniProtKB	Chain	1	888	.	.	.	ID=PRO_0000187203;Note=Ribonucleoside-diphosphate reductase large chain 1	
+P21524	UniProtKB	Domain	1	92	.	.	.	Note=ATP-cone;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00492	
+P21524	UniProtKB	Region	11	17	.	.	.	Note=Allosteric activator binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21524	UniProtKB	Region	217	218	.	.	.	Note=Substrate binding	
+P21524	UniProtKB	Region	285	288	.	.	.	Note=Allosteric effector binding%2C determines substrate specificity	
+P21524	UniProtKB	Region	426	430	.	.	.	Note=Substrate binding	
+P21524	UniProtKB	Region	607	611	.	.	.	Note=Substrate binding	
+P21524	UniProtKB	Active site	426	426	.	.	.	Note=Proton acceptor	
+P21524	UniProtKB	Active site	428	428	.	.	.	Note=Cysteine radical intermediate	
+P21524	UniProtKB	Active site	430	430	.	.	.	Note=Proton acceptor	
+P21524	UniProtKB	Binding site	5	5	.	.	.	Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21524	UniProtKB	Binding site	53	53	.	.	.	Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21524	UniProtKB	Binding site	88	88	.	.	.	Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21524	UniProtKB	Binding site	202	202	.	.	.	Note=Substrate	
+P21524	UniProtKB	Binding site	247	247	.	.	.	Note=Substrate%3B via amide nitrogen	
+P21524	UniProtKB	Site	218	218	.	.	.	Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21524	UniProtKB	Site	226	226	.	.	.	Note=Allosteric effector binding%2C determines substrate specificity	
+P21524	UniProtKB	Site	256	256	.	.	.	Note=Allosteric effector binding%2C determines substrate specificity	
+P21524	UniProtKB	Site	443	443	.	.	.	Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21524	UniProtKB	Site	741	741	.	.	.	Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21524	UniProtKB	Site	742	742	.	.	.	Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21524	UniProtKB	Site	883	883	.	.	.	Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21524	UniProtKB	Site	886	886	.	.	.	Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21524	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P21524	UniProtKB	Modified residue	816	816	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21672	
+P21524	UniProtKB	Modified residue	837	837	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P21524	UniProtKB	Modified residue	887	887	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P21524	UniProtKB	Disulfide bond	218	443	.	.	.	Note=Redox-active;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537479;Dbxref=PMID:16537479	
+P21524	UniProtKB	Cross-link	387	387	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P21524	UniProtKB	Cross-link	853	853	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P21524	UniProtKB	Mutagenesis	428	428	.	.	.	Note=Completely abolishes reductase activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11893751;Dbxref=PMID:11893751	
+P21524	UniProtKB	Sequence conflict	329	329	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21524	UniProtKB	Sequence conflict	587	589	.	.	.	Note=TLR->NLK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21524	UniProtKB	Sequence conflict	666	666	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21524	UniProtKB	Sequence conflict	679	679	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21524	UniProtKB	Helix	19	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+P21524	UniProtKB	Turn	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+P21524	UniProtKB	Helix	36	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+P21524	UniProtKB	Helix	53	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+P21524	UniProtKB	Turn	67	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+P21524	UniProtKB	Helix	79	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX	
+P21524	UniProtKB	Helix	94	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Turn	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	118	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	128	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	137	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	145	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	158	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX	
+P21524	UniProtKB	Helix	167	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	183	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	197	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	202	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	218	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	228	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Turn	243	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S8A	
+P21524	UniProtKB	Beta strand	247	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Turn	263	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	272	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Turn	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX	
+P21524	UniProtKB	Beta strand	297	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	308	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Turn	312	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	317	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX	
+P21524	UniProtKB	Beta strand	328	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	336	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	347	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Turn	353	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	359	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	364	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	380	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	385	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	403	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	407	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Turn	415	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+P21524	UniProtKB	Beta strand	441	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	445	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	450	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	454	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX	
+P21524	UniProtKB	Beta strand	458	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EUD	
+P21524	UniProtKB	Beta strand	463	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX	
+P21524	UniProtKB	Helix	467	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	493	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	506	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	512	519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	526	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	564	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	571	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	581	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZLG	
+P21524	UniProtKB	Helix	585	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	611	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	619	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVS	
+P21524	UniProtKB	Beta strand	627	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX	
+P21524	UniProtKB	Beta strand	634	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+P21524	UniProtKB	Beta strand	638	641	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+P21524	UniProtKB	Helix	643	651	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	657	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Turn	665	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	678	683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	687	689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Helix	692	703	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	714	718	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX	
+P21524	UniProtKB	Helix	721	734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	737	741	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T	
+P21524	UniProtKB	Beta strand	743	745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX	
+P21524	UniProtKB	Turn	748	751	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+P21524	UniProtKB	Helix	760	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+P21524	UniProtKB	Helix	764	766	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+P21524	UniProtKB	Turn	789	791	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ	
+##sequence-region Q07844 1 837
+Q07844	UniProtKB	Chain	1	837	.	.	.	ID=PRO_0000084762;Note=Ribosome biogenesis ATPase RIX7	
+Q07844	UniProtKB	Nucleotide binding	246	253	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07844	UniProtKB	Nucleotide binding	574	581	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07844	UniProtKB	Modified residue	42	42	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P26785 1 198
+P26785	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921	
+P26785	UniProtKB	Chain	2	198	.	.	.	ID=PRO_0000133792;Note=60S ribosomal protein L16-B	
+P26785	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine%3B partial;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921	
+P26785	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P26785	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P26785	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P26785	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P26785	UniProtKB	Cross-link	176	176	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P26785	UniProtKB	Sequence conflict	14	14	.	.	.	Note=L->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P46990 1 184
+P46990	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943	
+P46990	UniProtKB	Chain	2	184	.	.	.	ID=PRO_0000125348;Note=60S ribosomal protein L17-B	
+P46990	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05740	
+P46990	UniProtKB	Cross-link	46	46	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P38222 1 552
+P38222	UniProtKB	Chain	1	552	.	.	.	ID=PRO_0000202472;Note=Ribosomal lysine N-methyltransferase 3	
+P38222	UniProtKB	Domain	26	335	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+P38222	UniProtKB	Compositional bias	418	427	.	.	.	Note=Poly-Glu	
+P38222	UniProtKB	Binding site	334	334	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+##sequence-region P36105 1 138
+P36105	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P36105	UniProtKB	Chain	2	138	.	.	.	ID=PRO_0000132043;Note=60S ribosomal protein L14-A	
+P36105	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P36105	UniProtKB	Beta strand	19	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Beta strand	25	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Beta strand	32	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Beta strand	40	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Helix	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Beta strand	53	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Helix	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Beta strand	63	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Helix	78	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Helix	90	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Helix	98	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Helix	114	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P36105	UniProtKB	Turn	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX49 1 186
+P0CX49	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894	
+P0CX49	UniProtKB	Chain	2	186	.	.	.	ID=PRO_0000132784;Note=60S ribosomal protein L18-A	
+P0CX49	UniProtKB	Modified residue	50	50	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802	
+P0CX49	UniProtKB	Cross-link	116	116	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX49	UniProtKB	Helix	24	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Helix	43	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Helix	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Helix	64	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Turn	74	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P0CX49	UniProtKB	Beta strand	79	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Beta strand	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Helix	108	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Beta strand	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Helix	124	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Beta strand	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Helix	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Helix	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Turn	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Turn	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P0CX49	UniProtKB	Beta strand	169	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3N	
+P0CX49	UniProtKB	Beta strand	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX49	UniProtKB	Helix	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U51	
+##sequence-region P0CX24 1 172
+P0CX24	UniProtKB	Chain	1	172	.	.	.	ID=PRO_0000409758;Note=60S ribosomal protein L20-B	
+P0CX24	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX24	UniProtKB	Cross-link	125	125	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX24	UniProtKB	Cross-link	131	131	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX24	UniProtKB	Cross-link	149	149	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q12672 1 160
+Q12672	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000149683;Note=60S ribosomal protein L21-B	
+Q12672	UniProtKB	Cross-link	32	32	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P0CX41 1 137
+P0CX41	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16096273;Dbxref=PMID:22814378,PMID:16096273	
+P0CX41	UniProtKB	Chain	2	137	.	.	.	ID=PRO_0000128630;Note=60S ribosomal protein L23-A	
+P0CX41	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16096273;Dbxref=PMID:22814378,PMID:16096273	
+P0CX41	UniProtKB	Modified residue	106	106	.	.	.	Note=N6%2CN6-dimethyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17327221;Dbxref=PMID:17327221	
+P0CX41	UniProtKB	Modified residue	110	110	.	.	.	Note=N6%2CN6-dimethyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17327221;Dbxref=PMID:17327221	
+P0CX41	UniProtKB	Beta strand	22	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Beta strand	27	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Beta strand	33	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Beta strand	57	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Beta strand	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Beta strand	74	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Beta strand	92	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Beta strand	99	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Turn	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P0CX41	UniProtKB	Beta strand	109	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Helix	120	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Helix	127	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX41	UniProtKB	Beta strand	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P35196 1 286
+P35196	UniProtKB	Chain	1	286	.	.	.	ID=PRO_0000123759;Note=Dehydrodolichyl diphosphate synthase complex subunit RER2	
+P35196	UniProtKB	Mutagenesis	164	164	.	.	.	Note=In RER2-1%3B loss of activity. G->D	
+P35196	UniProtKB	Mutagenesis	209	209	.	.	.	Note=In RER2-2%3B loss of activity. S->N	
+##sequence-region P30775 1 413
+P30775	UniProtKB	Modified residue	287	287	.	.	.	Note=N5-methylglutamine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16321977;Dbxref=PMID:16321977	
+##sequence-region P53893 1 1110
+P53893	UniProtKB	Chain	1	1110	.	.	.	ID=PRO_0000091559;Note=Ribosome assembly protein 1	
+P53893	UniProtKB	Domain	17	262	.	.	.	Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P53893	UniProtKB	Nucleotide binding	26	33	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53893	UniProtKB	Nucleotide binding	102	106	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53893	UniProtKB	Nucleotide binding	156	159	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53893	UniProtKB	Modified residue	431	431	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q06208 1 395
+Q06208	UniProtKB	Chain	1	395	.	.	.	ID=PRO_0000097337;Note=Protein RIF2	
+Q06208	UniProtKB	Sequence conflict	387	387	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06208	UniProtKB	Helix	37	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6	
+Q06208	UniProtKB	Helix	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6	
+Q06208	UniProtKB	Helix	71	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Helix	93	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Beta strand	104	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Beta strand	109	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Helix	119	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Beta strand	137	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Helix	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Helix	189	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Turn	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6	
+Q06208	UniProtKB	Beta strand	204	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Beta strand	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ5	
+Q06208	UniProtKB	Helix	226	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Beta strand	245	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Helix	260	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Beta strand	274	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Helix	284	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Helix	304	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Helix	323	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Helix	337	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Helix	355	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Turn	368	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1	
+Q06208	UniProtKB	Helix	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6	
+##sequence-region Q03778 1 218
+Q03778	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03778	UniProtKB	Chain	20	218	.	.	.	ID=PRO_0000030437;Note=Riboflavin kinase	
+Q03778	UniProtKB	Active site	155	155	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03778	UniProtKB	Metal binding	72	72	.	.	.	Note=Magnesium or zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03792 1 727
+Q03792	UniProtKB	Chain	1	727	.	.	.	ID=PRO_0000207746;Note=Calpain-like protease 1	
+Q03792	UniProtKB	Domain	70	317	.	.	.	Note=Calpain catalytic	
+Q03792	UniProtKB	Active site	128	128	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03792	UniProtKB	Active site	271	271	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03792	UniProtKB	Active site	296	296	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03792	UniProtKB	Mutagenesis	128	128	.	.	.	Note=Loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9928935;Dbxref=PMID:9928935	
+##sequence-region Q08961 1 583
+Q08961	UniProtKB	Chain	1	583	.	.	.	ID=PRO_0000228984;Note=Ribosomal lysine N-methyltransferase 1	
+Q08961	UniProtKB	Domain	22	274	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+Q08961	UniProtKB	Coiled coil	378	407	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08961	UniProtKB	Coiled coil	433	459	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08961	UniProtKB	Binding site	273	273	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+##sequence-region P22336 1 621
+P22336	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P22336	UniProtKB	Chain	2	621	.	.	.	ID=PRO_0000097268;Note=Replication factor A protein 1	
+P22336	UniProtKB	DNA binding	197	284	.	.	.	Note=OB	
+P22336	UniProtKB	Zinc finger	486	508	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22336	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P22336	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22336	UniProtKB	Helix	10	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X	
+P22336	UniProtKB	Helix	18	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X	
+P22336	UniProtKB	Beta strand	28	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X	
+P22336	UniProtKB	Turn	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X	
+P22336	UniProtKB	Beta strand	44	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X	
+P22336	UniProtKB	Beta strand	53	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X	
+P22336	UniProtKB	Helix	63	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X	
+P22336	UniProtKB	Beta strand	79	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X	
+P22336	UniProtKB	Turn	91	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X	
+P22336	UniProtKB	Beta strand	95	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X	
+P22336	UniProtKB	Helix	120	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X	
+P22336	UniProtKB	Helix	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+P22336	UniProtKB	Turn	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+P22336	UniProtKB	Beta strand	198	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+P22336	UniProtKB	Beta strand	218	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+P22336	UniProtKB	Beta strand	231	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+P22336	UniProtKB	Helix	239	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+P22336	UniProtKB	Beta strand	251	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+P22336	UniProtKB	Beta strand	261	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+P22336	UniProtKB	Turn	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+P22336	UniProtKB	Beta strand	270	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+P22336	UniProtKB	Beta strand	276	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+P22336	UniProtKB	Beta strand	285	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX	
+##sequence-region P26754 1 273
+P26754	UniProtKB	Chain	1	273	.	.	.	ID=PRO_0000097275;Note=Replication factor A protein 2	
+P26754	UniProtKB	DNA binding	69	157	.	.	.	Note=OB	
+P26754	UniProtKB	Compositional bias	1	30	.	.	.	Note=Gly/Ser-rich	
+P26754	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P26754	UniProtKB	Modified residue	122	122	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:17287358,PMID:18407956	
+##sequence-region P26755 1 122
+P26755	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000097279;Note=Replication factor A protein 3	
+##sequence-region P40348 1 353
+P40348	UniProtKB	Chain	1	353	.	.	.	ID=PRO_0000121760;Note=Replication factor C subunit 2	
+P40348	UniProtKB	Nucleotide binding	65	73	.	.	.	Note=ATP	
+P40348	UniProtKB	Binding site	28	28	.	.	.	Note=ATP%3B via carbonyl oxygen	
+P40348	UniProtKB	Binding site	32	32	.	.	.	Note=ATP	
+P40348	UniProtKB	Binding site	171	171	.	.	.	Note=ATP	
+P40348	UniProtKB	Binding site	229	229	.	.	.	Note=ATP	
+P40348	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40348	UniProtKB	Sequence conflict	12	12	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40348	UniProtKB	Helix	27	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Turn	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	46	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Beta strand	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	71	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Beta strand	91	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Beta strand	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	109	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Beta strand	135	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	147	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Turn	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Beta strand	164	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	178	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Beta strand	184	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	194	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Turn	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	214	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	228	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	239	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	253	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	266	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	280	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	300	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Beta strand	312	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	316	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40348	UniProtKB	Helix	339	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+##sequence-region P40339 1 323
+P40339	UniProtKB	Chain	1	323	.	.	.	ID=PRO_0000121771;Note=Replication factor C subunit 4	
+P40339	UniProtKB	Nucleotide binding	49	57	.	.	.	Note=ATP	
+P40339	UniProtKB	Binding site	12	12	.	.	.	Note=ATP%3B via carbonyl oxygen	
+P40339	UniProtKB	Binding site	24	24	.	.	.	Note=ATP%3B via amide nitrogen	
+P40339	UniProtKB	Binding site	145	145	.	.	.	Note=ATP	
+P40339	UniProtKB	Binding site	203	203	.	.	.	Note=ATP	
+P40339	UniProtKB	Helix	11	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	28	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Beta strand	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	55	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	71	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Beta strand	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	86	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	92	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Beta strand	109	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	121	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	128	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Turn	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Beta strand	138	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	152	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Beta strand	158	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	168	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	188	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	202	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Beta strand	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	221	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	233	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	245	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Turn	255	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	263	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	282	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P40339	UniProtKB	Helix	306	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+##sequence-region P38251 1 354
+P38251	UniProtKB	Chain	1	354	.	.	.	ID=PRO_0000121765;Note=Replication factor C subunit 5	
+P38251	UniProtKB	Nucleotide binding	43	51	.	.	.	Note=ATP	
+P38251	UniProtKB	Binding site	5	5	.	.	.	Note=ATP%3B via carbonyl oxygen	
+P38251	UniProtKB	Binding site	17	17	.	.	.	Note=ATP	
+P38251	UniProtKB	Binding site	231	231	.	.	.	Note=ATP	
+P38251	UniProtKB	Turn	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	20	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Turn	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Beta strand	39	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	49	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	56	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Beta strand	91	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	106	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Turn	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Beta strand	136	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	148	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Turn	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Beta strand	165	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	179	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Beta strand	185	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	195	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	217	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	230	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	239	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Turn	243	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	258	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	276	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Turn	291	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	296	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Turn	306	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	315	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+P38251	UniProtKB	Helix	338	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ	
+##sequence-region P06781 1 192
+P06781	UniProtKB	Chain	1	189	.	.	.	ID=PRO_0000198946;Note=GTP-binding protein RHO2	
+P06781	UniProtKB	Propeptide	190	192	.	.	.	ID=PRO_0000281276;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06781	UniProtKB	Nucleotide binding	14	21	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06781	UniProtKB	Nucleotide binding	61	65	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06781	UniProtKB	Nucleotide binding	119	122	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06781	UniProtKB	Motif	36	44	.	.	.	Note=Effector region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06781	UniProtKB	Modified residue	189	189	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06781	UniProtKB	Lipidation	188	188	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+P06781	UniProtKB	Lipidation	189	189	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P06781	UniProtKB	Sequence conflict	48	48	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12362 1 591
+Q12362	UniProtKB	Chain	1	591	.	.	.	ID=PRO_0000162725;Note=Bifunctional protein RIB2	
+Q12362	UniProtKB	Domain	99	168	.	.	.	Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182	
+Q12362	UniProtKB	Domain	433	552	.	.	.	Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083	
+Q12362	UniProtKB	Region	1	432	.	.	.	Note=tRNA pseudouridine synthase	
+Q12362	UniProtKB	Region	433	591	.	.	.	Note=DRAP deaminase	
+Q12362	UniProtKB	Active site	211	211	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12362	UniProtKB	Active site	484	484	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12362	UniProtKB	Metal binding	482	482	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12362	UniProtKB	Metal binding	515	515	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12362	UniProtKB	Metal binding	525	525	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q3E757 1 174
+Q3E757	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260	
+Q3E757	UniProtKB	Chain	2	174	.	.	.	ID=PRO_0000125105;Note=60S ribosomal protein L11-B	
+Q3E757	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260	
+Q3E757	UniProtKB	Modified residue	75	75	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802	
+Q3E757	UniProtKB	Sequence conflict	138	138	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q3E757	UniProtKB	Beta strand	14	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Beta strand	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+Q3E757	UniProtKB	Helix	28	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Beta strand	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Beta strand	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Beta strand	66	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Helix	74	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Beta strand	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Beta strand	102	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Helix	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Turn	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Beta strand	125	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Turn	134	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Helix	137	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Beta strand	141	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Q	
+Q3E757	UniProtKB	Helix	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Helix	156	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Turn	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E757	UniProtKB	Beta strand	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P03871 1 373
+P03871	UniProtKB	Chain	1	373	.	.	.	ID=PRO_0000150892;Note=Partitioning protein REP1	
+P03871	UniProtKB	Region	1	129	.	.	.	Note=Interaction with REP2 and self-association	
+P03871	UniProtKB	Region	1	76	.	.	.	Note=Interaction with REP2	
+P03871	UniProtKB	Region	349	373	.	.	.	Note=Nuclear localization	
+P03871	UniProtKB	Natural variant	8	8	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. A->V	
+P03871	UniProtKB	Natural variant	22	22	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. V->I	
+P03871	UniProtKB	Natural variant	38	38	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. P->S	
+P03871	UniProtKB	Natural variant	87	87	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. I->R	
+P03871	UniProtKB	Natural variant	107	107	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. T->A	
+P03871	UniProtKB	Natural variant	111	123	.	.	.	Note=In strain: ATCC 44827. GLDINVKGTLNRR->VRYQCKRHVKPQ	
+P03871	UniProtKB	Natural variant	117	117	.	.	.	Note=In strain: ATCC 7754. K->R	
+P03871	UniProtKB	Natural variant	131	132	.	.	.	Note=In strain: ATCC 44827. KG->N	
+P03871	UniProtKB	Natural variant	149	149	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. A->D	
+P03871	UniProtKB	Natural variant	177	177	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. Q->K	
+P03871	UniProtKB	Natural variant	184	184	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. P->Q	
+P03871	UniProtKB	Natural variant	198	198	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. I->V	
+P03871	UniProtKB	Natural variant	204	204	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. K->R	
+P03871	UniProtKB	Natural variant	211	214	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. DKGH->GL	
+P03871	UniProtKB	Natural variant	220	222	.	.	.	Note=In strain: ATCC 44827. LPP->QPR	
+P03871	UniProtKB	Natural variant	225	228	.	.	.	Note=In strain: ATCC 44827. DPSR->NSSP	
+P03871	UniProtKB	Natural variant	231	231	.	.	.	Note=In strain: ATCC 44827. N->S	
+P03871	UniProtKB	Natural variant	239	241	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. SLT->NLI	
+P03871	UniProtKB	Natural variant	246	246	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. E->A	
+P03871	UniProtKB	Natural variant	253	253	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. G->S	
+P03871	UniProtKB	Natural variant	261	261	.	.	.	Note=In strain: ATCC 7754. K->R	
+P03871	UniProtKB	Natural variant	270	270	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. T->A	
+P03871	UniProtKB	Natural variant	372	373	.	.	.	Note=In strain: ATCC 44827 and ATCC 7754. DG->NE	
+P03871	UniProtKB	Mutagenesis	32	32	.	.	.	Note=Abolishes interaction with REP2 and STB. T->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	43	43	.	.	.	Note=Abolishes interaction with REP2%2C but not with STB. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	50	50	.	.	.	Note=Abolishes interaction with REP2%2C but not with STB. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Abolishes interaction with REP2%2C but not with STB. V->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	93	93	.	.	.	Note=Abolishes interaction with REP2%2C but not with STB. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	154	154	.	.	.	Note=Abolishes interaction with STB%2C but not with REP2. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	200	200	.	.	.	Note=Abolishes interaction with REP2%2C but not with STB. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	276	276	.	.	.	Note=Abolishes interaction with REP2%2C but not with STB. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	297	297	.	.	.	Note=Abolishes interaction with STB%2C but not with REP2. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	301	301	.	.	.	Note=Abolishes interaction with REP2%2C but not with STB. Y->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	308	308	.	.	.	Note=Abolishes interaction with REP2%2C but not with STB. I->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	317	317	.	.	.	Note=Abolishes interaction with STB%2C but not with REP2. Y->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+P03871	UniProtKB	Mutagenesis	330	330	.	.	.	Note=Abolishes interaction with STB%2C but not with REP2. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893	
+##sequence-region P12689 1 985
+P12689	UniProtKB	Chain	1	985	.	.	.	ID=PRO_0000173995;Note=DNA repair protein REV1	
+P12689	UniProtKB	Domain	161	249	.	.	.	Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P12689	UniProtKB	Domain	358	554	.	.	.	Note=UmuC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00216	
+P12689	UniProtKB	Nucleotide binding	362	366	.	.	.	Note=dCTP binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195463,ECO:0000269|PubMed:18275815;Dbxref=PMID:16195463,PMID:18275815	
+P12689	UniProtKB	Nucleotide binding	402	408	.	.	.	Note=dCTP binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195463,ECO:0000269|PubMed:18275815;Dbxref=PMID:16195463,PMID:18275815	
+P12689	UniProtKB	Region	319	329	.	.	.	Note=Interaction with target DNA	
+P12689	UniProtKB	Region	395	397	.	.	.	Note=Interaction with target DNA	
+P12689	UniProtKB	Region	554	557	.	.	.	Note=Interaction with target DNA	
+P12689	UniProtKB	Region	620	628	.	.	.	Note=Interaction with target DNA	
+P12689	UniProtKB	Metal binding	362	362	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00216,ECO:0000269|PubMed:18275815;Dbxref=PMID:18275815	
+P12689	UniProtKB	Metal binding	362	362	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00216,ECO:0000269|PubMed:18275815;Dbxref=PMID:18275815	
+P12689	UniProtKB	Metal binding	363	363	.	.	.	Note=Magnesium 2%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00216,ECO:0000269|PubMed:18275815;Dbxref=PMID:18275815	
+P12689	UniProtKB	Metal binding	467	467	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00216,ECO:0000269|PubMed:18275815;Dbxref=PMID:18275815	
+P12689	UniProtKB	Metal binding	468	468	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00216,ECO:0000269|PubMed:18275815;Dbxref=PMID:18275815	
+P12689	UniProtKB	Binding site	324	324	.	.	.	Note=dCTP;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195463,ECO:0000269|PubMed:18275815;Dbxref=PMID:16195463,PMID:18275815	
+P12689	UniProtKB	Binding site	414	414	.	.	.	Note=dCTP;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195463,ECO:0000269|PubMed:18275815;Dbxref=PMID:16195463,PMID:18275815	
+P12689	UniProtKB	Binding site	467	467	.	.	.	Note=dCTP;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195463,ECO:0000269|PubMed:18275815;Dbxref=PMID:16195463,PMID:18275815	
+P12689	UniProtKB	Site	681	681	.	.	.	Note=Interaction with target DNA	
+P12689	UniProtKB	Site	692	692	.	.	.	Note=Interaction with target DNA	
+P12689	UniProtKB	Site	694	694	.	.	.	Note=Interaction with target DNA	
+P12689	UniProtKB	Mutagenesis	193	193	.	.	.	Note=Loss of activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2492497;Dbxref=PMID:2492497	
+P12689	UniProtKB	Mutagenesis	467	468	.	.	.	Note=Loss of dCTP transferase activity. DE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11316789;Dbxref=PMID:11316789	
+P12689	UniProtKB	Sequence conflict	646	646	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12689	UniProtKB	Sequence conflict	816	816	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12689	UniProtKB	Turn	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3	
+P12689	UniProtKB	Beta strand	170	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3	
+P12689	UniProtKB	Helix	181	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3	
+P12689	UniProtKB	Beta strand	194	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3	
+P12689	UniProtKB	Turn	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3	
+P12689	UniProtKB	Beta strand	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3	
+P12689	UniProtKB	Helix	215	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3	
+P12689	UniProtKB	Turn	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3	
+P12689	UniProtKB	Beta strand	224	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M2I	
+P12689	UniProtKB	Helix	230	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3	
+P12689	UniProtKB	Helix	244	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3	
+P12689	UniProtKB	Helix	315	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	324	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Turn	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	355	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Turn	364	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	368	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	377	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Turn	384	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	389	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	395	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	401	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	405	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	418	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	432	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	438	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	459	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	468	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	485	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	506	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	514	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	534	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	539	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	547	549	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	555	564	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	571	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	580	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	591	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Turn	599	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	605	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	614	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	623	627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	636	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	659	671	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	687	701	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	704	718	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Helix	722	724	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+P12689	UniProtKB	Beta strand	725	737	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4	
+##sequence-region P38206 1 574
+P38206	UniProtKB	Chain	1	574	.	.	.	ID=PRO_0000212420;Note=Oligosaccharide translocation protein RFT1	
+P38206	UniProtKB	Topological domain	1	24	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	46	48	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	70	110	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	132	148	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	149	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	170	181	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	203	218	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	219	239	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	240	319	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	320	340	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	341	372	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	394	413	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	414	434	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	435	443	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	444	464	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	465	469	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	470	490	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	491	509	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	510	530	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	531	532	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Transmembrane	533	553	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Topological domain	554	574	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38206	UniProtKB	Sequence conflict	74	75	.	.	.	Note=IR->MF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38206	UniProtKB	Sequence conflict	207	216	.	.	.	Note=PMGVVTSDID->QWGLSHRTLT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q00453 1 211
+Q00453	UniProtKB	Chain	1	211	.	.	.	ID=PRO_0000046817;Note=Probable transcription repressor protein RGM1	
+Q00453	UniProtKB	Zinc finger	19	44	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q00453	UniProtKB	Zinc finger	50	73	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q00453	UniProtKB	Motif	6	11	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q00453	UniProtKB	Compositional bias	95	211	.	.	.	Note=Pro-rich	
+Q00453	UniProtKB	Sequence conflict	114	114	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P50861 1 169
+P50861	UniProtKB	Chain	1	169	.	.	.	ID=PRO_0000134857;Note=6%2C7-dimethyl-8-ribityllumazine synthase	
+P50861	UniProtKB	Region	61	63	.	.	.	Note=5-amino-6-(D-ribitylamino)uracil binding	
+P50861	UniProtKB	Region	90	92	.	.	.	Note=5-amino-6-(D-ribitylamino)uracil binding	
+P50861	UniProtKB	Region	95	96	.	.	.	Note=1-deoxy-L-glycero-tetrulose 4-phosphate binding	
+P50861	UniProtKB	Active site	98	98	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50861	UniProtKB	Binding site	27	27	.	.	.	Note=5-amino-6-(D-ribitylamino)uracil	
+P50861	UniProtKB	Binding site	123	123	.	.	.	Note=5-amino-6-(D-ribitylamino)uracil%3B via amide nitrogen and carbonyl oxygen	
+P50861	UniProtKB	Binding site	137	137	.	.	.	Note=1-deoxy-L-glycero-tetrulose 4-phosphate	
+P50861	UniProtKB	Sequence conflict	44	44	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50861	UniProtKB	Sequence conflict	51	51	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50861	UniProtKB	Beta strand	20	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+P50861	UniProtKB	Helix	29	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+P50861	UniProtKB	Helix	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+P50861	UniProtKB	Beta strand	53	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+P50861	UniProtKB	Helix	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+P50861	UniProtKB	Helix	64	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+P50861	UniProtKB	Beta strand	83	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+P50861	UniProtKB	Beta strand	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+P50861	UniProtKB	Helix	98	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+P50861	UniProtKB	Beta strand	124	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+P50861	UniProtKB	Helix	131	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+P50861	UniProtKB	Helix	149	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB	
+##sequence-region P38234 1 210
+P38234	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000200767;Note=Protein RFS1	
+P38234	UniProtKB	Domain	4	203	.	.	.	Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088	
+##sequence-region P48743 1 811
+P48743	UniProtKB	Chain	1	811	.	.	.	ID=PRO_0000215295;Note=RFX-like DNA-binding protein RFX1	
+P48743	UniProtKB	DNA binding	285	360	.	.	.	Note=RFX-type winged-helix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00858	
+P48743	UniProtKB	Modified residue	173	173	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q06407 1 1009
+Q06407	UniProtKB	Chain	1	1009	.	.	.	ID=PRO_0000075900;Note=Rho-type GTPase-activating protein 2	
+Q06407	UniProtKB	Domain	11	68	.	.	.	Note=LIM zinc-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125	
+Q06407	UniProtKB	Domain	69	129	.	.	.	Note=LIM zinc-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125	
+Q06407	UniProtKB	Domain	788	1006	.	.	.	Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172	
+Q06407	UniProtKB	Modified residue	763	763	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P38339 1 666
+P38339	UniProtKB	Chain	1	666	.	.	.	ID=PRO_0000056736;Note=RHO GTPase-activating protein RGD1	
+P38339	UniProtKB	Domain	33	295	.	.	.	Note=F-BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01077	
+P38339	UniProtKB	Domain	472	663	.	.	.	Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172	
+P38339	UniProtKB	Coiled coil	139	226	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38339	UniProtKB	Modified residue	386	386	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38339	UniProtKB	Helix	33	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC	
+P38339	UniProtKB	Helix	43	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC	
+P38339	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC	
+P38339	UniProtKB	Helix	97	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC	
+P38339	UniProtKB	Helix	195	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC	
+P38339	UniProtKB	Helix	233	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC	
+P38339	UniProtKB	Helix	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC	
+P38339	UniProtKB	Helix	283	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC	
+P38339	UniProtKB	Helix	292	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC	
+P38339	UniProtKB	Beta strand	470	472	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	474	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	487	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Turn	500	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Turn	504	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	513	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	527	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	541	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Beta strand	558	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	565	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	568	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	580	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	596	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	616	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	623	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+P38339	UniProtKB	Helix	646	662	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K	
+##sequence-region P40160 1 425
+P40160	UniProtKB	Chain	1	425	.	.	.	ID=PRO_0000213532;Note=Serine/threonine-protein kinase RIO2	
+P40160	UniProtKB	Domain	95	257	.	.	.	Note=Protein kinase	
+P40160	UniProtKB	Active site	229	229	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40160	UniProtKB	Binding site	123	123	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40160	UniProtKB	Modified residue	346	346	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40160	UniProtKB	Mutagenesis	73	73	.	.	.	Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with V-186%2C H-210%2C D-364%2C G-371 and G-417. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929	
+P40160	UniProtKB	Mutagenesis	105	105	.	.	.	Note=No change in activity. K->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12690111;Dbxref=PMID:12690111	
+P40160	UniProtKB	Mutagenesis	186	186	.	.	.	Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with H-73%2C H-210%2C D-364%2C G-371 and G-417. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929	
+P40160	UniProtKB	Mutagenesis	210	210	.	.	.	Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with H-73%2C V-186%2C D-364%2C G-371 and G-417. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929	
+P40160	UniProtKB	Mutagenesis	227	227	.	.	.	Note=No change in activity. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12690111;Dbxref=PMID:12690111	
+P40160	UniProtKB	Mutagenesis	229	229	.	.	.	Note=Decrease in activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12690111;Dbxref=PMID:12690111	
+P40160	UniProtKB	Mutagenesis	364	364	.	.	.	Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with H-73%2C V-186%2C H-210%2C G-371 and G-417. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929	
+P40160	UniProtKB	Mutagenesis	371	371	.	.	.	Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with H-73%2C V-186%2C H-210%2C D-364 and G-417. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929	
+P40160	UniProtKB	Mutagenesis	417	417	.	.	.	Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with H-73%2C V-186%2C H-210%2C D-364 and G-371. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929	
+##sequence-region P49723 1 345
+P49723	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000190465;Note=Ribonucleoside-diphosphate reductase small chain 2	
+P49723	UniProtKB	Active site	131	131	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10014	
+P49723	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378	
+P49723	UniProtKB	Modified residue	169	169	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P49723	UniProtKB	Modified residue	332	332	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P49723	UniProtKB	Modified residue	334	334	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P49723	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P49723	UniProtKB	Cross-link	337	337	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P49723	UniProtKB	Sequence conflict	127	127	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P49723	UniProtKB	Helix	4	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SMS	
+P49723	UniProtKB	Helix	13	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Turn	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Turn	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	43	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Turn	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Turn	69	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	78	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	101	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	111	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SMS	
+P49723	UniProtKB	Helix	148	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	155	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Beta strand	169	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	175	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Turn	188	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	191	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Beta strand	202	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	207	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	240	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Turn	265	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SMS	
+P49723	UniProtKB	Helix	277	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P49723	UniProtKB	Helix	316	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SMS	
+##sequence-region P38145 1 238
+P38145	UniProtKB	Chain	1	238	.	.	.	ID=PRO_0000068174;Note=Riboflavin synthase	
+P38145	UniProtKB	Repeat	1	103	.	.	.	Note=Lumazine-binding 1	
+P38145	UniProtKB	Repeat	104	205	.	.	.	Note=Lumazine-binding 2	
+P38145	UniProtKB	Region	4	6	.	.	.	Note=Lumazine 1 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92	
+P38145	UniProtKB	Region	54	56	.	.	.	Note=Lumazine 2 binding%3B shared with one trimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92	
+P38145	UniProtKB	Region	68	73	.	.	.	Note=Lumazine 2 binding%3B shared with one trimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFU8	
+P38145	UniProtKB	Region	107	109	.	.	.	Note=Lumazine 2 binding%3B shared with one trimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92	
+P38145	UniProtKB	Region	152	154	.	.	.	Note=Lumazine 1 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92	
+P38145	UniProtKB	Region	170	175	.	.	.	Note=Lumazine 1 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92	
+P38145	UniProtKB	Binding site	143	143	.	.	.	Note=Lumazine 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92	
+P38145	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P40188 1 164
+P40188	UniProtKB	Chain	1	164	.	.	.	ID=PRO_0000202987;Note=Respiratory growth induced protein 2	
+##sequence-region Q00245 1 231
+Q00245	UniProtKB	Chain	1	228	.	.	.	ID=PRO_0000198947;Note=GTP-binding protein RHO3	
+Q00245	UniProtKB	Propeptide	229	231	.	.	.	ID=PRO_0000281277;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00245	UniProtKB	Nucleotide binding	23	30	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00245	UniProtKB	Nucleotide binding	70	74	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00245	UniProtKB	Nucleotide binding	128	131	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00245	UniProtKB	Motif	45	53	.	.	.	Note=Effector region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00245	UniProtKB	Modified residue	228	228	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00245	UniProtKB	Lipidation	228	228	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00245	UniProtKB	Sequence conflict	129	129	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53879 1 331
+P53879	UniProtKB	Chain	1	328	.	.	.	ID=PRO_0000198949;Note=GTP-binding protein RHO5	
+P53879	UniProtKB	Propeptide	329	331	.	.	.	ID=PRO_0000281279;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53879	UniProtKB	Nucleotide binding	10	17	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53879	UniProtKB	Nucleotide binding	87	91	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53879	UniProtKB	Nucleotide binding	156	159	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53879	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53879	UniProtKB	Modified residue	228	228	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53879	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53879	UniProtKB	Modified residue	244	244	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53879	UniProtKB	Modified residue	328	328	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53879	UniProtKB	Lipidation	328	328	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53879	UniProtKB	Cross-link	276	276	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P53879	UniProtKB	Mutagenesis	91	91	.	.	.	Note=Cells sensitive to calcofluor%2C caffeine and Congo red. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12118069;Dbxref=PMID:12118069	
+##sequence-region P09938 1 399
+P09938	UniProtKB	Chain	1	399	.	.	.	ID=PRO_0000190464;Note=Ribonucleoside-diphosphate reductase small chain 1	
+P09938	UniProtKB	Active site	183	183	.	.	.	.	
+P09938	UniProtKB	Metal binding	145	145	.	.	.	Note=Iron 1	
+P09938	UniProtKB	Metal binding	176	176	.	.	.	Note=Iron 1	
+P09938	UniProtKB	Metal binding	176	176	.	.	.	Note=Iron 2	
+P09938	UniProtKB	Metal binding	179	179	.	.	.	Note=Iron 1	
+P09938	UniProtKB	Metal binding	239	239	.	.	.	Note=Iron 2	
+P09938	UniProtKB	Metal binding	273	273	.	.	.	Note=Iron 2	
+P09938	UniProtKB	Metal binding	276	276	.	.	.	Note=Iron 2	
+P09938	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P09938	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P09938	UniProtKB	Modified residue	41	41	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P09938	UniProtKB	Sequence conflict	101	103	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09938	UniProtKB	Sequence conflict	111	111	.	.	.	Note=E->ETAE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09938	UniProtKB	Helix	27	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	38	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	51	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	63	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	94	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	118	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	128	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	147	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	153	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	163	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	194	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	208	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Beta strand	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	228	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Turn	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	244	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	260	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	293	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	317	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	324	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Turn	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+P09938	UniProtKB	Helix	355	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0	
+##sequence-region P21672 1 869
+P21672	UniProtKB	Chain	1	869	.	.	.	ID=PRO_0000187204;Note=Ribonucleoside-diphosphate reductase large chain 2	
+P21672	UniProtKB	Domain	1	92	.	.	.	Note=ATP-cone;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00492	
+P21672	UniProtKB	Region	11	17	.	.	.	Note=Allosteric activator binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Region	217	218	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Region	285	288	.	.	.	Note=Allosteric effector binding%2C determines substrate specificity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Region	426	430	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Region	607	611	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Active site	426	426	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Active site	428	428	.	.	.	Note=Cysteine radical intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Active site	430	430	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Binding site	5	5	.	.	.	Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Binding site	53	53	.	.	.	Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Binding site	88	88	.	.	.	Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Binding site	202	202	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Binding site	247	247	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Site	218	218	.	.	.	Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Site	226	226	.	.	.	Note=Allosteric effector binding%2C determines substrate specificity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Site	256	256	.	.	.	Note=Allosteric effector binding%2C determines substrate specificity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Site	443	443	.	.	.	Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Site	741	741	.	.	.	Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Site	742	742	.	.	.	Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Site	864	864	.	.	.	Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Site	867	867	.	.	.	Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21524	
+P21672	UniProtKB	Modified residue	806	806	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P21672	UniProtKB	Modified residue	827	827	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21524	
+P21672	UniProtKB	Modified residue	868	868	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21524	
+P21672	UniProtKB	Disulfide bond	218	443	.	.	.	Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21672	UniProtKB	Cross-link	387	387	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21524	
+P21672	UniProtKB	Sequence conflict	21	22	.	.	.	Note=RI->VL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21672	UniProtKB	Sequence conflict	37	37	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21672	UniProtKB	Sequence conflict	58	58	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21672	UniProtKB	Sequence conflict	69	69	.	.	.	Note=T->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21672	UniProtKB	Sequence conflict	83	83	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21672	UniProtKB	Sequence conflict	212	212	.	.	.	Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21672	UniProtKB	Sequence conflict	249	249	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P21672	UniProtKB	Sequence conflict	311	311	.	.	.	Note=F->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P26784 1 199
+P26784	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921	
+P26784	UniProtKB	Chain	2	199	.	.	.	ID=PRO_0000133791;Note=60S ribosomal protein L16-A	
+P26784	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921	
+P26784	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26785	
+P26784	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26785	
+P26784	UniProtKB	Cross-link	177	177	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P26784	UniProtKB	Sequence conflict	14	14	.	.	.	Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P26784	UniProtKB	Sequence conflict	21	21	.	.	.	Note=S->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P26784	UniProtKB	Beta strand	5	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Helix	16	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Beta strand	32	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Helix	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Beta strand	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Helix	47	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Helix	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Helix	76	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Turn	86	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P26784	UniProtKB	Helix	93	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Beta strand	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Helix	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Beta strand	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U51	
+P26784	UniProtKB	Helix	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Helix	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Beta strand	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Helix	138	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Helix	150	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26784	UniProtKB	Turn	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P26784	UniProtKB	Helix	189	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P38066 1 345
+P38066	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000151786;Note=GTP cyclohydrolase-2	
+P38066	UniProtKB	Nucleotide binding	143	147	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38066	UniProtKB	Nucleotide binding	197	199	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38066	UniProtKB	Active site	231	231	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38066	UniProtKB	Active site	233	233	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38066	UniProtKB	Metal binding	148	148	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38066	UniProtKB	Metal binding	159	159	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38066	UniProtKB	Metal binding	161	161	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38066	UniProtKB	Binding site	164	164	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38066	UniProtKB	Binding site	219	219	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38066	UniProtKB	Binding site	254	254	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38066	UniProtKB	Binding site	259	259	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q99258 1 208
+Q99258	UniProtKB	Chain	1	208	.	.	.	ID=PRO_0000151829;Note=3%2C4-dihydroxy-2-butanone 4-phosphate synthase	
+Q99258	UniProtKB	Region	26	27	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99258	UniProtKB	Region	145	149	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99258	UniProtKB	Metal binding	27	27	.	.	.	Note=Magnesium or manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99258	UniProtKB	Metal binding	27	27	.	.	.	Note=Magnesium or manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99258	UniProtKB	Metal binding	148	148	.	.	.	Note=Magnesium or manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99258	UniProtKB	Binding site	31	31	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99258	UniProtKB	Binding site	169	169	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99258	UniProtKB	Site	131	131	.	.	.	Note=Essential for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99258	UniProtKB	Site	169	169	.	.	.	Note=Essential for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99258	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P29539 1 1916
+P29539	UniProtKB	Chain	1	1916	.	.	.	ID=PRO_0000097336;Note=Telomere length regulator protein RIF1	
+P29539	UniProtKB	Modified residue	97	97	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P29539	UniProtKB	Modified residue	1637	1637	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P29539	UniProtKB	Modified residue	1795	1795	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P29539	UniProtKB	Modified residue	1852	1852	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P29539	UniProtKB	Sequence conflict	580	580	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29539	UniProtKB	Sequence conflict	732	732	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29539	UniProtKB	Sequence conflict	732	732	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P29539	UniProtKB	Helix	1859	1861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJS	
+P29539	UniProtKB	Helix	1866	1876	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJS	
+P29539	UniProtKB	Helix	1880	1885	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJS	
+P29539	UniProtKB	Helix	1888	1907	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJS	
+##sequence-region P38127 1 377
+P38127	UniProtKB	Chain	1	377	.	.	.	ID=PRO_0000090690;Note=Mitochondrial carrier protein RIM2	
+P38127	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38127	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38127	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38127	UniProtKB	Transmembrane	238	258	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38127	UniProtKB	Transmembrane	286	306	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38127	UniProtKB	Transmembrane	347	368	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38127	UniProtKB	Repeat	50	163	.	.	.	Note=Solcar 1	
+P38127	UniProtKB	Repeat	173	262	.	.	.	Note=Solcar 2	
+P38127	UniProtKB	Repeat	286	375	.	.	.	Note=Solcar 3	
+##sequence-region P23796 1 513
+P23796	UniProtKB	Chain	1	513	.	.	.	ID=PRO_0000097353;Note=tRNA A64-2'-O-ribosylphosphate transferase	
+##sequence-region P38883 1 763
+P38883	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38883	UniProtKB	Chain	2	763	.	.	.	ID=PRO_0000202938;Note=Pre-rRNA-processing protein RIX1	
+P38883	UniProtKB	Compositional bias	690	763	.	.	.	Note=Glu-rich	
+P38883	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38883	UniProtKB	Sequence conflict	762	762	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CX53 1 165
+P0CX53	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17005568;Dbxref=PMID:17005568	
+P0CX53	UniProtKB	Chain	2	165	.	.	.	ID=PRO_0000104467;Note=60S ribosomal protein L12-A	
+P0CX53	UniProtKB	Modified residue	2	2	.	.	.	Note=N%2CN-dimethylproline%3B by NTM1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:20481588;Dbxref=PMID:18957409,PMID:20481588	
+P0CX53	UniProtKB	Modified residue	4	4	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B by RKM2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17005568,ECO:0000269|PubMed:18957409;Dbxref=PMID:17005568,PMID:18957409	
+P0CX53	UniProtKB	Modified residue	11	11	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B by RKM2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17005568;Dbxref=PMID:17005568	
+P0CX53	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX53	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P0CX53	UniProtKB	Modified residue	67	67	.	.	.	Note=N5-methylarginine%3B by RMT2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11856739,ECO:0000269|PubMed:18957409;Dbxref=PMID:11856739,PMID:18957409	
+P0CX53	UniProtKB	Cross-link	130	130	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX53	UniProtKB	Cross-link	146	146	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX53	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Abolishes monomethylation by RMT2. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11856739;Dbxref=PMID:11856739	
+##sequence-region Q12690 1 199
+Q12690	UniProtKB	Chain	1	199	.	.	.	ID=PRO_0000192938;Note=60S ribosomal protein L13-A	
+Q12690	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P40212	
+Q12690	UniProtKB	Modified residue	152	152	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P40212	
+Q12690	UniProtKB	Helix	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Beta strand	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Helix	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Y	
+Q12690	UniProtKB	Helix	28	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Turn	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Beta strand	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Helix	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Beta strand	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Helix	77	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Helix	87	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Helix	106	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Beta strand	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Turn	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Beta strand	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Helix	166	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q12690	UniProtKB	Helix	180	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P05748 1 204
+P05748	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:6814480;Dbxref=PMID:1544921,PMID:6814480	
+P05748	UniProtKB	Chain	2	204	.	.	.	ID=PRO_0000127566;Note=60S ribosomal protein L15-A	
+P05748	UniProtKB	Sequence conflict	28	28	.	.	.	Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05748	UniProtKB	Helix	3	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Helix	17	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Beta strand	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Helix	45	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Beta strand	59	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Helix	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Beta strand	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Helix	98	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Turn	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Beta strand	113	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Beta strand	125	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Beta strand	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56	
+P05748	UniProtKB	Helix	140	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Turn	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Helix	149	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Helix	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Turn	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Helix	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Helix	166	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Helix	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Beta strand	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Helix	187	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05748	UniProtKB	Beta strand	197	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P38927 1 245
+P38927	UniProtKB	Chain	1	245	.	.	.	ID=PRO_0000126116;Note=DNA polymerase zeta processivity subunit	
+P38927	UniProtKB	Domain	3	203	.	.	.	Note=HORMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00109	
+##sequence-region Q00246 1 291
+Q00246	UniProtKB	Chain	1	288	.	.	.	ID=PRO_0000198948;Note=GTP-binding protein RHO4	
+Q00246	UniProtKB	Propeptide	289	291	.	.	.	ID=PRO_0000281278;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00246	UniProtKB	Nucleotide binding	79	86	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00246	UniProtKB	Nucleotide binding	127	131	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00246	UniProtKB	Nucleotide binding	185	188	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00246	UniProtKB	Motif	101	109	.	.	.	Note=Effector region;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00246	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00246	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00246	UniProtKB	Modified residue	276	276	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q00246	UniProtKB	Modified residue	288	288	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00246	UniProtKB	Lipidation	288	288	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00246	UniProtKB	Sequence conflict	43	48	.	.	.	Note=PRLPTP->QIAYS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00246	UniProtKB	Sequence conflict	143	143	.	.	.	Note=T->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00246	UniProtKB	Sequence conflict	201	211	.	.	.	Note=PSSAESLAKRL->QVQQNPWPSVW;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00246	UniProtKB	Sequence conflict	213	218	.	.	.	Note=AFAHIQ->HLHIFK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33312 1 244
+P33312	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000135942;Note=2%2C5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase	
+P33312	UniProtKB	Nucleotide binding	182	186	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33312	UniProtKB	Binding site	79	79	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33312	UniProtKB	Binding site	83	83	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33312	UniProtKB	Binding site	159	159	.	.	.	Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33312	UniProtKB	Helix	10	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Helix	19	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Beta strand	31	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Beta strand	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Helix	58	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Beta strand	71	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Helix	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Beta strand	101	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Helix	117	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Beta strand	131	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Beta strand	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Turn	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Helix	161	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Beta strand	176	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Helix	183	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Turn	193	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Beta strand	197	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Beta strand	223	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+P33312	UniProtKB	Beta strand	232	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7	
+##sequence-region P38615 1 370
+P38615	UniProtKB	Chain	1	370	.	.	.	ID=PRO_0000086319;Note=Serine/threonine-protein kinase RIM11/MSD1	
+P38615	UniProtKB	Domain	39	322	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38615	UniProtKB	Nucleotide binding	45	53	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38615	UniProtKB	Active site	164	164	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P38615	UniProtKB	Binding site	68	68	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38615	UniProtKB	Modified residue	199	199	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10679022;Dbxref=PMID:17330950,PMID:19779198,PMID:10679022	
+P38615	UniProtKB	Sequence conflict	57	57	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38615	UniProtKB	Sequence conflict	331	331	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38615	UniProtKB	Sequence conflict	343	343	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32445 1 135
+P32445	UniProtKB	Transit peptide	1	17	.	.	.	Note=Mitochondrion	
+P32445	UniProtKB	Chain	18	135	.	.	.	ID=PRO_0000033262;Note=Single-stranded DNA-binding protein RIM1%2C mitochondrial	
+P32445	UniProtKB	Domain	19	117	.	.	.	Note=SSB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00252	
+##sequence-region Q12196 1 484
+Q12196	UniProtKB	Chain	1	484	.	.	.	ID=PRO_0000213531;Note=Serine/threonine-protein kinase RIO1	
+Q12196	UniProtKB	Domain	76	402	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12196	UniProtKB	Region	403	484	.	.	.	Note=Interaction with CKA2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716	
+Q12196	UniProtKB	Region	440	484	.	.	.	Note=Asociation with (pre-)40S ribosomal subunit;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24948609;Dbxref=PMID:24948609	
+Q12196	UniProtKB	Compositional bias	436	484	.	.	.	Note=Lys-rich	
+Q12196	UniProtKB	Active site	244	244	.	.	.	Note=Proton acceptor	
+Q12196	UniProtKB	Active site	261	261	.	.	.	Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BRS2	
+Q12196	UniProtKB	Metal binding	249	249	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BRS2	
+Q12196	UniProtKB	Metal binding	261	261	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BRS2	
+Q12196	UniProtKB	Binding site	125	125	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BRS2	
+Q12196	UniProtKB	Binding site	198	198	.	.	.	Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BRS2	
+Q12196	UniProtKB	Modified residue	402	402	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716	
+Q12196	UniProtKB	Modified residue	403	403	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716	
+Q12196	UniProtKB	Modified residue	409	409	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716	
+Q12196	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716	
+Q12196	UniProtKB	Modified residue	417	417	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716	
+Q12196	UniProtKB	Modified residue	419	419	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716	
+Q12196	UniProtKB	Mutagenesis	125	125	.	.	.	Note=No activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12135737;Dbxref=PMID:12135737	
+Q12196	UniProtKB	Mutagenesis	244	244	.	.	.	Note=Inhibits cell growth%3B enhances association with pre-40S ribosomal subunits%3B inhibits 20S pre-rRNA to mature 18S rRNA processing%3B translation initiation-like defect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24948609;Dbxref=PMID:24948609	
+Q12196	UniProtKB	Mutagenesis	244	244	.	.	.	Note=No activity. D->E%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12135737;Dbxref=PMID:12135737	
+Q12196	UniProtKB	Mutagenesis	261	261	.	.	.	Note=Inhibits cell growth. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24948609;Dbxref=PMID:24948609	
+Q12196	UniProtKB	Sequence conflict	203	203	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12504 1 494
+Q12504	UniProtKB	Chain	1	494	.	.	.	ID=PRO_0000097367;Note=Ribosomal lysine N-methyltransferase 4	
+Q12504	UniProtKB	Domain	25	265	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+Q12504	UniProtKB	Compositional bias	201	206	.	.	.	Note=Poly-Glu	
+Q12504	UniProtKB	Binding site	264	264	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+Q12504	UniProtKB	Sequence conflict	10	13	.	.	.	Note=NFVC->KLCF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12504	UniProtKB	Sequence conflict	168	174	.	.	.	Note=RVATSFE->TCVANCPSK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12367 1 367
+Q12367	UniProtKB	Chain	1	367	.	.	.	ID=PRO_0000262873;Note=Ribosomal lysine N-methyltransferase 5	
+Q12367	UniProtKB	Region	170	172	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+Q12367	UniProtKB	Binding site	110	110	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+Q12367	UniProtKB	Binding site	192	192	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+Q12367	UniProtKB	Binding site	256	256	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+Q12367	UniProtKB	Binding site	288	288	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867	
+##sequence-region P41805 1 221
+P41805	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P41805	UniProtKB	Chain	2	221	.	.	.	ID=PRO_0000147129;Note=60S ribosomal protein L10	
+P41805	UniProtKB	Repeat	167	181	.	.	.	Note=1	
+P41805	UniProtKB	Repeat	200	216	.	.	.	Note=2	
+P41805	UniProtKB	Region	167	216	.	.	.	Note=2 X 15-17 AA approximate repeats	
+P41805	UniProtKB	Modified residue	143	143	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P41805	UniProtKB	Modified residue	205	205	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P41805	UniProtKB	Cross-link	40	40	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P41805	UniProtKB	Cross-link	101	101	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P41805	UniProtKB	Mutagenesis	194	194	.	.	.	Note=In QSR1-1%3B synthetic lethal. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7730379;Dbxref=PMID:7730379	
+P41805	UniProtKB	Helix	6	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+##sequence-region P38741 1 713
+P38741	UniProtKB	Chain	1	713	.	.	.	ID=PRO_0000082031;Note=Meiotic activator RIM4	
+P38741	UniProtKB	Domain	93	172	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P38741	UniProtKB	Domain	346	420	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P38741	UniProtKB	Compositional bias	288	299	.	.	.	Note=Poly-Asn	
+P38741	UniProtKB	Compositional bias	581	594	.	.	.	Note=Poly-Asn	
+P38741	UniProtKB	Modified residue	525	525	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38741	UniProtKB	Mutagenesis	96	96	.	.	.	Note=Leads to absolute sporulation defect. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10806425;Dbxref=PMID:10806425	
+P38741	UniProtKB	Mutagenesis	139	139	.	.	.	Note=Leads to absolute sporulation defect. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10806425;Dbxref=PMID:10806425	
+P38741	UniProtKB	Mutagenesis	349	349	.	.	.	Note=Leads to mild sporulation defect. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10806425;Dbxref=PMID:10806425	
+P38741	UniProtKB	Mutagenesis	385	385	.	.	.	Note=Leads to absolute sporulation defect. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10806425;Dbxref=PMID:10806425	
+P38741	UniProtKB	Sequence conflict	385	385	.	.	.	Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0C0W9 1 174
+P0C0W9	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921	
+P0C0W9	UniProtKB	Chain	2	174	.	.	.	ID=PRO_0000125104;Note=60S ribosomal protein L11-A	
+P0C0W9	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921	
+P0C0W9	UniProtKB	Modified residue	75	75	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802	
+P0C0W9	UniProtKB	Sequence conflict	12	12	.	.	.	Note=L->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0C0W9	UniProtKB	Sequence conflict	25	25	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CX54 1 165
+P0CX54	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17005568;Dbxref=PMID:17005568	
+P0CX54	UniProtKB	Chain	2	165	.	.	.	ID=PRO_0000409773;Note=60S ribosomal protein L12-B	
+P0CX54	UniProtKB	Modified residue	2	2	.	.	.	Note=N%2CN-dimethylproline%3B by NTM1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:20481588;Dbxref=PMID:18957409,PMID:20481588	
+P0CX54	UniProtKB	Modified residue	4	4	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B by RKM2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17005568,ECO:0000269|PubMed:18957409;Dbxref=PMID:17005568,PMID:18957409	
+P0CX54	UniProtKB	Modified residue	11	11	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B by RKM2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17005568;Dbxref=PMID:17005568	
+P0CX54	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX54	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P0CX54	UniProtKB	Modified residue	67	67	.	.	.	Note=N5-methylarginine%3B by RMT2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11856739,ECO:0000269|PubMed:18957409;Dbxref=PMID:11856739,PMID:18957409	
+P0CX54	UniProtKB	Cross-link	130	130	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX54	UniProtKB	Cross-link	146	146	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX54	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Abolishes monomethylation by RMT2. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11856739;Dbxref=PMID:11856739	
+##sequence-region P54780 1 204
+P54780	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:6814480;Dbxref=PMID:1544921,PMID:6814480	
+P54780	UniProtKB	Chain	2	204	.	.	.	ID=PRO_0000127567;Note=60S ribosomal protein L15-B	
+P54780	UniProtKB	Sequence conflict	28	28	.	.	.	Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CX44 1 217
+P0CX44	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260	
+P0CX44	UniProtKB	Chain	2	217	.	.	.	ID=PRO_0000409768;Note=60S ribosomal protein L1-B	
+P0CX44	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260	
+P0CX44	UniProtKB	Modified residue	47	47	.	.	.	Note=N6-methyllysine%3B by RKM5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460220;Dbxref=PMID:21460220	
+P0CX44	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P0CX44	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P0CX23 1 172
+P0CX23	UniProtKB	Chain	1	172	.	.	.	ID=PRO_0000278969;Note=60S ribosomal protein L20-A	
+P0CX23	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX23	UniProtKB	Cross-link	125	125	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX23	UniProtKB	Cross-link	131	131	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX23	UniProtKB	Cross-link	149	149	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX23	UniProtKB	Beta strand	5	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Beta strand	25	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Helix	34	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Turn	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Helix	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Beta strand	56	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Beta strand	73	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Beta strand	86	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Helix	99	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Beta strand	121	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Beta strand	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P0CX23	UniProtKB	Helix	138	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Helix	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Beta strand	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N	
+P0CX23	UniProtKB	Beta strand	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX23	UniProtKB	Beta strand	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P05749 1 121
+P05749	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:6814480;Dbxref=PMID:10601260,PMID:6814480	
+P05749	UniProtKB	Chain	2	121	.	.	.	ID=PRO_0000215514;Note=60S ribosomal protein L22-A	
+P05749	UniProtKB	Sequence conflict	49	49	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05749	UniProtKB	Beta strand	13	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05749	UniProtKB	Helix	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05749	UniProtKB	Turn	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P05749	UniProtKB	Helix	30	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05749	UniProtKB	Beta strand	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05749	UniProtKB	Beta strand	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05749	UniProtKB	Turn	49	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05749	UniProtKB	Beta strand	54	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05749	UniProtKB	Beta strand	60	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05749	UniProtKB	Helix	73	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05749	UniProtKB	Turn	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05749	UniProtKB	Beta strand	94	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05749	UniProtKB	Beta strand	102	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P24000 1 155
+P24000	UniProtKB	Chain	1	155	.	.	.	ID=PRO_0000136895;Note=60S ribosomal protein L24-B	
+P24000	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P0C2H6 1 136
+P0C2H6	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P0C2H6	UniProtKB	Chain	2	136	.	.	.	ID=PRO_0000126092;Note=60S ribosomal protein L27-A	
+P0C2H6	UniProtKB	Turn	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56	
+P0C2H6	UniProtKB	Beta strand	9	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Beta strand	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Beta strand	22	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Beta strand	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Beta strand	40	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Beta strand	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N	
+P0C2H6	UniProtKB	Helix	61	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Beta strand	69	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Helix	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Beta strand	80	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Helix	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Turn	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Turn	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Helix	104	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Turn	123	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H6	UniProtKB	Helix	128	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX46 1 254
+P0CX46	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:18782943;Dbxref=PMID:1544921,PMID:18782943	
+P0CX46	UniProtKB	Chain	2	254	.	.	.	ID=PRO_0000409769;Note=60S ribosomal protein L2-B	
+P0CX46	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX46	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX46	UniProtKB	Modified residue	159	159	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX46	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX46	UniProtKB	Modified residue	249	249	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX46	UniProtKB	Cross-link	46	46	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX46	UniProtKB	Cross-link	93	93	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX46	UniProtKB	Cross-link	119	119	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX46	UniProtKB	Cross-link	145	145	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P0C2H8 1 113
+P0C2H8	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943	
+P0C2H8	UniProtKB	Chain	2	113	.	.	.	ID=PRO_0000153788;Note=60S ribosomal protein L31-A	
+P0C2H8	UniProtKB	Beta strand	9	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H8	UniProtKB	Helix	16	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H8	UniProtKB	Turn	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H8	UniProtKB	Helix	28	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H8	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H8	UniProtKB	Helix	53	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H8	UniProtKB	Helix	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F	
+P0C2H8	UniProtKB	Beta strand	69	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H8	UniProtKB	Beta strand	86	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H8	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C2H8	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Q	
+##sequence-region P51402 1 88
+P51402	UniProtKB	Chain	1	88	.	.	.	ID=PRO_0000139723;Note=60S ribosomal protein L37-B	
+P51402	UniProtKB	Zinc finger	19	37	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P51402	UniProtKB	Metal binding	19	19	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102	
+P51402	UniProtKB	Metal binding	22	22	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102	
+P51402	UniProtKB	Metal binding	34	34	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102	
+P51402	UniProtKB	Metal binding	37	37	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102	
+##sequence-region P0CX45 1 254
+P0CX45	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:18782943;Dbxref=PMID:1544921,PMID:18782943	
+P0CX45	UniProtKB	Chain	2	254	.	.	.	ID=PRO_0000129761;Note=60S ribosomal protein L2-A	
+P0CX45	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX45	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX45	UniProtKB	Modified residue	159	159	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX45	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX45	UniProtKB	Modified residue	249	249	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX45	UniProtKB	Cross-link	46	46	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX45	UniProtKB	Cross-link	93	93	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX45	UniProtKB	Cross-link	119	119	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX45	UniProtKB	Cross-link	145	145	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX45	UniProtKB	Helix	6	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Helix	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Helix	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Helix	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P0CX45	UniProtKB	Helix	34	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	41	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	58	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	68	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	87	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Helix	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	112	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	118	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56	
+P0CX45	UniProtKB	Beta strand	134	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Turn	141	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	145	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Q	
+P0CX45	UniProtKB	Beta strand	155	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	163	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P0CX45	UniProtKB	Helix	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Helix	182	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	191	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P0CX45	UniProtKB	Helix	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Helix	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Turn	210	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P0CX45	UniProtKB	Turn	214	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Turn	231	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX45	UniProtKB	Beta strand	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P14120 1 105
+P14120	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:3316213;Dbxref=PMID:10601260,PMID:3316213	
+P14120	UniProtKB	Chain	2	105	.	.	.	ID=PRO_0000146143;Note=60S ribosomal protein L30	
+P14120	UniProtKB	Cross-link	22	22	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14120	UniProtKB	Cross-link	53	53	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14120	UniProtKB	Cross-link	83	83	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P14120	UniProtKB	Helix	7	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU	
+P14120	UniProtKB	Beta strand	21	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU	
+P14120	UniProtKB	Helix	26	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU	
+P14120	UniProtKB	Beta strand	40	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU	
+P14120	UniProtKB	Helix	53	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU	
+P14120	UniProtKB	Beta strand	67	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU	
+P14120	UniProtKB	Helix	79	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU	
+P14120	UniProtKB	Beta strand	88	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU	
+P14120	UniProtKB	Helix	100	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU	
+##sequence-region P05744 1 107
+P05744	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943	
+P05744	UniProtKB	Chain	2	107	.	.	.	ID=PRO_0000192807;Note=60S ribosomal protein L33-A	
+P05744	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P05744	UniProtKB	Cross-link	47	47	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05744	UniProtKB	Sequence conflict	24	24	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05744	UniProtKB	Beta strand	8	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05744	UniProtKB	Beta strand	23	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05744	UniProtKB	Helix	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05744	UniProtKB	Turn	42	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05744	UniProtKB	Beta strand	48	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05744	UniProtKB	Beta strand	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05744	UniProtKB	Beta strand	63	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05744	UniProtKB	Beta strand	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05744	UniProtKB	Beta strand	81	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05744	UniProtKB	Turn	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05744	UniProtKB	Beta strand	97	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P87262 1 121
+P87262	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000131845;Note=60S ribosomal protein L34-A	
+P87262	UniProtKB	Beta strand	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P87262	UniProtKB	Helix	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P87262	UniProtKB	Beta strand	19	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P87262	UniProtKB	Turn	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U53	
+P87262	UniProtKB	Beta strand	30	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P87262	UniProtKB	Turn	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P87262	UniProtKB	Beta strand	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U50	
+P87262	UniProtKB	Helix	59	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P87262	UniProtKB	Helix	67	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P87262	UniProtKB	Turn	75	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P87262	UniProtKB	Helix	83	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX84 1 120
+P0CX84	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894	
+P0CX84	UniProtKB	Chain	2	120	.	.	.	ID=PRO_0000130552;Note=60S ribosomal protein L35-A	
+P0CX84	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX84	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX84	UniProtKB	Helix	6	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX84	UniProtKB	Helix	14	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX84	UniProtKB	Helix	43	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX84	UniProtKB	Turn	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX84	UniProtKB	Helix	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX84	UniProtKB	Helix	86	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX84	UniProtKB	Helix	94	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX84	UniProtKB	Helix	102	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX84	UniProtKB	Beta strand	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P05745 1 100
+P05745	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P05745	UniProtKB	Chain	2	100	.	.	.	ID=PRO_0000195020;Note=60S ribosomal protein L36-A	
+P05745	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylthreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P05745	UniProtKB	Beta strand	6	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05745	UniProtKB	Helix	26	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05745	UniProtKB	Helix	35	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05745	UniProtKB	Helix	52	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05745	UniProtKB	Helix	66	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05745	UniProtKB	Beta strand	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Z	
+P05745	UniProtKB	Helix	80	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05745	UniProtKB	Turn	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P49626 1 362
+P49626	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921	
+P49626	UniProtKB	Chain	2	362	.	.	.	ID=PRO_0000129368;Note=60S ribosomal protein L4-B	
+P49626	UniProtKB	Region	277	362	.	.	.	Note=C-terminal-extended nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P49626	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921	
+P49626	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Leads to a slower growth at higher temperatures but allows RPL4 assembly into the 60S subunit%3B when associated with E-98. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P49626	UniProtKB	Mutagenesis	98	98	.	.	.	Note=Leads to a slower growth at higher temperatures but allows RPL4 assembly into the mature 60S%3B when associated with E-95. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P49626	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-290 and A-295. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P49626	UniProtKB	Mutagenesis	290	290	.	.	.	Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-289 and A-295. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P49626	UniProtKB	Mutagenesis	295	295	.	.	.	Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-289 and A-290. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P49626	UniProtKB	Mutagenesis	314	314	.	.	.	Note=Significantly diminished nuclear localization%3B when associated with A-315 and A-319. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P49626	UniProtKB	Mutagenesis	315	315	.	.	.	Note=Significantly diminished nuclear localization%3B when associated with A-314 and A-319. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P49626	UniProtKB	Mutagenesis	319	319	.	.	.	Note=Significantly diminished nuclear localization%3B when associated with A-314 and A-315. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P49626	UniProtKB	Mutagenesis	332	332	.	.	.	Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-334. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P49626	UniProtKB	Mutagenesis	334	334	.	.	.	Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with e-332. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803	
+P49626	UniProtKB	Sequence conflict	88	88	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02753 1 160
+Q02753	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+Q02753	UniProtKB	Chain	2	160	.	.	.	ID=PRO_0000149682;Note=60S ribosomal protein L21-A	
+Q02753	UniProtKB	Cross-link	32	32	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12672	
+Q02753	UniProtKB	Turn	7	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q02753	UniProtKB	Turn	12	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q02753	UniProtKB	Helix	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q02753	UniProtKB	Beta strand	39	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q02753	UniProtKB	Helix	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q02753	UniProtKB	Beta strand	61	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q02753	UniProtKB	Beta strand	69	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q02753	UniProtKB	Beta strand	83	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q02753	UniProtKB	Helix	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q02753	UniProtKB	Beta strand	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q02753	UniProtKB	Helix	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+Q02753	UniProtKB	Helix	103	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q02753	UniProtKB	Turn	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX82 1 189
+P0CX82	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:6355773;Dbxref=PMID:1544921,PMID:6355773	
+P0CX82	UniProtKB	Chain	2	189	.	.	.	ID=PRO_0000131184;Note=60S ribosomal protein L19-A	
+P0CX82	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX82	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX82	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX82	UniProtKB	Cross-link	21	21	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX82	UniProtKB	Cross-link	53	53	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX82	UniProtKB	Cross-link	60	60	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX82	UniProtKB	Cross-link	146	146	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX82	UniProtKB	Cross-link	186	186	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX82	UniProtKB	Sequence conflict	54	54	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CX82	UniProtKB	Helix	5	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Helix	19	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Beta strand	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P0CX82	UniProtKB	Helix	29	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Helix	38	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Helix	61	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Turn	72	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Helix	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Helix	85	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Helix	91	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Turn	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Helix	117	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Beta strand	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Beta strand	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56	
+P0CX82	UniProtKB	Helix	135	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Turn	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX82	UniProtKB	Helix	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P56628 1 122
+P56628	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000215515;Note=60S ribosomal protein L22-B	
+##sequence-region P0CX83 1 189
+P0CX83	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:6355773;Dbxref=PMID:1544921,PMID:6355773	
+P0CX83	UniProtKB	Chain	2	189	.	.	.	ID=PRO_0000410446;Note=60S ribosomal protein L19-B	
+P0CX83	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX83	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX83	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX83	UniProtKB	Cross-link	21	21	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX83	UniProtKB	Cross-link	53	53	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX83	UniProtKB	Cross-link	60	60	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX83	UniProtKB	Cross-link	146	146	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX83	UniProtKB	Cross-link	186	186	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P36144 1 274
+P36144	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000203217;Note=Ribosome biogenesis protein UTP30	
+##sequence-region P05743 1 127
+P05743	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943	
+P05743	UniProtKB	Chain	2	127	.	.	.	ID=PRO_0000130801;Note=60S ribosomal protein L26-A	
+P05743	UniProtKB	Beta strand	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P05743	UniProtKB	Helix	12	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Helix	24	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Beta strand	32	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Helix	37	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Beta strand	55	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Turn	62	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Beta strand	67	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Helix	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Beta strand	79	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Beta strand	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Beta strand	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Helix	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Beta strand	104	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05743	UniProtKB	Helix	113	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region Q03942 1 479
+Q03942	UniProtKB	Chain	1	479	.	.	.	ID=PRO_0000253809;Note=Ribosomal lysine N-methyltransferase 2	
+Q03942	UniProtKB	Domain	22	325	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+Q03942	UniProtKB	Binding site	324	324	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+##sequence-region P40212 1 199
+P40212	UniProtKB	Chain	1	199	.	.	.	ID=PRO_0000192939;Note=60S ribosomal protein L13-B	
+P40212	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40212	UniProtKB	Modified residue	152	152	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38754 1 138
+P38754	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36105	
+P38754	UniProtKB	Chain	2	138	.	.	.	ID=PRO_0000132044;Note=60S ribosomal protein L14-B	
+P38754	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36105	
+##sequence-region P05740 1 184
+P05740	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943	
+P05740	UniProtKB	Chain	2	184	.	.	.	ID=PRO_0000125347;Note=60S ribosomal protein L17-A	
+P05740	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P05740	UniProtKB	Cross-link	46	46	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05740	UniProtKB	Sequence conflict	104	114	.	.	.	Note=AKGLDATKLYV->VCQEYYMFSTR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05740	UniProtKB	Helix	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Beta strand	14	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Helix	26	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Turn	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Helix	41	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Beta strand	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56	
+P05740	UniProtKB	Beta strand	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Helix	71	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Beta strand	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P05740	UniProtKB	Helix	85	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Beta strand	111	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Beta strand	125	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Beta strand	135	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Beta strand	144	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05740	UniProtKB	Helix	170	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX50 1 186
+P0CX50	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894	
+P0CX50	UniProtKB	Chain	2	186	.	.	.	ID=PRO_0000409771;Note=60S ribosomal protein L18-B	
+P0CX50	UniProtKB	Modified residue	50	50	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802	
+P0CX50	UniProtKB	Cross-link	116	116	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P0CX43 1 217
+P0CX43	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260	
+P0CX43	UniProtKB	Chain	2	217	.	.	.	ID=PRO_0000125842;Note=60S ribosomal protein L1-A	
+P0CX43	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260	
+P0CX43	UniProtKB	Modified residue	47	47	.	.	.	Note=N6-methyllysine%3B by RKM5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460220;Dbxref=PMID:21460220	
+P0CX43	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P0CX43	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P04449 1 155
+P04449	UniProtKB	Chain	1	155	.	.	.	ID=PRO_0000136894;Note=60S ribosomal protein L24-A	
+P04449	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24000	
+P04449	UniProtKB	Turn	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Beta strand	18	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Beta strand	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P04449	UniProtKB	Beta strand	28	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Helix	34	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Helix	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Helix	53	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Turn	59	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Helix	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Beta strand	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Turn	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Beta strand	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Helix	98	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Helix	113	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P04449	UniProtKB	Turn	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P53221 1 127
+P53221	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943	
+P53221	UniProtKB	Chain	2	127	.	.	.	ID=PRO_0000130802;Note=60S ribosomal protein L26-B	
+##sequence-region P0C2H7 1 136
+P0C2H7	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000278967;Note=60S ribosomal protein L27-B	
+##sequence-region P41056 1 107
+P41056	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943	
+P41056	UniProtKB	Chain	2	107	.	.	.	ID=PRO_0000192808;Note=60S ribosomal protein L33-B	
+P41056	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine%3B partial;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05744	
+P41056	UniProtKB	Cross-link	47	47	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05744	
+P41056	UniProtKB	Sequence conflict	24	24	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12338 1 110
+Q12338	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000248387;Note=Ribonuclease H2 subunit C	
+Q12338	UniProtKB	Sequence conflict	64	64	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32385 1 249
+P32385	UniProtKB	Chain	1	249	.	.	.	ID=PRO_0000081810;Note=Ribonucleoprotein 1	
+P32385	UniProtKB	Domain	35	114	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P32385	UniProtKB	Domain	140	231	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+##sequence-region P25367 1 405
+P25367	UniProtKB	Chain	1	405	.	.	.	ID=PRO_0000097390;Note=[PIN+] prion protein RNQ1	
+P25367	UniProtKB	Region	153	402	.	.	.	Note=Prion domain (PrD)	
+P25367	UniProtKB	Modified residue	143	143	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25367	UniProtKB	Cross-link	5	5	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25367	UniProtKB	Cross-link	84	84	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25367	UniProtKB	Natural variant	166	169	.	.	.	Note=In strain: SCI7.2/b%2C SCI11.5/a and SCI11.5/c. Missing	
+P25367	UniProtKB	Natural variant	171	172	.	.	.	Note=In strain: SCI7.2/a%2C SCI7.2/d%2C SCI11.5/b and SCI11.5/d. Missing	
+P25367	UniProtKB	Natural variant	289	299	.	.	.	Note=In strain: SCI7.2/b%2C SCI7.2/d and SCI11.5/c. Missing	
+P25367	UniProtKB	Natural variant	293	303	.	.	.	Note=In strain: SCI9. Missing	
+P25367	UniProtKB	Natural variant	360	360	.	.	.	Note=In strain: SCI3%2C SCI4%2C SCI7.2/a%2C SCI7.2/b%2C SCI7.2/d%2C SCI11.5/a%2C SCI11.5/b%2C SCI11.5/c and SCI11.5/d. Q->H	
+P25367	UniProtKB	Natural variant	372	372	.	.	.	Note=In strain: SCI7.2/b%2C SCI7.2/d and SCI11.5/c. P->PQHNGQQQSNEYGRP	
+P25367	UniProtKB	Natural variant	383	383	.	.	.	Note=In strain: SCI7.2/b%2CSCI7.2/d and SCI11.5/c. Q->H	
+P25367	UniProtKB	Natural variant	387	387	.	.	.	Note=In strain: SCI4. F->L	
+P25367	UniProtKB	Sequence conflict	181	181	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02555 1 471
+Q02555	UniProtKB	Chain	1	471	.	.	.	ID=PRO_0000180466;Note=Ribonuclease 3	
+Q02555	UniProtKB	Domain	227	331	.	.	.	Note=RNase III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00177	
+Q02555	UniProtKB	Domain	369	437	.	.	.	Note=DRBM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00266	
+Q02555	UniProtKB	Helix	46	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	73	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	88	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	97	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	116	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	140	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	208	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	229	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	238	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	265	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	278	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	290	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Beta strand	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T16	
+Q02555	UniProtKB	Turn	306	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	313	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	331	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	358	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Helix	370	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O	
+Q02555	UniProtKB	Helix	381	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O	
+Q02555	UniProtKB	Beta strand	386	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O	
+Q02555	UniProtKB	Beta strand	394	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4N	
+Q02555	UniProtKB	Beta strand	400	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O	
+Q02555	UniProtKB	Turn	407	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4L	
+Q02555	UniProtKB	Beta strand	411	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O	
+Q02555	UniProtKB	Helix	420	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O	
+Q02555	UniProtKB	Helix	435	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O	
+Q02555	UniProtKB	Helix	450	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG	
+Q02555	UniProtKB	Beta strand	455	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T16	
+##sequence-region P39956 1 796
+P39956	UniProtKB	Chain	1	796	.	.	.	ID=PRO_0000046849;Note=DNA damage-responsive transcriptional repressor RPH1	
+P39956	UniProtKB	Domain	14	55	.	.	.	Note=JmjN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00537	
+P39956	UniProtKB	Domain	193	355	.	.	.	Note=JmjC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538	
+P39956	UniProtKB	Zinc finger	709	732	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39956	UniProtKB	Zinc finger	738	763	.	.	.	Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39956	UniProtKB	Motif	455	471	.	.	.	Note=Bipartite nuclear localization signal	
+P39956	UniProtKB	Modified residue	399	399	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39956	UniProtKB	Modified residue	430	430	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39956	UniProtKB	Modified residue	459	459	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39956	UniProtKB	Modified residue	557	557	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39956	UniProtKB	Modified residue	561	561	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39956	UniProtKB	Modified residue	575	575	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P39956	UniProtKB	Modified residue	584	584	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39956	UniProtKB	Modified residue	652	652	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39956	UniProtKB	Modified residue	689	689	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P39956	UniProtKB	Beta strand	9	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	27	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	41	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	62	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	74	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	98	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Turn	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPW	
+P39956	UniProtKB	Helix	142	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Turn	149	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	157	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPW	
+P39956	UniProtKB	Helix	162	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Turn	175	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	182	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPW	
+P39956	UniProtKB	Beta strand	222	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	231	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	242	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	253	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	263	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	275	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Turn	285	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Helix	294	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Turn	299	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	305	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	314	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+P39956	UniProtKB	Beta strand	323	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT	
+##sequence-region P23250 1 407
+P23250	UniProtKB	Chain	1	407	.	.	.	ID=PRO_0000197113;Note=Negative RAS protein regulator protein	
+P23250	UniProtKB	Domain	90	158	.	.	.	Note=Myb-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133	
+P23250	UniProtKB	Sequence conflict	37	37	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	37	37	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	71	73	.	.	.	Note=SNS->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	71	73	.	.	.	Note=SNS->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	91	91	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	91	91	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	170	174	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	170	174	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	190	190	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	240	240	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	240	240	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	242	242	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	242	242	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	252	252	.	.	.	Note=N->NNNNSNN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P23250	UniProtKB	Sequence conflict	252	252	.	.	.	Note=N->NNNNSNN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38886 1 268
+P38886	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+P38886	UniProtKB	Chain	2	268	.	.	.	ID=PRO_0000173834;Note=26S proteasome regulatory subunit RPN10	
+P38886	UniProtKB	Domain	5	190	.	.	.	Note=VWFA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00219	
+P38886	UniProtKB	Domain	223	242	.	.	.	Note=UIM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+P38886	UniProtKB	Compositional bias	248	255	.	.	.	Note=Poly-Gln	
+P38886	UniProtKB	Beta strand	4	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Helix	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Beta strand	19	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Helix	25	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Beta strand	48	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Beta strand	55	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Beta strand	60	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Helix	69	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Helix	87	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Beta strand	106	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Helix	122	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Beta strand	137	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Helix	154	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Beta strand	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Beta strand	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Beta strand	176	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+P38886	UniProtKB	Helix	181	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1	
+##sequence-region P53196 1 417
+P53196	UniProtKB	Chain	1	417	.	.	.	ID=PRO_0000051475;Note=26S proteasome regulatory subunit RPN14	
+P53196	UniProtKB	Repeat	134	173	.	.	.	Note=WD 1	
+P53196	UniProtKB	Repeat	176	215	.	.	.	Note=WD 2	
+P53196	UniProtKB	Repeat	242	281	.	.	.	Note=WD 3	
+P53196	UniProtKB	Repeat	285	325	.	.	.	Note=WD 4	
+P53196	UniProtKB	Repeat	330	371	.	.	.	Note=WD 5	
+P53196	UniProtKB	Repeat	380	416	.	.	.	Note=WD 6	
+P53196	UniProtKB	Beta strand	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Helix	14	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	27	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	38	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Turn	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	60	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	76	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Turn	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	96	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	108	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	127	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	139	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	148	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	158	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Turn	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	172	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	181	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Turn	188	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	192	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	202	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Turn	207	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	211	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	226	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Helix	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	257	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	268	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Turn	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	278	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	290	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	302	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	310	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	324	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	335	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	344	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Turn	350	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	353	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	366	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ACP	
+P53196	UniProtKB	Beta strand	376	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	387	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	394	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	399	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Turn	405	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+P53196	UniProtKB	Beta strand	408	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1	
+##sequence-region P40011 1 234
+P40011	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40011	UniProtKB	Chain	2	234	.	.	.	ID=PRO_0000202621;Note=4-hydroxy-4-methyl-2-oxoglutarate aldolase	
+P40011	UniProtKB	Region	100	103	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40011	UniProtKB	Metal binding	123	123	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40011	UniProtKB	Binding site	122	122	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40011	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40011	UniProtKB	Helix	3	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Helix	12	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Turn	26	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	45	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	74	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Helix	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Helix	101	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	114	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Helix	124	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	134	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Turn	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	148	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	157	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	166	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	174	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Beta strand	181	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Turn	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Helix	192	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Helix	219	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+P40011	UniProtKB	Helix	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q	
+##sequence-region P35178 1 278
+P35178	UniProtKB	Chain	1	278	.	.	.	ID=PRO_0000097452;Note=Ribosomal RNA-processing protein 1	
+P35178	UniProtKB	Compositional bias	266	274	.	.	.	Note=Poly-Glu	
+P35178	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P35178	UniProtKB	Modified residue	267	267	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q08285 1 240
+Q08285	UniProtKB	Chain	1	240	.	.	.	ID=PRO_0000097453;Note=Exosome complex component RRP40	
+Q08285	UniProtKB	Domain	67	137	.	.	.	Note=S1 motif	
+Q08285	UniProtKB	Sequence conflict	160	160	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08285	UniProtKB	Beta strand	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	19	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Turn	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	40	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	53	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	71	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	81	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	95	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	118	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	133	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Turn	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	154	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Helix	160	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Helix	174	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	185	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Turn	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Beta strand	193	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Helix	201	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08285	UniProtKB	Helix	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+Q08285	UniProtKB	Helix	223	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+##sequence-region Q05636 1 305
+Q05636	UniProtKB	Chain	1	305	.	.	.	ID=PRO_0000139974;Note=Exosome complex component RRP45	
+Q05636	UniProtKB	Helix	9	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	36	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	46	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	54	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	76	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Helix	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q05636	UniProtKB	Helix	99	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Turn	113	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	123	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Turn	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	130	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Helix	147	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	167	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	173	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Turn	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	194	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Helix	206	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	218	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Helix	225	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	232	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	243	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Helix	258	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q05636	UniProtKB	Beta strand	299	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8	
+##sequence-region Q05022 1 1729
+Q05022	UniProtKB	Chain	1	1729	.	.	.	ID=PRO_0000205763;Note=rRNA biogenesis protein RRP5	
+Q05022	UniProtKB	Domain	119	200	.	.	.	Note=S1 motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q05022	UniProtKB	Domain	338	410	.	.	.	Note=S1 motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q05022	UniProtKB	Domain	510	580	.	.	.	Note=S1 motif 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q05022	UniProtKB	Domain	607	676	.	.	.	Note=S1 motif 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q05022	UniProtKB	Domain	690	769	.	.	.	Note=S1 motif 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q05022	UniProtKB	Domain	794	863	.	.	.	Note=S1 motif 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q05022	UniProtKB	Domain	895	971	.	.	.	Note=S1 motif 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q05022	UniProtKB	Domain	1003	1083	.	.	.	Note=S1 motif 8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q05022	UniProtKB	Domain	1088	1159	.	.	.	Note=S1 motif 9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q05022	UniProtKB	Domain	1177	1245	.	.	.	Note=S1 motif 10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q05022	UniProtKB	Domain	1265	1336	.	.	.	Note=S1 motif 11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q05022	UniProtKB	Repeat	1455	1487	.	.	.	Note=HAT 1	
+Q05022	UniProtKB	Repeat	1561	1594	.	.	.	Note=HAT 2	
+Q05022	UniProtKB	Repeat	1632	1664	.	.	.	Note=HAT 3	
+Q05022	UniProtKB	Repeat	1666	1701	.	.	.	Note=HAT 4	
+Q05022	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950	
+Q05022	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q05022	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q05022	UniProtKB	Modified residue	1724	1724	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q05022	UniProtKB	Helix	1409	1416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1461	1470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1475	1487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1491	1504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1510	1527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1530	1543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1546	1560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1563	1577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Turn	1578	1580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1583	1594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1598	1611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1614	1616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1617	1630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1634	1647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1652	1665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1668	1679	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1685	1702	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+Q05022	UniProtKB	Helix	1705	1719	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S	
+##sequence-region P25368 1 297
+P25368	UniProtKB	Chain	1	297	.	.	.	ID=PRO_0000097457;Note=Ribosomal RNA-processing protein 7	
+P25368	UniProtKB	Sequence conflict	66	66	.	.	.	Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25368	UniProtKB	Beta strand	14	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Beta strand	34	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Helix	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Beta strand	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Helix	64	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Beta strand	84	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Helix	100	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Beta strand	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Helix	131	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Helix	147	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Helix	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Helix	165	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Helix	177	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D	
+P25368	UniProtKB	Helix	256	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MBY	
+P25368	UniProtKB	Helix	269	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MBY	
+##sequence-region P25381 1 491
+P25381	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25381	UniProtKB	Chain	18	491	.	.	.	ID=PRO_0000027205;Note=Subtilase-type proteinase RRT12	
+P25381	UniProtKB	Domain	156	389	.	.	.	Note=Peptidase S8	
+P25381	UniProtKB	Active site	174	174	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25381	UniProtKB	Active site	205	205	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25381	UniProtKB	Active site	365	365	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25381	UniProtKB	Glycosylation	38	38	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25381	UniProtKB	Glycosylation	64	64	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25381	UniProtKB	Glycosylation	106	106	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25381	UniProtKB	Glycosylation	121	121	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25381	UniProtKB	Glycosylation	268	268	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25381	UniProtKB	Glycosylation	356	356	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25381	UniProtKB	Glycosylation	449	449	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25381	UniProtKB	Mutagenesis	365	365	.	.	.	Note=Abolishes protease activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19779569;Dbxref=PMID:19779569	
+##sequence-region P32611 1 393
+P32611	UniProtKB	Transit peptide	1	43	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32611	UniProtKB	Chain	44	393	.	.	.	ID=PRO_0000030512;Note=54S ribosomal protein RML2%2C mitochondrial	
+P32611	UniProtKB	Mutagenesis	336	342	.	.	.	Note=Loss of function. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9079633;Dbxref=PMID:9079633	
+P32611	UniProtKB	Mutagenesis	343	343	.	.	.	Note=Causes a cold-sensitive respiratory growth defect. Does not impair assembly of the ribosomal subunit. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9079633;Dbxref=PMID:9079633	
+##sequence-region P53942 1 307
+P53942	UniProtKB	Chain	1	307	.	.	.	ID=PRO_0000111718;Note=Ribonuclease H2 subunit A	
+P53942	UniProtKB	Metal binding	39	39	.	.	.	Note=Divalent metal cation	
+P53942	UniProtKB	Metal binding	40	40	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53942	UniProtKB	Metal binding	155	155	.	.	.	Note=Divalent metal cation	
+P53942	UniProtKB	Mutagenesis	39	39	.	.	.	Note=Abolishes enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14734815;Dbxref=PMID:14734815	
+P53942	UniProtKB	Mutagenesis	155	155	.	.	.	Note=Abolishes enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14734815;Dbxref=PMID:14734815	
+P53942	UniProtKB	Mutagenesis	183	183	.	.	.	Note=Strongly impairs enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14734815;Dbxref=PMID:14734815	
+##sequence-region P45818 1 564
+P45818	UniProtKB	Chain	1	564	.	.	.	ID=PRO_0000055063;Note=ATP-dependent RNA helicase ROK1	
+P45818	UniProtKB	Domain	153	333	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P45818	UniProtKB	Domain	344	506	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P45818	UniProtKB	Nucleotide binding	166	173	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P45818	UniProtKB	Motif	122	150	.	.	.	Note=Q motif	
+P45818	UniProtKB	Motif	280	283	.	.	.	Note=DEAD box	
+P45818	UniProtKB	Mutagenesis	166	166	.	.	.	Note=No cell growth and 2-fold decrease in ATPase activity in vitro. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593	
+P45818	UniProtKB	Mutagenesis	172	172	.	.	.	Note=Slow cell growth. K->G%2CR%2CS%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593	
+P45818	UniProtKB	Mutagenesis	172	172	.	.	.	Note=No cell growth and drastic decrease in ATPase activity in vitro. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593	
+P45818	UniProtKB	Mutagenesis	280	280	.	.	.	Note=Slow cell growth. D->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593	
+##sequence-region P36121 1 282
+P36121	UniProtKB	Chain	1	282	.	.	.	ID=PRO_0000203203;Note=DNA-directed RNA polymerase III subunit RPC5	
+P36121	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P32565 1 945
+P32565	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901	
+P32565	UniProtKB	Chain	2	945	.	.	.	ID=PRO_0000173808;Note=26S proteasome regulatory subunit RPN2	
+P32565	UniProtKB	Repeat	366	399	.	.	.	Note=PC 1	
+P32565	UniProtKB	Repeat	403	440	.	.	.	Note=PC 2	
+P32565	UniProtKB	Repeat	445	479	.	.	.	Note=PC 3	
+P32565	UniProtKB	Repeat	480	514	.	.	.	Note=PC 4	
+P32565	UniProtKB	Repeat	516	549	.	.	.	Note=PC 5	
+P32565	UniProtKB	Repeat	550	585	.	.	.	Note=PC 6	
+P32565	UniProtKB	Repeat	586	618	.	.	.	Note=PC 7	
+P32565	UniProtKB	Repeat	620	654	.	.	.	Note=PC 8	
+P32565	UniProtKB	Repeat	655	692	.	.	.	Note=PC 9	
+P32565	UniProtKB	Repeat	698	734	.	.	.	Note=PC 10	
+P32565	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901	
+P32565	UniProtKB	Modified residue	801	801	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32565	UniProtKB	Modified residue	932	932	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32565	UniProtKB	Sequence conflict	333	334	.	.	.	Note=SV->RL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32565	UniProtKB	Helix	7	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	18	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	43	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	58	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	75	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	96	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	131	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	150	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	163	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	179	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	200	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	222	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	235	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	251	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	267	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	284	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	293	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	311	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	326	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	340	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	347	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	353	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	362	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	379	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	382	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	387	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	398	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	412	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	417	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	437	453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	460	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	475	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	495	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	511	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	525	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	529	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	533	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	545	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	559	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	565	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	581	594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	596	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	602	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	606	608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	609	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	615	628	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	630	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	635	645	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	650	663	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	669	671	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	675	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	689	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	693	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	709	711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	713	715	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	720	722	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	727	736	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	737	741	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	743	752	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	753	755	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	757	762	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	763	766	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	767	769	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	772	775	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Turn	779	782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	866	869	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	878	881	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	886	894	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Beta strand	898	908	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+P32565	UniProtKB	Helix	920	924	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY	
+##sequence-region P36523 1 253
+P36523	UniProtKB	Transit peptide	1	28	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P36523	UniProtKB	Chain	29	253	.	.	.	ID=PRO_0000030572;Note=54S ribosomal protein L15%2C mitochondrial	
+P36523	UniProtKB	Sequence conflict	58	58	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36526 1 146
+P36526	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1764528,ECO:0000269|PubMed:2060626;Dbxref=PMID:1764528,PMID:2060626	
+P36526	UniProtKB	Chain	17	146	.	.	.	ID=PRO_0000030574;Note=54S ribosomal protein L27%2C mitochondrial	
+P36526	UniProtKB	Sequence conflict	17	17	.	.	.	Note=L->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36526	UniProtKB	Sequence conflict	21	21	.	.	.	Note=W->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36526	UniProtKB	Sequence conflict	48	48	.	.	.	Note=G->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36526	UniProtKB	Sequence conflict	57	57	.	.	.	Note=R->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36526	UniProtKB	Sequence conflict	72	72	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36526	UniProtKB	Sequence conflict	77	77	.	.	.	Note=V->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36526	UniProtKB	Sequence conflict	101	101	.	.	.	Note=L->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36526	UniProtKB	Sequence conflict	122	122	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36526	UniProtKB	Sequence conflict	126	126	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P14063 1 131
+P14063	UniProtKB	Transit peptide	1	12	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2666132,ECO:0000269|PubMed:3060376;Dbxref=PMID:2666132,PMID:3060376	
+P14063	UniProtKB	Chain	13	131	.	.	.	ID=PRO_0000030579;Note=54S ribosomal protein L31%2C mitochondrial	
+##sequence-region P02381 1 398
+P02381	UniProtKB	Chain	1	398	.	.	.	ID=PRO_0000220076;Note=Ribosomal protein VAR1%2C mitochondrial	
+P02381	UniProtKB	Sequence conflict	169	170	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02381	UniProtKB	Sequence conflict	169	170	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02381	UniProtKB	Sequence conflict	200	200	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02381	UniProtKB	Sequence conflict	200	200	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02381	UniProtKB	Sequence conflict	200	200	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02381	UniProtKB	Sequence conflict	284	284	.	.	.	Note=N->NNNNNNN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03441 1 430
+Q03441	UniProtKB	Chain	1	430	.	.	.	ID=PRO_0000097360;Note=Sporulation protein RMD1	
+##sequence-region P53140 1 646
+P53140	UniProtKB	Transit peptide	1	14	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53140	UniProtKB	Chain	15	646	.	.	.	ID=PRO_0000202752;Note=Protein RMD9%2C mitochondrial	
+P53140	UniProtKB	Mutagenesis	363	363	.	.	.	Note=Causes respiratory deficiency in absence of RSM28. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194786;Dbxref=PMID:17194786	
+P53140	UniProtKB	Sequence conflict	426	426	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12530 1 201
+Q12530	UniProtKB	Chain	1	201	.	.	.	ID=PRO_0000270572;Note=Ribonuclease MRP protein subunit RMP1	
+Q12530	UniProtKB	Transmembrane	86	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12530	UniProtKB	Compositional bias	183	193	.	.	.	Note=Poly-Lys;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12530	UniProtKB	Mutagenesis	103	103	.	.	.	Note=In RMP1-6%3B temperature-sensitive phenotype. Defective in 5.8S rRNA processing. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637077;Dbxref=PMID:15637077	
+##sequence-region Q03305 1 412
+Q03305	UniProtKB	Chain	1	412	.	.	.	ID=PRO_0000228980;Note=Protein arginine N-methyltransferase 2	
+Q03305	UniProtKB	Domain	189	412	.	.	.	Note=RMT2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892	
+Q03305	UniProtKB	Region	250	255	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892	
+Q03305	UniProtKB	Region	271	273	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892	
+Q03305	UniProtKB	Region	298	299	.	.	.	Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892	
+Q03305	UniProtKB	Binding site	196	196	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892	
+Q03305	UniProtKB	Binding site	226	226	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892	
+Q03305	UniProtKB	Binding site	319	319	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892	
+Q03305	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03305	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q04740 1 348
+Q04740	UniProtKB	Chain	1	348	.	.	.	ID=PRO_0000195438;Note=Ribonuclease H	
+Q04740	UniProtKB	Domain	184	346	.	.	.	Note=RNase H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408	
+Q04740	UniProtKB	Metal binding	193	193	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408	
+Q04740	UniProtKB	Metal binding	193	193	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408	
+Q04740	UniProtKB	Metal binding	235	235	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408	
+Q04740	UniProtKB	Metal binding	264	264	.	.	.	Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408	
+Q04740	UniProtKB	Metal binding	338	338	.	.	.	Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408	
+Q04740	UniProtKB	Beta strand	6	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK	
+Q04740	UniProtKB	Beta strand	12	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK	
+Q04740	UniProtKB	Beta strand	17	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK	
+Q04740	UniProtKB	Helix	22	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK	
+Q04740	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK	
+Q04740	UniProtKB	Beta strand	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK	
+Q04740	UniProtKB	Helix	43	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK	
+##sequence-region P22138 1 1203
+P22138	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P22138	UniProtKB	Chain	2	1203	.	.	.	ID=PRO_0000048080;Note=DNA-directed RNA polymerase I subunit RPA135	
+P22138	UniProtKB	Zinc finger	1104	1131	.	.	.	Note=C4-type	
+P22138	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P22138	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P22138	UniProtKB	Modified residue	1156	1156	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22138	UniProtKB	Mutagenesis	1104	1104	.	.	.	Note=No effect%3B when associated with A-1107%3B A-1128 and A-1131. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555487;Dbxref=PMID:14555487	
+P22138	UniProtKB	Mutagenesis	1107	1107	.	.	.	Note=Lethal. Abolishes recruitment of RPA1 to Pol I. No effect%3B when associated with A-1104%3B A-1128 and A-1131. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555487;Dbxref=PMID:14555487	
+P22138	UniProtKB	Mutagenesis	1127	1127	.	.	.	Note=Responsible of suppression of RPA190-5 and RPA190-1 mutations. C->R	
+P22138	UniProtKB	Mutagenesis	1128	1128	.	.	.	Note=No effect%3B when associated with A-1104%3B A-1107 and A-1131. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555487;Dbxref=PMID:14555487	
+P22138	UniProtKB	Mutagenesis	1131	1131	.	.	.	Note=No effect%3B when associated with A-1104%3B A-1107 and A-1128. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555487;Dbxref=PMID:14555487	
+P22138	UniProtKB	Helix	18	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	36	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Helix	60	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	71	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	86	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Beta strand	94	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	108	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Beta strand	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Helix	123	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	134	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	150	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	171	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	177	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	199	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	205	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	214	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	220	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	229	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	245	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	258	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	267	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	273	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	285	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	300	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	314	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	323	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	335	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	342	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Helix	346	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	360	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	367	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	387	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Helix	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	400	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	405	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	443	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	457	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	485	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	493	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	502	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	507	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	516	518	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	522	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	525	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	537	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	542	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	558	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Helix	561	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	573	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	583	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	591	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	598	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	618	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Beta strand	625	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	633	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	639	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	649	655	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	656	659	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	660	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	666	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	674	677	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	678	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	683	685	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	687	689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	693	696	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	699	703	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	707	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	712	722	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	733	735	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	739	745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	751	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	755	759	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	762	764	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	769	777	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	779	781	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	786	790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	791	795	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	796	799	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	801	810	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	813	815	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	823	826	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	835	838	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	844	846	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	857	863	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	864	867	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	868	873	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	880	888	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	892	894	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	900	909	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	916	919	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	924	931	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	933	935	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	938	942	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Beta strand	946	949	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	951	953	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	955	957	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	960	975	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	988	990	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Helix	992	1003	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	1009	1011	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	1016	1018	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	1026	1036	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	1040	1043	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Beta strand	1045	1049	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	1054	1056	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	1063	1065	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Beta strand	1069	1071	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	1073	1082	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	1085	1092	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	1093	1097	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	1098	1104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Turn	1105	1107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	1110	1115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	1120	1122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P22138	UniProtKB	Beta strand	1126	1131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	1135	1139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	1155	1157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	1158	1160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	1166	1168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	1173	1179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Helix	1180	1191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P22138	UniProtKB	Beta strand	1194	1201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+##sequence-region P20435 1 155
+P20435	UniProtKB	Chain	1	155	.	.	.	ID=PRO_0000133797;Note=DNA-directed RNA polymerases I%2C II%2C and III subunit RPABC2	
+P20435	UniProtKB	Region	111	132	.	.	.	Note=Leucine-zipper	
+P20435	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P20435	UniProtKB	Helix	56	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P20435	UniProtKB	Beta strand	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20435	UniProtKB	Helix	87	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20435	UniProtKB	Helix	117	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20435	UniProtKB	Beta strand	132	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20435	UniProtKB	Beta strand	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I3Q	
+P20435	UniProtKB	Beta strand	143	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20435	UniProtKB	Turn	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+##sequence-region P28000 1 142
+P28000	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000149319;Note=DNA-directed RNA polymerases I and III subunit RPAC2	
+P28000	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P28000	UniProtKB	Modified residue	33	33	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P28000	UniProtKB	Cross-link	134	134	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P28000	UniProtKB	Beta strand	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P28000	UniProtKB	Turn	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P28000	UniProtKB	Beta strand	58	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P28000	UniProtKB	Helix	70	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P28000	UniProtKB	Beta strand	86	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P28000	UniProtKB	Beta strand	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3H	
+P28000	UniProtKB	Beta strand	100	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P28000	UniProtKB	Beta strand	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P28000	UniProtKB	Helix	113	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+##sequence-region P04050 1 1733
+P04050	UniProtKB	Chain	1	1733	.	.	.	ID=PRO_0000073946;Note=DNA-directed RNA polymerase II subunit RPB1	
+P04050	UniProtKB	Repeat	1549	1555	.	.	.	Note=1	
+P04050	UniProtKB	Repeat	1556	1562	.	.	.	Note=2	
+P04050	UniProtKB	Repeat	1563	1569	.	.	.	Note=3	
+P04050	UniProtKB	Repeat	1570	1576	.	.	.	Note=4	
+P04050	UniProtKB	Repeat	1577	1583	.	.	.	Note=5	
+P04050	UniProtKB	Repeat	1584	1590	.	.	.	Note=6	
+P04050	UniProtKB	Repeat	1591	1597	.	.	.	Note=7	
+P04050	UniProtKB	Repeat	1598	1604	.	.	.	Note=8	
+P04050	UniProtKB	Repeat	1605	1611	.	.	.	Note=9	
+P04050	UniProtKB	Repeat	1612	1618	.	.	.	Note=10	
+P04050	UniProtKB	Repeat	1619	1625	.	.	.	Note=11	
+P04050	UniProtKB	Repeat	1626	1632	.	.	.	Note=12	
+P04050	UniProtKB	Repeat	1633	1639	.	.	.	Note=13	
+P04050	UniProtKB	Repeat	1640	1646	.	.	.	Note=14	
+P04050	UniProtKB	Repeat	1647	1653	.	.	.	Note=15	
+P04050	UniProtKB	Repeat	1654	1660	.	.	.	Note=16	
+P04050	UniProtKB	Repeat	1661	1667	.	.	.	Note=17	
+P04050	UniProtKB	Repeat	1668	1674	.	.	.	Note=18	
+P04050	UniProtKB	Repeat	1675	1681	.	.	.	Note=19	
+P04050	UniProtKB	Repeat	1682	1688	.	.	.	Note=20	
+P04050	UniProtKB	Repeat	1689	1695	.	.	.	Note=21	
+P04050	UniProtKB	Repeat	1696	1702	.	.	.	Note=22	
+P04050	UniProtKB	Repeat	1703	1709	.	.	.	Note=23	
+P04050	UniProtKB	Repeat	1710	1716	.	.	.	Note=24%3B approximate	
+P04050	UniProtKB	Region	248	260	.	.	.	Note=Lid loop	
+P04050	UniProtKB	Region	306	323	.	.	.	Note=Rudder loop	
+P04050	UniProtKB	Region	810	822	.	.	.	Note=Bridging helix	
+P04050	UniProtKB	Region	1549	1716	.	.	.	Note=C-terminal domain (CTD)%3B 24 X 7 AA approximate tandem repeats of Y-S-P-T-S-P-[A-S-N-G]	
+P04050	UniProtKB	Metal binding	67	67	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	70	70	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	77	77	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	80	80	.	.	.	Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	107	107	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	110	110	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	148	148	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	167	167	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	481	481	.	.	.	Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	481	481	.	.	.	Note=Magnesium 2%3B shared with RPB2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	483	483	.	.	.	Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	483	483	.	.	.	Note=Magnesium 2%3B shared with RPB2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Metal binding	485	485	.	.	.	Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824	
+P04050	UniProtKB	Modified residue	1471	1471	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04050	UniProtKB	Cross-link	695	695	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P04050	UniProtKB	Cross-link	1246	1246	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P04050	UniProtKB	Cross-link	1350	1350	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P04050	UniProtKB	Natural variant	1653	1659	.	.	.	Note=In strain: A364A. Missing	
+P04050	UniProtKB	Sequence conflict	1514	1514	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04050	UniProtKB	Sequence conflict	1524	1524	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04050	UniProtKB	Sequence conflict	1601	1601	.	.	.	Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04050	UniProtKB	Beta strand	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	24	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXX	
+P04050	UniProtKB	Beta strand	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVT	
+P04050	UniProtKB	Beta strand	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWC	
+P04050	UniProtKB	Beta strand	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P04050	UniProtKB	Beta strand	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P04050	UniProtKB	Beta strand	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P04050	UniProtKB	Beta strand	84	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	96	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P04050	UniProtKB	Beta strand	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVQ	
+P04050	UniProtKB	Helix	120	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2I	
+P04050	UniProtKB	Helix	131	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P04050	UniProtKB	Beta strand	173	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P04050	UniProtKB	Beta strand	181	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	187	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	198	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	204	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S2H	
+P04050	UniProtKB	Helix	216	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	226	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	231	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	235	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	244	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	257	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P04050	UniProtKB	Helix	261	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	281	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P04050	UniProtKB	Helix	286	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	307	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P04050	UniProtKB	Beta strand	313	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P04050	UniProtKB	Beta strand	318	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P04050	UniProtKB	Helix	325	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P04050	UniProtKB	Turn	330	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	338	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	341	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Y7N	
+P04050	UniProtKB	Beta strand	347	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	363	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	368	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	375	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	382	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	385	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	395	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	398	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	402	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	408	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P04050	UniProtKB	Beta strand	412	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	415	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P04050	UniProtKB	Turn	419	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	431	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	441	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	452	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	455	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	472	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	475	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	482	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	486	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	495	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	507	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	511	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	514	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	518	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	525	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	536	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1N	
+P04050	UniProtKB	Beta strand	540	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	543	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	553	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P04050	UniProtKB	Beta strand	567	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	571	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	574	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	588	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	596	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2I	
+P04050	UniProtKB	Beta strand	600	602	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO2	
+P04050	UniProtKB	Beta strand	604	608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	611	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	619	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	626	628	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P04050	UniProtKB	Helix	629	637	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	639	658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	666	669	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	673	699	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	706	708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P04050	UniProtKB	Helix	710	736	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	742	749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	750	752	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K83	
+P04050	UniProtKB	Helix	755	762	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	770	774	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I3Q	
+P04050	UniProtKB	Beta strand	778	781	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P04050	UniProtKB	Beta strand	782	784	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	794	798	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	804	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	810	845	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	863	867	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	868	870	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	875	877	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	878	882	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	884	886	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	890	897	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	901	903	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YU9	
+P04050	UniProtKB	Turn	904	906	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	910	912	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	913	915	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S15	
+P04050	UniProtKB	Helix	916	919	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	923	946	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	947	949	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	953	958	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	960	970	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	975	977	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K83	
+P04050	UniProtKB	Helix	983	994	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1005	1013	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1016	1025	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1028	1033	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1039	1056	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1064	1076	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1079	1082	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q	
+P04050	UniProtKB	Helix	1086	1088	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVQ	
+P04050	UniProtKB	Beta strand	1089	1091	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P04050	UniProtKB	Beta strand	1092	1094	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q	
+P04050	UniProtKB	Helix	1097	1104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	1105	1107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1115	1120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1122	1126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1128	1138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1143	1145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1147	1154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1158	1160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1164	1166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1167	1171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1172	1174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P04050	UniProtKB	Beta strand	1179	1182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P04050	UniProtKB	Beta strand	1190	1197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1199	1204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1209	1220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1221	1223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1224	1228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1233	1235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1237	1242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1258	1270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1272	1275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1282	1292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1296	1310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1313	1316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1317	1322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M3Y	
+P04050	UniProtKB	Turn	1324	1326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1328	1330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P04050	UniProtKB	Helix	1332	1339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1341	1357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	1358	1360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1365	1374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Turn	1375	1377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1378	1380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1384	1386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1388	1390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1392	1394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P04050	UniProtKB	Helix	1396	1399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P04050	UniProtKB	Turn	1400	1402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P04050	UniProtKB	Helix	1406	1415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1424	1429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1437	1439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Beta strand	1440	1445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P04050	UniProtKB	Helix	1447	1450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P04050	UniProtKB	Beta strand	1677	1680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LO6	
+##sequence-region P20433 1 221
+P20433	UniProtKB	Chain	1	221	.	.	.	ID=PRO_0000073984;Note=DNA-directed RNA polymerase II subunit RPB4	
+P20433	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P20433	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P20433	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P20433	UniProtKB	Beta strand	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO2	
+P20433	UniProtKB	Helix	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P20433	UniProtKB	Beta strand	24	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P20433	UniProtKB	Helix	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOU	
+P20433	UniProtKB	Beta strand	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P20433	UniProtKB	Turn	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VUM	
+P20433	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P20433	UniProtKB	Beta strand	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P20433	UniProtKB	Helix	52	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P20433	UniProtKB	Turn	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXX	
+P20433	UniProtKB	Helix	119	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P20433	UniProtKB	Helix	139	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P20433	UniProtKB	Helix	157	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P20433	UniProtKB	Turn	169	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P20433	UniProtKB	Helix	174	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P20433	UniProtKB	Helix	188	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P20433	UniProtKB	Helix	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P20433	UniProtKB	Turn	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+P20433	UniProtKB	Helix	204	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14	
+##sequence-region Q02773 1 1202
+Q02773	UniProtKB	Transit peptide	1	122	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1409716;Dbxref=PMID:1409716	
+Q02773	UniProtKB	Chain	123	1202	.	.	.	ID=PRO_0000022247;Note=Ribonuclease P protein component%2C mitochondrial	
+##sequence-region Q04847 1 553
+Q04847	UniProtKB	Chain	1	553	.	.	.	ID=PRO_0000203342;Note=Non-SCF-type F-box protein ROY1	
+Q04847	UniProtKB	Domain	3	49	.	.	.	Note=F-box	
+##sequence-region P50106 1 137
+P50106	UniProtKB	Chain	1	137	.	.	.	ID=PRO_0000073962;Note=DNA-directed RNA polymerase I subunit RPA14	
+P50106	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50106	UniProtKB	Turn	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P50106	UniProtKB	Beta strand	20	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P50106	UniProtKB	Helix	33	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P50106	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RF4	
+P50106	UniProtKB	Helix	81	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+##sequence-region P04051 1 1460
+P04051	UniProtKB	Chain	1	1460	.	.	.	ID=PRO_0000073953;Note=DNA-directed RNA polymerase III subunit RPC1	
+P04051	UniProtKB	Region	858	870	.	.	.	Note=Bridging helix;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04051	UniProtKB	Metal binding	67	67	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04051	UniProtKB	Metal binding	70	70	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04051	UniProtKB	Metal binding	77	77	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04051	UniProtKB	Metal binding	80	80	.	.	.	Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04051	UniProtKB	Metal binding	107	107	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04051	UniProtKB	Metal binding	110	110	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04051	UniProtKB	Metal binding	154	154	.	.	.	Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04051	UniProtKB	Metal binding	511	511	.	.	.	Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04051	UniProtKB	Metal binding	513	513	.	.	.	Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04051	UniProtKB	Metal binding	515	515	.	.	.	Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04051	UniProtKB	Mutagenesis	506	506	.	.	.	Note=Temperature-sensitive. T->I	
+P04051	UniProtKB	Mutagenesis	509	509	.	.	.	Note=Temperature-sensitive. N->Y	
+P04051	UniProtKB	Mutagenesis	518	518	.	.	.	Note=Temperature-sensitive. N->Q	
+##sequence-region P32349 1 654
+P32349	UniProtKB	Chain	1	654	.	.	.	ID=PRO_0000073966;Note=DNA-directed RNA polymerase III subunit RPC3	
+P32349	UniProtKB	Region	581	602	.	.	.	Note=Leucine-zipper	
+P32349	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32349	UniProtKB	Modified residue	392	392	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32349	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32349	UniProtKB	Sequence conflict	637	637	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P17890 1 251
+P17890	UniProtKB	Chain	1	251	.	.	.	ID=PRO_0000073980;Note=DNA-directed RNA polymerase III subunit RPC7	
+P17890	UniProtKB	Compositional bias	202	248	.	.	.	Note=Asp/Glu-rich (acidic)	
+P17890	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P17890	UniProtKB	Sequence conflict	12	12	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P17890	UniProtKB	Sequence conflict	205	205	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35718 1 212
+P35718	UniProtKB	Chain	1	212	.	.	.	ID=PRO_0000073996;Note=DNA-directed RNA polymerase III subunit RPC8	
+P35718	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P35718	UniProtKB	Beta strand	2	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Helix	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Helix	22	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Turn	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	43	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	66	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	84	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	96	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	108	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Turn	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Turn	123	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	127	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	137	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	145	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Beta strand	193	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+P35718	UniProtKB	Helix	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ	
+##sequence-region P46969 1 238
+P46969	UniProtKB	Chain	1	238	.	.	.	ID=PRO_0000171595;Note=Ribulose-phosphate 3-epimerase	
+P46969	UniProtKB	Region	156	159	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46969	UniProtKB	Region	207	208	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46969	UniProtKB	Active site	36	36	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46969	UniProtKB	Active site	185	185	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46969	UniProtKB	Metal binding	34	34	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46969	UniProtKB	Metal binding	36	36	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46969	UniProtKB	Metal binding	80	80	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46969	UniProtKB	Metal binding	185	185	.	.	.	Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46969	UniProtKB	Binding site	9	9	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46969	UniProtKB	Binding site	80	80	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46969	UniProtKB	Binding site	187	187	.	.	.	Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03465 1 531
+Q03465	UniProtKB	Chain	1	531	.	.	.	ID=PRO_0000173871;Note=Protein RPN4	
+Q03465	UniProtKB	Motif	382	398	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03465	UniProtKB	Compositional bias	211	229	.	.	.	Note=Asp/Glu-rich (acidic)	
+Q03465	UniProtKB	Compositional bias	300	315	.	.	.	Note=Asp/Glu-rich (acidic)	
+Q03465	UniProtKB	Sequence conflict	231	231	.	.	.	Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12377 1 434
+Q12377	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901	
+Q12377	UniProtKB	Chain	2	434	.	.	.	ID=PRO_0000173860;Note=26S proteasome regulatory subunit RPN6	
+Q12377	UniProtKB	Domain	229	401	.	.	.	Note=PCI	
+Q12377	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901	
+Q12377	UniProtKB	Mutagenesis	132	132	.	.	.	Note=In rpn6-2%3B temperature-sensitive mutant that shows defects in proteasome assembly when incubated at 37 degrees Celsius%3B when associated with P-377. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611133;Dbxref=PMID:15611133	
+Q12377	UniProtKB	Mutagenesis	377	377	.	.	.	Note=In rpn6-2%3B temperature-sensitive mutant that shows defects in proteasome assembly when incubated at 37 degrees Celsius%3B when associated with L-132. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611133;Dbxref=PMID:15611133	
+Q12377	UniProtKB	Helix	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	59	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Turn	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	71	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Turn	84	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	94	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Beta strand	106	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	112	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	131	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Turn	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	152	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	171	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	192	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	212	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	232	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	254	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	276	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Turn	284	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	294	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	311	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Turn	317	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	322	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	329	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Beta strand	354	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	359	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	370	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Beta strand	388	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Turn	392	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Beta strand	396	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q12377	UniProtKB	Helix	407	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+##sequence-region Q06506 1 573
+Q06506	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06506	UniProtKB	Chain	2	573	.	.	.	ID=PRO_0000269482;Note=Ribosomal RNA-processing protein 9	
+Q06506	UniProtKB	Repeat	234	273	.	.	.	Note=WD 1	
+Q06506	UniProtKB	Repeat	278	317	.	.	.	Note=WD 2	
+Q06506	UniProtKB	Repeat	320	359	.	.	.	Note=WD 3	
+Q06506	UniProtKB	Repeat	397	435	.	.	.	Note=WD 4	
+Q06506	UniProtKB	Repeat	471	509	.	.	.	Note=WD 5	
+Q06506	UniProtKB	Repeat	516	562	.	.	.	Note=WD 6	
+Q06506	UniProtKB	Coiled coil	32	106	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06506	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q06506	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06506	UniProtKB	Turn	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	141	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	157	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	186	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	194	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	209	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Helix	218	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	239	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	248	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	258	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Turn	265	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	269	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	283	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	292	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	302	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Turn	309	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	313	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	327	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	332	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	345	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Turn	351	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	355	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Helix	365	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	402	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	412	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	422	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	433	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Turn	437	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	477	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	484	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	492	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	496	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	508	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	519	528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	537	546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+Q06506	UniProtKB	Beta strand	562	569	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X	
+##sequence-region P40042 1 185
+P40042	UniProtKB	Chain	1	185	.	.	.	ID=PRO_0000051472;Note=Regulator of rDNA transcription protein 13	
+P40042	UniProtKB	Repeat	9	48	.	.	.	Note=WD 1	
+P40042	UniProtKB	Repeat	71	108	.	.	.	Note=WD 2	
+P40042	UniProtKB	Repeat	111	148	.	.	.	Note=WD 3	
+##sequence-region Q07829 1 113
+Q07829	UniProtKB	Chain	1	113	.	.	.	ID=PRO_0000299603;Note=Regulator of rDNA transcription protein 7	
+Q07829	UniProtKB	Transmembrane	13	35	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07829	UniProtKB	Transmembrane	70	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07829	UniProtKB	Sequence conflict	10	10	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08745 1 105
+Q08745	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000116376;Note=40S ribosomal protein S10-A	
+Q08745	UniProtKB	Helix	5	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q08745	UniProtKB	Beta strand	19	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q08745	UniProtKB	Beta strand	33	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q08745	UniProtKB	Helix	39	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q08745	UniProtKB	Beta strand	53	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q08745	UniProtKB	Turn	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q08745	UniProtKB	Beta strand	63	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q08745	UniProtKB	Helix	70	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q08745	UniProtKB	Helix	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+Q08745	UniProtKB	Turn	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U52	
+##sequence-region P46784 1 105
+P46784	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000116377;Note=40S ribosomal protein S10-B	
+P46784	UniProtKB	Helix	5	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P46784	UniProtKB	Beta strand	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P46784	UniProtKB	Beta strand	33	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P46784	UniProtKB	Helix	39	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P46784	UniProtKB	Beta strand	54	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P46784	UniProtKB	Beta strand	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P46784	UniProtKB	Helix	70	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+##sequence-region P0CX48 1 156
+P0CX48	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:1544921	
+P0CX48	UniProtKB	Chain	2	156	.	.	.	ID=PRO_0000409770;Note=40S ribosomal protein S11-B	
+P0CX48	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:1544921	
+P0CX48	UniProtKB	Cross-link	15	15	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX48	UniProtKB	Cross-link	46	46	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX48	UniProtKB	Cross-link	56	56	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX48	UniProtKB	Cross-link	57	57	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX48	UniProtKB	Cross-link	79	79	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX48	UniProtKB	Cross-link	96	96	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX48	UniProtKB	Cross-link	105	105	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX48	UniProtKB	Cross-link	133	133	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX48	UniProtKB	Cross-link	141	141	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX48	UniProtKB	Cross-link	148	148	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX48	UniProtKB	Sequence conflict	12	13	.	.	.	Note=AF->FA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40693 1 322
+P40693	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40693	UniProtKB	Chain	2	322	.	.	.	ID=PRO_0000104658;Note=Ribosome biogenesis protein RLP7	
+P40693	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40693	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40693	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40693	UniProtKB	Modified residue	278	278	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+##sequence-region Q04599 1 285
+##sequence-region P32904 1 214
+P32904	UniProtKB	Transit peptide	1	16	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978	
+P32904	UniProtKB	Chain	17	214	.	.	.	ID=PRO_0000030546;Note=54S ribosomal protein L6%2C mitochondrial	
+P32904	UniProtKB	Sequence conflict	19	19	.	.	.	Note=V->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32904	UniProtKB	Sequence conflict	27	27	.	.	.	Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32904	UniProtKB	Sequence conflict	201	214	.	.	.	Note=VNDETIKLKDKKIK->GTVKQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P31334 1 269
+P31334	UniProtKB	Transit peptide	1	19	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1597181,ECO:0000269|PubMed:3060376;Dbxref=PMID:1597181,PMID:3060376	
+P31334	UniProtKB	Chain	20	269	.	.	.	ID=PRO_0000030536;Note=54S ribosomal protein L9%2C mitochondrial	
+P31334	UniProtKB	Sequence conflict	21	21	.	.	.	Note=S->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P31334	UniProtKB	Sequence conflict	139	139	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36521 1 249
+P36521	UniProtKB	Transit peptide	1	31	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P36521	UniProtKB	Chain	32	249	.	.	.	ID=PRO_0000030440;Note=54S ribosomal protein L11%2C mitochondrial	
+P36521	UniProtKB	Sequence conflict	35	35	.	.	.	Note=S->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36521	UniProtKB	Sequence conflict	42	42	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36521	UniProtKB	Sequence conflict	48	48	.	.	.	Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36521	UniProtKB	Sequence conflict	51	51	.	.	.	Note=T->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36521	UniProtKB	Sequence conflict	56	56	.	.	.	Note=T->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36521	UniProtKB	Sequence conflict	60	60	.	.	.	Note=L->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53875 1 158
+P53875	UniProtKB	Transit peptide	1	73	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978	
+P53875	UniProtKB	Chain	74	158	.	.	.	ID=PRO_0000030447;Note=54S ribosomal protein L19%2C mitochondrial	
+##sequence-region P36525 1 258
+P36525	UniProtKB	Transit peptide	1	21	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626	
+P36525	UniProtKB	Chain	22	258	.	.	.	ID=PRO_0000030509;Note=54S ribosomal protein L24%2C mitochondrial	
+P36525	UniProtKB	Sequence conflict	72	72	.	.	.	Note=G->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36525	UniProtKB	Sequence conflict	76	76	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P36525	UniProtKB	Sequence conflict	130	130	.	.	.	Note=G->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06678 1 367
+Q06678	UniProtKB	Transit peptide	1	29	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06678	UniProtKB	Chain	30	367	.	.	.	ID=PRO_0000023284;Note=54S ribosomal protein L35%2C mitochondrial	
+Q06678	UniProtKB	Sequence conflict	113	113	.	.	.	Note=P->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P19956 1 98
+P19956	UniProtKB	Chain	1	98	.	.	.	ID=PRO_0000087696;Note=54S ribosomal protein L44%2C mitochondrial	
+##sequence-region P40858 1 161
+P40858	UniProtKB	Transit peptide	1	35	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40858	UniProtKB	Chain	36	161	.	.	.	ID=PRO_0000030483;Note=54S ribosomal protein L49%2C mitochondrial	
+P40858	UniProtKB	Sequence conflict	115	115	.	.	.	Note=T->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25298 1 677
+P25298	UniProtKB	Chain	1	677	.	.	.	ID=PRO_0000205761;Note=mRNA 3'-end-processing protein RNA14	
+P25298	UniProtKB	Repeat	56	88	.	.	.	Note=HAT 1	
+P25298	UniProtKB	Repeat	90	124	.	.	.	Note=HAT 2	
+P25298	UniProtKB	Repeat	138	170	.	.	.	Note=HAT 3	
+P25298	UniProtKB	Repeat	181	214	.	.	.	Note=HAT 4	
+P25298	UniProtKB	Repeat	257	289	.	.	.	Note=HAT 5	
+P25298	UniProtKB	Repeat	298	330	.	.	.	Note=HAT 6	
+P25298	UniProtKB	Helix	633	641	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+P25298	UniProtKB	Helix	645	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+P25298	UniProtKB	Helix	655	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B	
+##sequence-region Q02805 1 837
+Q02805	UniProtKB	Chain	1	837	.	.	.	ID=PRO_0000097396;Note=Protein ROD1	
+Q02805	UniProtKB	Motif	487	490	.	.	.	Note=PY-motif	
+Q02805	UniProtKB	Motif	656	659	.	.	.	Note=PY-motif	
+Q02805	UniProtKB	Compositional bias	3	6	.	.	.	Note=Poly-Ser	
+Q02805	UniProtKB	Compositional bias	524	601	.	.	.	Note=Asn-rich	
+Q02805	UniProtKB	Compositional bias	684	815	.	.	.	Note=Ser-rich	
+Q02805	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02805	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q02805	UniProtKB	Modified residue	436	436	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q02805	UniProtKB	Modified residue	536	536	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02805	UniProtKB	Modified residue	720	720	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q02805	UniProtKB	Modified residue	725	725	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02805	UniProtKB	Cross-link	401	401	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q02805	UniProtKB	Mutagenesis	487	488	.	.	.	Note=Reduced binding to RSP5. PP->QA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163175;Dbxref=PMID:12163175	
+Q02805	UniProtKB	Mutagenesis	656	657	.	.	.	Note=Reduced binding to RSP5. PP->QA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163175;Dbxref=PMID:12163175	
+Q02805	UniProtKB	Sequence conflict	618	618	.	.	.	Note=Y->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43602 1 733
+P43602	UniProtKB	Chain	1	733	.	.	.	ID=PRO_0000202690;Note=Protein ROG3	
+P43602	UniProtKB	Motif	460	463	.	.	.	Note=PY-motif	
+P43602	UniProtKB	Motif	625	628	.	.	.	Note=PY-motif	
+P43602	UniProtKB	Compositional bias	641	710	.	.	.	Note=Ser-rich	
+P43602	UniProtKB	Mutagenesis	460	461	.	.	.	Note=Reduced binding to RSP5. PP->QA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163175;Dbxref=PMID:12163175	
+P43602	UniProtKB	Mutagenesis	625	626	.	.	.	Note=Reduced binding to RSP5. PP->QA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163175;Dbxref=PMID:12163175	
+##sequence-region P53046 1 1155
+P53046	UniProtKB	Chain	1	1155	.	.	.	ID=PRO_0000080968;Note=RHO1 GDP-GTP exchange protein 1	
+P53046	UniProtKB	Domain	464	651	.	.	.	Note=DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00062	
+P53046	UniProtKB	Domain	842	1137	.	.	.	Note=CNH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00795	
+P53046	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53046	UniProtKB	Modified residue	154	154	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53046	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53046	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53046	UniProtKB	Modified residue	433	433	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53046	UniProtKB	Sequence conflict	214	214	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	214	214	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	250	250	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	279	281	.	.	.	Note=KLS->QLG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	385	385	.	.	.	Note=Y->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	515	515	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	557	557	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	844	844	.	.	.	Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	852	852	.	.	.	Note=H->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	897	897	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	959	959	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	960	960	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	961	961	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	1037	1037	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53046	UniProtKB	Sequence conflict	1151	1151	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03691 1 256
+Q03691	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03691	UniProtKB	Chain	25	256	.	.	.	ID=PRO_0000203327;Note=Protein ROT1	
+Q03691	UniProtKB	Topological domain	25	235	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03691	UniProtKB	Transmembrane	236	256	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03691	UniProtKB	Glycosylation	103	103	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17914748;Dbxref=PMID:17914748	
+Q03691	UniProtKB	Glycosylation	107	107	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17914748;Dbxref=PMID:17914748	
+Q03691	UniProtKB	Glycosylation	139	139	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17914748;Dbxref=PMID:17914748	
+##sequence-region P47006 1 233
+P47006	UniProtKB	Chain	1	233	.	.	.	ID=PRO_0000203031;Note=DNA-directed RNA polymerase I subunit RPA34	
+P47006	UniProtKB	Compositional bias	184	233	.	.	.	Note=Glu/Lys-rich	
+P47006	UniProtKB	Compositional bias	208	215	.	.	.	Note=Poly-Lys	
+P47006	UniProtKB	Compositional bias	221	230	.	.	.	Note=Poly-Lys	
+P47006	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47006	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P47006	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47006	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47006	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P47006	UniProtKB	Beta strand	52	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P47006	UniProtKB	Turn	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P47006	UniProtKB	Beta strand	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P47006	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P47006	UniProtKB	Beta strand	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P47006	UniProtKB	Beta strand	85	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P47006	UniProtKB	Helix	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P47006	UniProtKB	Beta strand	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P47006	UniProtKB	Beta strand	106	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P47006	UniProtKB	Beta strand	116	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P47006	UniProtKB	Beta strand	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P47006	UniProtKB	Beta strand	134	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P47006	UniProtKB	Helix	150	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P47006	UniProtKB	Helix	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+##sequence-region P46669 1 326
+P46669	UniProtKB	Chain	1	326	.	.	.	ID=PRO_0000073960;Note=DNA-directed RNA polymerase I subunit RPA43	
+P46669	UniProtKB	Modified residue	244	244	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46669	UniProtKB	Modified residue	251	251	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46669	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46669	UniProtKB	Modified residue	269	269	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46669	UniProtKB	Modified residue	285	285	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P46669	UniProtKB	Sequence conflict	318	318	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46669	UniProtKB	Helix	11	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P46669	UniProtKB	Beta strand	30	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	38	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Helix	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P46669	UniProtKB	Helix	57	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Turn	75	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	79	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	103	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	109	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	114	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	132	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	142	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Turn	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	153	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	216	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P46669	UniProtKB	Beta strand	227	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	239	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	244	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	264	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P46669	UniProtKB	Turn	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P46669	UniProtKB	Helix	273	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P46669	UniProtKB	Beta strand	307	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+##sequence-region P20434 1 215
+P20434	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000146086;Note=DNA-directed RNA polymerases I%2C II%2C and III subunit RPABC1	
+P20434	UniProtKB	Sequence conflict	37	37	.	.	.	Note=L->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20434	UniProtKB	Turn	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWC	
+P20434	UniProtKB	Helix	7	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Helix	32	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Helix	39	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVQ	
+P20434	UniProtKB	Helix	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Beta strand	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Helix	66	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Beta strand	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVY	
+P20434	UniProtKB	Beta strand	78	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Beta strand	84	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Helix	90	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Beta strand	106	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Helix	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Turn	122	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Beta strand	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1M	
+P20434	UniProtKB	Beta strand	131	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Helix	137	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Helix	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Beta strand	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RZD	
+P20434	UniProtKB	Beta strand	152	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Helix	158	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Helix	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Beta strand	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P20434	UniProtKB	Beta strand	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2I	
+P20434	UniProtKB	Helix	183	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Beta strand	195	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Beta strand	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+P20434	UniProtKB	Beta strand	210	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF	
+##sequence-region P20436 1 146
+P20436	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P20436	UniProtKB	Chain	2	146	.	.	.	ID=PRO_0000074001;Note=DNA-directed RNA polymerases I%2C II%2C and III subunit RPABC3	
+P20436	UniProtKB	Region	16	39	.	.	.	Note=Non-specific ssDNA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20436	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P20436	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P20436	UniProtKB	Beta strand	7	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20436	UniProtKB	Beta strand	21	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20436	UniProtKB	Beta strand	37	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20436	UniProtKB	Helix	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20436	UniProtKB	Beta strand	54	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20436	UniProtKB	Turn	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20436	UniProtKB	Helix	89	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M	
+P20436	UniProtKB	Beta strand	93	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20436	UniProtKB	Beta strand	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I	
+P20436	UniProtKB	Beta strand	112	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20436	UniProtKB	Beta strand	121	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20436	UniProtKB	Turn	129	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20436	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P20436	UniProtKB	Beta strand	140	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+##sequence-region P22139 1 70
+P22139	UniProtKB	Chain	1	70	.	.	.	ID=PRO_0000121342;Note=DNA-directed RNA polymerases I%2C II%2C and III subunit RPABC5	
+P22139	UniProtKB	Metal binding	7	7	.	.	.	Note=Zinc	
+P22139	UniProtKB	Metal binding	10	10	.	.	.	Note=Zinc	
+P22139	UniProtKB	Metal binding	44	44	.	.	.	Note=Zinc	
+P22139	UniProtKB	Metal binding	45	45	.	.	.	Note=Zinc	
+P22139	UniProtKB	Cross-link	59	59	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P22139	UniProtKB	Turn	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P22139	UniProtKB	Helix	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M3Y	
+P22139	UniProtKB	Helix	18	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P22139	UniProtKB	Turn	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I6H	
+P22139	UniProtKB	Helix	32	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P22139	UniProtKB	Helix	44	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P22139	UniProtKB	Helix	57	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+##sequence-region Q04307 1 110
+Q04307	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000121478;Note=DNA-directed RNA polymerase III subunit RPC10	
+Q04307	UniProtKB	Zinc finger	5	29	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04307	UniProtKB	Zinc finger	65	108	.	.	.	Note=TFIIS-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00472	
+##sequence-region P25441 1 422
+P25441	UniProtKB	Chain	1	422	.	.	.	ID=PRO_0000073969;Note=DNA-directed RNA polymerase III subunit RPC4	
+P25441	UniProtKB	Motif	25	29	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25441	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25441	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25441	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25441	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25441	UniProtKB	Modified residue	224	224	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956	
+P25441	UniProtKB	Modified residue	228	228	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P25441	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P25441	UniProtKB	Sequence conflict	42	42	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25441	UniProtKB	Sequence conflict	264	264	.	.	.	Note=L->LGL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25441	UniProtKB	Sequence conflict	284	285	.	.	.	Note=NA->KR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25441	UniProtKB	Sequence conflict	392	392	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12167 1 365
+Q12167	UniProtKB	Chain	1	365	.	.	.	ID=PRO_0000244438;Note=Required for respiratory growth protein 1%2C mitochondrial	
+Q12167	UniProtKB	Sequence conflict	364	364	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12754 1 1228
+Q12754	UniProtKB	Chain	1	1228	.	.	.	ID=PRO_0000270563;Note=Ribosomal RNA-processing protein 12	
+Q12754	UniProtKB	Modified residue	1059	1059	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12754	UniProtKB	Modified residue	1067	1067	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q06511 1 250
+Q06511	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000270562;Note=Ribosomal RNA-processing protein 15	
+Q06511	UniProtKB	Compositional bias	77	80	.	.	.	Note=Poly-Glu;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06511	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P32786 1 894
+P32786	UniProtKB	Chain	1	894	.	.	.	ID=PRO_0000097448;Note=RNA polymerase I-specific transcription initiation factor RRN6	
+P32786	UniProtKB	Compositional bias	882	888	.	.	.	Note=Lys-rich (basic)	
+P32786	UniProtKB	Sequence conflict	39	39	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32786	UniProtKB	Sequence conflict	39	39	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32786	UniProtKB	Sequence conflict	663	663	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32786	UniProtKB	Helix	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	61	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+P32786	UniProtKB	Beta strand	193	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	207	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	216	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	220	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	246	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	265	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	272	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	284	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	295	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	300	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	315	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	323	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	344	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	361	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	372	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	379	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Turn	385	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	389	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	404	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Turn	409	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+P32786	UniProtKB	Beta strand	414	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	422	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	428	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	439	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+P32786	UniProtKB	Beta strand	450	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	462	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	476	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Turn	485	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	488	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+P32786	UniProtKB	Beta strand	495	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	500	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+P32786	UniProtKB	Beta strand	505	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	535	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	546	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Helix	572	578	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Helix	583	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Helix	587	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Turn	613	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+P32786	UniProtKB	Helix	617	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Helix	645	647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	657	659	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Helix	664	667	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Helix	672	685	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	688	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Helix	697	704	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Helix	711	723	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Beta strand	725	727	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+P32786	UniProtKB	Helix	729	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Turn	752	754	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Helix	755	765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P32786	UniProtKB	Helix	768	773	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+##sequence-region P25359 1 394
+P25359	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25359	UniProtKB	Chain	2	394	.	.	.	ID=PRO_0000139970;Note=Exosome complex component RRP43	
+P25359	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25359	UniProtKB	Modified residue	26	26	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25359	UniProtKB	Mutagenesis	162	162	.	.	.	Note=Interaction with RRP46 abolished%3B when associated with T-246. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597	
+P25359	UniProtKB	Mutagenesis	212	212	.	.	.	Note=Interaction with RRP46 abolished. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597	
+P25359	UniProtKB	Mutagenesis	230	230	.	.	.	Note=Interaction with RRP46 abolished%3B when associated with T-274 and Y-276. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597	
+P25359	UniProtKB	Mutagenesis	246	246	.	.	.	Note=Interaction with RRP46 abolished%3B when associated with F-162. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597	
+P25359	UniProtKB	Mutagenesis	274	274	.	.	.	Note=Interaction with RRP46 abolished%3B when associated with Y-230 and Y-276. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597	
+P25359	UniProtKB	Mutagenesis	276	276	.	.	.	Note=Interaction with RRP46 abolished%3B when associated with Y-230 and T-274. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597	
+P25359	UniProtKB	Sequence conflict	102	102	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25359	UniProtKB	Sequence conflict	363	363	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25359	UniProtKB	Beta strand	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+P25359	UniProtKB	Helix	19	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Helix	27	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Turn	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+P25359	UniProtKB	Beta strand	52	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Helix	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1	
+P25359	UniProtKB	Beta strand	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Beta strand	75	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Beta strand	85	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Helix	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+P25359	UniProtKB	Helix	109	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+P25359	UniProtKB	Helix	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Beta strand	131	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Helix	146	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Helix	167	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Beta strand	175	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Beta strand	184	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Beta strand	209	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Helix	227	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Beta strand	242	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Beta strand	257	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+P25359	UniProtKB	Beta strand	265	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+P25359	UniProtKB	Beta strand	275	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Helix	288	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Beta strand	293	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Helix	304	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Helix	322	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+P25359	UniProtKB	Beta strand	327	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Helix	338	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Beta strand	345	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Turn	353	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+P25359	UniProtKB	Beta strand	357	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P25359	UniProtKB	Helix	371	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+##sequence-region P50943 1 142
+P50943	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000203437;Note=Putative regulator of rDNA transcription protein 16	
+P50943	UniProtKB	Transmembrane	19	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50943	UniProtKB	Transmembrane	84	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50943	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53117 1 311
+P53117	UniProtKB	Chain	1	311	.	.	.	ID=PRO_0000202734;Note=Regulator of rDNA transcription protein 6	
+P53117	UniProtKB	Transmembrane	32	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53117	UniProtKB	Transmembrane	271	291	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q01855 1 142
+Q01855	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260	
+Q01855	UniProtKB	Chain	2	142	.	.	.	ID=PRO_0000130051;Note=40S ribosomal protein S15	
+Q01855	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260	
+Q01855	UniProtKB	Cross-link	24	24	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q01855	UniProtKB	Cross-link	35	35	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q01855	UniProtKB	Cross-link	64	64	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q01855	UniProtKB	Beta strand	16	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Helix	22	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Helix	30	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Helix	39	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Beta strand	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Helix	54	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Beta strand	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Beta strand	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Helix	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Beta strand	93	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Helix	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Helix	116	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q01855	UniProtKB	Beta strand	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F	
+##sequence-region P38701 1 121
+P38701	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.4;Dbxref=PMID:22814378,PMID:10601260	
+P38701	UniProtKB	Chain	2	121	.	.	.	ID=PRO_0000146692;Note=40S ribosomal protein S20	
+P38701	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.4;Dbxref=PMID:22814378,PMID:10601260	
+P38701	UniProtKB	Cross-link	6	6	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38701	UniProtKB	Cross-link	8	8	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38701	UniProtKB	Cross-link	21	21	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38701	UniProtKB	Cross-link	32	32	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38701	UniProtKB	Cross-link	101	101	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38701	UniProtKB	Beta strand	22	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38701	UniProtKB	Helix	31	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38701	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N	
+P38701	UniProtKB	Beta strand	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38701	UniProtKB	Beta strand	61	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38701	UniProtKB	Beta strand	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38701	UniProtKB	Beta strand	79	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38701	UniProtKB	Helix	97	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P38701	UniProtKB	Beta strand	112	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0C0V8 1 87
+P0C0V8	UniProtKB	Chain	1	87	.	.	.	ID=PRO_0000194761;Note=40S ribosomal protein S21-A	
+P0C0V8	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P0C0V8	UniProtKB	Beta strand	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P0C0V8	UniProtKB	Turn	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0V8	UniProtKB	Beta strand	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0V8	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0V8	UniProtKB	Beta strand	50	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0V8	UniProtKB	Helix	57	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0V8	UniProtKB	Turn	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P0C0V8	UniProtKB	Helix	65	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0V8	UniProtKB	Turn	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0V8	UniProtKB	Beta strand	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P08518 1 1224
+P08518	UniProtKB	Chain	1	1224	.	.	.	ID=PRO_0000048091;Note=DNA-directed RNA polymerase II subunit RPB2	
+P08518	UniProtKB	Zinc finger	1163	1185	.	.	.	Note=C4-type	
+P08518	UniProtKB	Region	467	478	.	.	.	Note=Fork loop 1	
+P08518	UniProtKB	Metal binding	837	837	.	.	.	Note=Magnesium%3B shared with RPB1	
+P08518	UniProtKB	Metal binding	1163	1163	.	.	.	Note=Zinc	
+P08518	UniProtKB	Metal binding	1166	1166	.	.	.	Note=Zinc	
+P08518	UniProtKB	Metal binding	1182	1182	.	.	.	Note=Zinc	
+P08518	UniProtKB	Metal binding	1185	1185	.	.	.	Note=Zinc	
+P08518	UniProtKB	Modified residue	919	919	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P08518	UniProtKB	Sequence conflict	1003	1006	.	.	.	Note=AEGI->RRRY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08518	UniProtKB	Beta strand	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1M	
+P08518	UniProtKB	Helix	29	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I6H	
+P08518	UniProtKB	Helix	45	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	58	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P08518	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GTJ	
+P08518	UniProtKB	Beta strand	96	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P08518	UniProtKB	Helix	114	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	125	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	141	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2I	
+P08518	UniProtKB	Beta strand	166	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	176	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I3Q	
+P08518	UniProtKB	Helix	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	186	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	202	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	208	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	214	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	224	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	232	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	245	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	253	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	264	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K83	
+P08518	UniProtKB	Beta strand	269	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	277	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVQ	
+P08518	UniProtKB	Helix	282	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	294	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	308	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	321	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	327	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	337	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P08518	UniProtKB	Helix	342	344	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GTJ	
+P08518	UniProtKB	Helix	345	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	359	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWA	
+P08518	UniProtKB	Turn	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	367	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	371	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	390	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P08518	UniProtKB	Helix	401	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	404	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	409	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	434	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S2H	
+P08518	UniProtKB	Helix	444	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P08518	UniProtKB	Helix	451	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	467	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P08518	UniProtKB	Helix	474	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P08518	UniProtKB	Beta strand	477	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3	
+P08518	UniProtKB	Beta strand	480	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	488	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	497	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	510	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOU	
+P08518	UniProtKB	Helix	516	518	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	519	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	530	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	533	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K83	
+P08518	UniProtKB	Beta strand	536	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	552	560	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	563	565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P08518	UniProtKB	Helix	566	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	571	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	574	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P08518	UniProtKB	Beta strand	578	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	585	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	593	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	607	609	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	614	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	619	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	623	627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	633	641	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	646	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P08518	UniProtKB	Beta strand	650	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	655	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	681	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	689	694	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	695	698	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	703	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	707	710	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	725	727	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1N	
+P08518	UniProtKB	Beta strand	739	741	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P08518	UniProtKB	Helix	745	748	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	753	755	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	756	758	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	759	761	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	764	773	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	774	776	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	779	781	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YU9	
+P08518	UniProtKB	Turn	783	787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	791	798	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	803	805	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	809	812	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	813	816	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	821	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	829	832	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	833	837	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	838	842	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	843	847	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	848	851	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	853	861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	866	869	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWC	
+P08518	UniProtKB	Beta strand	873	875	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	880	882	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	886	888	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR	
+P08518	UniProtKB	Helix	890	892	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	895	899	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOU	
+P08518	UniProtKB	Beta strand	904	906	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ	
+P08518	UniProtKB	Beta strand	910	912	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	914	916	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K83	
+P08518	UniProtKB	Beta strand	935	940	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P08518	UniProtKB	Beta strand	947	956	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	958	960	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	962	972	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	979	981	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	983	985	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50	
+P08518	UniProtKB	Beta strand	987	994	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	996	998	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	1009	1012	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	1014	1016	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	1018	1021	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	1023	1038	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	1046	1049	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	1052	1060	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	1061	1063	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	1068	1070	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	1071	1073	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q	
+P08518	UniProtKB	Turn	1075	1077	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	1080	1084	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q	
+P08518	UniProtKB	Beta strand	1085	1097	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	1099	1101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	1104	1106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	1113	1115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P08518	UniProtKB	Helix	1122	1124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P08518	UniProtKB	Beta strand	1128	1130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14	
+P08518	UniProtKB	Helix	1132	1141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	1144	1151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	1152	1156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7	
+P08518	UniProtKB	Beta strand	1159	1166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	1172	1174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	1175	1178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	1179	1182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Turn	1183	1186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	1187	1195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Helix	1198	1209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+P08518	UniProtKB	Beta strand	1215	1218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF	
+##sequence-region P32561 1 433
+P32561	UniProtKB	Chain	1	433	.	.	.	ID=PRO_0000114724;Note=Histone deacetylase RPD3	
+P32561	UniProtKB	Region	19	331	.	.	.	Note=Histone deacetylase	
+P32561	UniProtKB	Motif	320	340	.	.	.	Note=ESA1-RPD3 motif	
+P32561	UniProtKB	Active site	151	151	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32561	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P32561	UniProtKB	Modified residue	408	408	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32561	UniProtKB	Mutagenesis	150	150	.	.	.	Note=Impairs histone deacetylase activity and transcription repression. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9512514;Dbxref=PMID:9512514	
+P32561	UniProtKB	Mutagenesis	151	151	.	.	.	Note=Impairs histone deacetylase activity and transcription repression. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9512514;Dbxref=PMID:9512514	
+P32561	UniProtKB	Mutagenesis	188	188	.	.	.	Note=Impairs histone deacetylase activity and transcription repression. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9512514;Dbxref=PMID:9512514	
+P32561	UniProtKB	Mutagenesis	322	322	.	.	.	Note=Reduces strongly HDAC activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+P32561	UniProtKB	Mutagenesis	325	325	.	.	.	Note=Reduces strongly HDAC activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+P32561	UniProtKB	Mutagenesis	327	327	.	.	.	Note=Reduces strongly HDAC activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+P32561	UniProtKB	Mutagenesis	328	328	.	.	.	Note=Reduces strongly HDAC activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+P32561	UniProtKB	Mutagenesis	329	329	.	.	.	Note=Reduces strongly HDAC activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+P32561	UniProtKB	Mutagenesis	332	332	.	.	.	Note=Reduces strongly HDAC activity. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+P32561	UniProtKB	Mutagenesis	334	334	.	.	.	Note=Reduces strongly HDAC activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+P32561	UniProtKB	Mutagenesis	335	335	.	.	.	Note=Reduces strongly HDAC activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+P32561	UniProtKB	Mutagenesis	338	338	.	.	.	Note=Reduces strongly HDAC activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+P32561	UniProtKB	Mutagenesis	339	339	.	.	.	Note=Reduces strongly HDAC activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674	
+##sequence-region P38805 1 295
+P38805	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000120255;Note=Ribosome production factor 1	
+P38805	UniProtKB	Domain	93	276	.	.	.	Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034	
+P38805	UniProtKB	Region	254	271	.	.	.	Note=RNA-binding	
+##sequence-region P43588 1 306
+P43588	UniProtKB	Chain	1	306	.	.	.	ID=PRO_0000213960;Note=Ubiquitin carboxyl-terminal hydrolase RPN11	
+P43588	UniProtKB	Domain	27	162	.	.	.	Note=MPN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+P43588	UniProtKB	Motif	109	122	.	.	.	Note=JAMM motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+P43588	UniProtKB	Metal binding	109	109	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+P43588	UniProtKB	Metal binding	111	111	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+P43588	UniProtKB	Metal binding	122	122	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+P43588	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+P43588	UniProtKB	Natural variant	208	208	.	.	.	Note=In strain: NRRL Y-53. K->Q	
+P43588	UniProtKB	Natural variant	239	239	.	.	.	Note=In strain: NRRL Y-53. A->T	
+P43588	UniProtKB	Natural variant	262	262	.	.	.	Note=In strain: NRRL Y-53. T->S	
+P43588	UniProtKB	Natural variant	280	281	.	.	.	Note=In strain: NRRL Y-53. LS->IF	
+P43588	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Stabilizes ubiquitin pathway substrates%3B when associated wirh Ala-111. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12183636;Dbxref=PMID:12183636	
+P43588	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Stabilizes ubiquitin pathway substrates%3B when associated wirh Ala-109. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12183636;Dbxref=PMID:12183636	
+P43588	UniProtKB	Beta strand	26	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Helix	31	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Beta strand	50	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Beta strand	62	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Helix	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Helix	85	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Turn	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Beta strand	103	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Beta strand	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OCM	
+P43588	UniProtKB	Helix	120	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Beta strand	137	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Turn	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Beta strand	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P43588	UniProtKB	Beta strand	153	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Helix	162	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OCM	
+P43588	UniProtKB	Helix	182	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OCM	
+P43588	UniProtKB	Beta strand	195	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Beta strand	200	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Helix	207	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Turn	214	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+P43588	UniProtKB	Turn	220	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P43588	UniProtKB	Helix	230	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P43588	UniProtKB	Helix	263	270	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P43588	UniProtKB	Helix	276	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+##sequence-region P38764 1 993
+P38764	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+P38764	UniProtKB	Chain	2	993	.	.	.	ID=PRO_0000173815;Note=26S proteasome regulatory subunit RPN1	
+P38764	UniProtKB	Repeat	417	449	.	.	.	Note=PC 1	
+P38764	UniProtKB	Repeat	450	487	.	.	.	Note=PC 2	
+P38764	UniProtKB	Repeat	488	522	.	.	.	Note=PC 3	
+P38764	UniProtKB	Repeat	523	563	.	.	.	Note=PC 4	
+P38764	UniProtKB	Repeat	566	598	.	.	.	Note=PC 5	
+P38764	UniProtKB	Repeat	778	809	.	.	.	Note=PC 6	
+P38764	UniProtKB	Repeat	810	844	.	.	.	Note=PC 7	
+P38764	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38764	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38764	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38764	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38764	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38764	UniProtKB	Modified residue	695	695	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38764	UniProtKB	Helix	485	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T	
+P38764	UniProtKB	Helix	497	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T	
+P38764	UniProtKB	Helix	503	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T	
+P38764	UniProtKB	Beta strand	516	518	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T	
+P38764	UniProtKB	Helix	520	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T	
+P38764	UniProtKB	Helix	540	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T	
+P38764	UniProtKB	Helix	555	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T	
+P38764	UniProtKB	Helix	562	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T	
+P38764	UniProtKB	Turn	573	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T	
+P38764	UniProtKB	Helix	579	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T	
+P38764	UniProtKB	Turn	594	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3U	
+P38764	UniProtKB	Helix	597	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T	
+P38764	UniProtKB	Turn	608	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3U	
+##sequence-region P40016 1 523
+P40016	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+P40016	UniProtKB	Chain	2	523	.	.	.	ID=PRO_0000173827;Note=26S proteasome regulatory subunit RPN3	
+P40016	UniProtKB	Domain	343	447	.	.	.	Note=PCI	
+P40016	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+P40016	UniProtKB	Modified residue	454	454	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40016	UniProtKB	Sequence conflict	355	355	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40016	UniProtKB	Sequence conflict	355	355	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40016	UniProtKB	Helix	132	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	153	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	163	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	175	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	201	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	227	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	248	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	266	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	289	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Beta strand	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	307	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	330	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Beta strand	334	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	337	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	343	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	357	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	376	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Turn	381	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	384	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Beta strand	400	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	404	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	416	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Beta strand	434	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Turn	438	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Beta strand	442	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+P40016	UniProtKB	Helix	456	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+##sequence-region P13433 1 1351
+P13433	UniProtKB	Active site	945	945	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13433	UniProtKB	Active site	1014	1014	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13433	UniProtKB	Active site	1189	1189	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13433	UniProtKB	Sequence conflict	485	485	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13433	UniProtKB	Sequence conflict	900	901	.	.	.	Note=NP->KS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06109 1 277
+Q06109	UniProtKB	Chain	1	277	.	.	.	ID=PRO_0000242626;Note=Required for respiratory growth protein 8%2C mitochondrial	
+##sequence-region Q02983 1 363
+Q02983	UniProtKB	Chain	1	363	.	.	.	ID=PRO_0000097447;Note=RNA polymerase I-specific transcription initiation factor RRN5	
+Q02983	UniProtKB	Sequence conflict	25	25	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02983	UniProtKB	Sequence conflict	197	198	.	.	.	Note=SA->RP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02983	UniProtKB	Sequence conflict	260	260	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38204 1 145
+P38204	UniProtKB	Chain	1	145	.	.	.	ID=PRO_0000097445;Note=RNA polymerase I-specific transcription initiation factor RRN10	
+##sequence-region P40992 1 514
+P40992	UniProtKB	Chain	1	514	.	.	.	ID=PRO_0000097450;Note=RNA polymerase I-specific transcription initiation factor RRN7	
+P40992	UniProtKB	Zinc finger	3	36	.	.	.	Note=RRN7-type	
+P40992	UniProtKB	Region	37	66	.	.	.	Note=B-reader	
+P40992	UniProtKB	Region	67	101	.	.	.	Note=B-linker	
+P40992	UniProtKB	Region	102	210	.	.	.	Note=N-terminal cyclin fold	
+P40992	UniProtKB	Region	211	320	.	.	.	Note=C-terminal cyclin fold	
+P40992	UniProtKB	Compositional bias	71	87	.	.	.	Note=Gln-rich	
+P40992	UniProtKB	Metal binding	10	10	.	.	.	Note=Zinc;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40992	UniProtKB	Metal binding	15	15	.	.	.	Note=Zinc;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40992	UniProtKB	Metal binding	29	29	.	.	.	Note=Zinc;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40992	UniProtKB	Metal binding	33	33	.	.	.	Note=Zinc;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40992	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Impaired binding to Pol I. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21921198;Dbxref=PMID:21921198	
+P40992	UniProtKB	Mutagenesis	33	33	.	.	.	Note=Impaired binding to Pol I. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21921198;Dbxref=PMID:21921198	
+P40992	UniProtKB	Beta strand	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+P40992	UniProtKB	Helix	101	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	128	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	158	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	178	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Beta strand	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+P40992	UniProtKB	Beta strand	193	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	209	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Turn	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	225	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Turn	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	249	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	265	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Beta strand	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Beta strand	294	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+P40992	UniProtKB	Helix	302	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	330	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	345	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Beta strand	358	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	362	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	371	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	406	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	438	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	472	490	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+P40992	UniProtKB	Helix	495	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+##sequence-region P0CX47 1 156
+P0CX47	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921	
+P0CX47	UniProtKB	Chain	2	156	.	.	.	ID=PRO_0000128523;Note=40S ribosomal protein S11-A	
+P0CX47	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921	
+P0CX47	UniProtKB	Cross-link	15	15	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX47	UniProtKB	Cross-link	46	46	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX47	UniProtKB	Cross-link	56	56	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX47	UniProtKB	Cross-link	57	57	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX47	UniProtKB	Cross-link	79	79	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX47	UniProtKB	Cross-link	96	96	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX47	UniProtKB	Cross-link	105	105	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX47	UniProtKB	Cross-link	133	133	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX47	UniProtKB	Cross-link	141	141	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX47	UniProtKB	Cross-link	148	148	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX47	UniProtKB	Sequence conflict	12	13	.	.	.	Note=AF->FA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CX47	UniProtKB	Beta strand	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Beta strand	23	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P0CX47	UniProtKB	Beta strand	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Helix	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Turn	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Beta strand	70	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Beta strand	83	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Turn	95	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Beta strand	99	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Beta strand	122	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Beta strand	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Beta strand	137	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Beta strand	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX47	UniProtKB	Helix	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P22276 1 1149
+P22276	UniProtKB	Chain	1	1149	.	.	.	ID=PRO_0000048096;Note=DNA-directed RNA polymerase III subunit RPC2	
+P22276	UniProtKB	Zinc finger	1095	1110	.	.	.	Note=C4-type;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22276	UniProtKB	Metal binding	1095	1095	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22276	UniProtKB	Metal binding	1098	1098	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22276	UniProtKB	Metal binding	1107	1107	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22276	UniProtKB	Metal binding	1110	1110	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22276	UniProtKB	Sequence conflict	213	213	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32910 1 317
+P32910	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000073977;Note=DNA-directed RNA polymerase III subunit RPC6	
+P32910	UniProtKB	Mutagenesis	89	89	.	.	.	Note=Cold-sensitive. Abolishes interaction with BRF1/TDS4. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9312031;Dbxref=PMID:9312031	
+P32910	UniProtKB	Mutagenesis	102	103	.	.	.	Note=Cold-sensitive. No effect on interaction with BRF1/TDS4. RE->VA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9312031;Dbxref=PMID:9312031	
+P32910	UniProtKB	Mutagenesis	135	138	.	.	.	Note=Temperature-sensitive%3B cold-sensitive. Abolishes interaction with BRF1/TDS4. Stabilizes Pol III open complex formation. KSVK->ASVA	
+P32910	UniProtKB	Mutagenesis	135	135	.	.	.	Note=Cold-sensitive. Abolishes interaction with BRF1/TDS4. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9312031;Dbxref=PMID:9312031	
+P32910	UniProtKB	Mutagenesis	171	173	.	.	.	Note=Cold-sensitive. Abolishes interaction with BRF1/TDS4. DIE->AIA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9312031;Dbxref=PMID:9312031	
+P32910	UniProtKB	Mutagenesis	171	171	.	.	.	Note=Cold-sensitive. Abolishes interaction with BRF1/TDS4. D->H	
+##sequence-region P36160 1 344
+P36160	UniProtKB	Chain	1	344	.	.	.	ID=PRO_0000120256;Note=Ribosome biogenesis protein RPF2	
+P36160	UniProtKB	Domain	28	243	.	.	.	Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034	
+P36160	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P36160	UniProtKB	Beta strand	30	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Helix	40	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Beta strand	56	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Turn	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Helix	73	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Beta strand	85	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Beta strand	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Beta strand	99	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Beta strand	109	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Helix	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Beta strand	140	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Helix	147	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Helix	152	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Beta strand	171	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Helix	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Beta strand	180	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Beta strand	199	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Beta strand	220	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Beta strand	229	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+P36160	UniProtKB	Helix	242	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+##sequence-region O13563 1 156
+O13563	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+O13563	UniProtKB	Chain	2	156	.	.	.	ID=PRO_0000268704;Note=26S proteasome regulatory subunit RPN13	
+O13563	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+O13563	UniProtKB	Modified residue	133	133	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+O13563	UniProtKB	Modified residue	135	135	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+O13563	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+O13563	UniProtKB	Alternative sequence	1	2	.	.	.	ID=VSP_058121;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+O13563	UniProtKB	Beta strand	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Beta strand	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Turn	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Beta strand	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Beta strand	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Turn	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Beta strand	46	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Beta strand	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Turn	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Beta strand	73	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Beta strand	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Beta strand	86	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+O13563	UniProtKB	Beta strand	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D	
+##sequence-region Q08723 1 338
+Q08723	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+Q08723	UniProtKB	Chain	2	338	.	.	.	ID=PRO_0000213951;Note=26S proteasome regulatory subunit RPN8	
+Q08723	UniProtKB	Domain	8	143	.	.	.	Note=MPN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182	
+Q08723	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901	
+Q08723	UniProtKB	Modified residue	314	314	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08723	UniProtKB	Modified residue	317	317	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08723	UniProtKB	Modified residue	319	319	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+Q08723	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08723	UniProtKB	Sequence conflict	126	126	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08723	UniProtKB	Beta strand	7	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Helix	12	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Beta strand	34	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Beta strand	42	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Beta strand	56	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Beta strand	62	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Helix	70	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Beta strand	87	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Beta strand	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q08723	UniProtKB	Helix	103	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Beta strand	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Beta strand	119	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Beta strand	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Beta strand	133	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Turn	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OCN	
+Q08723	UniProtKB	Beta strand	151	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Beta strand	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Helix	165	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y	
+Q08723	UniProtKB	Helix	186	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q08723	UniProtKB	Helix	223	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+Q08723	UniProtKB	Helix	261	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK	
+##sequence-region Q12532 1 1038
+Q12532	UniProtKB	Chain	1	1038	.	.	.	ID=PRO_0000244627;Note=Ribosome quality control complex subunit 2	
+Q12532	UniProtKB	Coiled coil	350	383	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12532	UniProtKB	Coiled coil	713	768	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12532	UniProtKB	Coiled coil	830	912	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12532	UniProtKB	Compositional bias	720	752	.	.	.	Note=Poly-Glu	
+Q12532	UniProtKB	Modified residue	797	797	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12532	UniProtKB	Mutagenesis	9	9	.	.	.	Note=Abolishes CAT tail synthesis and heat shock response%2C but still binds to 60S ribosomal subunits and supports LTN1-dependent ubiquitination of nascent chains%3B when associated with A-98 and A-99. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25554787;Dbxref=PMID:25554787	
+Q12532	UniProtKB	Mutagenesis	98	98	.	.	.	Note=Abolishes CAT tail synthesis and heat shock response%2C but still binds to 60S ribosomal subunits and supports LTN1-dependent ubiquitination of nascent chains%3B when associated with A-9 and A-99. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25554787;Dbxref=PMID:25554787	
+Q12532	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Abolishes CAT tail synthesis and heat shock response%2C but still binds to 60S ribosomal subunits and supports LTN1-dependent ubiquitination of nascent chains%3B when associated with A-9 and A-98. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25554787;Dbxref=PMID:25554787	
+##sequence-region P53437 1 365
+P53437	UniProtKB	Chain	1	365	.	.	.	ID=PRO_0000097451;Note=RNA polymerase I-specific transcription initiation factor RRN9	
+P53437	UniProtKB	Sequence conflict	255	255	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04031 1 235
+Q04031	UniProtKB	Chain	1	235	.	.	.	ID=PRO_0000253822;Note=Ribosomal RNA-processing protein 17	
+Q04031	UniProtKB	Coiled coil	49	110	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04031	UniProtKB	Modified residue	113	113	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04031	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04031	UniProtKB	Modified residue	122	122	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P38961 1 392
+P38961	UniProtKB	Chain	1	392	.	.	.	ID=PRO_0000202594;Note=25S rRNA (adenine(645)-N(1))-methyltransferase	
+P38961	UniProtKB	Coiled coil	32	61	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38961	UniProtKB	Coiled coil	344	382	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38961	UniProtKB	Binding site	156	156	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43159	
+P38961	UniProtKB	Binding site	207	207	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43159	
+P38961	UniProtKB	Binding site	242	242	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43159	
+P38961	UniProtKB	Binding site	254	254	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43159	
+P38961	UniProtKB	Binding site	271	271	.	.	.	Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43159	
+P38961	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38961	UniProtKB	Mutagenesis	209	209	.	.	.	Note=Impaired methyltransferase activity and ribosomal 60S subunit biogenesis. Does not affect pre-rRNA cleavage at site A2 activity. G->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23180764;Dbxref=PMID:23180764	
+P38961	UniProtKB	Mutagenesis	390	390	.	.	.	Note=In RRP8-1%3B no effect. Synthetic lethal with GAR1 mutant allele lacking its N- and C-terminal glycine/arginine-rich (GAR) domains. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10864042;Dbxref=PMID:10864042	
+##sequence-region P40571 1 144
+P40571	UniProtKB	Chain	1	144	.	.	.	ID=PRO_0000153847;Note=Ribonuclease P protein subunit RPR2	
+P40571	UniProtKB	Metal binding	90	90	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40571	UniProtKB	Metal binding	93	93	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40571	UniProtKB	Metal binding	115	115	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40571	UniProtKB	Metal binding	117	117	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P39677 1 819
+P39677	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03059	
+P39677	UniProtKB	Chain	31	819	.	.	.	ID=PRO_0000007453;Note=Ribosome-releasing factor 2%2C mitochondrial	
+P39677	UniProtKB	Domain	39	327	.	.	.	Note=tr-type G	
+P39677	UniProtKB	Nucleotide binding	48	55	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03059	
+P39677	UniProtKB	Nucleotide binding	113	117	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03059	
+P39677	UniProtKB	Nucleotide binding	165	168	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03059	
+##sequence-region Q08774 1 242
+Q08774	UniProtKB	Chain	1	242	.	.	.	ID=PRO_0000245286;Note=Required for respiratory growth protein 7%2C mitochondrial	
+##sequence-region Q04712 1 507
+Q04712	UniProtKB	Chain	1	507	.	.	.	ID=PRO_0000203257;Note=RNA polymerase I-specific transcription initiation factor RRN11	
+Q04712	UniProtKB	Helix	11	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Helix	75	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Beta strand	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+Q04712	UniProtKB	Helix	159	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Helix	169	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Helix	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Helix	182	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Beta strand	196	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Helix	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Helix	208	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Helix	229	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Helix	250	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Beta strand	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Helix	267	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Beta strand	278	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Beta strand	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Beta strand	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+Q04712	UniProtKB	Helix	307	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Helix	346	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Beta strand	353	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+Q04712	UniProtKB	Helix	362	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Helix	402	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+Q04712	UniProtKB	Turn	418	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61	
+Q04712	UniProtKB	Helix	429	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X	
+##sequence-region P36080 1 434
+P36080	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P36080	UniProtKB	Chain	2	434	.	.	.	ID=PRO_0000203167;Note=Ribosomal RNA-processing protein 14	
+P36080	UniProtKB	Coiled coil	162	230	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36080	UniProtKB	Coiled coil	293	360	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36080	UniProtKB	Compositional bias	122	130	.	.	.	Note=Asp/Glu-rich (acidic)	
+P36080	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P46948 1 246
+P46948	UniProtKB	Chain	1	246	.	.	.	ID=PRO_0000139962;Note=Exosome complex component SKI6	
+P46948	UniProtKB	Mutagenesis	62	63	.	.	.	Note=Impairs RNA-binding (at the proposed ring entry site). KS->ED;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19879841;Dbxref=PMID:19879841	
+P46948	UniProtKB	Mutagenesis	95	96	.	.	.	Note=Impairs RNA-binding (at the proposed ring exit site). RR->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19879841;Dbxref=PMID:19879841	
+P46948	UniProtKB	Beta strand	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1	
+P46948	UniProtKB	Beta strand	25	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Turn	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	37	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	47	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	60	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	71	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	82	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Helix	95	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Turn	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	121	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Helix	135	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	158	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	169	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Helix	176	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	182	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Beta strand	193	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Helix	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P46948	UniProtKB	Helix	210	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+##sequence-region Q12277 1 265
+Q12277	UniProtKB	Chain	1	265	.	.	.	ID=PRO_0000139966;Note=Exosome complex component RRP42	
+Q12277	UniProtKB	Helix	5	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	34	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	44	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1	
+Q12277	UniProtKB	Beta strand	57	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Turn	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	76	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Helix	90	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Turn	105	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Helix	111	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	117	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Helix	138	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	153	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Turn	163	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q12277	UniProtKB	Beta strand	171	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	186	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	196	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Helix	203	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	210	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	226	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Beta strand	233	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Helix	241	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q12277	UniProtKB	Helix	256	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+##sequence-region P53256 1 223
+P53256	UniProtKB	Chain	1	223	.	.	.	ID=PRO_0000139978;Note=Exosome complex component RRP46	
+P53256	UniProtKB	Beta strand	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Beta strand	11	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Beta strand	24	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Turn	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Beta strand	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Beta strand	47	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Beta strand	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Helix	61	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Helix	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Beta strand	87	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Turn	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Helix	106	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Beta strand	127	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Turn	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Beta strand	145	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Helix	151	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Beta strand	157	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Turn	169	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Beta strand	173	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Helix	188	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P53256	UniProtKB	Helix	218	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+##sequence-region P40470 1 206
+P40470	UniProtKB	Chain	1	206	.	.	.	ID=PRO_0000202961;Note=Regulator of rDNA transcription protein 14	
+P40470	UniProtKB	Compositional bias	66	100	.	.	.	Note=Lys-rich	
+P40470	UniProtKB	Modified residue	197	197	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40470	UniProtKB	Modified residue	202	202	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40470	UniProtKB	Modified residue	203	203	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P43607 1 289
+P43607	UniProtKB	Chain	1	289	.	.	.	ID=PRO_0000082029;Note=Regulator of rDNA transcription protein 5	
+P43607	UniProtKB	Domain	18	105	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+##sequence-region Q08219 1 342
+Q08219	UniProtKB	Chain	1	342	.	.	.	ID=PRO_0000203488;Note=Outer spore wall protein RRT8	
+Q08219	UniProtKB	Topological domain	1	109	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q08219	UniProtKB	Transmembrane	110	130	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08219	UniProtKB	Topological domain	131	131	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q08219	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08219	UniProtKB	Topological domain	153	240	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q08219	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08219	UniProtKB	Topological domain	262	299	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+Q08219	UniProtKB	Transmembrane	300	320	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08219	UniProtKB	Topological domain	321	342	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+Q08219	UniProtKB	Sequence conflict	138	138	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P07281 1 144
+P07281	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:6814480;Dbxref=PMID:10601260,PMID:6814480	
+P07281	UniProtKB	Chain	2	144	.	.	.	ID=PRO_0000153836;Note=40S ribosomal protein S19-B	
+##sequence-region Q3E792 1 108
+Q3E792	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+Q3E792	UniProtKB	Chain	2	108	.	.	.	ID=PRO_0000043376;Note=40S ribosomal protein S25-A	
+Q3E792	UniProtKB	Modified residue	2	2	.	.	.	Note=N%2CN-dimethylproline%3B by NTM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20481588;Dbxref=PMID:20481588	
+Q3E792	UniProtKB	Natural variant	8	8	.	.	.	Note=In strain: SK1. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+Q3E792	UniProtKB	Natural variant	13	13	.	.	.	Note=In strain: SK1. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+Q3E792	UniProtKB	Sequence conflict	16	16	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q3E792	UniProtKB	Beta strand	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E792	UniProtKB	Helix	45	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E792	UniProtKB	Helix	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E792	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E792	UniProtKB	Helix	62	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E792	UniProtKB	Helix	73	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E792	UniProtKB	Beta strand	84	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E792	UniProtKB	Beta strand	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+Q3E792	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P39939 1 119
+P39939	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000204529;Note=40S ribosomal protein S26-B	
+P39939	UniProtKB	Sequence conflict	110	110	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39939	UniProtKB	Beta strand	6	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39939	UniProtKB	Beta strand	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39939	UniProtKB	Turn	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39939	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39939	UniProtKB	Turn	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39939	UniProtKB	Beta strand	37	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39939	UniProtKB	Helix	49	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39939	UniProtKB	Beta strand	58	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39939	UniProtKB	Beta strand	66	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39939	UniProtKB	Helix	76	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39939	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F	
+P39939	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P41058 1 56
+P41058	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943	
+P41058	UniProtKB	Chain	2	56	.	.	.	ID=PRO_0000131033;Note=40S ribosomal protein S29-B	
+P41058	UniProtKB	Metal binding	21	21	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41058	UniProtKB	Metal binding	24	24	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41058	UniProtKB	Metal binding	39	39	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41058	UniProtKB	Metal binding	42	42	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41058	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41058	UniProtKB	Sequence conflict	7	7	.	.	.	Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P26783 1 225
+P26783	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921	
+P26783	UniProtKB	Chain	2	225	.	.	.	ID=PRO_0000124540;Note=40S ribosomal protein S5	
+P26783	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921	
+P26783	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P26783	UniProtKB	Cross-link	45	45	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P26783	UniProtKB	Cross-link	203	203	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P26783	UniProtKB	Sequence conflict	21	21	.	.	.	Note=T->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P26783	UniProtKB	Helix	31	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Beta strand	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P26783	UniProtKB	Turn	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Turn	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Helix	83	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Helix	89	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Helix	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Helix	107	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Helix	129	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Beta strand	143	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Beta strand	151	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Beta strand	157	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Helix	164	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Beta strand	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Helix	190	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26783	UniProtKB	Beta strand	206	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P26783	UniProtKB	Helix	209	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P48164 1 190
+P48164	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P48164	UniProtKB	Chain	2	190	.	.	.	ID=PRO_0000174213;Note=40S ribosomal protein S7-B	
+P48164	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P48164	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P48164	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q06488 1 889
+Q06488	UniProtKB	Chain	1	889	.	.	.	ID=PRO_0000211212;Note=Chromatin structure-remodeling complex subunit RSC2	
+Q06488	UniProtKB	Domain	35	103	.	.	.	Note=Bromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+Q06488	UniProtKB	Domain	295	365	.	.	.	Note=Bromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+Q06488	UniProtKB	Domain	408	526	.	.	.	Note=BAH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370	
+Q06488	UniProtKB	Compositional bias	667	716	.	.	.	Note=Gln-rich	
+Q06488	UniProtKB	Modified residue	612	612	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06488	UniProtKB	Modified residue	682	682	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q06488	UniProtKB	Mutagenesis	468	468	.	.	.	Note=In dpm3%3B defective in plasmid maintenance. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12024034;Dbxref=PMID:12024034	
+Q06488	UniProtKB	Mutagenesis	601	601	.	.	.	Note=In dpm18%3B defective in plasmid maintenance. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12024034;Dbxref=PMID:12024034	
+Q06488	UniProtKB	Beta strand	403	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	408	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	415	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	428	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	443	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Helix	453	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	462	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	470	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Helix	480	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	483	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	488	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Helix	492	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	498	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	508	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	513	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Turn	517	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	521	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Helix	528	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Helix	534	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	543	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	547	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Helix	559	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	621	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Turn	627	630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+Q06488	UniProtKB	Beta strand	631	633	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7	
+##sequence-region P43609 1 557
+P43609	UniProtKB	Chain	1	557	.	.	.	ID=PRO_0000197114;Note=Chromatin structure-remodeling complex protein RSC8	
+P43609	UniProtKB	Domain	80	177	.	.	.	Note=SWIRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00247	
+P43609	UniProtKB	Domain	310	362	.	.	.	Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624	
+P43609	UniProtKB	Zinc finger	254	298	.	.	.	Note=ZZ-type	
+P43609	UniProtKB	Coiled coil	38	77	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43609	UniProtKB	Coiled coil	462	494	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43609	UniProtKB	Modified residue	485	485	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43609	UniProtKB	Mutagenesis	347	351	.	.	.	Note=Loss of function. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12419236;Dbxref=PMID:12419236	
+P43609	UniProtKB	Sequence conflict	192	192	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03246 1 237
+Q03246	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000128525;Note=37S ribosomal protein S17%2C mitochondrial	
+##sequence-region P36056 1 628
+P36056	UniProtKB	Transit peptide	1	15	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36056	UniProtKB	Chain	16	628	.	.	.	ID=PRO_0000203144;Note=Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22%2C mitochondrial	
+##sequence-region Q03976 1 319
+Q03976	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03976	UniProtKB	Chain	31	319	.	.	.	ID=PRO_0000268705;Note=37S ribosomal protein S24%2C mitochondrial	
+##sequence-region Q02950 1 344
+Q02950	UniProtKB	Chain	1	344	.	.	.	ID=PRO_0000087701;Note=37S ribosomal protein MRP51%2C mitochondrial	
+Q02950	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02950	UniProtKB	Mutagenesis	235	235	.	.	.	Note=Suppresses defects in the 5'UTLs of COX2 and COX3 mitochondrial mRNAs. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754	
+Q02950	UniProtKB	Mutagenesis	241	241	.	.	.	Note=Suppresses defects in the 5'UTLs of COX2 and COX3 mitochondrial mRNAs. N->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754	
+Q02950	UniProtKB	Mutagenesis	260	260	.	.	.	Note=Suppresses defects in the 5'UTLs of COX2 and COX3 mitochondrial mRNAs. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754	
+Q02950	UniProtKB	Mutagenesis	261	261	.	.	.	Note=Suppresses defects in the 5'UTLs of COX2 and COX3 mitochondrial mRNAs. P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754	
+Q02950	UniProtKB	Mutagenesis	279	279	.	.	.	Note=Suppresses defects in the 5'UTLs of COX2 and COX3 mitochondrial mRNAs. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754	
+##sequence-region Q03919 1 77
+Q03919	UniProtKB	Chain	1	76	.	.	.	ID=PRO_0000035979;Note=NEDD8-like protein RUB1	
+Q03919	UniProtKB	Propeptide	77	77	.	.	.	ID=PRO_0000035980;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03919	UniProtKB	Domain	1	74	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+Q03919	UniProtKB	Cross-link	76	76	.	.	.	Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+##sequence-region Q12464 1 471
+Q12464	UniProtKB	Chain	1	471	.	.	.	ID=PRO_0000165675;Note=RuvB-like protein 2	
+Q12464	UniProtKB	Nucleotide binding	75	82	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12464	UniProtKB	Mutagenesis	75	75	.	.	.	Note=Lethal. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11604509;Dbxref=PMID:11604509	
+Q12464	UniProtKB	Mutagenesis	80	80	.	.	.	Note=Growth defect at 37 degrees Celsius. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11604509;Dbxref=PMID:11604509	
+Q12464	UniProtKB	Mutagenesis	81	81	.	.	.	Note=Defect in snoRNA accumulation. Growth defect at 37 degrees Celsius. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10787406,ECO:0000269|PubMed:11278922,ECO:0000269|PubMed:11604509;Dbxref=PMID:10787406,PMID:11278922,PMID:11604509	
+Q12464	UniProtKB	Mutagenesis	81	81	.	.	.	Note=Lethal. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10787406,ECO:0000269|PubMed:11278922,ECO:0000269|PubMed:11604509;Dbxref=PMID:10787406,PMID:11278922,PMID:11604509	
+Q12464	UniProtKB	Mutagenesis	81	81	.	.	.	Note=Growth defect at 37 degrees Celsius. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10787406,ECO:0000269|PubMed:11278922,ECO:0000269|PubMed:11604509;Dbxref=PMID:10787406,PMID:11278922,PMID:11604509	
+Q12464	UniProtKB	Mutagenesis	296	296	.	.	.	Note=Lethal. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11604509;Dbxref=PMID:11604509	
+Q12464	UniProtKB	Mutagenesis	297	297	.	.	.	Note=Lethal. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278922;Dbxref=PMID:11278922	
+##sequence-region Q3E754 1 87
+Q3E754	UniProtKB	Chain	1	87	.	.	.	ID=PRO_0000194762;Note=40S ribosomal protein S21-B	
+Q3E754	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+##sequence-region P0CX31 1 135
+P0CX31	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921	
+P0CX31	UniProtKB	Chain	2	135	.	.	.	ID=PRO_0000137636;Note=40S ribosomal protein S24-A	
+P0CX31	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921	
+P0CX31	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P0CX31	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX31	UniProtKB	Cross-link	21	21	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX31	UniProtKB	Sequence conflict	16	16	.	.	.	Note=P->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CX31	UniProtKB	Beta strand	7	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX31	UniProtKB	Helix	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX31	UniProtKB	Beta strand	20	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX31	UniProtKB	Beta strand	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P0CX31	UniProtKB	Helix	37	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX31	UniProtKB	Turn	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX31	UniProtKB	Helix	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX31	UniProtKB	Beta strand	55	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX31	UniProtKB	Beta strand	66	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX31	UniProtKB	Helix	79	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX31	UniProtKB	Helix	88	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX31	UniProtKB	Beta strand	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U52	
+P0CX31	UniProtKB	Helix	105	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX31	UniProtKB	Beta strand	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56	
+P0CX31	UniProtKB	Helix	123	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region Q08932 1 381
+Q08932	UniProtKB	Chain	1	381	.	.	.	ID=PRO_0000097460;Note=Ribosome assembly 1 protein	
+Q08932	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08932	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08932	UniProtKB	Helix	240	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+Q08932	UniProtKB	Helix	261	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+Q08932	UniProtKB	Helix	320	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF	
+Q08932	UniProtKB	Helix	343	349	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF	
+##sequence-region P38781 1 883
+P38781	UniProtKB	Chain	1	883	.	.	.	ID=PRO_0000114974;Note=Chromatin structure-remodeling complex protein RSC30	
+P38781	UniProtKB	DNA binding	14	45	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P38781	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38781	UniProtKB	Mutagenesis	15	15	.	.	.	Note=Complete inactivation. C->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11336698;Dbxref=PMID:11336698	
+##sequence-region Q05043 1 376
+Q05043	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000203272;Note=Respiration factor 1	
+##sequence-region Q03430 1 361
+Q03430	UniProtKB	Mutagenesis	121	187	.	.	.	Note=In RSM28-1%3B allows translation of defective COX2 mRNAs. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15701796;Dbxref=PMID:15701796	
+##sequence-region Q03201 1 203
+Q03201	UniProtKB	Transit peptide	1	14	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03201	UniProtKB	Chain	15	203	.	.	.	ID=PRO_0000042756;Note=37S ribosomal protein S10%2C mitochondrial	
+Q03201	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38175 1 177
+P38175	UniProtKB	Transit peptide	1	17	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38175	UniProtKB	Chain	18	177	.	.	.	ID=PRO_0000202444;Note=37S ribosomal protein MRP21%2C mitochondrial	
+P38175	UniProtKB	Mutagenesis	115	115	.	.	.	Note=In MRP21-1%3B suppresses translation defects of mutations in the 5'-untranslated leaders of mitochondrial mRNAs. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754	
+P38175	UniProtKB	Mutagenesis	121	121	.	.	.	Note=In MRP21-3%3B suppresses translation defects of mutations in the 5'-untranslated leaders of mitochondrial mRNAs. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754	
+##sequence-region P21771 1 286
+P21771	UniProtKB	Transit peptide	1	33	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2263452;Dbxref=PMID:2263452	
+P21771	UniProtKB	Chain	34	286	.	.	.	ID=PRO_0000030613;Note=37S ribosomal protein S28%2C mitochondrial	
+##sequence-region P38786 1 293
+P38786	UniProtKB	Chain	1	293	.	.	.	ID=PRO_0000140034;Note=Ribonuclease P/MRP protein subunit RPP1	
+##sequence-region Q05468 1 723
+Q05468	UniProtKB	Chain	1	723	.	.	.	ID=PRO_0000253842;Note=Ribosome quality control complex subunit 1	
+Q05468	UniProtKB	Compositional bias	120	125	.	.	.	Note=Poly-Asp	
+Q05468	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+Q05468	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q05468	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q04225 1 511
+Q04225	UniProtKB	Chain	1	511	.	.	.	ID=PRO_0000051202;Note=Ribosome assembly protein RRB1	
+Q04225	UniProtKB	Repeat	319	359	.	.	.	Note=WD 1	
+Q04225	UniProtKB	Repeat	364	404	.	.	.	Note=WD 2	
+Q04225	UniProtKB	Repeat	415	455	.	.	.	Note=WD 3	
+Q04225	UniProtKB	Repeat	477	510	.	.	.	Note=WD 4	
+Q04225	UniProtKB	Modified residue	5	5	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38771 1 230
+P38771	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38771	UniProtKB	Chain	25	230	.	.	.	ID=PRO_0000031091;Note=Ribosome-recycling factor%2C mitochondrial	
+##sequence-region P40156 1 214
+P40156	UniProtKB	Transit peptide	1	18	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40156	UniProtKB	Chain	19	214	.	.	.	ID=PRO_0000203389;Note=Required for respiratory growth protein 9%2C mitochondrial	
+##sequence-region P38766 1 723
+P38766	UniProtKB	Chain	1	723	.	.	.	ID=PRO_0000101986;Note=ATP-dependent DNA helicase RRM3	
+P38766	UniProtKB	Nucleotide binding	254	261	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03177	
+P38766	UniProtKB	DNA binding	682	701	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03177	
+P38766	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38766	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Reduces the interaction with POL30%3B when associated with A-42 or D-42. F->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239216;Dbxref=PMID:12239216	
+P38766	UniProtKB	Mutagenesis	42	42	.	.	.	Note=Reduces the interaction with POL30%3B when associated with A-42 or D-42. F->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239216;Dbxref=PMID:12239216	
+##sequence-region P36070 1 627
+P36070	UniProtKB	Chain	1	627	.	.	.	ID=PRO_0000211430;Note=RNA polymerase I-specific transcription initiation factor RRN3	
+P36070	UniProtKB	Compositional bias	252	259	.	.	.	Note=Poly-Asp	
+P36070	UniProtKB	Compositional bias	267	274	.	.	.	Note=Poly-Asp	
+P36070	UniProtKB	Compositional bias	277	280	.	.	.	Note=Poly-Asp	
+P36070	UniProtKB	Compositional bias	546	549	.	.	.	Note=Poly-Asn	
+P36070	UniProtKB	Helix	49	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	69	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	90	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	103	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	113	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	130	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	151	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	166	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	187	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	205	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	226	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	323	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	326	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	349	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	357	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Turn	371	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	383	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	393	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Beta strand	410	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	414	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	436	457	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	458	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Beta strand	463	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	467	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	471	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	488	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	499	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	502	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	516	519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	522	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	541	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	579	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	600	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	607	609	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+P36070	UniProtKB	Helix	613	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1	
+##sequence-region P38712 1 501
+P38712	UniProtKB	Chain	1	501	.	.	.	ID=PRO_0000055064;Note=ATP-dependent rRNA helicase RRP3	
+P38712	UniProtKB	Domain	112	284	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P38712	UniProtKB	Domain	307	461	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P38712	UniProtKB	Nucleotide binding	125	132	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P38712	UniProtKB	Coiled coil	3	44	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38712	UniProtKB	Motif	81	109	.	.	.	Note=Q motif;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38712	UniProtKB	Motif	231	234	.	.	.	Note=DEAD box;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38712	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38712	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38712	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38712	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Leads to defects in A1 and A2 processing. K->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16449634;Dbxref=PMID:16449634	
+P38712	UniProtKB	Mutagenesis	231	231	.	.	.	Note=Leads to defects in A1 and A2 processing. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16449634;Dbxref=PMID:16449634	
+P38712	UniProtKB	Mutagenesis	263	263	.	.	.	Note=Leads to defects in A1 and A2 processing. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16449634;Dbxref=PMID:16449634	
+##sequence-region Q08162 1 1001
+Q08162	UniProtKB	Chain	1	1001	.	.	.	ID=PRO_0000166423;Note=Exosome complex exonuclease DIS3	
+Q08162	UniProtKB	Domain	904	1001	.	.	.	Note=S1 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180	
+Q08162	UniProtKB	Region	1	235	.	.	.	Note=Endoribonuclease	
+Q08162	UniProtKB	Mutagenesis	47	47	.	.	.	Note=Slow growth%3B when associated with S-52 and S-55. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19060898;Dbxref=PMID:19060898	
+Q08162	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Slow growth%3B when associated with S-47 and S-55. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19060898;Dbxref=PMID:19060898	
+Q08162	UniProtKB	Mutagenesis	55	55	.	.	.	Note=Slow growth%3B when associated with S-47 and S-52. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19060898;Dbxref=PMID:19060898	
+Q08162	UniProtKB	Mutagenesis	171	171	.	.	.	Note=Abolishes endoribonucleolytic activity%3B no effect on growth. No growth%3B when associated with N-551. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19060898;Dbxref=PMID:19060898	
+Q08162	UniProtKB	Mutagenesis	198	198	.	.	.	Note=Abolishes endoribonucleolytic activity%3B no effect on growth. No growth%3B when associated with N-551. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19060898;Dbxref=PMID:19060898	
+Q08162	UniProtKB	Mutagenesis	551	551	.	.	.	Note=Exoribonucleolytic activity abolished. Accumulation of partially processed 5.8S rRNA and partially degraded 5' ETS. No growth%3B when associated with A-171. No growth%3B when associated with A-198. D->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17173052,ECO:0000269|PubMed:18374646,ECO:0000269|PubMed:19060898;Dbxref=PMID:17173052,PMID:18374646,PMID:19060898	
+Q08162	UniProtKB	Beta strand	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+Q08162	UniProtKB	Beta strand	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Beta strand	18	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Beta strand	33	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q08162	UniProtKB	Helix	55	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Turn	80	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q08162	UniProtKB	Beta strand	85	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Helix	92	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Turn	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8	
+Q08162	UniProtKB	Beta strand	110	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Helix	115	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Helix	126	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Beta strand	144	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Turn	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Turn	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Helix	166	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Turn	186	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Beta strand	191	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Helix	199	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q08162	UniProtKB	Helix	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+Q08162	UniProtKB	Beta strand	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Helix	218	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Helix	228	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Helix	232	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q08162	UniProtKB	Helix	261	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	272	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	282	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	287	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	293	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	299	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	304	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	315	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	323	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Turn	336	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	367	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Beta strand	385	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Beta strand	389	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	402	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	420	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	434	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	441	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	447	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	458	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+Q08162	UniProtKB	Beta strand	464	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	478	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	497	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	507	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	519	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	526	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	531	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	540	546	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	552	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	564	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	573	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	579	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8	
+Q08162	UniProtKB	Helix	582	590	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	594	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8	
+Q08162	UniProtKB	Beta strand	599	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8	
+Q08162	UniProtKB	Helix	606	609	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Turn	610	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	619	630	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	636	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	654	662	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	663	665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q08162	UniProtKB	Helix	669	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	701	705	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	707	710	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	712	717	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	722	745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Turn	747	749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	751	755	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	760	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	764	774	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	783	791	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	801	810	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	817	820	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	821	823	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	826	829	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Turn	832	835	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	836	838	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8	
+Q08162	UniProtKB	Turn	845	847	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	849	861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	869	872	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	874	908	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	912	922	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	925	929	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Turn	931	933	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	936	940	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	941	944	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Helix	948	950	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	952	954	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Turn	955	958	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	959	962	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	964	967	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08162	UniProtKB	Beta strand	971	974	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	978	983	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	985	987	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q08162	UniProtKB	Turn	989	991	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q08162	UniProtKB	Beta strand	995	997	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU	
+Q08162	UniProtKB	Beta strand	998	1000	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+##sequence-region P48589 1 143
+P48589	UniProtKB	Chain	1	143	.	.	.	ID=PRO_0000122340;Note=40S ribosomal protein S12	
+P48589	UniProtKB	Cross-link	85	85	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P48589	UniProtKB	Cross-link	95	95	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P48589	UniProtKB	Cross-link	114	114	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P48589	UniProtKB	Sequence conflict	90	92	.	.	.	Note=KVA->EGLP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48589	UniProtKB	Helix	26	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P48589	UniProtKB	Beta strand	41	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P48589	UniProtKB	Helix	45	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P48589	UniProtKB	Turn	51	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P48589	UniProtKB	Beta strand	58	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P48589	UniProtKB	Beta strand	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P48589	UniProtKB	Helix	70	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P48589	UniProtKB	Beta strand	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P48589	UniProtKB	Helix	94	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P48589	UniProtKB	Beta strand	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P48589	UniProtKB	Beta strand	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P48589	UniProtKB	Helix	131	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P07280 1 144
+P07280	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6814480;Dbxref=PMID:6814480	
+P07280	UniProtKB	Chain	2	144	.	.	.	ID=PRO_0000153835;Note=40S ribosomal protein S19-A	
+P07280	UniProtKB	Mutagenesis	15	15	.	.	.	Note=Partial loss of function%3B decreased 18S rRNA%2C decreases binding to 20S pre-rRNA complex%2C slow growth in double RPS19A/RPS19B mutant. I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17726054;Dbxref=PMID:17726054	
+P07280	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Loss of mature 18S rRNA%2C protein doesn't bind 20S pre-RNA complex. Lethal in double RPS19A/RPS19B mutant. R->E%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17726054;Dbxref=PMID:17726054	
+P07280	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Loss of mature 18S rRNA%2C protein binds 20S pre-RNA complex poorly. Lethal in double RPS19A/RPS19B mutant. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17726054;Dbxref=PMID:17726054	
+P07280	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Lethal in double RPS19A/RPS19B mutant%2C considerable decrease in 18S rRNA production. I->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16159874,ECO:0000269|PubMed:17726054;Dbxref=PMID:16159874,PMID:17726054	
+P07280	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Decreases mature 18S rRNA%2C protein binds 20S pre-RNA complex poorly. Lethal in double RPS19A/RPS19B mutant. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17726054;Dbxref=PMID:17726054	
+P07280	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Decreases mature 18S rRNA%2C protein binds 20S pre-RNA complex poorly. Lethal in double RPS19A/RPS19B mutant. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17726054;Dbxref=PMID:17726054	
+P07280	UniProtKB	Helix	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P07280	UniProtKB	Helix	11	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P07280	UniProtKB	Beta strand	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P07280	UniProtKB	Beta strand	39	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P07280	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P07280	UniProtKB	Helix	54	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P07280	UniProtKB	Beta strand	68	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P07280	UniProtKB	Helix	73	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P07280	UniProtKB	Beta strand	83	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P07280	UniProtKB	Beta strand	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P07280	UniProtKB	Helix	98	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P07280	UniProtKB	Beta strand	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P07280	UniProtKB	Beta strand	120	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P07280	UniProtKB	Helix	126	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P23248 1 255
+P23248	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03122,ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921	
+P23248	UniProtKB	Chain	2	255	.	.	.	ID=PRO_0000153542;Note=40S ribosomal protein S1-B	
+P23248	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine%3B partial;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P33442,ECO:0000255|HAMAP-Rule:MF_03122	
+P23248	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23248	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P23248	UniProtKB	Cross-link	248	248	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P39516 1 138
+P39516	UniProtKB	Chain	1	138	.	.	.	ID=PRO_0000123360;Note=40S ribosomal protein S14-B	
+P39516	UniProtKB	Sequence conflict	3	3	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CX52 1 143
+P0CX52	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921	
+P0CX52	UniProtKB	Chain	2	143	.	.	.	ID=PRO_0000409772;Note=40S ribosomal protein S16-B	
+P0CX52	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921	
+P0CX52	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P0CX52	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX52	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX52	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX52	UniProtKB	Cross-link	30	30	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX52	UniProtKB	Cross-link	47	47	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX52	UniProtKB	Cross-link	59	59	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P0CX56 1 146
+P0CX56	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.3;Dbxref=PMID:22814378,PMID:10601260	
+P0CX56	UniProtKB	Chain	2	146	.	.	.	ID=PRO_0000409774;Note=40S ribosomal protein S18-B	
+P0CX56	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.3;Dbxref=PMID:22814378,PMID:10601260	
+P0CX56	UniProtKB	Modified residue	48	48	.	.	.	Note=N6-methyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802	
+P0CX56	UniProtKB	Cross-link	36	36	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX56	UniProtKB	Cross-link	49	49	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX56	UniProtKB	Cross-link	80	80	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX56	UniProtKB	Cross-link	96	96	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX56	UniProtKB	Sequence conflict	27	29	.	.	.	Note=KIV->EFG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CX29 1 145
+P0CX29	UniProtKB	Chain	1	145	.	.	.	ID=PRO_0000146482;Note=40S ribosomal protein S23-A	
+P0CX29	UniProtKB	Modified residue	64	64	.	.	.	Note=3%2C4-dihydroxyproline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462	
+P0CX29	UniProtKB	Cross-link	56	56	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX29	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Lethal mutation. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462	
+P0CX29	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Lethal mutation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462	
+P0CX29	UniProtKB	Turn	9	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P0CX29	UniProtKB	Helix	12	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Helix	27	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Helix	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Beta strand	40	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Beta strand	45	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Beta strand	68	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Turn	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Beta strand	82	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Beta strand	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Turn	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Beta strand	101	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Beta strand	108	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Beta strand	115	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P0CX29	UniProtKB	Beta strand	122	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Turn	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P0CX29	UniProtKB	Helix	132	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX29	UniProtKB	Beta strand	137	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56	
+##sequence-region P0CX32 1 135
+P0CX32	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:1544921	
+P0CX32	UniProtKB	Chain	2	135	.	.	.	ID=PRO_0000409762;Note=40S ribosomal protein S24-B	
+P0CX32	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:1544921	
+P0CX32	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P0CX32	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX32	UniProtKB	Cross-link	21	21	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX32	UniProtKB	Sequence conflict	16	16	.	.	.	Note=P->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0C0T4 1 108
+P0C0T4	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+P0C0T4	UniProtKB	Chain	2	108	.	.	.	ID=PRO_0000030634;Note=40S ribosomal protein S25-B	
+P0C0T4	UniProtKB	Modified residue	2	2	.	.	.	Note=N%2CN-dimethylproline%3B by NTM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20481588;Dbxref=PMID:20481588	
+##sequence-region P0CX35 1 261
+P0CX35	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P0CX35	UniProtKB	Chain	2	261	.	.	.	ID=PRO_0000130843;Note=40S ribosomal protein S4-A	
+P0CX35	UniProtKB	Domain	42	105	.	.	.	Note=S4 RNA-binding	
+P0CX35	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P0CX35	UniProtKB	Modified residue	115	115	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX35	UniProtKB	Modified residue	247	247	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P0CX35	UniProtKB	Cross-link	62	62	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX35	UniProtKB	Cross-link	134	134	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX35	UniProtKB	Cross-link	161	161	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX35	UniProtKB	Cross-link	168	168	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX35	UniProtKB	Cross-link	174	174	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX35	UniProtKB	Cross-link	179	179	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX35	UniProtKB	Cross-link	211	211	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX35	UniProtKB	Cross-link	233	233	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX35	UniProtKB	Turn	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Helix	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	22	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	33	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Helix	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Helix	44	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Turn	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Helix	59	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	89	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Helix	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U52	
+P0CX35	UniProtKB	Beta strand	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Z	
+P0CX35	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	122	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Helix	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	137	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Turn	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P0CX35	UniProtKB	Beta strand	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	159	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	164	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	169	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Turn	187	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U53	
+P0CX35	UniProtKB	Beta strand	197	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Q	
+P0CX35	UniProtKB	Beta strand	207	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	217	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Helix	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	225	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Beta strand	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P0CX35	UniProtKB	Beta strand	234	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Turn	240	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Helix	248	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX35	UniProtKB	Turn	256	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+##sequence-region P32832 1 435
+P32832	UniProtKB	Chain	1	435	.	.	.	ID=PRO_0000057945;Note=Chromatin structure-remodeling complex subunit RSC7	
+P32832	UniProtKB	Region	248	435	.	.	.	Note=Functional region%3B able to complement all NPL6 null allele phenotypes	
+P32832	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q03124 1 581
+Q03124	UniProtKB	Chain	1	581	.	.	.	ID=PRO_0000097475;Note=Chromatin structure-remodeling complex subunit RSC9	
+Q03124	UniProtKB	DNA binding	395	476	.	.	.	Note=RFX-type winged-helix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00858	
+Q03124	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03124	UniProtKB	Sequence conflict	60	60	.	.	.	Note=Y->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04693 1 1361
+Q04693	UniProtKB	Chain	1	1361	.	.	.	ID=PRO_0000218638;Note=Pre-mRNA-splicing factor RSE1	
+##sequence-region P38792 1 359
+P38792	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38792	UniProtKB	Chain	2	359	.	.	.	ID=PRO_0000097455;Note=Exosome complex component RRP4	
+P38792	UniProtKB	Domain	107	187	.	.	.	Note=S1 motif	
+P38792	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38792	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38792	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38792	UniProtKB	Natural variant	136	136	.	.	.	Note=In RRP4-1%3B temperature-sensitive(ts) lethal mutation. L->P	
+P38792	UniProtKB	Beta strand	7	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+P38792	UniProtKB	Beta strand	60	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	65	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	79	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	94	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	111	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	121	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Helix	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Helix	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+P38792	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+P38792	UniProtKB	Helix	154	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Helix	159	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	168	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+P38792	UniProtKB	Beta strand	182	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	188	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+P38792	UniProtKB	Beta strand	196	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Helix	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	213	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Turn	218	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	221	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	229	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Helix	238	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Helix	244	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1	
+P38792	UniProtKB	Helix	270	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	279	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+P38792	UniProtKB	Helix	291	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Helix	316	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Beta strand	329	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Helix	332	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+P38792	UniProtKB	Helix	338	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+##sequence-region Q12149 1 733
+Q12149	UniProtKB	Chain	1	733	.	.	.	ID=PRO_0000097456;Note=Exosome complex exonuclease RRP6	
+Q12149	UniProtKB	Domain	435	515	.	.	.	Note=HRDC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00328	
+Q12149	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12149	UniProtKB	Modified residue	520	520	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12149	UniProtKB	Modified residue	640	640	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12149	UniProtKB	Modified residue	645	645	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12149	UniProtKB	Sequence conflict	402	402	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12149	UniProtKB	Helix	8	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC	
+Q12149	UniProtKB	Helix	28	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC	
+Q12149	UniProtKB	Helix	36	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC	
+Q12149	UniProtKB	Helix	76	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC	
+Q12149	UniProtKB	Helix	132	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1	
+Q12149	UniProtKB	Helix	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	184	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	219	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	233	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	244	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	250	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	262	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Turn	267	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	274	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	278	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	286	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	294	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	309	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	314	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	328	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Turn	343	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	351	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36	
+Q12149	UniProtKB	Helix	356	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	369	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	386	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	404	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	413	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Beta strand	421	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	436	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C0Y	
+Q12149	UniProtKB	Helix	439	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	460	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	466	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	480	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	492	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Helix	498	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ	
+Q12149	UniProtKB	Turn	534	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q12149	UniProtKB	Helix	539	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q12149	UniProtKB	Turn	555	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1	
+Q12149	UniProtKB	Beta strand	570	572	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q12149	UniProtKB	Turn	573	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q12149	UniProtKB	Beta strand	582	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q12149	UniProtKB	Beta strand	591	594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q12149	UniProtKB	Helix	596	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q12149	UniProtKB	Helix	612	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+Q12149	UniProtKB	Beta strand	617	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD	
+##sequence-region Q08746 1 203
+Q08746	UniProtKB	Chain	1	203	.	.	.	ID=PRO_0000185379;Note=Regulator of ribosome biosynthesis	
+Q08746	UniProtKB	Beta strand	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+Q08746	UniProtKB	Helix	23	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+Q08746	UniProtKB	Beta strand	27	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+Q08746	UniProtKB	Helix	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+Q08746	UniProtKB	Helix	46	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+Q08746	UniProtKB	Beta strand	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+Q08746	UniProtKB	Beta strand	88	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL	
+##sequence-region P38192 1 103
+P38192	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000202456;Note=Regulator of rDNA transcription protein 1	
+P38192	UniProtKB	Transmembrane	9	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38192	UniProtKB	Transmembrane	40	57	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C0W1 1 130
+P0C0W1	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:6814480;Dbxref=PMID:10601260,PMID:6814480	
+P0C0W1	UniProtKB	Chain	2	130	.	.	.	ID=PRO_0000126623;Note=40S ribosomal protein S22-A	
+P0C0W1	UniProtKB	Helix	6	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Beta strand	23	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Helix	32	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Beta strand	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Beta strand	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Beta strand	60	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Beta strand	70	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Helix	85	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Beta strand	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Beta strand	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Beta strand	101	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Beta strand	109	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Helix	113	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0C0W1	UniProtKB	Beta strand	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P35997 1 82
+P35997	UniProtKB	Chain	1	82	.	.	.	ID=PRO_0000149066;Note=40S ribosomal protein S27-A	
+P35997	UniProtKB	Zinc finger	37	59	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35997	UniProtKB	Modified residue	40	40	.	.	.	Note=S-methylcysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22650761;Dbxref=PMID:22650761	
+P35997	UniProtKB	Beta strand	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P35997	UniProtKB	Helix	12	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P35997	UniProtKB	Beta strand	22	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P35997	UniProtKB	Beta strand	32	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P35997	UniProtKB	Beta strand	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P35997	UniProtKB	Beta strand	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P35997	UniProtKB	Beta strand	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P35997	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P35997	UniProtKB	Beta strand	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P35997	UniProtKB	Beta strand	78	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0C0X0 1 67
+P0C0X0	UniProtKB	Chain	1	67	.	.	.	ID=PRO_0000136843;Note=40S ribosomal protein S28-B	
+P0C0X0	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260	
+##sequence-region P25443 1 254
+P25443	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921	
+P25443	UniProtKB	Chain	2	254	.	.	.	ID=PRO_0000131684;Note=40S ribosomal protein S2	
+P25443	UniProtKB	Domain	76	139	.	.	.	Note=S5 DRBM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00268	
+P25443	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921	
+P25443	UniProtKB	Modified residue	11	11	.	.	.	Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20035717,ECO:0000269|PubMed:22650761;Dbxref=PMID:20035717,PMID:22650761	
+P25443	UniProtKB	Modified residue	11	11	.	.	.	Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20035717,ECO:0000269|PubMed:22650761;Dbxref=PMID:20035717,PMID:22650761	
+P25443	UniProtKB	Cross-link	33	33	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25443	UniProtKB	Helix	40	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Helix	53	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Helix	66	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Beta strand	80	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Beta strand	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Beta strand	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Beta strand	98	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Beta strand	107	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Helix	121	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Beta strand	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Beta strand	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56	
+P25443	UniProtKB	Beta strand	153	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Beta strand	158	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Beta strand	165	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Beta strand	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Helix	182	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Beta strand	195	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Helix	207	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Helix	220	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Helix	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Helix	239	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P25443	UniProtKB	Helix	244	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX34 1 63
+P0CX34	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P0CX34	UniProtKB	Chain	2	63	.	.	.	ID=PRO_0000409763;Note=40S ribosomal protein S30-B	
+P0CX34	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX34	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q05942 1 220
+Q05942	UniProtKB	Chain	1	220	.	.	.	ID=PRO_0000097468;Note=Ribosome assembly protein 3	
+Q05942	UniProtKB	Compositional bias	29	42	.	.	.	Note=Ser-rich	
+Q05942	UniProtKB	Modified residue	83	83	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05942	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05942	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53236 1 928
+P53236	UniProtKB	Chain	1	928	.	.	.	ID=PRO_0000211211;Note=Chromatin structure-remodeling complex subunit RSC1	
+P53236	UniProtKB	Domain	27	95	.	.	.	Note=Bromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+P53236	UniProtKB	Domain	255	325	.	.	.	Note=Bromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+P53236	UniProtKB	Domain	368	486	.	.	.	Note=BAH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370	
+P53236	UniProtKB	Modified residue	670	670	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53236	UniProtKB	Mutagenesis	228	230	.	.	.	Note=Loss of function. GRP->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10619019;Dbxref=PMID:10619019	
+P53236	UniProtKB	Sequence conflict	112	112	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53236	UniProtKB	Sequence conflict	302	302	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53236	UniProtKB	Sequence conflict	520	520	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53236	UniProtKB	Sequence conflict	712	712	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53236	UniProtKB	Sequence conflict	820	820	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02206 1 625
+Q02206	UniProtKB	Chain	1	625	.	.	.	ID=PRO_0000211213;Note=Chromatin structure-remodeling complex subunit RSC4	
+Q02206	UniProtKB	Domain	72	141	.	.	.	Note=Bromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+Q02206	UniProtKB	Domain	205	275	.	.	.	Note=Bromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+Q02206	UniProtKB	Modified residue	199	199	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02206	UniProtKB	Modified residue	545	545	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02206	UniProtKB	Sequence conflict	390	390	.	.	.	Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02206	UniProtKB	Sequence conflict	390	390	.	.	.	Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02206	UniProtKB	Helix	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	58	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Turn	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	90	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	102	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	115	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R10	
+Q02206	UniProtKB	Helix	139	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	169	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	187	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Beta strand	205	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0S	
+Q02206	UniProtKB	Helix	211	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Turn	219	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	223	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	235	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	250	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	273	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Helix	293	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+Q02206	UniProtKB	Turn	313	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y	
+##sequence-region P33442 1 255
+P33442	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03122,ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P33442	UniProtKB	Chain	2	255	.	.	.	ID=PRO_0000153541;Note=40S ribosomal protein S1-A	
+P33442	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine%3B partial;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03122,ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P33442	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P33442	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P33442	UniProtKB	Cross-link	248	248	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23248	
+P33442	UniProtKB	Turn	23	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	29	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	41	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Helix	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	65	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Helix	71	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88	
+P33442	UniProtKB	Beta strand	83	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	93	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M	
+P33442	UniProtKB	Beta strand	99	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Helix	107	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P33442	UniProtKB	Beta strand	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P33442	UniProtKB	Helix	159	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	176	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Helix	180	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Turn	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Helix	192	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	208	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Beta strand	215	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Helix	225	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P33442	UniProtKB	Helix	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+##sequence-region P0CX37 1 236
+P0CX37	UniProtKB	Chain	1	236	.	.	.	ID=PRO_0000137342;Note=40S ribosomal protein S6-A	
+P0CX37	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX37	UniProtKB	Cross-link	116	116	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX37	UniProtKB	Cross-link	131	131	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX37	UniProtKB	Cross-link	149	149	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX37	UniProtKB	Cross-link	214	214	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX37	UniProtKB	Beta strand	2	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Turn	8	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Beta strand	12	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Helix	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Helix	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Beta strand	31	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Beta strand	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Turn	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Beta strand	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Beta strand	49	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Beta strand	69	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P0CX37	UniProtKB	Beta strand	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U51	
+P0CX37	UniProtKB	Beta strand	93	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Beta strand	106	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Helix	122	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Helix	138	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Turn	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P0CX37	UniProtKB	Helix	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Helix	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Beta strand	160	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Beta strand	168	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Helix	181	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Beta strand	219	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX37	UniProtKB	Turn	223	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX40 1 200
+P0CX40	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943	
+P0CX40	UniProtKB	Chain	2	200	.	.	.	ID=PRO_0000409766;Note=40S ribosomal protein S8-B	
+P0CX40	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX40	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX40	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P0CX40	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P0CX40	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX40	UniProtKB	Modified residue	107	107	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P0CX40	UniProtKB	Modified residue	154	154	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX40	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX40	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P0CX40	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX40	UniProtKB	Sequence conflict	49	49	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08417 1 382
+Q08417	UniProtKB	Chain	1	382	.	.	.	ID=PRO_0000262738;Note=Sphingoid long-chain base transporter RSB1	
+Q08417	UniProtKB	Topological domain	1	34	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Topological domain	56	57	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Transmembrane	58	78	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Topological domain	79	90	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Transmembrane	91	111	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Topological domain	112	135	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Topological domain	157	171	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Transmembrane	172	192	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Topological domain	193	241	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Transmembrane	242	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Topological domain	263	281	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Transmembrane	282	302	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Topological domain	303	382	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08417	UniProtKB	Glycosylation	3	3	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407254;Dbxref=PMID:16407254	
+Q08417	UniProtKB	Glycosylation	6	6	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407254;Dbxref=PMID:16407254	
+Q08417	UniProtKB	Mutagenesis	3	3	.	.	.	Note=Increases sensitivity towards LCBs. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407254;Dbxref=PMID:16407254	
+Q08417	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Increases sensitivity towards LCBs. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407254;Dbxref=PMID:16407254	
+##sequence-region P46974 1 1380
+P46974	UniProtKB	Chain	1	1380	.	.	.	ID=PRO_0000046861;Note=Respiration factor 2	
+P46974	UniProtKB	Zinc finger	151	173	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P46974	UniProtKB	Zinc finger	179	202	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P46974	UniProtKB	Compositional bias	64	67	.	.	.	Note=Poly-Phe	
+P46974	UniProtKB	Compositional bias	424	433	.	.	.	Note=Poly-Gln	
+P46974	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46974	UniProtKB	Modified residue	322	322	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46974	UniProtKB	Modified residue	544	544	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46974	UniProtKB	Modified residue	632	632	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P46974	UniProtKB	Sequence conflict	1117	1118	.	.	.	Note=NL->IF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46974	UniProtKB	Sequence conflict	1131	1131	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40033 1 138
+##sequence-region Q03516 1 953
+Q03516	UniProtKB	Chain	1	953	.	.	.	ID=PRO_0000203348;Note=Uncharacterized protein RSN1	
+Q03516	UniProtKB	Transmembrane	23	43	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03516	UniProtKB	Transmembrane	103	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03516	UniProtKB	Transmembrane	148	168	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03516	UniProtKB	Transmembrane	392	412	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03516	UniProtKB	Transmembrane	435	455	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03516	UniProtKB	Transmembrane	481	501	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03516	UniProtKB	Transmembrane	540	560	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03516	UniProtKB	Transmembrane	575	595	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03516	UniProtKB	Transmembrane	599	619	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03516	UniProtKB	Transmembrane	642	662	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03516	UniProtKB	Transmembrane	666	686	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03516	UniProtKB	Modified residue	949	949	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P32905 1 252
+P32905	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03015,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:9298649;Dbxref=PMID:10601260,PMID:9298649	
+P32905	UniProtKB	Chain	2	252	.	.	.	ID=PRO_0000134370;Note=40S ribosomal protein S0-A	
+P32905	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03015,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:9298649;Dbxref=PMID:10601260,PMID:9298649	
+P32905	UniProtKB	Beta strand	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F	
+P32905	UniProtKB	Helix	11	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Turn	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Helix	31	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88	
+P32905	UniProtKB	Beta strand	37	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Turn	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Beta strand	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Helix	50	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Beta strand	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Helix	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Beta strand	73	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Helix	80	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Beta strand	96	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Beta strand	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Beta strand	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P32905	UniProtKB	Beta strand	119	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Turn	126	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Helix	130	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Turn	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Beta strand	143	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Beta strand	149	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P32905	UniProtKB	Beta strand	157	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Beta strand	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Y	
+P32905	UniProtKB	Helix	169	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Beta strand	183	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Beta strand	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P32905	UniProtKB	Helix	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+##sequence-region P38120 1 278
+P38120	UniProtKB	Transit peptide	1	10	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38120	UniProtKB	Chain	11	278	.	.	.	ID=PRO_0000030653;Note=37S ribosomal protein S9%2C mitochondrial	
+##sequence-region P40063 1 208
+P40063	UniProtKB	Chain	1	208	.	.	.	ID=PRO_0000202644;Note=Regulator of Ty1 transposition protein 105	
+##sequence-region P40161 1 455
+P40161	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40161	UniProtKB	Chain	2	455	.	.	.	ID=PRO_0000203392;Note=Histone chaperone RTT106	
+P40161	UniProtKB	Domain	68	200	.	.	.	Note=PH 1	
+P40161	UniProtKB	Domain	217	301	.	.	.	Note=PH 2	
+P40161	UniProtKB	Region	2	67	.	.	.	Note=Dimeric region	
+P40161	UniProtKB	Region	68	301	.	.	.	Note=Double PH domain	
+P40161	UniProtKB	Region	315	455	.	.	.	Note=Disordered acidic region	
+P40161	UniProtKB	Compositional bias	351	448	.	.	.	Note=Asp/Glu-rich	
+P40161	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40161	UniProtKB	Modified residue	408	408	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40161	UniProtKB	Modified residue	411	411	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40161	UniProtKB	Modified residue	450	450	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40161	UniProtKB	Mutagenesis	259	259	.	.	.	Note=Decreases histone-binding. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22307274;Dbxref=PMID:22307274	
+P40161	UniProtKB	Mutagenesis	261	261	.	.	.	Note=Impairs histone-binding. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22307274;Dbxref=PMID:22307274	
+P40161	UniProtKB	Mutagenesis	269	269	.	.	.	Note=Impairs histone-binding. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22307274;Dbxref=PMID:22307274	
+P40161	UniProtKB	Mutagenesis	288	288	.	.	.	Note=Decreases histone-binding. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22307274;Dbxref=PMID:22307274	
+P40161	UniProtKB	Mutagenesis	291	291	.	.	.	Note=Impairs histone-binding. Y->A	
+P40161	UniProtKB	Mutagenesis	294	294	.	.	.	Note=Impairs histone-binding. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22307274;Dbxref=PMID:22307274	
+P40161	UniProtKB	Helix	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LH0	
+P40161	UniProtKB	Helix	11	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LH0	
+P40161	UniProtKB	Helix	27	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LH0	
+P40161	UniProtKB	Beta strand	60	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LH0	
+P40161	UniProtKB	Beta strand	71	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	87	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Turn	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	102	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	111	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Helix	119	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	137	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Helix	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	156	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Helix	162	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Helix	183	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	220	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	237	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	249	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Helix	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	256	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	266	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Beta strand	280	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Helix	288	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+P40161	UniProtKB	Helix	291	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS	
+##sequence-region Q07794 1 436
+Q07794	UniProtKB	Chain	1	436	.	.	.	ID=PRO_0000268738;Note=Histone acetyltransferase RTT109	
+Q07794	UniProtKB	Domain	2	404	.	.	.	Note=Rtt109-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01064	
+Q07794	UniProtKB	Mutagenesis	89	89	.	.	.	Note=Losses histone acetylase activity. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17272723;Dbxref=PMID:17272723	
+Q07794	UniProtKB	Mutagenesis	287	288	.	.	.	Note=Reduces histone acetylase activity. DD->AA%2CNN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17272723;Dbxref=PMID:17272723	
+Q07794	UniProtKB	Helix	3	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Beta strand	16	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Beta strand	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Beta strand	37	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q68	
+Q07794	UniProtKB	Beta strand	44	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Beta strand	60	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Beta strand	79	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	100	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Beta strand	121	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	144	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66	
+Q07794	UniProtKB	Beta strand	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66	
+Q07794	UniProtKB	Helix	164	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66	
+Q07794	UniProtKB	Helix	169	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66	
+Q07794	UniProtKB	Beta strand	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66	
+Q07794	UniProtKB	Helix	182	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QM0	
+Q07794	UniProtKB	Beta strand	186	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66	
+Q07794	UniProtKB	Beta strand	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	204	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Beta strand	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QM0	
+Q07794	UniProtKB	Helix	215	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Beta strand	239	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	249	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Beta strand	259	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q68	
+Q07794	UniProtKB	Beta strand	264	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	273	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CZ7	
+Q07794	UniProtKB	Helix	278	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	289	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Turn	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	308	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	320	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Turn	324	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66	
+Q07794	UniProtKB	Beta strand	328	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Beta strand	336	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Turn	346	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	355	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	373	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Beta strand	396	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN	
+Q07794	UniProtKB	Helix	411	423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66	
+##sequence-region P53732 1 153
+P53732	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53732	UniProtKB	Chain	21	153	.	.	.	ID=PRO_0000146483;Note=37S ribosomal protein S12%2C mitochondrial	
+##sequence-region P53064 1 558
+P53064	UniProtKB	Chain	1	558	.	.	.	ID=PRO_0000097512;Note=RNA polymerase-associated protein RTF1	
+P53064	UniProtKB	Domain	238	370	.	.	.	Note=Plus3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00693	
+P53064	UniProtKB	Compositional bias	72	76	.	.	.	Note=Poly-Glu	
+P53064	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53064	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53064	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P53064	UniProtKB	Modified residue	477	477	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53064	UniProtKB	Turn	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EMX	
+P53064	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EMX	
+P53064	UniProtKB	Helix	89	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EMX	
+P53064	UniProtKB	Helix	100	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EMX	
+##sequence-region P0CX30 1 145
+P0CX30	UniProtKB	Chain	1	145	.	.	.	ID=PRO_0000409761;Note=40S ribosomal protein S23-B	
+P0CX30	UniProtKB	Modified residue	64	64	.	.	.	Note=3%2C4-dihydroxyproline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462	
+P0CX30	UniProtKB	Cross-link	56	56	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX30	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Lethal mutation. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462	
+P0CX30	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Lethal mutation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462	
+##sequence-region P41057 1 56
+P41057	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943	
+P41057	UniProtKB	Chain	2	56	.	.	.	ID=PRO_0000131032;Note=40S ribosomal protein S29-A	
+P41057	UniProtKB	Metal binding	21	21	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41057	UniProtKB	Metal binding	24	24	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41057	UniProtKB	Metal binding	39	39	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41057	UniProtKB	Metal binding	42	42	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41057	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41058	
+P41057	UniProtKB	Sequence conflict	7	7	.	.	.	Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41057	UniProtKB	Sequence conflict	14	14	.	.	.	Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41057	UniProtKB	Beta strand	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P41057	UniProtKB	Beta strand	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P41057	UniProtKB	Helix	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P41057	UniProtKB	Turn	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P41057	UniProtKB	Beta strand	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P41057	UniProtKB	Helix	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P41057	UniProtKB	Helix	40	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P05750 1 240
+P05750	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:1544921,PMID:18782943	
+P05750	UniProtKB	Chain	2	240	.	.	.	ID=PRO_0000130332;Note=40S ribosomal protein S3	
+P05750	UniProtKB	Domain	21	92	.	.	.	Note=KH type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00118	
+P05750	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P05750	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P05750	UniProtKB	Modified residue	97	97	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P05750	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P05750	UniProtKB	Modified residue	146	146	.	.	.	Note=Omega-N-methylarginine%3B by SFM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22650761;Dbxref=PMID:22650761	
+P05750	UniProtKB	Modified residue	221	221	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P05750	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P05750	UniProtKB	Cross-link	106	106	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05750	UniProtKB	Cross-link	132	132	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05750	UniProtKB	Cross-link	141	141	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05750	UniProtKB	Cross-link	151	151	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05750	UniProtKB	Cross-link	200	200	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05750	UniProtKB	Cross-link	212	212	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05750	UniProtKB	Sequence conflict	17	17	.	.	.	Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05750	UniProtKB	Sequence conflict	223	224	.	.	.	Note=KD->NH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05750	UniProtKB	Helix	15	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Turn	29	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Beta strand	34	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Beta strand	45	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Helix	55	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Helix	64	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Beta strand	83	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Helix	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Helix	98	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Helix	115	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Beta strand	134	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Beta strand	152	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Helix	163	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Beta strand	168	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Beta strand	181	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P05750	UniProtKB	Helix	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+##sequence-region O13516 1 197
+O13516	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6814480;Dbxref=PMID:6814480	
+O13516	UniProtKB	Chain	2	197	.	.	.	ID=PRO_0000132703;Note=40S ribosomal protein S9-A	
+O13516	UniProtKB	Domain	107	181	.	.	.	Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182	
+O13516	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05755	
+O13516	UniProtKB	Cross-link	180	180	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05755	
+O13516	UniProtKB	Sequence conflict	20	22	.	.	.	Note=ESS->QSB;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+O13516	UniProtKB	Beta strand	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Helix	21	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Beta strand	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Helix	40	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Helix	67	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F	
+O13516	UniProtKB	Beta strand	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Turn	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Helix	101	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Helix	109	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Beta strand	116	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+O13516	UniProtKB	Helix	122	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Beta strand	135	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Helix	150	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Beta strand	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Y	
+O13516	UniProtKB	Beta strand	160	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Helix	171	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+O13516	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region Q07979 1 502
+Q07979	UniProtKB	Chain	1	502	.	.	.	ID=PRO_0000097473;Note=Chromatin structure-remodeling complex protein RSC58	
+##sequence-region Q12481 1 300
+Q12481	UniProtKB	Chain	1	300	.	.	.	ID=PRO_0000268165;Note=rRNA biogenesis protein RRP36	
+Q12481	UniProtKB	Coiled coil	184	248	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12481	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12481	UniProtKB	Modified residue	41	41	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12481	UniProtKB	Modified residue	42	42	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q3E811 1 62
+Q3E811	UniProtKB	Chain	1	62	.	.	.	ID=PRO_0000262879;Note=Regulator of rDNA transcription protein 15	
+##sequence-region P05756 1 151
+P05756	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:6814480;Dbxref=PMID:10601260,PMID:6814480	
+P05756	UniProtKB	Chain	2	151	.	.	.	ID=PRO_0000115689;Note=40S ribosomal protein S13	
+P05756	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P05756	UniProtKB	Cross-link	39	39	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05756	UniProtKB	Cross-link	43	43	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05756	UniProtKB	Sequence conflict	25	25	.	.	.	Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05756	UniProtKB	Sequence conflict	32	32	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P05756	UniProtKB	Beta strand	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05756	UniProtKB	Helix	30	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05756	UniProtKB	Helix	47	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05756	UniProtKB	Turn	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P05756	UniProtKB	Helix	63	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05756	UniProtKB	Beta strand	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05756	UniProtKB	Helix	71	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05756	UniProtKB	Helix	86	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05756	UniProtKB	Turn	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P05756	UniProtKB	Helix	109	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05756	UniProtKB	Helix	143	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P06367 1 137
+P06367	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921	
+P06367	UniProtKB	Chain	2	137	.	.	.	ID=PRO_0000123359;Note=40S ribosomal protein S14-A	
+P06367	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921	
+P06367	UniProtKB	Sequence conflict	72	72	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06367	UniProtKB	Sequence conflict	123	123	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06367	UniProtKB	Beta strand	14	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Beta strand	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Beta strand	25	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Beta strand	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Beta strand	35	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Turn	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Beta strand	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N	
+P06367	UniProtKB	Beta strand	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Helix	57	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Beta strand	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Beta strand	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U	
+P06367	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Helix	99	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Turn	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P06367	UniProtKB	Beta strand	111	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P06367	UniProtKB	Turn	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Z	
+##sequence-region P39938 1 119
+P39938	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000204528;Note=40S ribosomal protein S26-A	
+P39938	UniProtKB	Beta strand	8	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88	
+P39938	UniProtKB	Beta strand	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P39938	UniProtKB	Turn	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P39938	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P39938	UniProtKB	Helix	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P39938	UniProtKB	Beta strand	37	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P39938	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88	
+P39938	UniProtKB	Helix	50	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P39938	UniProtKB	Beta strand	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P39938	UniProtKB	Beta strand	67	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P39938	UniProtKB	Helix	76	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P39938	UniProtKB	Turn	89	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+##sequence-region P38711 1 82
+P38711	UniProtKB	Chain	1	82	.	.	.	ID=PRO_0000149067;Note=40S ribosomal protein S27-B	
+P38711	UniProtKB	Zinc finger	37	59	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P05759 1 152
+P05759	UniProtKB	Chain	1	76	.	.	.	ID=PRO_0000396487;Note=Ubiquitin	
+P05759	UniProtKB	Chain	77	152	.	.	.	ID=PRO_0000137688;Note=40S ribosomal protein S31	
+P05759	UniProtKB	Domain	1	76	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+P05759	UniProtKB	Zinc finger	121	144	.	.	.	Note=C4-type	
+P05759	UniProtKB	Compositional bias	77	99	.	.	.	Note=Lys-rich (highly basic)	
+P05759	UniProtKB	Modified residue	122	122	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P05759	UniProtKB	Cross-link	76	76	.	.	.	Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)	
+P05759	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P05759	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P05759	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550	
+P05759	UniProtKB	Beta strand	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P05759	UniProtKB	Beta strand	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05759	UniProtKB	Beta strand	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P05759	UniProtKB	Beta strand	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P05759	UniProtKB	Beta strand	120	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P05759	UniProtKB	Turn	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88	
+P05759	UniProtKB	Beta strand	128	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P05759	UniProtKB	Beta strand	139	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX51 1 143
+P0CX51	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921	
+P0CX51	UniProtKB	Chain	2	143	.	.	.	ID=PRO_0000111503;Note=40S ribosomal protein S16-A	
+P0CX51	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921	
+P0CX51	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P0CX51	UniProtKB	Modified residue	61	61	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX51	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX51	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX51	UniProtKB	Cross-link	30	30	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX51	UniProtKB	Cross-link	47	47	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX51	UniProtKB	Cross-link	59	59	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX51	UniProtKB	Beta strand	5	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX51	UniProtKB	Beta strand	16	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX51	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX51	UniProtKB	Turn	36	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX51	UniProtKB	Beta strand	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P0CX51	UniProtKB	Turn	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX51	UniProtKB	Helix	46	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX51	UniProtKB	Helix	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX51	UniProtKB	Beta strand	63	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX51	UniProtKB	Helix	76	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX51	UniProtKB	Helix	99	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX51	UniProtKB	Beta strand	114	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX51	UniProtKB	Beta strand	129	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P14127 1 136
+P14127	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000141547;Note=40S ribosomal protein S17-B	
+##sequence-region P0CX55 1 146
+P0CX55	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.3;Dbxref=PMID:22814378,PMID:10601260	
+P0CX55	UniProtKB	Chain	2	146	.	.	.	ID=PRO_0000132227;Note=40S ribosomal protein S18-A	
+P0CX55	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.3;Dbxref=PMID:22814378,PMID:10601260	
+P0CX55	UniProtKB	Modified residue	48	48	.	.	.	Note=N6-methyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802	
+P0CX55	UniProtKB	Cross-link	36	36	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX55	UniProtKB	Cross-link	49	49	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX55	UniProtKB	Cross-link	80	80	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX55	UniProtKB	Cross-link	96	96	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX55	UniProtKB	Beta strand	13	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Beta strand	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Beta strand	24	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Helix	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Helix	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Helix	40	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Turn	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Helix	63	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Turn	76	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Helix	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Helix	103	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Helix	122	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX55	UniProtKB	Beta strand	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88	
+P0CX55	UniProtKB	Beta strand	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region Q3E7Y3 1 130
+Q3E7Y3	UniProtKB	Chain	1	130	.	.	.	ID=PRO_0000126624;Note=40S ribosomal protein S22-B	
+##sequence-region Q3E7X9 1 67
+Q3E7X9	UniProtKB	Chain	1	67	.	.	.	ID=PRO_0000136842;Note=40S ribosomal protein S28-A	
+Q3E7X9	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260	
+Q3E7X9	UniProtKB	Beta strand	9	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E7X9	UniProtKB	Beta strand	25	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E7X9	UniProtKB	Beta strand	39	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E7X9	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+Q3E7X9	UniProtKB	Beta strand	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX33 1 63
+P0CX33	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260	
+P0CX33	UniProtKB	Chain	2	63	.	.	.	ID=PRO_0000174009;Note=40S ribosomal protein S30-A	
+P0CX33	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX33	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX33	UniProtKB	Turn	9	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX33	UniProtKB	Helix	13	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX33	UniProtKB	Helix	33	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX33	UniProtKB	Turn	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88	
+P0CX33	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P0CX36 1 261
+P0CX36	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6814480;Dbxref=PMID:6814480	
+P0CX36	UniProtKB	Chain	2	261	.	.	.	ID=PRO_0000409764;Note=40S ribosomal protein S4-B	
+P0CX36	UniProtKB	Domain	42	105	.	.	.	Note=S4 RNA-binding	
+P0CX36	UniProtKB	Modified residue	32	32	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P0CX36	UniProtKB	Modified residue	115	115	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX36	UniProtKB	Modified residue	247	247	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P0CX36	UniProtKB	Cross-link	62	62	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX36	UniProtKB	Cross-link	134	134	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX36	UniProtKB	Cross-link	161	161	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX36	UniProtKB	Cross-link	168	168	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX36	UniProtKB	Cross-link	174	174	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX36	UniProtKB	Cross-link	179	179	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX36	UniProtKB	Cross-link	211	211	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX36	UniProtKB	Cross-link	233	233	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P0CX38 1 236
+P0CX38	UniProtKB	Chain	1	236	.	.	.	ID=PRO_0000409765;Note=40S ribosomal protein S6-B	
+P0CX38	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX38	UniProtKB	Cross-link	116	116	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX38	UniProtKB	Cross-link	131	131	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX38	UniProtKB	Cross-link	149	149	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX38	UniProtKB	Cross-link	214	214	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P0CX38	UniProtKB	Sequence conflict	181	181	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P0CX39 1 200
+P0CX39	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943	
+P0CX39	UniProtKB	Chain	2	200	.	.	.	ID=PRO_0000122258;Note=40S ribosomal protein S8-A	
+P0CX39	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX39	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P0CX39	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P0CX39	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P0CX39	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX39	UniProtKB	Modified residue	107	107	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P0CX39	UniProtKB	Modified residue	154	154	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX39	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX39	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P0CX39	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P0CX39	UniProtKB	Sequence conflict	49	49	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CX39	UniProtKB	Sequence conflict	101	102	.	.	.	Note=IV->MS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P0CX39	UniProtKB	Beta strand	7	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Turn	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P0CX39	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Beta strand	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Beta strand	43	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Beta strand	53	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Beta strand	62	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Helix	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Beta strand	72	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Beta strand	80	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Helix	89	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Helix	107	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Helix	138	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Beta strand	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3N	
+P0CX39	UniProtKB	Helix	154	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Turn	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Beta strand	166	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Helix	173	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Beta strand	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P0CX39	UniProtKB	Helix	186	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P05755 1 195
+P05755	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6814480;Dbxref=PMID:6814480	
+P05755	UniProtKB	Chain	2	195	.	.	.	ID=PRO_0000132704;Note=40S ribosomal protein S9-B	
+P05755	UniProtKB	Domain	107	181	.	.	.	Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182	
+P05755	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P05755	UniProtKB	Cross-link	180	180	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P05755	UniProtKB	Sequence conflict	20	22	.	.	.	Note=ESS->QSB;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P02407 1 136
+P02407	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000141546;Note=40S ribosomal protein S17-A	
+P02407	UniProtKB	Helix	7	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02407	UniProtKB	Helix	21	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02407	UniProtKB	Helix	28	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02407	UniProtKB	Beta strand	39	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02407	UniProtKB	Helix	44	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02407	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56	
+P02407	UniProtKB	Helix	73	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02407	UniProtKB	Beta strand	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P02407	UniProtKB	Helix	104	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region Q06639 1 885
+Q06639	UniProtKB	Chain	1	885	.	.	.	ID=PRO_0000114973;Note=Chromatin structure-remodeling complex protein RSC3	
+Q06639	UniProtKB	DNA binding	14	42	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+Q06639	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q06639	UniProtKB	Modified residue	236	236	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06639	UniProtKB	Mutagenesis	14	14	.	.	.	Note=Complete inactivation. C->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11336698;Dbxref=PMID:11336698	
+##sequence-region P40018 1 196
+P40018	UniProtKB	Chain	1	196	.	.	.	ID=PRO_0000125527;Note=Small nuclear ribonucleoprotein-associated protein B	
+P40018	UniProtKB	Motif	105	132	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40018	UniProtKB	Beta strand	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40018	UniProtKB	Helix	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40018	UniProtKB	Beta strand	19	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40018	UniProtKB	Beta strand	29	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40018	UniProtKB	Beta strand	43	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40018	UniProtKB	Beta strand	78	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40018	UniProtKB	Turn	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40018	UniProtKB	Beta strand	92	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region O14464 1 93
+##sequence-region P38165 1 486
+P38165	UniProtKB	Chain	1	486	.	.	.	ID=PRO_0000127434;Note=Retrograde regulation protein 3	
+P38165	UniProtKB	Domain	285	344	.	.	.	Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981	
+P38165	UniProtKB	Motif	27	35	.	.	.	Note=9aaTAD 1	
+P38165	UniProtKB	Motif	189	197	.	.	.	Note=9aaTAD 2	
+P38165	UniProtKB	Modified residue	81	81	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38165	UniProtKB	Modified residue	123	123	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38165	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38165	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38165	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38165	UniProtKB	Modified residue	236	236	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38165	UniProtKB	Modified residue	241	241	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38165	UniProtKB	Modified residue	269	269	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q12443 1 393
+Q12443	UniProtKB	Chain	1	393	.	.	.	ID=PRO_0000168169;Note=Reticulon-like protein 2	
+Q12443	UniProtKB	Topological domain	1	60	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12443	UniProtKB	Transmembrane	61	81	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12443	UniProtKB	Topological domain	82	149	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12443	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12443	UniProtKB	Topological domain	171	393	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12443	UniProtKB	Domain	30	236	.	.	.	Note=Reticulon;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00170	
+Q12443	UniProtKB	Modified residue	278	278	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12443	UniProtKB	Glycosylation	137	137	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05900 1 231
+Q05900	UniProtKB	Chain	1	231	.	.	.	ID=PRO_0000097528;Note=U1 small nuclear ribonucleoprotein C	
+Q05900	UniProtKB	Zinc finger	4	36	.	.	.	Note=Matrin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03153	
+Q05900	UniProtKB	Mutagenesis	13	13	.	.	.	Note=Gives rise to unstable commitment complexes. L->A%2CD%2CE%2CF%2CG%2CH%2CK%2CP%2CR%2CS%2CT%2CW%2CY;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11172727,ECO:0000269|PubMed:15465910;Dbxref=PMID:11172727,PMID:15465910	
+Q05900	UniProtKB	Mutagenesis	13	13	.	.	.	Note=No effect. L->C%2CI%2CM%2CN%2CQ%2CV;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11172727,ECO:0000269|PubMed:15465910;Dbxref=PMID:11172727,PMID:15465910	
+##sequence-region P26786 1 190
+P26786	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921	
+P26786	UniProtKB	Chain	2	190	.	.	.	ID=PRO_0000174212;Note=40S ribosomal protein S7-A	
+P26786	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921	
+P26786	UniProtKB	Cross-link	124	124	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P26786	UniProtKB	Sequence conflict	24	24	.	.	.	Note=F->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P26786	UniProtKB	Helix	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	9	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Helix	16	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Helix	31	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	35	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	45	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	56	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P26786	UniProtKB	Helix	67	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	71	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Helix	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	87	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Helix	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P26786	UniProtKB	Helix	118	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	135	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88	
+P26786	UniProtKB	Beta strand	148	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P26786	UniProtKB	Helix	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Turn	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Helix	166	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P26786	UniProtKB	Beta strand	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P26786	UniProtKB	Beta strand	181	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region P25632 1 483
+P25632	UniProtKB	Chain	1	483	.	.	.	ID=PRO_0000097474;Note=Chromatin structure-remodeling complex protein RSC6	
+##sequence-region P28778 1 131
+P28778	UniProtKB	Chain	1	131	.	.	.	ID=PRO_0000087697;Note=37S ribosomal protein MRP17%2C mitochondrial	
+##sequence-region Q05543 1 409
+Q05543	UniProtKB	Chain	1	409	.	.	.	ID=PRO_0000268707;Note=Regulator of Ty1 transposition protein 103	
+Q05543	UniProtKB	Domain	1	135	.	.	.	Note=CID;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00724	
+Q05543	UniProtKB	Compositional bias	267	296	.	.	.	Note=Asp-rich	
+Q05543	UniProtKB	Helix	5	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4	
+Q05543	UniProtKB	Helix	19	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4	
+Q05543	UniProtKB	Helix	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4	
+Q05543	UniProtKB	Helix	36	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4	
+Q05543	UniProtKB	Beta strand	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4	
+Q05543	UniProtKB	Helix	54	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4	
+Q05543	UniProtKB	Helix	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4	
+Q05543	UniProtKB	Helix	78	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4	
+Q05543	UniProtKB	Helix	87	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4	
+Q05543	UniProtKB	Helix	100	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4	
+Q05543	UniProtKB	Helix	121	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4	
+##sequence-region P53305 1 110
+P53305	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000202847;Note=Mitochondrial 37S ribosomal protein S27	
+P53305	UniProtKB	Compositional bias	103	110	.	.	.	Note=Poly-Lys	
+##sequence-region P19955 1 123
+P19955	UniProtKB	Transit peptide	1	8	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2693936;Dbxref=PMID:2693936	
+P19955	UniProtKB	Chain	9	123	.	.	.	ID=PRO_0000030587;Note=37S ribosomal protein YMR-31%2C mitochondrial	
+##sequence-region Q12751 1 981
+Q12751	UniProtKB	Chain	1	981	.	.	.	ID=PRO_0000203322;Note=RNA polymerase II assembly factor RTP1	
+Q12751	UniProtKB	Repeat	64	101	.	.	.	Note=HEAT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12751	UniProtKB	Repeat	161	199	.	.	.	Note=HEAT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12751	UniProtKB	Repeat	226	261	.	.	.	Note=HEAT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12751	UniProtKB	Repeat	366	403	.	.	.	Note=HEAT 4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12751	UniProtKB	Repeat	609	646	.	.	.	Note=HEAT 5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12751	UniProtKB	Repeat	655	692	.	.	.	Note=HEAT 6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12751	UniProtKB	Repeat	765	799	.	.	.	Note=HEAT 7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12751	UniProtKB	Repeat	800	836	.	.	.	Note=HEAT 8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12751	UniProtKB	Repeat	945	980	.	.	.	Note=HEAT 9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12751	UniProtKB	Compositional bias	49	56	.	.	.	Note=Poly-Ser;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12751	UniProtKB	Compositional bias	669	674	.	.	.	Note=Poly-Ser;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12751	UniProtKB	Compositional bias	815	818	.	.	.	Note=Poly-Lys;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P17558 1 318
+P17558	UniProtKB	Chain	1	318	.	.	.	ID=PRO_0000030589;Note=37S ribosomal protein PET123%2C mitochondrial	
+##sequence-region Q12378 1 196
+Q12378	UniProtKB	Chain	1	196	.	.	.	ID=PRO_0000244439;Note=RNA polymerase II subunit B1 CTD phosphatase RTR2	
+Q12378	UniProtKB	Zinc finger	52	123	.	.	.	Note=RTR1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812	
+Q12378	UniProtKB	Metal binding	75	75	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812	
+Q12378	UniProtKB	Metal binding	80	80	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812	
+Q12378	UniProtKB	Metal binding	99	99	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812	
+Q12378	UniProtKB	Metal binding	103	103	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812	
+##sequence-region Q12330 1 94
+Q12330	UniProtKB	Chain	1	94	.	.	.	ID=PRO_0000125535;Note=Small nuclear ribonucleoprotein E	
+Q12330	UniProtKB	Helix	13	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12330	UniProtKB	Beta strand	27	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12330	UniProtKB	Beta strand	34	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12330	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12330	UniProtKB	Beta strand	52	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12330	UniProtKB	Beta strand	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q12330	UniProtKB	Helix	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P38850 1 1070
+P38850	UniProtKB	Chain	1	1070	.	.	.	ID=PRO_0000097502;Note=Regulator of Ty1 transposition protein 107	
+P38850	UniProtKB	Domain	2	103	.	.	.	Note=BRCT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P38850	UniProtKB	Domain	117	213	.	.	.	Note=BRCT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P38850	UniProtKB	Domain	260	352	.	.	.	Note=BRCT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P38850	UniProtKB	Domain	369	453	.	.	.	Note=BRCT 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P38850	UniProtKB	Domain	829	910	.	.	.	Note=BRCT 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P38850	UniProtKB	Domain	934	1049	.	.	.	Note=BRCT 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
+P38850	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38850	UniProtKB	Modified residue	532	532	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38850	UniProtKB	Modified residue	591	591	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38850	UniProtKB	Modified residue	593	593	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38850	UniProtKB	Modified residue	720	720	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38850	UniProtKB	Modified residue	800	800	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38850	UniProtKB	Modified residue	806	806	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38850	UniProtKB	Helix	822	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Beta strand	837	844	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Helix	851	859	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Beta strand	862	864	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Helix	870	872	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Beta strand	876	878	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Helix	886	891	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Beta strand	899	901	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Helix	904	913	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Helix	927	930	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7I	
+P38850	UniProtKB	Helix	937	942	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Beta strand	945	947	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Helix	949	952	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Beta strand	957	961	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Helix	968	977	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Beta strand	982	986	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Turn	988	990	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Helix	993	995	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Beta strand	1011	1015	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Helix	1019	1032	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Beta strand	1038	1041	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Helix	1043	1051	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+P38850	UniProtKB	Beta strand	1063	1067	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K	
+##sequence-region P42847 1 217
+P42847	UniProtKB	Transit peptide	1	59	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978	
+P42847	UniProtKB	Chain	60	217	.	.	.	ID=PRO_0000030586;Note=37S ribosomal protein S18%2C mitochondrial	
+##sequence-region Q01163 1 450
+Q01163	UniProtKB	Transit peptide	1	14	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01163	UniProtKB	Chain	15	450	.	.	.	ID=PRO_0000202743;Note=37S ribosomal protein S23%2C mitochondrial	
+Q01163	UniProtKB	Nucleotide binding	150	157	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P51398	
+##sequence-region P40496 1 264
+P40496	UniProtKB	Chain	1	264	.	.	.	ID=PRO_0000202972;Note=37S ribosomal protein S25%2C mitochondrial	
+##sequence-region P53292 1 345
+P53292	UniProtKB	Transit peptide	1	27	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53292	UniProtKB	Chain	28	345	.	.	.	ID=PRO_0000202837;Note=37S ribosomal protein S35%2C mitochondrial	
+##sequence-region Q08281 1 1341
+Q08281	UniProtKB	Chain	1	1341	.	.	.	ID=PRO_0000223528;Note=Restriction of telomere capping protein 1	
+Q08281	UniProtKB	Repeat	207	248	.	.	.	Note=WD 1	
+Q08281	UniProtKB	Repeat	256	296	.	.	.	Note=WD 2	
+Q08281	UniProtKB	Repeat	305	342	.	.	.	Note=WD 3	
+Q08281	UniProtKB	Repeat	367	406	.	.	.	Note=WD 4	
+Q08281	UniProtKB	Repeat	439	486	.	.	.	Note=WD 5	
+Q08281	UniProtKB	Repeat	489	527	.	.	.	Note=WD 6	
+Q08281	UniProtKB	Repeat	843	883	.	.	.	Note=WD 7	
+Q08281	UniProtKB	Repeat	1129	1169	.	.	.	Note=WD 8	
+Q08281	UniProtKB	Repeat	1216	1255	.	.	.	Note=WD 9	
+Q08281	UniProtKB	Zinc finger	1293	1335	.	.	.	Note=RING-type%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+Q08281	UniProtKB	Compositional bias	753	765	.	.	.	Note=Poly-Asp	
+Q08281	UniProtKB	Modified residue	1036	1036	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08281	UniProtKB	Modified residue	1080	1080	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08281	UniProtKB	Modified residue	1087	1087	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08281	UniProtKB	Modified residue	1089	1089	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08281	UniProtKB	Modified residue	1123	1123	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08281	UniProtKB	Modified residue	1133	1133	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08281	UniProtKB	Sequence conflict	393	393	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08281	UniProtKB	Sequence conflict	393	393	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08281	UniProtKB	Sequence conflict	548	548	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08281	UniProtKB	Sequence conflict	548	548	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08281	UniProtKB	Sequence conflict	1222	1222	.	.	.	Note=D->DV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40084 1 226
+P40084	UniProtKB	Chain	1	226	.	.	.	ID=PRO_0000202653;Note=RNA polymerase II subunit B1 CTD phosphatase RTR1	
+P40084	UniProtKB	Zinc finger	50	136	.	.	.	Note=RTR1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812	
+P40084	UniProtKB	Metal binding	73	73	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812	
+P40084	UniProtKB	Metal binding	78	78	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812	
+P40084	UniProtKB	Metal binding	112	112	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812	
+P40084	UniProtKB	Metal binding	116	116	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812	
+P40084	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18408053;Dbxref=PMID:18408053	
+P40084	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Loss of function%3B when associated with S-116. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18408053;Dbxref=PMID:18408053	
+P40084	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Loss of function%3B when associated with S-112. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18408053;Dbxref=PMID:18408053	
+P40084	UniProtKB	Helix	4	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	23	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Beta strand	38	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Beta strand	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	45	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	57	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	91	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	105	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Beta strand	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	114	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Turn	136	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	146	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	158	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+P40084	UniProtKB	Helix	168	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y	
+##sequence-region Q00916 1 300
+Q00916	UniProtKB	Chain	1	300	.	.	.	ID=PRO_0000081886;Note=U1 small nuclear ribonucleoprotein 70 kDa homolog	
+Q00916	UniProtKB	Domain	107	198	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+Q00916	UniProtKB	Mutagenesis	18	98	.	.	.	Note=Severely temperature-sensitive. Defective in pre-mRNA splicing. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7565787;Dbxref=PMID:7565787	
+Q00916	UniProtKB	Mutagenesis	18	93	.	.	.	Note=Fails to complement the growth and splicing defective%2C temperature-sensitive phenotype of the null allele at 30 degrees Celsius. No association with U1 snRNP. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8643384;Dbxref=PMID:8643384	
+Q00916	UniProtKB	Mutagenesis	92	248	.	.	.	Note=Associates with U1 snRNP. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7565787,ECO:0000269|PubMed:8643384;Dbxref=PMID:7565787,PMID:8643384	
+Q00916	UniProtKB	Mutagenesis	148	148	.	.	.	Note=No splicing defects. Associates with U1 snRNP%3B when associated with T-150 and L-152. K->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7565787,ECO:0000269|PubMed:8643384;Dbxref=PMID:7565787,PMID:8643384	
+Q00916	UniProtKB	Mutagenesis	150	150	.	.	.	Note=No splicing defects. Associates with U1 snRNP%3B when associated with L-148 and L-152. Y->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7565787,ECO:0000269|PubMed:8643384;Dbxref=PMID:7565787,PMID:8643384	
+Q00916	UniProtKB	Mutagenesis	152	152	.	.	.	Note=No splicing defects. Associates with U1 snRNP%3B when associated with L-148 and T-150. F->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7565787,ECO:0000269|PubMed:8643384;Dbxref=PMID:7565787,PMID:8643384	
+##sequence-region P32605 1 298
+P32605	UniProtKB	Chain	1	298	.	.	.	ID=PRO_0000081891;Note=U1 small nuclear ribonucleoprotein A	
+P32605	UniProtKB	Domain	2	113	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P32605	UniProtKB	Domain	227	298	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P32605	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Sensitive in DMS protection of U1 snRNA%3B when associated with 6-I-N-7. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	6	7	.	.	.	Note=Sensitive in DMS protection of U1 snRNA%3B when associated with I-4. FQ->IN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Sensitive in DMS protection of U1 snRNA%3B when associated with 65-D--L-67. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	65	67	.	.	.	Note=Sensitive in DMS protection of U1 snRNA%3B when associated with I-63. VSI->DIL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	69	72	.	.	.	Note=Sensitive in DMS protection of U1 snRNA. RSSK->LKTM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	74	75	.	.	.	Note=Sensitive in DMS protection of U1 snRNA%3B when associated with 79-V-I-80. TN->RG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	79	80	.	.	.	Note=Sensitive in DMS protection of U1 snRNA%3B when associated with 74-R-G-75. LT->VI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	228	228	.	.	.	Note=Splicing defects%3B when associated with 230-F--T-232. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	230	232	.	.	.	Note=Splicing defects%3B when associated with I-228. LIQ->FLT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	258	260	.	.	.	Note=Splicing defects. VSV->PGH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	262	263	.	.	.	Note=Splicing defects%3B when associated with F-268. NL->DI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	268	268	.	.	.	Note=Splicing defects%3B when associated with 262-D-I-263. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	291	293	.	.	.	Note=Splicing defects%3B when associated with S-295. DVT->AMK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Mutagenesis	295	295	.	.	.	Note=Splicing defects%3B when associated with 291-A--K-293. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781	
+P32605	UniProtKB	Sequence conflict	1	3	.	.	.	Note=MSA->MTNKNR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08963 1 238
+Q08963	UniProtKB	Chain	1	238	.	.	.	ID=PRO_0000074189;Note=U2 small nuclear ribonucleoprotein A'	
+Q08963	UniProtKB	Repeat	53	74	.	.	.	Note=LRR 1	
+Q08963	UniProtKB	Repeat	75	95	.	.	.	Note=LRR 2	
+Q08963	UniProtKB	Repeat	97	118	.	.	.	Note=LRR 3	
+Q08963	UniProtKB	Domain	132	170	.	.	.	Note=LRRCT	
+Q08963	UniProtKB	Helix	5	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q08963	UniProtKB	Beta strand	13	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q08963	UniProtKB	Beta strand	34	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q08963	UniProtKB	Helix	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q08963	UniProtKB	Beta strand	55	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q08963	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q08963	UniProtKB	Beta strand	100	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q08963	UniProtKB	Helix	111	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q08963	UniProtKB	Beta strand	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q08963	UniProtKB	Helix	133	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q08963	UniProtKB	Helix	140	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q08963	UniProtKB	Beta strand	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P54999 1 86
+P54999	UniProtKB	Chain	1	86	.	.	.	ID=PRO_0000125544;Note=Small nuclear ribonucleoprotein F	
+P54999	UniProtKB	Helix	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R	
+P54999	UniProtKB	Beta strand	25	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R	
+P54999	UniProtKB	Beta strand	36	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R	
+P54999	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R	
+P54999	UniProtKB	Beta strand	51	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R	
+P54999	UniProtKB	Beta strand	63	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R	
+P54999	UniProtKB	Beta strand	70	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R	
+P54999	UniProtKB	Helix	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R	
+P54999	UniProtKB	Beta strand	78	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R	
+##sequence-region P25343 1 265
+P25343	UniProtKB	Chain	1	265	.	.	.	ID=PRO_0000192960;Note=Reduced viability upon starvation protein 161	
+P25343	UniProtKB	Domain	15	239	.	.	.	Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00361	
+P25343	UniProtKB	Coiled coil	126	193	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25343	UniProtKB	Sequence conflict	95	95	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P22470 1 610
+P22470	UniProtKB	Chain	1	610	.	.	.	ID=PRO_0000056162;Note=Protein SAN1	
+P22470	UniProtKB	Zinc finger	240	280	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+##sequence-region P53330 1 157
+P53330	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000097501;Note=Regulator of Ty1 transposition protein 102	
+P53330	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53330	UniProtKB	Modified residue	122	122	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53330	UniProtKB	Helix	3	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+P53330	UniProtKB	Beta strand	25	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+P53330	UniProtKB	Beta strand	60	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+P53330	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+##sequence-region Q02608 1 121
+Q02608	UniProtKB	Chain	1	121	.	.	.	ID=PRO_0000167326;Note=37S ribosomal protein S16%2C mitochondrial	
+##sequence-region P53047 1 317
+P53047	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000097510;Note=Protein RTA1	
+P53047	UniProtKB	Topological domain	1	16	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Topological domain	38	64	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Topological domain	86	99	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Topological domain	121	142	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Transmembrane	143	163	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Topological domain	164	178	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Topological domain	200	214	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Transmembrane	215	235	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Topological domain	236	259	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Transmembrane	260	280	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Topological domain	281	317	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53047	UniProtKB	Sequence conflict	234	234	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53850 1 401
+P53850	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000203384;Note=Restriction of telomere capping protein 4	
+P53850	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q12108 1 567
+Q12108	UniProtKB	Chain	1	567	.	.	.	ID=PRO_0000237657;Note=Restriction of telomere capping protein 5	
+##sequence-region P32608 1 588
+P32608	UniProtKB	Chain	1	588	.	.	.	ID=PRO_0000194312;Note=Retrograde regulation protein 2	
+##sequence-region Q04947 1 295
+Q04947	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000168168;Note=Reticulon-like protein 1	
+Q04947	UniProtKB	Topological domain	1	50	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04947	UniProtKB	Transmembrane	51	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04947	UniProtKB	Topological domain	74	142	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04947	UniProtKB	Transmembrane	143	163	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04947	UniProtKB	Topological domain	164	295	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04947	UniProtKB	Domain	20	220	.	.	.	Note=Reticulon;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00170	
+Q04947	UniProtKB	Coiled coil	265	295	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04947	UniProtKB	Compositional bias	9	16	.	.	.	Note=Poly-Gln	
+Q04947	UniProtKB	Modified residue	186	186	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q04947	UniProtKB	Modified residue	219	219	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04947	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40962 1 232
+P40962	UniProtKB	Chain	1	232	.	.	.	ID=PRO_0000046850;Note=Zinc finger protein RTS2	
+P40962	UniProtKB	Zinc finger	24	48	.	.	.	Note=C2H2-type	
+##sequence-region P20606 1 190
+P20606	UniProtKB	Chain	1	190	.	.	.	ID=PRO_0000206275;Note=Small COPII coat GTPase SAR1	
+P20606	UniProtKB	Nucleotide binding	30	37	.	.	.	Note=GTP	
+P20606	UniProtKB	Nucleotide binding	73	76	.	.	.	Note=GTP	
+P20606	UniProtKB	Nucleotide binding	132	135	.	.	.	Note=GTP	
+P20606	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P20606	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P20606	UniProtKB	Cross-link	133	133	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P20606	UniProtKB	Mutagenesis	32	32	.	.	.	Note=No cell growth at 37 degrees Celsius. Decreases GTP binding and ER-to-Golgi vesicle transport. D->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7822237,ECO:0000269|PubMed:8889833,ECO:0000269|PubMed:9756629;Dbxref=PMID:7822237,PMID:8889833,PMID:9756629	
+P20606	UniProtKB	Mutagenesis	36	36	.	.	.	Note=No cell growth at 23 or 37 degrees Celsius. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7822237;Dbxref=PMID:7822237	
+P20606	UniProtKB	Mutagenesis	54	54	.	.	.	Note=No cell growth at 23 or 37 degrees Celsius. Decreases GTP binding and impairs ER-to-Golgi vesicle transport. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7822237,ECO:0000269|PubMed:9756629;Dbxref=PMID:7822237,PMID:9756629	
+P20606	UniProtKB	Mutagenesis	73	73	.	.	.	Note=No cell growth at 23 or 37 degrees Celsius. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7822237;Dbxref=PMID:7822237	
+P20606	UniProtKB	Mutagenesis	77	77	.	.	.	Note=No cell growth at 23 or 37 degrees Celsius. Impairs ER-to-Golgi vesicle transport. H->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7822237,ECO:0000269|PubMed:9756629;Dbxref=PMID:7822237,PMID:9756629	
+P20606	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Decreases guanine nucleotide binding. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8889833,ECO:0000269|PubMed:9756629;Dbxref=PMID:8889833,PMID:9756629	
+P20606	UniProtKB	Mutagenesis	132	132	.	.	.	Note=No cell growth at 37 degrees Celsius. N->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7822237,ECO:0000269|PubMed:8889833;Dbxref=PMID:7822237,PMID:8889833	
+P20606	UniProtKB	Mutagenesis	171	171	.	.	.	Note=Normal cell growth. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7822237;Dbxref=PMID:7822237	
+P20606	UniProtKB	Beta strand	25	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Helix	36	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Beta strand	58	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Beta strand	67	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Helix	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Helix	84	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Beta strand	93	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Helix	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Helix	106	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Helix	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Beta strand	127	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV	
+P20606	UniProtKB	Helix	142	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Beta strand	166	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Turn	173	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P20606	UniProtKB	Helix	179	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+##sequence-region P28707 1 216
+P28707	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P28707	UniProtKB	Chain	2	216	.	.	.	ID=PRO_0000218959;Note=Co-chaperone protein SBA1	
+P28707	UniProtKB	Domain	5	108	.	.	.	Note=CS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00547	
+P28707	UniProtKB	Repeat	141	156	.	.	.	.	
+P28707	UniProtKB	Repeat	160	174	.	.	.	.	
+P28707	UniProtKB	Compositional bias	203	213	.	.	.	Note=Poly-Glu	
+P28707	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P28707	UniProtKB	Beta strand	17	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Beta strand	23	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Beta strand	33	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Beta strand	44	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Beta strand	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Beta strand	67	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Beta strand	77	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Beta strand	91	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Beta strand	98	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Beta strand	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Beta strand	115	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Turn	121	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+P28707	UniProtKB	Beta strand	127	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9	
+##sequence-region P06105 1 1222
+P06105	UniProtKB	Chain	1	1222	.	.	.	ID=PRO_0000050128;Note=Protein SCP160	
+P06105	UniProtKB	Domain	177	249	.	.	.	Note=KH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P06105	UniProtKB	Domain	634	702	.	.	.	Note=KH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P06105	UniProtKB	Domain	712	771	.	.	.	Note=KH 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P06105	UniProtKB	Domain	782	851	.	.	.	Note=KH 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P06105	UniProtKB	Domain	861	929	.	.	.	Note=KH 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P06105	UniProtKB	Domain	939	1001	.	.	.	Note=KH 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P06105	UniProtKB	Domain	1153	1216	.	.	.	Note=KH 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117	
+P06105	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P06105	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06105	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P06105	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P06105	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06105	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P06105	UniProtKB	Modified residue	630	630	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P06105	UniProtKB	Modified residue	1112	1112	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P06105	UniProtKB	Sequence conflict	287	287	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06105	UniProtKB	Sequence conflict	303	303	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06105	UniProtKB	Sequence conflict	308	308	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06105	UniProtKB	Sequence conflict	330	330	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06105	UniProtKB	Sequence conflict	362	362	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06105	UniProtKB	Sequence conflict	411	411	.	.	.	Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06105	UniProtKB	Sequence conflict	884	884	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06105	UniProtKB	Sequence conflict	886	886	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06105	UniProtKB	Sequence conflict	960	960	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06105	UniProtKB	Sequence conflict	1067	1067	.	.	.	Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06105	UniProtKB	Sequence conflict	1087	1087	.	.	.	Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P52871 1 88
+P52871	UniProtKB	Chain	1	88	.	.	.	ID=PRO_0000157262;Note=Protein transport protein SBH2	
+P52871	UniProtKB	Topological domain	1	61	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52871	UniProtKB	Transmembrane	62	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40541 1 1150
+P40541	UniProtKB	Chain	1	1150	.	.	.	ID=PRO_0000120191;Note=Cohesin subunit SCC3	
+P40541	UniProtKB	Domain	367	457	.	.	.	Note=SCD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00750	
+P40541	UniProtKB	Coiled coil	305	349	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40541	UniProtKB	Compositional bias	44	48	.	.	.	Note=Poly-Glu	
+P40541	UniProtKB	Compositional bias	65	70	.	.	.	Note=Poly-Asp	
+P40541	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40541	UniProtKB	Modified residue	628	628	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40541	UniProtKB	Sequence conflict	939	939	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40541	UniProtKB	Helix	675	678	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	680	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	700	707	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	721	736	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Turn	742	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	747	761	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	764	788	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	798	808	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	810	819	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	826	835	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	837	839	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	840	843	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	844	846	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	849	854	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	858	876	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Turn	890	893	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	894	911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Turn	917	919	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	920	946	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	953	962	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	969	989	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	1002	1005	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	1016	1032	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	1038	1045	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Turn	1046	1050	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+P40541	UniProtKB	Helix	1053	1058	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ	
+##sequence-region P03878 1 556
+P03878	UniProtKB	Region	1	240	.	.	.	Note=COX1 exons 1 to 4 encoded	
+P03878	UniProtKB	Region	241	556	.	.	.	Note=COX1 intron 4 encoded	
+P03878	UniProtKB	Natural variant	457	458	.	.	.	Note=In strain: D273-10B. IS->KT	
+P03878	UniProtKB	Mutagenesis	362	362	.	.	.	Note=Confers mRNA maturase activity. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6285204;Dbxref=PMID:6285204	
+P03878	UniProtKB	Sequence conflict	57	57	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03878	UniProtKB	Sequence conflict	69	69	.	.	.	Note=F->CT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03878	UniProtKB	Sequence conflict	224	224	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03878	UniProtKB	Sequence conflict	315	315	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03878	UniProtKB	Sequence conflict	320	320	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P03877 1 415
+P03877	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P03877	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P03877	UniProtKB	Region	1	81	.	.	.	Note=COX1 exons 1 to 3 encoded	
+P03877	UniProtKB	Region	82	415	.	.	.	Note=COX1 intron 3 encoded	
+P03877	UniProtKB	Compositional bias	88	92	.	.	.	Note=Poly-Asn	
+P03877	UniProtKB	Compositional bias	284	291	.	.	.	Note=Poly-Asn	
+P03877	UniProtKB	Natural variant	55	55	.	.	.	Note=In strain: Capensis / YB4237. F->Y	
+P03877	UniProtKB	Natural variant	60	60	.	.	.	Note=In strain: Capensis / YB4237. V->A	
+P03877	UniProtKB	Natural variant	71	71	.	.	.	Note=In strain: Capensis / YB4237. V->W	
+P03877	UniProtKB	Natural variant	76	76	.	.	.	Note=In strain: Capensis / YB4237. I->M	
+P03877	UniProtKB	Natural variant	399	399	.	.	.	Note=In strain: Capensis / YB4237. R->M	
+P03877	UniProtKB	Sequence conflict	122	122	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03877	UniProtKB	Sequence conflict	176	176	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03877	UniProtKB	Sequence conflict	200	200	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03877	UniProtKB	Sequence conflict	217	218	.	.	.	Note=TI->NQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03877	UniProtKB	Sequence conflict	247	248	.	.	.	Note=GM->IL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03877	UniProtKB	Sequence conflict	269	269	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03877	UniProtKB	Sequence conflict	284	284	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P03877	UniProtKB	Sequence conflict	380	380	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11792 1 824
+P11792	UniProtKB	Chain	1	824	.	.	.	ID=PRO_0000086638;Note=Serine/threonine-protein kinase SCH9	
+P11792	UniProtKB	Domain	185	361	.	.	.	Note=C2	
+P11792	UniProtKB	Domain	412	671	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P11792	UniProtKB	Domain	672	748	.	.	.	Note=AGC-kinase C-terminal	
+P11792	UniProtKB	Nucleotide binding	418	426	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P11792	UniProtKB	Compositional bias	227	267	.	.	.	Note=Asn-rich	
+P11792	UniProtKB	Active site	538	538	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P11792	UniProtKB	Binding site	441	441	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P11792	UniProtKB	Modified residue	570	570	.	.	.	Note=Phosphothreonine%3B by PKH1 or PKH2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17560372;Dbxref=PMID:17560372	
+P11792	UniProtKB	Modified residue	711	711	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17560372;Dbxref=PMID:17560372	
+P11792	UniProtKB	Modified residue	723	723	.	.	.	Note=Phosphothreonine%3B by TORC1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:17560372;Dbxref=PMID:17330950,PMID:19779198,PMID:17560372	
+P11792	UniProtKB	Modified residue	726	726	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:17560372;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:17560372	
+P11792	UniProtKB	Modified residue	737	737	.	.	.	Note=Phosphothreonine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17560372;Dbxref=PMID:17560372	
+P11792	UniProtKB	Modified residue	758	758	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17560372;Dbxref=PMID:17560372	
+P11792	UniProtKB	Modified residue	765	765	.	.	.	Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17560372;Dbxref=PMID:17560372	
+P11792	UniProtKB	Sequence conflict	366	366	.	.	.	Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11792	UniProtKB	Sequence conflict	751	751	.	.	.	Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P10663 1 115
+P10663	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000131017;Note=37S ribosomal protein MRP2%2C mitochondrial	
+##sequence-region P47150 1 247
+P47150	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47150	UniProtKB	Chain	27	247	.	.	.	ID=PRO_0000124541;Note=37S ribosomal protein S7%2C mitochondrial	
+##sequence-region P12686 1 339
+P12686	UniProtKB	Transit peptide	1	37	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978	
+P12686	UniProtKB	Chain	38	339	.	.	.	ID=PRO_0000030585;Note=37S ribosomal protein MRP13%2C mitochondrial	
+P12686	UniProtKB	Sequence conflict	114	114	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12686	UniProtKB	Sequence conflict	328	334	.	.	.	Note=PPPQEST->HSQDQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53733 1 91
+P53733	UniProtKB	Chain	1	91	.	.	.	ID=PRO_0000130025;Note=37S ribosomal protein S19%2C mitochondrial	
+##sequence-region P47141 1 266
+P47141	UniProtKB	Chain	1	266	.	.	.	ID=PRO_0000203110;Note=37S ribosomal protein S26%2C mitochondrial	
+##sequence-region P32607 1 177
+P32607	UniProtKB	Chain	1	177	.	.	.	ID=PRO_0000127433;Note=Retrograde regulation protein 1	
+P32607	UniProtKB	Domain	11	96	.	.	.	Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981	
+P32607	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32607	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32607	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32607	UniProtKB	Sequence conflict	105	113	.	.	.	Note=REEVELMVK->KRGGGTDGE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03940 1 463
+Q03940	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525518;Dbxref=PMID:15525518	
+Q03940	UniProtKB	Chain	2	463	.	.	.	ID=PRO_0000165661;Note=RuvB-like protein 1	
+Q03940	UniProtKB	Nucleotide binding	79	86	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03940	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylvaline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525518;Dbxref=PMID:15525518	
+Q03940	UniProtKB	Mutagenesis	85	85	.	.	.	Note=Lethal. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278922;Dbxref=PMID:11278922	
+Q03940	UniProtKB	Mutagenesis	312	312	.	.	.	Note=Lethal. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278922;Dbxref=PMID:11278922	
+##sequence-region P40204 1 77
+P40204	UniProtKB	Chain	1	77	.	.	.	ID=PRO_0000125552;Note=Small nuclear ribonucleoprotein G	
+P40204	UniProtKB	Beta strand	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40204	UniProtKB	Beta strand	13	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40204	UniProtKB	Turn	20	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40204	UniProtKB	Beta strand	23	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40204	UniProtKB	Beta strand	28	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40204	UniProtKB	Beta strand	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40204	UniProtKB	Beta strand	59	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40204	UniProtKB	Turn	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P40204	UniProtKB	Beta strand	68	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P32915 1 480
+P32915	UniProtKB	Chain	1	480	.	.	.	ID=PRO_0000131789;Note=Protein transport protein SEC61	
+P32915	UniProtKB	Topological domain	1	32	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Transmembrane	33	55	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Topological domain	56	75	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Transmembrane	76	95	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Topological domain	96	119	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Transmembrane	120	141	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Topological domain	142	146	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Topological domain	168	212	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Transmembrane	213	224	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Topological domain	225	240	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Transmembrane	241	260	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Topological domain	261	290	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Transmembrane	291	311	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Topological domain	312	361	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Transmembrane	362	381	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Topological domain	382	416	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Transmembrane	417	434	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Topological domain	435	437	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Transmembrane	438	459	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Topological domain	460	480	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32915	UniProtKB	Mutagenesis	273	273	.	.	.	Note=Severe growth defect. K->P%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991	
+P32915	UniProtKB	Mutagenesis	275	275	.	.	.	Note=Severe growth defect. R->D%2CG%2CP%2CQ%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991	
+P32915	UniProtKB	Mutagenesis	275	275	.	.	.	Note=Severe growth defect%3B lowers SRP-dependent and SRP-independent translocation. R->E%2CF%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991	
+P32915	UniProtKB	Mutagenesis	276	276	.	.	.	Note=Severe growth defect. G->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991	
+P32915	UniProtKB	Mutagenesis	405	405	.	.	.	Note=Severe growth defect. K->D%2CE%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991	
+P32915	UniProtKB	Mutagenesis	406	406	.	.	.	Note=Severe growth defect%3B lowers SRP-dependent translocation. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991	
+P32915	UniProtKB	Mutagenesis	406	406	.	.	.	Note=Severe growth defect%3B lowers SRP-dependent and SRP-independent translocation. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991	
+P32915	UniProtKB	Mutagenesis	406	406	.	.	.	Note=Severe growth defect. R->H%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991	
+##sequence-region P52870 1 82
+P52870	UniProtKB	Chain	1	82	.	.	.	ID=PRO_0000157261;Note=Protein transport protein SBH1	
+P52870	UniProtKB	Topological domain	1	53	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P52870	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12158 1 566
+Q12158	UniProtKB	Chain	1	566	.	.	.	ID=PRO_0000097881;Note=Sister chromatid cohesion protein 1	
+Q12158	UniProtKB	Compositional bias	258	261	.	.	.	Note=Poly-Asp	
+Q12158	UniProtKB	Site	180	181	.	.	.	Note=Cleavage%3B by ESP1	
+Q12158	UniProtKB	Site	268	269	.	.	.	Note=Cleavage%3B by ESP1	
+Q12158	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12158	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11371343;Dbxref=PMID:11371343	
+Q12158	UniProtKB	Modified residue	210	210	.	.	.	Note=N6-acetyllysine%3B by ECO1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+Q12158	UniProtKB	Modified residue	263	263	.	.	.	Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11371343;Dbxref=PMID:11371343	
+Q12158	UniProtKB	Modified residue	307	307	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12158	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12158	UniProtKB	Mutagenesis	175	175	.	.	.	Note=Reduces phosphorylation. Abolishes phosphorylation%3B when associated with A-263. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11371343;Dbxref=PMID:11371343	
+Q12158	UniProtKB	Mutagenesis	180	180	.	.	.	Note=Abolishes cleavage by ESP1%3B when associated with D-268. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10403247;Dbxref=PMID:10403247	
+Q12158	UniProtKB	Mutagenesis	210	210	.	.	.	Note=Loss of acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+Q12158	UniProtKB	Mutagenesis	252	252	.	.	.	Note=No effect on acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+Q12158	UniProtKB	Mutagenesis	263	263	.	.	.	Note=Reduces phosphorylation. Abolishes phosphorylation%3B when associated with A-175. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11371343;Dbxref=PMID:11371343	
+Q12158	UniProtKB	Mutagenesis	268	268	.	.	.	Note=Abolishes first cleavage by ESP1. Abolishes all cleavage by ESP1%3B when associated with D-180. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10403247;Dbxref=PMID:10403247	
+Q12158	UniProtKB	Mutagenesis	290	290	.	.	.	Note=No effect on acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+Q12158	UniProtKB	Mutagenesis	310	310	.	.	.	Note=No effect on acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+Q12158	UniProtKB	Mutagenesis	319	319	.	.	.	Note=No effect on acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+Q12158	UniProtKB	Mutagenesis	324	324	.	.	.	Note=No effect on acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574	
+Q12158	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+Q12158	UniProtKB	Helix	44	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+Q12158	UniProtKB	Turn	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+Q12158	UniProtKB	Beta strand	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+Q12158	UniProtKB	Helix	69	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+Q12158	UniProtKB	Beta strand	134	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP	
+Q12158	UniProtKB	Helix	484	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+Q12158	UniProtKB	Helix	504	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+Q12158	UniProtKB	Helix	522	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+Q12158	UniProtKB	Beta strand	539	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+Q12158	UniProtKB	Beta strand	551	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+Q12158	UniProtKB	Helix	557	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+##sequence-region P34758 1 872
+P34758	UniProtKB	Chain	1	872	.	.	.	ID=PRO_0000097621;Note=Protein SCD5	
+P34758	UniProtKB	Repeat	405	424	.	.	.	Note=1-1	
+P34758	UniProtKB	Repeat	439	458	.	.	.	Note=1-2	
+P34758	UniProtKB	Repeat	479	498	.	.	.	Note=1-3	
+P34758	UniProtKB	Repeat	534	545	.	.	.	Note=2-1	
+P34758	UniProtKB	Repeat	564	575	.	.	.	Note=2-2	
+P34758	UniProtKB	Repeat	593	604	.	.	.	Note=2-3	
+P34758	UniProtKB	Repeat	608	619	.	.	.	Note=2-4	
+P34758	UniProtKB	Repeat	623	634	.	.	.	Note=2-5	
+P34758	UniProtKB	Repeat	636	647	.	.	.	Note=2-5	
+P34758	UniProtKB	Repeat	650	661	.	.	.	Note=2-7	
+P34758	UniProtKB	Repeat	683	694	.	.	.	Note=2-8	
+P34758	UniProtKB	Repeat	717	728	.	.	.	Note=2-9	
+P34758	UniProtKB	Region	405	448	.	.	.	Note=3 X 20 AA approximate repeats	
+P34758	UniProtKB	Region	534	728	.	.	.	Note=9 X 12 AA approximate repeats	
+P34758	UniProtKB	Modified residue	564	564	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P21801 1 266
+P21801	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion	
+P21801	UniProtKB	Chain	21	266	.	.	.	ID=PRO_0000010353;Note=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit%2C mitochondrial	
+P21801	UniProtKB	Domain	36	127	.	.	.	Note=2Fe-2S ferredoxin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465	
+P21801	UniProtKB	Domain	169	199	.	.	.	Note=4Fe-4S ferredoxin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00711	
+P21801	UniProtKB	Metal binding	87	87	.	.	.	Note=Iron-sulfur 1 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Metal binding	92	92	.	.	.	Note=Iron-sulfur 1 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Metal binding	95	95	.	.	.	Note=Iron-sulfur 1 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Metal binding	107	107	.	.	.	Note=Iron-sulfur 1 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Metal binding	179	179	.	.	.	Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Metal binding	182	182	.	.	.	Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Metal binding	185	185	.	.	.	Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Metal binding	189	189	.	.	.	Note=Iron-sulfur 3 (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Metal binding	236	236	.	.	.	Note=Iron-sulfur 3 (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Metal binding	242	242	.	.	.	Note=Iron-sulfur 3 (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Metal binding	246	246	.	.	.	Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Binding site	194	194	.	.	.	Note=Ubiquinone%3B shared with DHSD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P21801	UniProtKB	Mutagenesis	260	266	.	.	.	Note=Abolishes SDH activity and complex assembly. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1390628;Dbxref=PMID:1390628	
+P21801	UniProtKB	Mutagenesis	260	260	.	.	.	Note=Abolishes SDH activity. No effect on complex assembly and stability%3B when associated with T-261. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1390628;Dbxref=PMID:1390628	
+P21801	UniProtKB	Mutagenesis	261	261	.	.	.	Note=Abolishes SDH activity. No effect on complex assembly and stability%3B when associated with T-260. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1390628;Dbxref=PMID:1390628	
+##sequence-region Q07534 1 307
+Q07534	UniProtKB	Chain	1	307	.	.	.	ID=PRO_0000240707;Note=Solute carrier family 25 member 38 homolog	
+Q07534	UniProtKB	Transmembrane	14	39	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064	
+Q07534	UniProtKB	Transmembrane	62	88	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064	
+Q07534	UniProtKB	Transmembrane	121	146	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064	
+Q07534	UniProtKB	Transmembrane	174	197	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064	
+Q07534	UniProtKB	Transmembrane	225	251	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064	
+Q07534	UniProtKB	Transmembrane	280	298	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064	
+Q07534	UniProtKB	Repeat	8	87	.	.	.	Note=Solcar 1	
+Q07534	UniProtKB	Repeat	115	199	.	.	.	Note=Solcar 2	
+Q07534	UniProtKB	Repeat	221	305	.	.	.	Note=Solcar 3	
+##sequence-region P43612 1 1002
+P43612	UniProtKB	Chain	1	1002	.	.	.	ID=PRO_0000097561;Note=SIT4-associating protein SAP155	
+P43612	UniProtKB	Compositional bias	938	997	.	.	.	Note=Asn-rich	
+P43612	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P43612	UniProtKB	Modified residue	255	255	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P43612	UniProtKB	Modified residue	613	613	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P43612	UniProtKB	Modified residue	618	618	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P43612	UniProtKB	Sequence conflict	663	663	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43612	UniProtKB	Sequence conflict	663	663	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43612	UniProtKB	Sequence conflict	668	668	.	.	.	Note=T->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43612	UniProtKB	Sequence conflict	674	690	.	.	.	Note=DLFKIKLYDTRIVSKIM->TYSKSNYMIRDCFQNN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43612	UniProtKB	Sequence conflict	815	824	.	.	.	Note=ELISPDIQVI->DYISRYSSN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P17121 1 654
+P17121	UniProtKB	Chain	1	654	.	.	.	ID=PRO_0000056764;Note=GTPase-activating protein SAC7	
+P17121	UniProtKB	Domain	134	393	.	.	.	Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172	
+P17121	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P17121	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P17121	UniProtKB	Modified residue	435	435	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P17121	UniProtKB	Modified residue	491	491	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P17121	UniProtKB	Modified residue	632	632	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q12136 1 610
+Q12136	UniProtKB	Chain	1	610	.	.	.	ID=PRO_0000114330;Note=Something about silencing protein 10	
+Q12136	UniProtKB	Compositional bias	75	86	.	.	.	Note=Poly-Glu	
+Q12136	UniProtKB	Compositional bias	167	172	.	.	.	Note=Poly-Glu	
+Q12136	UniProtKB	Compositional bias	360	365	.	.	.	Note=Poly-Glu	
+Q12136	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12136	UniProtKB	Modified residue	314	314	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12136	UniProtKB	Modified residue	316	316	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12136	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12136	UniProtKB	Modified residue	339	339	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12136	UniProtKB	Modified residue	477	477	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region Q04002 1 1493
+Q04002	UniProtKB	Chain	1	1493	.	.	.	ID=PRO_0000218603;Note=Sister chromatid cohesion protein 2	
+Q04002	UniProtKB	Repeat	695	732	.	.	.	Note=HEAT 1	
+Q04002	UniProtKB	Repeat	734	771	.	.	.	Note=HEAT 2	
+Q04002	UniProtKB	Repeat	806	843	.	.	.	Note=HEAT 3	
+Q04002	UniProtKB	Repeat	1132	1169	.	.	.	Note=HEAT 4	
+Q04002	UniProtKB	Repeat	1244	1281	.	.	.	Note=HEAT 5	
+Q04002	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	67	67	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphoserine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	157	157	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	236	236	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	305	305	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	320	320	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	360	360	.	.	.	Note=Phosphothreonine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	753	753	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	1179	1179	.	.	.	Note=Phosphoserine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	1182	1182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	1183	1183	.	.	.	Note=Phosphoserine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Modified residue	1185	1185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	67	67	.	.	.	Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-127%3B A-157%3B A-163%3B A-231%3B A-236%3B A-305 and A-320. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	67	67	.	.	.	Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-127%3B E-157%3B E-163%3B E-231%3B E-236%3B E-305 and E-320. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	127	127	.	.	.	Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-67%3B A-157%3B A-163%3B A-231%3B A-236%3B A-305 and A-320. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	127	127	.	.	.	Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-157%3B E-163%3B E-231%3B E-236%3B E-305 and E-320. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	157	157	.	.	.	Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-67%3B A-127%3B A-163%3B A-231%3B A-236%3B A-305 and A-320. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	157	157	.	.	.	Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-163%3B E-231%3B E-236%3B E-305 and E-320. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	163	163	.	.	.	Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-67%3B A-127%3B A-157%3B A-231%3B A-236%3B A-305 and A-320. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	163	163	.	.	.	Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-157%3B E-231%3B E-236%3B E-305 and E-320. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	231	231	.	.	.	Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-67%3B A-127%3B A-157%3B A-163%3B A-236%3B A-305 and A-320. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	231	231	.	.	.	Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-157%3B E-163%3B E-236%3B E-305 and E-320. In ssc2-2NE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-236%3B E-305 and E-320. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	236	236	.	.	.	Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-67%3B A-127%3B A-157%3B A-163%3B A-231%3B A-305 and A-320. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	236	236	.	.	.	Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-157%3B E-163%3B E-231%3B E-305 and E-320. In ssc2-2NE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-231%3B E-305 and E-320. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	305	305	.	.	.	Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%3B S-74%3B S-162%3B S-360%3B S-1179 and Ser-1183%3B when assocated with A-67%3B A-127%3B A-157%3B A-163%3B A-231%3B A-236 and A-320. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	305	305	.	.	.	Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-157%3B E-163%3B E-231%3B E-236 and E-320. In ssc2-2NE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-231%3B E-236 and E-320. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	320	320	.	.	.	Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at S-43%3B S-74%3B S-162%3B S-360%3B S-1179 and S-1183%3B when assocated with A-67%3B A-127%3B A-157%3B A-163%3B A-231%3B A-236 and A-305. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	320	320	.	.	.	Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-157%3B E-163%3B E-231%3B E-236 and E-305. In ssc2-2NE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-231%3B E-236 and E-305. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	753	753	.	.	.	Note=Mimics constitutive phosphorylation and causes inviability through protein instability. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	1182	1182	.	.	.	Note=In ssc2-CE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%3B when associated with E-1185. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Mutagenesis	1185	1185	.	.	.	Note=In ssc2-CE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%3B when associated with E-1182. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421	
+Q04002	UniProtKB	Turn	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+Q04002	UniProtKB	Helix	14	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+Q04002	UniProtKB	Turn	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+Q04002	UniProtKB	Helix	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+Q04002	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+Q04002	UniProtKB	Beta strand	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+Q04002	UniProtKB	Helix	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+Q04002	UniProtKB	Beta strand	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+Q04002	UniProtKB	Turn	106	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+Q04002	UniProtKB	Helix	112	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+Q04002	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+##sequence-region P40090 1 624
+P40090	UniProtKB	Chain	1	624	.	.	.	ID=PRO_0000193217;Note=MAU2 chromatid cohesion factor homolog	
+P40090	UniProtKB	Mutagenesis	256	256	.	.	.	Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-298%3B D-299%3B A-313%3B A-324%3B D-327%3B and D-331. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942	
+P40090	UniProtKB	Mutagenesis	298	298	.	.	.	Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B D-299%3B A-313%3B A-324%3B D-327%3B and D-331. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942	
+P40090	UniProtKB	Mutagenesis	299	299	.	.	.	Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B A-298%3B A-313%3B A-324%3B D-327%3B and D-331. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942	
+P40090	UniProtKB	Mutagenesis	313	313	.	.	.	Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B A-298%3B D-299%3B A-324%3B D-327%3B and D-331. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942	
+P40090	UniProtKB	Mutagenesis	324	324	.	.	.	Note=In scc4m35%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-327%3B A-331%3B A-540 and A-541. In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B A-298%3B D-299%3B A-313%3B D-327%3B and D-331. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942	
+P40090	UniProtKB	Mutagenesis	327	327	.	.	.	Note=In scc4m35%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-324%3B A-331%3B A-540 and A-541. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942	
+P40090	UniProtKB	Mutagenesis	327	327	.	.	.	Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B A-298%3B D-299%3B A-313%3B A-324 and D-331. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942	
+P40090	UniProtKB	Mutagenesis	331	331	.	.	.	Note=In scc4m35%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-324%3B A-327%3B A-540 and A-541. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942	
+P40090	UniProtKB	Mutagenesis	331	331	.	.	.	Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B A-298%3B D-299%3B A-313%3B A-324 and D-327. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942	
+P40090	UniProtKB	Mutagenesis	540	540	.	.	.	Note=In scc4m35%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-324%3B A-327%3B A-331 and A-541. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942	
+P40090	UniProtKB	Mutagenesis	541	541	.	.	.	Note=In scc4m35%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-324%3B A-327%3B A-331 and A-540. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942	
+P40090	UniProtKB	Beta strand	7	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	10	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Turn	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	34	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	62	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	83	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Turn	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	107	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	120	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	128	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	151	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	174	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	193	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	215	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	226	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	231	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	253	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Turn	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Beta strand	278	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Beta strand	286	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	293	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	298	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Turn	313	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	320	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	350	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	396	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	413	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	427	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Turn	450	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	453	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	475	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	480	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Turn	496	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	507	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	543	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	561	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	575	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	582	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+P40090	UniProtKB	Helix	602	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN	
+##sequence-region P45978 1 349
+P45978	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P45978	UniProtKB	Chain	2	349	.	.	.	ID=PRO_0000097622;Note=Protein SCD6	
+P45978	UniProtKB	Domain	193	229	.	.	.	Note=DFDF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00845	
+P45978	UniProtKB	Motif	241	257	.	.	.	Note=FFD box	
+P45978	UniProtKB	Motif	260	280	.	.	.	Note=TFG box	
+P45978	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P03882 1 235
+P03882	UniProtKB	Chain	1	235	.	.	.	ID=PRO_0000192785;Note=Intron-encoded endonuclease I-SceI	
+P03882	UniProtKB	Helix	6	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Beta strand	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OOR	
+P03882	UniProtKB	Helix	17	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	31	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Beta strand	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Beta strand	50	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R7M	
+P03882	UniProtKB	Beta strand	56	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	65	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Beta strand	84	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Beta strand	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0X	
+P03882	UniProtKB	Beta strand	95	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	110	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Beta strand	117	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	128	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	135	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Beta strand	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Beta strand	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OOR	
+P03882	UniProtKB	Beta strand	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	169	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Beta strand	187	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Beta strand	195	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	202	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	205	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+P03882	UniProtKB	Helix	218	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W	
+##sequence-region P32564 1 187
+P32564	UniProtKB	Chain	1	187	.	.	.	ID=PRO_0000097626;Note=Protein SCM4	
+P32564	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32564	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32564	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32564	UniProtKB	Transmembrane	162	182	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04951 1 389
+Q04951	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04951	UniProtKB	Propeptide	19	29	.	.	.	ID=PRO_0000011901;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9748433;Dbxref=PMID:9748433	
+Q04951	UniProtKB	Chain	30	389	.	.	.	ID=PRO_0000011902;Note=Probable family 17 glucosidase SCW10	
+Q04951	UniProtKB	Compositional bias	65	134	.	.	.	Note=Ser-rich	
+Q04951	UniProtKB	Active site	326	326	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04951	UniProtKB	Active site	380	380	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04951	UniProtKB	Glycosylation	279	279	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04951	UniProtKB	Sequence conflict	38	39	.	.	.	Note=AQ->QE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03323 1 175
+Q03323	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000114686;Note=COMPASS component SDC1	
+Q03323	UniProtKB	Region	121	162	.	.	.	Note=DPY-30	
+##sequence-region P13856 1 272
+P13856	UniProtKB	Chain	1	269	.	.	.	ID=PRO_0000082691;Note=Ras-related protein RSR1	
+P13856	UniProtKB	Propeptide	270	272	.	.	.	ID=PRO_0000281342;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13856	UniProtKB	Nucleotide binding	10	17	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13856	UniProtKB	Nucleotide binding	57	61	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13856	UniProtKB	Nucleotide binding	116	119	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13856	UniProtKB	Motif	32	40	.	.	.	Note=Effector region;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13856	UniProtKB	Modified residue	269	269	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P13856	UniProtKB	Lipidation	269	269	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P46654 1 252
+P46654	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03015,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.4;Dbxref=PMID:10601260	
+P46654	UniProtKB	Chain	2	252	.	.	.	ID=PRO_0000134371;Note=40S ribosomal protein S0-B	
+P46654	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03015,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.4;Dbxref=PMID:10601260	
+##sequence-region P10662 1 321
+P10662	UniProtKB	Transit peptide	1	13	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10662	UniProtKB	Chain	14	321	.	.	.	ID=PRO_0000087698;Note=37S ribosomal protein MRP1%2C mitochondrial	
+P10662	UniProtKB	Sequence conflict	113	113	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P10662	UniProtKB	Sequence conflict	319	319	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32902 1 394
+P32902	UniProtKB	Transit peptide	1	25	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32902	UniProtKB	Chain	26	394	.	.	.	ID=PRO_0000134345;Note=37S ribosomal protein MRP4%2C mitochondrial	
+##sequence-region P33759 1 307
+P33759	UniProtKB	Transit peptide	1	13	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33759	UniProtKB	Chain	14	307	.	.	.	ID=PRO_0000131688;Note=37S ribosomal protein S5%2C mitochondrial	
+P33759	UniProtKB	Domain	144	208	.	.	.	Note=S5 DRBM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00268	
+##sequence-region Q03799 1 155
+Q03799	UniProtKB	Chain	1	155	.	.	.	ID=PRO_0000126599;Note=37S ribosomal protein S8%2C mitochondrial	
+##sequence-region Q12100 1 620
+Q12100	UniProtKB	Chain	1	620	.	.	.	ID=PRO_0000248408;Note=Probable serine/threonine-protein kinase RTK1	
+Q12100	UniProtKB	Domain	302	575	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12100	UniProtKB	Nucleotide binding	308	316	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12100	UniProtKB	Active site	430	430	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q12100	UniProtKB	Binding site	330	330	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12100	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12100	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12100	UniProtKB	Modified residue	216	216	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12100	UniProtKB	Cross-link	334	334	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P53289 1 263
+P53289	UniProtKB	Chain	1	263	.	.	.	ID=PRO_0000202835;Note=Protein phosphatase type 2A regulatory subunit RTS3	
+P53289	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53289	UniProtKB	Modified residue	192	192	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53289	UniProtKB	Modified residue	214	214	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53289	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53289	UniProtKB	Natural variant	20	20	.	.	.	Note=V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.1	
+P53289	UniProtKB	Natural variant	201	201	.	.	.	Note=P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.1	
+##sequence-region Q12242 1 671
+Q12242	UniProtKB	Chain	1	671	.	.	.	ID=PRO_0000269644;Note=UBA domain-containing protein RUP1	
+Q12242	UniProtKB	Domain	1	41	.	.	.	Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
+Q12242	UniProtKB	Coiled coil	432	501	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12242	UniProtKB	Compositional bias	354	399	.	.	.	Note=Glu-rich	
+Q12242	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P39743 1 482
+P39743	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39743	UniProtKB	Chain	2	482	.	.	.	ID=PRO_0000192961;Note=Reduced viability upon starvation protein 167	
+P39743	UniProtKB	Domain	17	254	.	.	.	Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00361	
+P39743	UniProtKB	Domain	421	482	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P39743	UniProtKB	Coiled coil	31	64	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39743	UniProtKB	Coiled coil	174	204	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39743	UniProtKB	Compositional bias	292	427	.	.	.	Note=Ala/Gly/Pro-rich	
+P39743	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39743	UniProtKB	Modified residue	299	299	.	.	.	Note=Phosphoserine%3B by FUS3 and PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857883;Dbxref=PMID:12857883	
+P39743	UniProtKB	Modified residue	321	321	.	.	.	Note=Phosphoserine%3B by FUS3 and PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857883;Dbxref=PMID:12857883	
+P39743	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphoserine%3B by FUS3 and PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857883;Dbxref=PMID:12857883	
+P39743	UniProtKB	Cross-link	242	242	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P39743	UniProtKB	Cross-link	481	481	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P38255 1 430
+P38255	UniProtKB	Chain	1	430	.	.	.	ID=PRO_0000202482;Note=Transcriptional regulatory protein RXT2	
+##sequence-region P50110 1 327
+P50110	UniProtKB	Chain	1	327	.	.	.	ID=PRO_0000072630;Note=Sorting assembly machinery 37 kDa subunit	
+P50110	UniProtKB	Transmembrane	17	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50110	UniProtKB	Transmembrane	247	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40856 1 1058
+P40856	UniProtKB	Chain	1	1058	.	.	.	ID=PRO_0000046106;Note=SIT4-associating protein SAP185	
+P40856	UniProtKB	Cross-link	20	20	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P89114 1 91
+P89114	UniProtKB	Chain	1	91	.	.	.	ID=PRO_0000269645;Note=Pachytene arrest protein SAE3	
+##sequence-region P38352 1 637
+P38352	UniProtKB	Chain	1	637	.	.	.	ID=PRO_0000206658;Note=SCF-associated factor 1	
+P38352	UniProtKB	Domain	14	63	.	.	.	Note=F-box	
+P38352	UniProtKB	Repeat	109	202	.	.	.	Note=RCC1 1	
+P38352	UniProtKB	Repeat	565	635	.	.	.	Note=RCC1 2	
+P38352	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38352	UniProtKB	Modified residue	266	266	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38352	UniProtKB	Mutagenesis	24	24	.	.	.	Note=In saf1-5%3B impairs the interaction with SKP1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+P38352	UniProtKB	Mutagenesis	35	35	.	.	.	Note=In saf1-6%3B impairs the interaction with SKP1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+P38352	UniProtKB	Mutagenesis	263	263	.	.	.	Note=In saf1-4%3B impairs the protein stability%3B when associated with K-264. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+P38352	UniProtKB	Mutagenesis	264	264	.	.	.	Note=In saf1-4%3B impairs the protein stability%3B when associated with K-263. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+P38352	UniProtKB	Mutagenesis	372	372	.	.	.	Note=In saf1-1%3B impairs the protein stability. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+P38352	UniProtKB	Mutagenesis	387	387	.	.	.	Note=In saf1-2%3B impairs the protein stability. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+P38352	UniProtKB	Mutagenesis	580	580	.	.	.	Note=In saf1-3%3B impairs the protein stability. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885	
+##sequence-region P20840 1 650
+P20840	UniProtKB	Signal peptide	1	19	.	.	.	.	
+P20840	UniProtKB	Chain	20	627	.	.	.	ID=PRO_0000022265;Note=Alpha-agglutinin	
+P20840	UniProtKB	Propeptide	628	650	.	.	.	ID=PRO_0000022266;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20840	UniProtKB	Repeat	339	378	.	.	.	Note=1	
+P20840	UniProtKB	Repeat	384	423	.	.	.	Note=2	
+P20840	UniProtKB	Region	216	322	.	.	.	Note=Ig-like fold domain important for alpha-agglutinin activity%2C contributing to a functional binding site for a-agglutinin	
+P20840	UniProtKB	Region	339	423	.	.	.	Note=2 X 40 AA tandem repeats	
+P20840	UniProtKB	Compositional bias	331	359	.	.	.	Note=Ser/Thr-rich	
+P20840	UniProtKB	Site	348	348	.	.	.	Note=Not glycosylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Lipidation	627	627	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20840	UniProtKB	Glycosylation	79	79	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20840	UniProtKB	Glycosylation	109	109	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20840	UniProtKB	Glycosylation	135	135	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20840	UniProtKB	Glycosylation	248	248	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	282	282	.	.	.	Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	289	289	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	299	299	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	303	303	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	306	306	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	307	307	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	308	308	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	311	311	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	314	314	.	.	.	Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	315	315	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	316	316	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	329	329	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	331	331	.	.	.	Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	334	334	.	.	.	Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	335	335	.	.	.	Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	338	338	.	.	.	Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	339	339	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	340	340	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	341	341	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	342	342	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	345	345	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	346	346	.	.	.	Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	349	349	.	.	.	Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	350	350	.	.	.	Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Glycosylation	364	364	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20840	UniProtKB	Glycosylation	402	402	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20840	UniProtKB	Glycosylation	460	460	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20840	UniProtKB	Glycosylation	485	485	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20840	UniProtKB	Glycosylation	501	501	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20840	UniProtKB	Glycosylation	614	614	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20840	UniProtKB	Disulfide bond	97	114	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Disulfide bond	202	300	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821	
+P20840	UniProtKB	Mutagenesis	211	211	.	.	.	Note=Little effect on secreted alpha-agglutinin activity. T->I	
+P20840	UniProtKB	Mutagenesis	214	214	.	.	.	Note=No effect on secreted alpha-agglutinin activity. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	215	215	.	.	.	Note=Little or no effect on secreted alpha-agglutinin activity. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Complete loss of alpha-agglutinin activity. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	216	216	.	.	.	Note=No effect on secreted alpha-agglutinin activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Decreases secreted alpha-agglutinin activity by 100-fold. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Decreases secreted alpha-agglutinin activity by 10-fold. Y->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Little effect on secreted alpha-agglutinin activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Decreases secreted alpha-agglutinin activity by 10-fold. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Decreases secreted alpha-agglutinin activity by less than 2-fold. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	290	290	.	.	.	Note=Decreases secreted alpha-agglutinin activity by less than 2-fold. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	291	291	.	.	.	Note=Decreases secreted alpha-agglutinin activity by 4-fold. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	292	292	.	.	.	Note=Almost complete loss of secreted alpha-agglutinin activity. H->L%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	294	294	.	.	.	Note=Decreases secreted alpha-agglutinin activity by more than 20-fold. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	295	295	.	.	.	Note=Decreases secreted alpha-agglutinin activity by 2-fold. E->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	296	296	.	.	.	Note=Decreases secreted alpha-agglutinin activity by more than 20-fold. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	298	298	.	.	.	Note=Decreases secreted alpha-agglutinin activity by less than 2-fold. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	322	322	.	.	.	Note=Decreases secreted alpha-agglutinin activity by 60-fold. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	322	322	.	.	.	Note=Almost complete loss of secreted alpha-agglutinin activity by 10-fold. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	322	322	.	.	.	Note=Decreases secreted alpha-agglutinin activity by 15-fold. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	323	323	.	.	.	Note=Decreases secreted alpha-agglutinin activity by 2-fold. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	324	324	.	.	.	Note=Little effect on secreted alpha-agglutinin activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Mutagenesis	325	325	.	.	.	Note=Little effect on secreted alpha-agglutinin activity. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846	
+P20840	UniProtKB	Sequence conflict	449	449	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20840	UniProtKB	Sequence conflict	556	556	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20840	UniProtKB	Sequence conflict	581	581	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39954 1 449
+P39954	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39954	UniProtKB	Chain	2	449	.	.	.	ID=PRO_0000116937;Note=Adenosylhomocysteinase	
+P39954	UniProtKB	Nucleotide binding	160	162	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39954	UniProtKB	Nucleotide binding	223	228	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39954	UniProtKB	Nucleotide binding	302	304	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39954	UniProtKB	Binding site	58	58	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39954	UniProtKB	Binding site	134	134	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39954	UniProtKB	Binding site	159	159	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39954	UniProtKB	Binding site	189	189	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39954	UniProtKB	Binding site	193	193	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39954	UniProtKB	Binding site	194	194	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39954	UniProtKB	Binding site	246	246	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39954	UniProtKB	Binding site	349	349	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39954	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39954	UniProtKB	Modified residue	393	393	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P39954	UniProtKB	Cross-link	21	21	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P39954	UniProtKB	Cross-link	413	413	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q08985 1 325
+Q08985	UniProtKB	Chain	1	325	.	.	.	ID=PRO_0000114619;Note=Homocysteine S-methyltransferase 2	
+Q08985	UniProtKB	Domain	6	321	.	.	.	Note=Hcy-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333	
+Q08985	UniProtKB	Metal binding	239	239	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333	
+Q08985	UniProtKB	Metal binding	306	306	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333	
+Q08985	UniProtKB	Metal binding	307	307	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333	
+Q08985	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q08873 1 200
+Q08873	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08873	UniProtKB	Chain	2	200	.	.	.	ID=PRO_0000204795;Note=Transgelin	
+Q08873	UniProtKB	Domain	26	136	.	.	.	Note=Calponin-homology (CH);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044	
+Q08873	UniProtKB	Region	151	164	.	.	.	Note=Interaction with SH3 domain of ABP1	
+Q08873	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q08873	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q08873	UniProtKB	Mutagenesis	185	185	.	.	.	Note=Greatly reduces actin-binding and actin-bundling activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857851;Dbxref=PMID:12857851	
+Q08873	UniProtKB	Mutagenesis	185	185	.	.	.	Note=Moderately reduces actin-binding and actin-bundling activity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857851;Dbxref=PMID:12857851	
+##sequence-region P40075 1 244
+P40075	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5	
+P40075	UniProtKB	Chain	2	244	.	.	.	ID=PRO_0000213467;Note=Vesicle-associated membrane protein-associated protein SCS2	
+P40075	UniProtKB	Topological domain	2	222	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40075	UniProtKB	Transmembrane	223	243	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40075	UniProtKB	Topological domain	244	244	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40075	UniProtKB	Domain	3	126	.	.	.	Note=MSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00132	
+P40075	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5	
+P40075	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P40075	UniProtKB	Mutagenesis	40	40	.	.	.	Note=Disrupts binding to FFAT motif and causes OPI1 mislocalization. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15668246;Dbxref=PMID:15668246	
+P40075	UniProtKB	Mutagenesis	41	42	.	.	.	Note=Disrupts binding to FFAT motif and causes OPI1 mislocalization. TT->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15668246;Dbxref=PMID:15668246	
+P40075	UniProtKB	Mutagenesis	84	84	.	.	.	Note=Disrupts binding to FFAT motif%3B when associated with D-86. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16004875;Dbxref=PMID:16004875	
+P40075	UniProtKB	Mutagenesis	86	86	.	.	.	Note=Disrupts binding to FFAT motif%3B when associated with D-84. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16004875;Dbxref=PMID:16004875	
+P40075	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Reduces binding to FFAT motif and impairs OPI1 function. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15668246;Dbxref=PMID:15668246	
+##sequence-region Q08230 1 162
+Q08230	UniProtKB	Transit peptide	1	35	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19837041;Dbxref=PMID:19837041	
+Q08230	UniProtKB	Chain	36	162	.	.	.	ID=PRO_0000007814;Note=Succinate dehydrogenase assembly factor 2%2C mitochondrial	
+Q08230	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Loss of covalent FAD in SDH1. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23062074;Dbxref=PMID:23062074	
+Q08230	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Loss of covalent FAD in SDH1. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23062074;Dbxref=PMID:23062074	
+Q08230	UniProtKB	Mutagenesis	98	99	.	.	.	Note=No effect. EE->KK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23062074;Dbxref=PMID:23062074	
+Q08230	UniProtKB	Mutagenesis	113	113	.	.	.	Note=Loss of covalent FAD in SDH1. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23062074;Dbxref=PMID:23062074	
+Q08230	UniProtKB	Helix	62	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4	
+Q08230	UniProtKB	Helix	79	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4	
+Q08230	UniProtKB	Helix	98	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4	
+Q08230	UniProtKB	Helix	112	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4	
+Q08230	UniProtKB	Turn	123	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4	
+Q08230	UniProtKB	Helix	130	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4	
+Q08230	UniProtKB	Helix	136	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4	
+##sequence-region P40357 1 651
+P40357	UniProtKB	Chain	1	651	.	.	.	ID=PRO_0000213613;Note=Protein transport protein SEC9	
+P40357	UniProtKB	Domain	434	496	.	.	.	Note=t-SNARE coiled-coil homology 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+P40357	UniProtKB	Domain	588	650	.	.	.	Note=t-SNARE coiled-coil homology 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+P40357	UniProtKB	Modified residue	79	79	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40357	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40357	UniProtKB	Modified residue	186	186	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40357	UniProtKB	Modified residue	190	190	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40357	UniProtKB	Modified residue	213	213	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40357	UniProtKB	Modified residue	271	271	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40357	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40357	UniProtKB	Modified residue	315	315	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40357	UniProtKB	Modified residue	355	355	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40357	UniProtKB	Modified residue	359	359	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40357	UniProtKB	Helix	433	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B5N	
+P40357	UniProtKB	Helix	589	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B5N	
+##sequence-region Q01589 1 338
+Q01589	UniProtKB	Signal peptide	1	18	.	.	.	.	
+Q01589	UniProtKB	Chain	19	318	.	.	.	ID=PRO_0000022292;Note=Cell wall protein SED1	
+Q01589	UniProtKB	Propeptide	319	338	.	.	.	ID=PRO_0000022293;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01589	UniProtKB	Repeat	58	65	.	.	.	Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q01589	UniProtKB	Repeat	66	79	.	.	.	Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q01589	UniProtKB	Repeat	80	93	.	.	.	Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q01589	UniProtKB	Repeat	94	101	.	.	.	Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q01589	UniProtKB	Repeat	102	115	.	.	.	Note=1-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q01589	UniProtKB	Repeat	116	123	.	.	.	Note=1-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q01589	UniProtKB	Repeat	124	137	.	.	.	Note=1-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q01589	UniProtKB	Repeat	169	211	.	.	.	Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q01589	UniProtKB	Repeat	220	262	.	.	.	Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015	
+Q01589	UniProtKB	Region	58	137	.	.	.	Note=7 X approximate tandem repeats	
+Q01589	UniProtKB	Region	169	262	.	.	.	Note=2 X 43 AA repeats	
+Q01589	UniProtKB	Lipidation	318	318	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01589	UniProtKB	Glycosylation	22	22	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01589	UniProtKB	Glycosylation	56	56	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01589	UniProtKB	Glycosylation	78	78	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01589	UniProtKB	Glycosylation	92	92	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01589	UniProtKB	Glycosylation	114	114	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01589	UniProtKB	Glycosylation	136	136	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01589	UniProtKB	Glycosylation	152	152	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01589	UniProtKB	Natural variant	80	93	.	.	.	Note=In strain: CBS 1171 and in allele SED1-1%2C SED1-2%2C SED1-3%2C SED1-4%2C SED1-5%2C SED1-6 and SED1-7. Missing	
+Q01589	UniProtKB	Natural variant	94	94	.	.	.	Note=In allele SED1-2. T->TSTEAPTTDTTSEAPTTAIPTNG	
+Q01589	UniProtKB	Natural variant	94	94	.	.	.	Note=In allele SED1-5. T->TSTEAPTTDTTTEAPTTAIPTNG	
+Q01589	UniProtKB	Natural variant	94	94	.	.	.	Note=In allele SED1-3 and SED1-6. T->TSTEAPTTDTTTEAPTTALPTNGTSTEAPTDTTTEAPTTALPTNG	
+Q01589	UniProtKB	Natural variant	212	212	.	.	.	Note=In allele SED1-4%2C SED1-5 and SED1-6. P->PTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEK	
+Q01589	UniProtKB	Natural variant	212	212	.	.	.	Note=In allele SED1-7. P->PTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEKPTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEK	
+Q01589	UniProtKB	Sequence conflict	309	309	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q01590 1 340
+Q01590	UniProtKB	Chain	1	340	.	.	.	ID=PRO_0000210273;Note=Integral membrane protein SED5	
+Q01590	UniProtKB	Topological domain	1	319	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01590	UniProtKB	Transmembrane	320	340	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01590	UniProtKB	Domain	249	311	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+Q01590	UniProtKB	Coiled coil	146	173	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q01590	UniProtKB	Mutagenesis	206	206	.	.	.	Note=Loss of interaction with SEC23/SEC24 complex. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941276;Dbxref=PMID:12941276	
+Q01590	UniProtKB	Helix	1	4	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+Q01590	UniProtKB	Helix	7	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+##sequence-region P34228 1 1148
+P34228	UniProtKB	Chain	1	1148	.	.	.	ID=PRO_0000114977;Note=Putative transcription factor SEF1	
+P34228	UniProtKB	DNA binding	57	87	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P34228	UniProtKB	Compositional bias	278	322	.	.	.	Note=Thr-rich	
+P34228	UniProtKB	Compositional bias	536	539	.	.	.	Note=Poly-Asn	
+P34228	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34228	UniProtKB	Modified residue	263	263	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34228	UniProtKB	Modified residue	806	806	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P16658 1 377
+P16658	UniProtKB	Chain	1	377	.	.	.	ID=PRO_0000109462;Note=tRNA-splicing endonuclease subunit SEN2	
+P16658	UniProtKB	Coiled coil	119	174	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P16658	UniProtKB	Active site	289	289	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16658	UniProtKB	Active site	297	297	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16658	UniProtKB	Active site	328	328	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P16658	UniProtKB	Natural variant	292	292	.	.	.	Note=In the cold-sensitive allele sen2-3%3B defective in cleavage only at the 5'-splice site of tRNA precursors. G->E	
+##sequence-region P36123 1 1033
+P36123	UniProtKB	Chain	1	1033	.	.	.	ID=PRO_0000046107;Note=SIT4-associating protein SAP190	
+P36123	UniProtKB	Modified residue	774	774	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P36123	UniProtKB	Modified residue	857	857	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36123	UniProtKB	Modified residue	862	862	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36123	UniProtKB	Modified residue	892	892	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36123	UniProtKB	Modified residue	990	990	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36123	UniProtKB	Modified residue	991	991	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32368 1 623
+P32368	UniProtKB	Chain	1	623	.	.	.	ID=PRO_0000209737;Note=Phosphoinositide phosphatase SAC1	
+P32368	UniProtKB	Topological domain	1	521	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32368	UniProtKB	Transmembrane	522	544	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32368	UniProtKB	Topological domain	545	623	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32368	UniProtKB	Domain	115	454	.	.	.	Note=SAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00183	
+P32368	UniProtKB	Compositional bias	507	521	.	.	.	Note=Pro-rich	
+P32368	UniProtKB	Cross-link	246	246	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32368	UniProtKB	Cross-link	358	358	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32368	UniProtKB	Beta strand	5	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	13	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	28	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Turn	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	38	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	53	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	67	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	85	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Turn	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TU3	
+P32368	UniProtKB	Helix	106	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TU3	
+P32368	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	136	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	148	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Turn	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Turn	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	163	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	173	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	183	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	197	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	213	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	230	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Turn	242	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	247	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	261	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	269	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	279	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	297	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	313	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	330	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Turn	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	344	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	366	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	377	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Beta strand	386	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	396	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Helix	431	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+P32368	UniProtKB	Turn	449	451	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT	
+##sequence-region P46674 1 1301
+P46674	UniProtKB	Chain	1	1301	.	.	.	ID=PRO_0000097562;Note=Nuclear mRNA export protein SAC3	
+P46674	UniProtKB	Region	1	572	.	.	.	Note=Required for interaction with MEX67%2C SUB2 and THP1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12411502;Dbxref=PMID:12411502	
+P46674	UniProtKB	Region	573	1301	.	.	.	Note=Required for targeting SAC3 to the nuclear pore	
+P46674	UniProtKB	Region	733	860	.	.	.	Note=Interaction with CDC31;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15311284;Dbxref=PMID:15311284	
+P46674	UniProtKB	Modified residue	568	568	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46674	UniProtKB	Modified residue	748	748	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14718168;Dbxref=PMID:14718168	
+P46674	UniProtKB	Modified residue	866	866	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P46674	UniProtKB	Helix	258	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Turn	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	280	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	302	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	331	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	362	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	378	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	388	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	394	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	426	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	440	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	447	449	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	450	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	474	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	486	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Turn	502	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	508	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Beta strand	514	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	530	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	541	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V	
+P46674	UniProtKB	Helix	753	803	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB	
+##sequence-region P43589 1 448
+P43589	UniProtKB	Chain	1	448	.	.	.	ID=PRO_0000202682;Note=Pre-mRNA-splicing factor SAD1	
+P43589	UniProtKB	Domain	150	447	.	.	.	Note=USP	
+P43589	UniProtKB	Zinc finger	46	107	.	.	.	Note=UBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
+P43589	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P43589	UniProtKB	Helix	30	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Turn	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	55	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Turn	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	75	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Turn	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Turn	99	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	108	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	112	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	127	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	155	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	172	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	188	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	206	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	213	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	232	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	248	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	260	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	281	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	310	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	313	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	318	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	331	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	339	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	352	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Turn	355	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	363	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	368	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	375	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	403	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Turn	413	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	417	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	425	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Helix	431	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+P43589	UniProtKB	Beta strand	437	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX	
+##sequence-region P14693 1 329
+P14693	UniProtKB	Chain	1	329	.	.	.	ID=PRO_0000202903;Note=Sorting assembly machinery 35 kDa subunit	
+##sequence-region Q08986 1 587
+Q08986	UniProtKB	Chain	1	587	.	.	.	ID=PRO_0000054163;Note=S-adenosylmethionine permease SAM3	
+Q08986	UniProtKB	Topological domain	1	80	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	81	103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	104	109	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	110	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	130	162	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	163	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	184	186	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	187	207	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	208	219	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	220	240	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	241	266	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	288	302	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	303	323	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	324	360	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	361	381	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	382	406	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	407	427	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	428	431	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	432	452	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	453	475	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	476	496	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	497	509	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Transmembrane	510	530	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Topological domain	531	587	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q08986	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12372	
+Q08986	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08986	UniProtKB	Glycosylation	184	184	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08986	UniProtKB	Glycosylation	243	243	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53969 1 484
+P53969	UniProtKB	Chain	1	484	.	.	.	ID=PRO_0000215943;Note=Sorting assembly machinery 50 kDa subunit	
+##sequence-region P38429 1 201
+P38429	UniProtKB	Chain	1	201	.	.	.	ID=PRO_0000203345;Note=Transcriptional regulatory protein SAP30	
+P38429	UniProtKB	Compositional bias	26	58	.	.	.	Note=Asn-rich	
+P38429	UniProtKB	Sequence conflict	31	31	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38429	UniProtKB	Sequence conflict	48	48	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04003 1 481
+Q04003	UniProtKB	Chain	1	481	.	.	.	ID=PRO_0000097593;Note=Something about silencing protein 4	
+Q04003	UniProtKB	Coiled coil	90	120	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04003	UniProtKB	Coiled coil	139	160	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53324 1 424
+P53324	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53324	UniProtKB	Chain	2	424	.	.	.	ID=PRO_0000202862;Note=Steryl acetyl hydrolase 1	
+P53324	UniProtKB	Topological domain	2	45	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53324	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53324	UniProtKB	Topological domain	67	424	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53324	UniProtKB	Motif	176	178	.	.	.	Note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5NUF3	
+P53324	UniProtKB	Active site	250	250	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5NUF3	
+P53324	UniProtKB	Active site	395	395	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5NUF3	
+P53324	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53324	UniProtKB	Glycosylation	85	85	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53324	UniProtKB	Glycosylation	283	283	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53324	UniProtKB	Glycosylation	401	401	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38814 1 852
+P38814	UniProtKB	Chain	1	852	.	.	.	ID=PRO_0000202909;Note=Protein SBE22	
+P38814	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38814	UniProtKB	Modified residue	201	201	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38814	UniProtKB	Modified residue	459	459	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38814	UniProtKB	Modified residue	517	517	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38814	UniProtKB	Modified residue	520	520	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P42223 1 864
+P42223	UniProtKB	Chain	1	864	.	.	.	ID=PRO_0000097602;Note=Protein SBE2	
+P42223	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P42223	UniProtKB	Modified residue	83	83	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P42223	UniProtKB	Modified residue	450	450	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P42223	UniProtKB	Modified residue	532	532	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P25303 1 377
+P25303	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25303	UniProtKB	Chain	22	377	.	.	.	ID=PRO_0000071091;Note=DnaJ-related protein SCJ1	
+P25303	UniProtKB	Domain	23	88	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P25303	UniProtKB	Repeat	169	176	.	.	.	Note=CXXCXGXG motif	
+P25303	UniProtKB	Repeat	185	192	.	.	.	Note=CXXCXGXG motif	
+P25303	UniProtKB	Repeat	211	218	.	.	.	Note=CXXCXGXG motif	
+P25303	UniProtKB	Repeat	225	232	.	.	.	Note=CXXCXGXG motif	
+P25303	UniProtKB	Zinc finger	156	237	.	.	.	Note=CR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00546	
+P25303	UniProtKB	Motif	288	290	.	.	.	Note=Cell attachment site;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25303	UniProtKB	Motif	374	377	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138	
+P25303	UniProtKB	Compositional bias	95	132	.	.	.	Note=Gly-rich	
+##sequence-region P47052 1 634
+P47052	UniProtKB	Transit peptide	1	25	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47052	UniProtKB	Chain	26	634	.	.	.	ID=PRO_0000010343;Note=Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2%2C mitochondrial	
+P47052	UniProtKB	Nucleotide binding	53	58	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+P47052	UniProtKB	Nucleotide binding	76	91	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+P47052	UniProtKB	Nucleotide binding	443	444	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+P47052	UniProtKB	Active site	325	325	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+P47052	UniProtKB	Binding site	260	260	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+P47052	UniProtKB	Binding site	281	281	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+P47052	UniProtKB	Binding site	293	293	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+P47052	UniProtKB	Binding site	392	392	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+P47052	UniProtKB	Binding site	427	427	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+P47052	UniProtKB	Binding site	438	438	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+P47052	UniProtKB	Modified residue	84	84	.	.	.	Note=Tele-8alpha-FAD histidine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+##sequence-region P36047 1 338
+P36047	UniProtKB	Chain	1	338	.	.	.	ID=PRO_0000071447;Note=Protein phosphatase 1 regulatory subunit SDS22	
+P36047	UniProtKB	Repeat	43	64	.	.	.	Note=LRR 1	
+P36047	UniProtKB	Repeat	67	88	.	.	.	Note=LRR 2	
+P36047	UniProtKB	Repeat	91	113	.	.	.	Note=LRR 3	
+P36047	UniProtKB	Repeat	114	135	.	.	.	Note=LRR 4	
+P36047	UniProtKB	Repeat	136	157	.	.	.	Note=LRR 5	
+P36047	UniProtKB	Repeat	158	179	.	.	.	Note=LRR 6	
+P36047	UniProtKB	Repeat	182	203	.	.	.	Note=LRR 7	
+P36047	UniProtKB	Repeat	204	225	.	.	.	Note=LRR 8	
+P36047	UniProtKB	Repeat	226	247	.	.	.	Note=LRR 9	
+P36047	UniProtKB	Repeat	248	269	.	.	.	Note=LRR 10	
+P36047	UniProtKB	Repeat	270	292	.	.	.	Note=LRR 11	
+P36047	UniProtKB	Domain	306	338	.	.	.	Note=LRRCT	
+P36047	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q06245 1 871
+Q06245	UniProtKB	Chain	1	871	.	.	.	ID=PRO_0000118950;Note=Exocyst complex component SEC10	
+Q06245	UniProtKB	Coiled coil	74	101	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06245	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06245	UniProtKB	Modified residue	485	485	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06245	UniProtKB	Modified residue	507	507	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P48415 1 2195
+P48415	UniProtKB	Chain	1	2195	.	.	.	ID=PRO_0000097658;Note=COPII coat assembly protein SEC16	
+P48415	UniProtKB	Compositional bias	1997	2094	.	.	.	Note=Lys-rich	
+P48415	UniProtKB	Compositional bias	2078	2145	.	.	.	Note=Pro-rich	
+P48415	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P48415	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P48415	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P48415	UniProtKB	Modified residue	472	472	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	483	483	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P48415	UniProtKB	Modified residue	595	595	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	607	607	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198	
+P48415	UniProtKB	Modified residue	660	660	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	663	663	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	665	665	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	674	674	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P48415	UniProtKB	Modified residue	678	678	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P48415	UniProtKB	Modified residue	681	681	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P48415	UniProtKB	Modified residue	701	701	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	704	704	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P48415	UniProtKB	Modified residue	706	706	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P48415	UniProtKB	Modified residue	759	759	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P48415	UniProtKB	Modified residue	762	762	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P48415	UniProtKB	Modified residue	765	765	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P48415	UniProtKB	Modified residue	768	768	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	843	843	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P48415	UniProtKB	Modified residue	1511	1511	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P48415	UniProtKB	Modified residue	1515	1515	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P48415	UniProtKB	Modified residue	1578	1578	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P48415	UniProtKB	Modified residue	1602	1602	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	1603	1603	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P48415	UniProtKB	Modified residue	1611	1611	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P48415	UniProtKB	Modified residue	1617	1617	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	1778	1778	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P48415	UniProtKB	Modified residue	1875	1875	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P48415	UniProtKB	Modified residue	1973	1973	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	1986	1986	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P48415	UniProtKB	Modified residue	1992	1992	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P48415	UniProtKB	Modified residue	2049	2049	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P48415	UniProtKB	Modified residue	2130	2130	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P48415	UniProtKB	Mutagenesis	1059	1059	.	.	.	Note=In SEC16-4%3B ts accumulation of ER membranes. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593161;Dbxref=PMID:7593161	
+P48415	UniProtKB	Mutagenesis	1084	1084	.	.	.	Note=In SEC16-3%3B ts accumulation of ER membranes. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593161;Dbxref=PMID:7593161	
+P48415	UniProtKB	Mutagenesis	1089	1089	.	.	.	Note=In SEC16-2%3B ts accumulation of ER membranes. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593161;Dbxref=PMID:7593161	
+P48415	UniProtKB	Mutagenesis	1231	1231	.	.	.	Note=In SEC16-1%3B ts accumulation of ER membranes. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593161;Dbxref=PMID:7593161	
+P48415	UniProtKB	Sequence conflict	522	522	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48415	UniProtKB	Sequence conflict	560	560	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48415	UniProtKB	Beta strand	995	998	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Beta strand	1002	1007	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Beta strand	1027	1031	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1032	1034	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1040	1044	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1056	1073	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1080	1090	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1095	1102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1106	1113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1130	1141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1145	1154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1158	1166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1170	1182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1193	1205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Turn	1206	1208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1210	1219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1221	1229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1231	1240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1254	1269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1273	1282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Beta strand	1288	1293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1309	1323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1332	1334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1335	1347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1351	1366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+P48415	UniProtKB	Helix	1373	1388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+##sequence-region P18759 1 758
+P18759	UniProtKB	Chain	1	758	.	.	.	ID=PRO_0000084571;Note=Vesicular-fusion protein SEC18	
+P18759	UniProtKB	Nucleotide binding	281	288	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18759	UniProtKB	Nucleotide binding	564	571	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18759	UniProtKB	Modified residue	226	226	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P18759	UniProtKB	Sequence conflict	381	381	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18759	UniProtKB	Sequence conflict	381	381	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18759	UniProtKB	Beta strand	27	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Helix	37	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Turn	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Beta strand	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Turn	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Beta strand	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Turn	61	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Beta strand	64	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Beta strand	78	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Helix	83	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Beta strand	96	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Helix	104	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Beta strand	113	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Helix	136	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Beta strand	157	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Beta strand	165	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Beta strand	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+P18759	UniProtKB	Beta strand	203	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5	
+##sequence-region P28791 1 383
+P28791	UniProtKB	Chain	1	383	.	.	.	ID=PRO_0000097659;Note=Protein transport protein SEC20	
+P28791	UniProtKB	Topological domain	1	275	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28791	UniProtKB	Transmembrane	276	292	.	.	.	Note=Helical%3B Anchor for type IV membrane protein	
+P28791	UniProtKB	Topological domain	293	383	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28791	UniProtKB	Coiled coil	6	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P28791	UniProtKB	Motif	380	383	.	.	.	Note=Prevents secretion from ER	
+##sequence-region P15303 1 768
+P15303	UniProtKB	Chain	1	768	.	.	.	ID=PRO_0000205145;Note=Protein transport protein SEC23	
+P15303	UniProtKB	Metal binding	56	56	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239560;Dbxref=PMID:12239560	
+P15303	UniProtKB	Metal binding	61	61	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239560;Dbxref=PMID:12239560	
+P15303	UniProtKB	Metal binding	80	80	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239560;Dbxref=PMID:12239560	
+P15303	UniProtKB	Metal binding	83	83	.	.	.	Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239560;Dbxref=PMID:12239560	
+P15303	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P15303	UniProtKB	Helix	3	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	11	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	23	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	33	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV	
+P15303	UniProtKB	Turn	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V	
+P15303	UniProtKB	Turn	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV	
+P15303	UniProtKB	Turn	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV	
+P15303	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V	
+P15303	UniProtKB	Helix	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	108	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	123	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	134	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	156	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	172	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	190	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	224	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	228	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	231	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	262	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	283	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	294	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	311	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	322	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	342	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	355	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	369	373	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	378	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	394	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	399	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	412	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	437	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	443	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	456	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	484	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Turn	496	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	499	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	517	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	525	539	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	545	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	564	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV	
+P15303	UniProtKB	Helix	571	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Turn	578	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	582	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Turn	594	596	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	603	613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	618	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	628	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	634	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	645	647	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	653	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	659	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	668	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	678	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	682	684	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V	
+P15303	UniProtKB	Helix	685	703	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	710	715	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	719	721	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Helix	722	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+P15303	UniProtKB	Beta strand	740	742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV	
+P15303	UniProtKB	Helix	752	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O	
+##sequence-region P17065 1 759
+P17065	UniProtKB	Chain	1	759	.	.	.	ID=PRO_0000097661;Note=Rab guanine nucleotide exchange factor SEC2	
+P17065	UniProtKB	Region	451	508	.	.	.	Note=Required for proper polarized localization of the protein	
+P17065	UniProtKB	Coiled coil	26	164	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17065	UniProtKB	Coiled coil	651	682	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17065	UniProtKB	Coiled coil	732	759	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P17065	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P17065	UniProtKB	Modified residue	168	168	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P17065	UniProtKB	Modified residue	171	171	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P17065	UniProtKB	Modified residue	515	515	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P17065	UniProtKB	Mutagenesis	483	483	.	.	.	Note=In SEC2-78%3B temperature-sensitive%3B causes mislocalization of the protein%2C displaying many cytoplasmic punctae. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10747090;Dbxref=PMID:10747090	
+P17065	UniProtKB	Turn	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E7S	
+P17065	UniProtKB	Helix	52	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EQB	
+P17065	UniProtKB	Turn	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E7S	
+##sequence-region P38968 1 1273
+P38968	UniProtKB	Chain	1	1273	.	.	.	ID=PRO_0000051436;Note=Protein transport protein SEC31	
+P38968	UniProtKB	Repeat	6	46	.	.	.	Note=WD 1	
+P38968	UniProtKB	Repeat	60	99	.	.	.	Note=WD 2	
+P38968	UniProtKB	Repeat	106	146	.	.	.	Note=WD 3	
+P38968	UniProtKB	Repeat	158	198	.	.	.	Note=WD 4	
+P38968	UniProtKB	Repeat	207	250	.	.	.	Note=WD 5	
+P38968	UniProtKB	Repeat	255	295	.	.	.	Note=WD 6	
+P38968	UniProtKB	Repeat	298	338	.	.	.	Note=WD 7	
+P38968	UniProtKB	Repeat	385	405	.	.	.	Note=WD 8%3B interaction with SEC13	
+P38968	UniProtKB	Compositional bias	773	1149	.	.	.	Note=Pro-rich	
+P38968	UniProtKB	Modified residue	349	349	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38968	UniProtKB	Modified residue	836	836	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38968	UniProtKB	Modified residue	974	974	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38968	UniProtKB	Modified residue	977	977	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38968	UniProtKB	Modified residue	980	980	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38968	UniProtKB	Modified residue	988	988	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38968	UniProtKB	Modified residue	992	992	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38968	UniProtKB	Modified residue	999	999	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38968	UniProtKB	Modified residue	1050	1050	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P38968	UniProtKB	Modified residue	1053	1053	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38968	UniProtKB	Sequence conflict	317	317	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38968	UniProtKB	Sequence conflict	367	367	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38968	UniProtKB	Sequence conflict	367	367	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38968	UniProtKB	Sequence conflict	691	691	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38968	UniProtKB	Sequence conflict	754	754	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38968	UniProtKB	Sequence conflict	877	877	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38968	UniProtKB	Beta strand	6	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	17	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	22	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	43	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Helix	50	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	65	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	72	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	77	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	86	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	100	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	113	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	123	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	129	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Turn	138	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Turn	145	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	165	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	175	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	185	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Turn	190	193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	194	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	212	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	224	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	232	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	260	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	273	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	287	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	292	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	299	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	315	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	321	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+P38968	UniProtKB	Beta strand	385	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Turn	388	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Beta strand	391	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Beta strand	402	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	416	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	428	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	441	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	458	466	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	509	519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	523	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Turn	532	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	536	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	549	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	568	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	582	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	590	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	593	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	608	623	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Turn	624	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	628	637	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	641	650	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	652	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	666	685	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	697	711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Turn	712	714	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	716	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Helix	731	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+P38968	UniProtKB	Beta strand	909	911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV	
+P38968	UniProtKB	Helix	916	919	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV	
+##sequence-region P21825 1 274
+P21825	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P21825	UniProtKB	Chain	2	274	.	.	.	ID=PRO_0000206627;Note=Translocation protein SEC62	
+P21825	UniProtKB	Topological domain	2	149	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21825	UniProtKB	Transmembrane	150	169	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21825	UniProtKB	Topological domain	170	183	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21825	UniProtKB	Transmembrane	184	204	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21825	UniProtKB	Topological domain	205	274	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P21825	UniProtKB	Compositional bias	246	270	.	.	.	Note=Arg/Lys-rich (basic)	
+P21825	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P33754 1 206
+P33754	UniProtKB	Chain	1	206	.	.	.	ID=PRO_0000097663;Note=Translocation protein SEC66	
+P33754	UniProtKB	Topological domain	1	27	.	.	.	Note=Lumenal	
+P33754	UniProtKB	Transmembrane	28	48	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P33754	UniProtKB	Topological domain	49	206	.	.	.	Note=Cytoplasmic	
+P33754	UniProtKB	Glycosylation	5	5	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33754	UniProtKB	Glycosylation	12	12	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39742 1 193
+P39742	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8051213;Dbxref=PMID:8051213	
+P39742	UniProtKB	Chain	2	193	.	.	.	ID=PRO_0000097664;Note=Translocation protein SEC72	
+P39742	UniProtKB	Sequence conflict	33	33	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39742	UniProtKB	Sequence conflict	187	187	.	.	.	Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04675 1 128
+Q04675	UniProtKB	Chain	1	128	.	.	.	ID=PRO_0000194028;Note=tRNA-splicing endonuclease subunit SEN15	
+##sequence-region Q00416 1 2231
+Q00416	UniProtKB	Chain	1	2231	.	.	.	ID=PRO_0000080722;Note=Helicase SEN1	
+Q00416	UniProtKB	Nucleotide binding	1360	1364	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00416	UniProtKB	Motif	1909	1927	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q00416	UniProtKB	Compositional bias	1908	1961	.	.	.	Note=Lys-rich (basic)	
+Q00416	UniProtKB	Binding site	1339	1339	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00416	UniProtKB	Binding site	1619	1619	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00416	UniProtKB	Binding site	1655	1655	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00416	UniProtKB	Binding site	1787	1787	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q00416	UniProtKB	Mutagenesis	1597	1597	.	.	.	Note=Causes read-through of both a snoRNA gene terminator and the poly(A) site of a protein-coding gene. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157256;Dbxref=PMID:17157256	
+Q00416	UniProtKB	Mutagenesis	1747	1747	.	.	.	Note=In SEN1-1%3B gives rise to a temperature-sensitive mutant. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1569945;Dbxref=PMID:1569945	
+Q00416	UniProtKB	Helix	1100	1109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1114	1120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1129	1133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1137	1139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1150	1174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1181	1191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1194	1202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1203	1208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1215	1220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1233	1237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1240	1252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1256	1265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1269	1273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1279	1287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1289	1300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1301	1303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1307	1312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1323	1333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1337	1348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1351	1356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1363	1379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1406	1412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1413	1423	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1439	1441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1450	1453	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1457	1465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Turn	1466	1469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1542	1559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1561	1566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1568	1571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1573	1576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1584	1589	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1595	1599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1600	1604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1608	1613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1615	1617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1625	1629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Turn	1630	1633	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1636	1641	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1657	1667	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1678	1681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1685	1688	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1694	1700	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1717	1734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Turn	1735	1737	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1744	1749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1751	1765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1766	1769	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Turn	1770	1772	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1773	1777	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Turn	1778	1783	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1786	1792	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1802	1815	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1818	1827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1829	1832	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1836	1847	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Beta strand	1851	1854	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Turn	1856	1859	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+Q00416	UniProtKB	Helix	1864	1871	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN	
+##sequence-region P47008 1 294
+P47008	UniProtKB	Chain	1	294	.	.	.	ID=PRO_0000203033;Note=Phosphatidylinositol transfer protein SFH5	
+P47008	UniProtKB	Domain	100	266	.	.	.	Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056	
+P47008	UniProtKB	Sequence conflict	70	70	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05567 1 589
+Q05567	UniProtKB	Chain	1	589	.	.	.	ID=PRO_0000147018;Note=Sphingosine-1-phosphate lyase	
+Q05567	UniProtKB	Modified residue	380	380	.	.	.	Note=N6-(pyridoxal phosphate)lysine	
+Q05567	UniProtKB	Mutagenesis	172	172	.	.	.	Note=Loss of enzyme activity. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404	
+Q05567	UniProtKB	Mutagenesis	174	174	.	.	.	Note=Mildly decreased enzyme activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404	
+Q05567	UniProtKB	Mutagenesis	198	198	.	.	.	Note=Decreased enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404	
+Q05567	UniProtKB	Mutagenesis	380	380	.	.	.	Note=Loss of enzyme activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404	
+Q05567	UniProtKB	Mutagenesis	386	386	.	.	.	Note=Loss of enzyme activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404	
+Q05567	UniProtKB	Mutagenesis	554	554	.	.	.	Note=Decreased enzyme activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404	
+Q05567	UniProtKB	Helix	145	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Beta strand	169	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	178	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	199	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	203	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Beta strand	229	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	235	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Beta strand	260	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	269	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Beta strand	281	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	296	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Beta strand	305	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	317	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	326	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	331	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Beta strand	339	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	343	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	347	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	351	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	354	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Beta strand	373	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	378	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Beta strand	389	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	396	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	400	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Beta strand	417	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	425	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Beta strand	476	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	484	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	488	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	497	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Beta strand	511	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Turn	517	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	523	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+Q05567	UniProtKB	Helix	567	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6	
+##sequence-region P36136 1 271
+P36136	UniProtKB	Chain	1	271	.	.	.	ID=PRO_0000203211;Note=Sedoheptulose 1%2C7-bisphosphatase	
+P36136	UniProtKB	Region	24	25	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Region	99	102	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Active site	13	13	.	.	.	Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Active site	99	99	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Binding site	12	12	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Binding site	69	69	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Binding site	181	181	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Binding site	244	244	.	.	.	Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Site	176	176	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	12	12	.	.	.	Note=Impairs catalytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	13	13	.	.	.	Note=Impairs catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	16	16	.	.	.	Note=Impairs catalytic activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Leads to reduced substrate affinity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	24	24	.	.	.	Note=Leads to low activity and reduced substrate affinity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Leads to low activity and reduced substrate affinity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Leads to reduced substrate affinity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Impairs catalytic activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Impairs catalytic activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Leads to reduced substrate affinity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Impairs catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	178	178	.	.	.	Note=Leads to low activity and reduced substrate affinity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Mutagenesis	181	181	.	.	.	Note=Leads to reduced substrate affinity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268	
+P36136	UniProtKB	Beta strand	7	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	17	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Beta strand	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OI7	
+P36136	UniProtKB	Helix	34	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LG2	
+P36136	UniProtKB	Helix	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Beta strand	59	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	68	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Turn	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	83	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Beta strand	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	95	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	110	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Beta strand	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	130	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	141	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Beta strand	170	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	177	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Beta strand	191	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	199	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Beta strand	219	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Beta strand	237	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Beta strand	249	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Turn	254	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K	
+P36136	UniProtKB	Helix	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LG2	
+##sequence-region P39000 1 512
+P39000	UniProtKB	Chain	1	512	.	.	.	ID=PRO_0000202642;Note=Protein SHC1	
+P39000	UniProtKB	Repeat	318	353	.	.	.	Note=Sel1-like 1	
+P39000	UniProtKB	Repeat	354	389	.	.	.	Note=Sel1-like 2	
+P39000	UniProtKB	Repeat	390	429	.	.	.	Note=Sel1-like 3	
+P39000	UniProtKB	Repeat	433	470	.	.	.	Note=Sel1-like 4	
+P39000	UniProtKB	Sequence conflict	22	22	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39000	UniProtKB	Sequence conflict	33	33	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39000	UniProtKB	Sequence conflict	90	90	.	.	.	Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39000	UniProtKB	Sequence conflict	176	176	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39000	UniProtKB	Sequence conflict	233	233	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39000	UniProtKB	Sequence conflict	311	311	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02774 1 210
+Q02774	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000097740;Note=Secretory component protein SHR3	
+Q02774	UniProtKB	Topological domain	1	9	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02774	UniProtKB	Transmembrane	10	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02774	UniProtKB	Topological domain	29	59	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02774	UniProtKB	Transmembrane	60	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02774	UniProtKB	Topological domain	85	91	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02774	UniProtKB	Transmembrane	92	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02774	UniProtKB	Topological domain	115	130	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02774	UniProtKB	Transmembrane	131	160	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02774	UniProtKB	Topological domain	161	210	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02774	UniProtKB	Sequence conflict	125	129	.	.	.	Note=GEVTE->EKLR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q07657 1 551
+Q07657	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q07657	UniProtKB	Chain	2	551	.	.	.	ID=PRO_0000173545;Note=Seventh homolog of septin 1	
+Q07657	UniProtKB	Domain	20	339	.	.	.	Note=Septin-type G	
+Q07657	UniProtKB	Nucleotide binding	30	37	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07657	UniProtKB	Nucleotide binding	218	226	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07657	UniProtKB	Coiled coil	418	518	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07657	UniProtKB	Binding site	138	138	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07657	UniProtKB	Binding site	288	288	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07657	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q07657	UniProtKB	Modified residue	400	400	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07657	UniProtKB	Modified residue	408	408	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q07657	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q07657	UniProtKB	Modified residue	447	447	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q07657	UniProtKB	Modified residue	460	460	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07657	UniProtKB	Modified residue	519	519	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q07657	UniProtKB	Modified residue	520	520	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07657	UniProtKB	Modified residue	522	522	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07657	UniProtKB	Modified residue	525	525	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q07657	UniProtKB	Modified residue	539	539	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07657	UniProtKB	Modified residue	545	545	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q07657	UniProtKB	Modified residue	548	548	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q07657	UniProtKB	Cross-link	426	426	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
+Q07657	UniProtKB	Cross-link	437	437	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
+Q07657	UniProtKB	Mutagenesis	426	426	.	.	.	Note=Abolishes sumoylation in vitro%3B when associated with R-437. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719	
+Q07657	UniProtKB	Mutagenesis	437	437	.	.	.	Note=Abolishes sumoylation in vitro%3B when associated with R-426. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719	
+##sequence-region P38751 1 150
+P38751	UniProtKB	Chain	1	150	.	.	.	ID=PRO_0000097742;Note=Suppressor of HU sensitivity involved in recombination protein 1	
+P38751	UniProtKB	Sequence conflict	138	138	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P50263 1 79
+P50263	UniProtKB	Chain	1	79	.	.	.	ID=PRO_0000097764;Note=Protein SIP18	
+P50263	UniProtKB	Sequence conflict	47	48	.	.	.	Note=EG->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P50263	UniProtKB	Sequence conflict	76	79	.	.	.	Note=NMKK->HENMYVFGALTKSSYFFNGLFMNCLCLCSLYSKSISAYFSEFSSTNIYKSYLRLPSVLYYVCMMHTMMPNQLDAVGIQSSESLLM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38717 1 1229
+P38717	UniProtKB	Chain	1	1229	.	.	.	ID=PRO_0000097765;Note=Membrane-anchored lipid-binding protein SIP3	
+P38717	UniProtKB	Topological domain	1	1066	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:16847258,ECO:0000305|PubMed:26001273;Dbxref=PMID:16847258,PMID:26001273	
+P38717	UniProtKB	Transmembrane	1067	1087	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38717	UniProtKB	Topological domain	1088	1229	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P38717	UniProtKB	Domain	309	423	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P38717	UniProtKB	Domain	771	976	.	.	.	Note=VASt;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114	
+P38717	UniProtKB	Glycosylation	1206	1206	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+##sequence-region P06700 1 562
+P06700	UniProtKB	Chain	1	562	.	.	.	ID=PRO_0000110280;Note=NAD-dependent histone deacetylase SIR2	
+P06700	UniProtKB	Domain	245	529	.	.	.	Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P06700	UniProtKB	Nucleotide binding	262	281	.	.	.	Note=NAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23307867,ECO:0000269|Ref.28;Dbxref=PMID:23307867	
+P06700	UniProtKB	Nucleotide binding	344	347	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53686	
+P06700	UniProtKB	Nucleotide binding	471	473	.	.	.	Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23307867;Dbxref=PMID:23307867	
+P06700	UniProtKB	Nucleotide binding	496	498	.	.	.	Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23307867;Dbxref=PMID:23307867	
+P06700	UniProtKB	Active site	364	364	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236	
+P06700	UniProtKB	Metal binding	372	372	.	.	.	Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23307867,ECO:0000269|Ref.28;Dbxref=PMID:23307867	
+P06700	UniProtKB	Metal binding	375	375	.	.	.	Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23307867,ECO:0000269|Ref.28;Dbxref=PMID:23307867	
+P06700	UniProtKB	Metal binding	396	396	.	.	.	Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23307867,ECO:0000269|Ref.28;Dbxref=PMID:23307867	
+P06700	UniProtKB	Metal binding	399	399	.	.	.	Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23307867,ECO:0000269|Ref.28;Dbxref=PMID:23307867	
+P06700	UniProtKB	Binding site	513	513	.	.	.	Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23307867;Dbxref=PMID:23307867	
+P06700	UniProtKB	Mutagenesis	139	139	.	.	.	Note=Defects in telomeric silencing. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12399383;Dbxref=PMID:12399383	
+P06700	UniProtKB	Mutagenesis	270	270	.	.	.	Note=Defects in telomeric silencing. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12399383;Dbxref=PMID:12399383	
+P06700	UniProtKB	Mutagenesis	296	296	.	.	.	Note=Defects in telomeric silencing. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12399383;Dbxref=PMID:12399383	
+P06700	UniProtKB	Helix	102	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P06700	UniProtKB	Beta strand	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P06700	UniProtKB	Beta strand	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P06700	UniProtKB	Helix	132	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P06700	UniProtKB	Helix	163	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P06700	UniProtKB	Beta strand	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P06700	UniProtKB	Helix	178	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P06700	UniProtKB	Beta strand	213	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	244	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	255	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	263	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	280	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	284	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	292	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	298	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	306	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	312	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	324	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	338	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	349	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Turn	357	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	360	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	365	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Turn	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	381	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	385	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Turn	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	400	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Turn	417	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P06700	UniProtKB	Turn	433	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	437	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	451	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Turn	461	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	466	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	482	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	492	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	506	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	513	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Helix	533	537	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	541	547	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+P06700	UniProtKB	Beta strand	550	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH	
+##sequence-region P32900 1 734
+P32900	UniProtKB	Chain	1	734	.	.	.	ID=PRO_0000202924;Note=Protein SKG6	
+P32900	UniProtKB	Transmembrane	72	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32900	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32900	UniProtKB	Modified residue	169	169	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P32900	UniProtKB	Modified residue	191	191	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32900	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32900	UniProtKB	Modified residue	219	219	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32900	UniProtKB	Modified residue	221	221	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32900	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32900	UniProtKB	Modified residue	251	251	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32900	UniProtKB	Modified residue	369	369	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32900	UniProtKB	Modified residue	672	672	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32900	UniProtKB	Modified residue	717	717	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32900	UniProtKB	Sequence conflict	355	355	.	.	.	Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32900	UniProtKB	Sequence conflict	403	403	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32900	UniProtKB	Sequence conflict	450	450	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32900	UniProtKB	Sequence conflict	472	472	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32900	UniProtKB	Sequence conflict	497	497	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32900	UniProtKB	Sequence conflict	499	499	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32900	UniProtKB	Sequence conflict	510	510	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35207 1 1287
+P35207	UniProtKB	Chain	1	1287	.	.	.	ID=PRO_0000102084;Note=Antiviral helicase SKI2	
+P35207	UniProtKB	Domain	338	496	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P35207	UniProtKB	Domain	638	815	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P35207	UniProtKB	Nucleotide binding	351	358	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P35207	UniProtKB	Region	556	577	.	.	.	Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P35207	UniProtKB	Motif	444	447	.	.	.	Note=DEVH box	
+P35207	UniProtKB	Compositional bias	555	597	.	.	.	Note=Arg/Gly-rich	
+P35207	UniProtKB	Modified residue	209	209	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P35207	UniProtKB	Sequence conflict	326	326	.	.	.	Note=W->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35207	UniProtKB	Sequence conflict	759	760	.	.	.	Note=QM->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35207	UniProtKB	Beta strand	302	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	315	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	332	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	346	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	358	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	374	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	382	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	385	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	401	404	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	414	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	421	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	434	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	438	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	458	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	470	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	481	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	496	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	508	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	517	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	530	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	613	623	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	628	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	636	644	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Turn	645	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	654	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	673	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	679	688	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Turn	689	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	692	695	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	701	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	717	721	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	724	727	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	734	739	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	741	745	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	748	751	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	754	761	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	762	764	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Turn	767	769	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	771	778	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	786	794	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	808	817	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	821	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	830	854	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Turn	862	864	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4K	
+P35207	UniProtKB	Beta strand	865	868	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4K	
+P35207	UniProtKB	Helix	871	889	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	895	898	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	903	908	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	914	923	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Turn	924	927	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	928	933	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	943	945	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4K	
+P35207	UniProtKB	Helix	955	961	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Beta strand	971	976	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	977	979	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4K	
+P35207	UniProtKB	Beta strand	982	987	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	992	997	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1000	1015	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1031	1044	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1051	1053	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4K	
+P35207	UniProtKB	Helix	1061	1079	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Turn	1080	1082	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1088	1101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1113	1118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1126	1134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1137	1140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1143	1150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1151	1153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1169	1191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1198	1202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1203	1205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Turn	1208	1211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1212	1220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1224	1229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1235	1259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1262	1275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+P35207	UniProtKB	Helix	1278	1281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z	
+##sequence-region P17883 1 1432
+P17883	UniProtKB	Chain	1	1432	.	.	.	ID=PRO_0000106323;Note=Superkiller protein 3	
+P17883	UniProtKB	Repeat	4	37	.	.	.	Note=TPR 1	
+P17883	UniProtKB	Repeat	47	80	.	.	.	Note=TPR 2	
+P17883	UniProtKB	Repeat	425	458	.	.	.	Note=TPR 3	
+P17883	UniProtKB	Repeat	471	507	.	.	.	Note=TPR 4	
+P17883	UniProtKB	Repeat	508	541	.	.	.	Note=TPR 5	
+P17883	UniProtKB	Repeat	627	661	.	.	.	Note=TPR 6	
+P17883	UniProtKB	Repeat	702	735	.	.	.	Note=TPR 7	
+P17883	UniProtKB	Repeat	736	769	.	.	.	Note=TPR 8	
+P17883	UniProtKB	Repeat	945	985	.	.	.	Note=TPR 9	
+P17883	UniProtKB	Repeat	987	1018	.	.	.	Note=TPR 10	
+P17883	UniProtKB	Repeat	1226	1259	.	.	.	Note=TPR 11	
+P17883	UniProtKB	Sequence conflict	985	985	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08491 1 747
+Q08491	UniProtKB	Chain	1	747	.	.	.	ID=PRO_0000269648;Note=Superkiller protein 7	
+Q08491	UniProtKB	Domain	265	503	.	.	.	Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+Q08491	UniProtKB	Nucleotide binding	274	281	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08491	UniProtKB	Nucleotide binding	356	360	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08491	UniProtKB	Nucleotide binding	427	430	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q08491	UniProtKB	Region	274	281	.	.	.	Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+Q08491	UniProtKB	Region	331	335	.	.	.	Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+Q08491	UniProtKB	Region	356	359	.	.	.	Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+Q08491	UniProtKB	Region	427	430	.	.	.	Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+Q08491	UniProtKB	Region	467	469	.	.	.	Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+Q08491	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q08491	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q08491	UniProtKB	Helix	121	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08491	UniProtKB	Helix	150	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08491	UniProtKB	Beta strand	185	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08491	UniProtKB	Helix	197	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08491	UniProtKB	Helix	212	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA	
+Q08491	UniProtKB	Helix	258	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	266	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	280	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	296	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	306	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Turn	311	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKE	
+Q08491	UniProtKB	Helix	318	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	325	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	337	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	350	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	361	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Turn	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	368	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	378	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	390	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	401	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Turn	410	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	422	427	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	429	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	436	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	458	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	461	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Turn	468	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Helix	504	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Turn	522	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	528	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	542	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	562	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	568	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	573	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	593	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	597	600	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	604	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Turn	617	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	629	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	648	660	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	673	678	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	681	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	696	698	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	703	710	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	717	722	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	728	732	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+Q08491	UniProtKB	Beta strand	738	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD	
+##sequence-region P42843 1 763
+P42843	UniProtKB	Chain	1	763	.	.	.	ID=PRO_0000203366;Note=F-box protein SKP2	
+P42843	UniProtKB	Domain	54	100	.	.	.	Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080	
+P42843	UniProtKB	Compositional bias	22	28	.	.	.	Note=Poly-Glu	
+P42843	UniProtKB	Modified residue	594	594	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P42843	UniProtKB	Sequence conflict	16	16	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53327 1 1967
+P53327	UniProtKB	Chain	1	1967	.	.	.	ID=PRO_0000102085;Note=Antiviral helicase SLH1	
+P53327	UniProtKB	Domain	297	485	.	.	.	Note=Helicase ATP-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53327	UniProtKB	Domain	516	735	.	.	.	Note=Helicase C-terminal 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P53327	UniProtKB	Domain	795	1100	.	.	.	Note=SEC63 1	
+P53327	UniProtKB	Domain	1149	1324	.	.	.	Note=Helicase ATP-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53327	UniProtKB	Domain	1355	1550	.	.	.	Note=Helicase C-terminal 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P53327	UniProtKB	Domain	1626	1776	.	.	.	Note=SEC63 2	
+P53327	UniProtKB	Nucleotide binding	310	317	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53327	UniProtKB	Nucleotide binding	1162	1169	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P53327	UniProtKB	Motif	427	430	.	.	.	Note=DEVH box	
+P53327	UniProtKB	Motif	1266	1269	.	.	.	Note=DEAH box	
+P53327	UniProtKB	Sequence conflict	27	27	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53327	UniProtKB	Sequence conflict	51	51	.	.	.	Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53327	UniProtKB	Sequence conflict	51	51	.	.	.	Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53327	UniProtKB	Sequence conflict	193	193	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53327	UniProtKB	Sequence conflict	193	193	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53327	UniProtKB	Sequence conflict	438	438	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53327	UniProtKB	Sequence conflict	438	438	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38247 1 162
+P38247	UniProtKB	Chain	1	162	.	.	.	ID=PRO_0000202479;Note=Protein SLM4	
+P38247	UniProtKB	Transmembrane	127	144	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38247	UniProtKB	Helix	9	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Helix	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Beta strand	33	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Turn	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Beta strand	45	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Helix	59	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Beta strand	92	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Beta strand	103	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Beta strand	115	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Beta strand	125	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Helix	139	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+P38247	UniProtKB	Helix	151	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX	
+##sequence-region Q00772 1 484
+Q00772	UniProtKB	Chain	1	484	.	.	.	ID=PRO_0000186338;Note=Mitogen-activated protein kinase SLT2/MPK1	
+Q00772	UniProtKB	Domain	23	318	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q00772	UniProtKB	Nucleotide binding	29	37	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q00772	UniProtKB	Motif	190	192	.	.	.	Note=TXY	
+Q00772	UniProtKB	Compositional bias	370	391	.	.	.	Note=Poly-Gln	
+Q00772	UniProtKB	Active site	153	153	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q00772	UniProtKB	Binding site	54	54	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q00772	UniProtKB	Modified residue	190	190	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q00772	UniProtKB	Modified residue	192	192	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q00772	UniProtKB	Sequence conflict	56	56	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q00772	UniProtKB	Sequence conflict	467	467	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32908 1 1225
+P32908	UniProtKB	Chain	1	1225	.	.	.	ID=PRO_0000119011;Note=Structural maintenance of chromosomes protein 1	
+P32908	UniProtKB	Nucleotide binding	33	40	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32908	UniProtKB	Region	490	678	.	.	.	Note=Flexible hinge	
+P32908	UniProtKB	Coiled coil	173	489	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32908	UniProtKB	Coiled coil	679	1063	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32908	UniProtKB	Motif	1057	1061	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32908	UniProtKB	Compositional bias	1129	1164	.	.	.	Note=Ala/Asp-rich (DA-box)	
+P32908	UniProtKB	Mutagenesis	173	173	.	.	.	Note=In temperature-sensitive mutant SMC1-2. S->L	
+P32908	UniProtKB	Mutagenesis	458	458	.	.	.	Note=In temperature-sensitive mutant SMC1-1. N->D	
+P32908	UniProtKB	Beta strand	4	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	17	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	27	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	39	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	91	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	103	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	117	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	128	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Turn	142	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	156	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	162	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	170	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Turn	175	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	179	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	1051	1066	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	1068	1081	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	1096	1099	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	1101	1106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	1107	1109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	1114	1117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	1126	1128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	1131	1146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	1152	1158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Turn	1159	1162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	1165	1178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	1183	1188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	1192	1195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	1199	1207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Turn	1208	1211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Beta strand	1212	1219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+P32908	UniProtKB	Helix	1220	1222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W	
+##sequence-region P32566 1 505
+P32566	UniProtKB	Chain	1	505	.	.	.	ID=PRO_0000209870;Note=Cell wall assembly regulator SMI1	
+P32566	UniProtKB	Modified residue	202	202	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32566	UniProtKB	Modified residue	203	203	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32566	UniProtKB	Modified residue	376	376	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32566	UniProtKB	Modified residue	381	381	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32566	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32566	UniProtKB	Modified residue	400	400	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32566	UniProtKB	Cross-link	453	453	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32566	UniProtKB	Helix	87	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Helix	106	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Helix	118	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Helix	134	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Beta strand	157	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Helix	167	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Beta strand	221	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Turn	225	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Beta strand	230	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Beta strand	237	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Beta strand	244	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Beta strand	263	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Beta strand	272	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Helix	281	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Beta strand	313	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Turn	318	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+P32566	UniProtKB	Helix	327	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B	
+##sequence-region Q04174 1 516
+Q04174	UniProtKB	Chain	1	516	.	.	.	ID=PRO_0000071977;Note=GPI mannosyltransferase 4	
+Q04174	UniProtKB	Topological domain	1	5	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Transmembrane	6	26	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Topological domain	27	60	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Transmembrane	61	81	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Topological domain	82	175	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Transmembrane	176	196	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Topological domain	197	210	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Transmembrane	211	231	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Topological domain	232	270	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Transmembrane	271	291	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Topological domain	292	295	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Transmembrane	296	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Topological domain	317	317	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Transmembrane	318	338	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Topological domain	339	348	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Transmembrane	349	369	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Topological domain	370	516	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Glycosylation	403	403	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Glycosylation	452	452	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04174	UniProtKB	Sequence conflict	122	123	.	.	.	Note=IK->MQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q04174	UniProtKB	Sequence conflict	122	123	.	.	.	Note=IK->MQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q04174	UniProtKB	Sequence conflict	163	163	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q04174	UniProtKB	Sequence conflict	169	169	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q04174	UniProtKB	Sequence conflict	279	279	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38990 1 1142
+P38990	UniProtKB	Chain	1	1142	.	.	.	ID=PRO_0000086464;Note=SNF1-activating kinase 1	
+P38990	UniProtKB	Domain	133	448	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38990	UniProtKB	Nucleotide binding	139	147	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38990	UniProtKB	Active site	277	277	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P38990	UniProtKB	Binding site	162	162	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P38990	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38990	UniProtKB	Modified residue	964	964	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38990	UniProtKB	Modified residue	1126	1126	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+P38990	UniProtKB	Sequence conflict	171	171	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38990	UniProtKB	Sequence conflict	266	268	.	.	.	Note=EYL->DS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39955 1 897
+P39955	UniProtKB	Chain	1	897	.	.	.	ID=PRO_0000084761;Note=Protein SAP1	
+P39955	UniProtKB	Nucleotide binding	645	652	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39955	UniProtKB	Modified residue	536	536	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53036 1 818
+P53036	UniProtKB	Chain	1	818	.	.	.	ID=PRO_0000097585;Note=SIT4-associating protein SAP4	
+##sequence-region Q99314 1 248
+Q99314	UniProtKB	Chain	1	248	.	.	.	ID=PRO_0000097596;Note=Something about silencing protein 5	
+Q99314	UniProtKB	Domain	8	116	.	.	.	Note=YEATS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00376	
+Q99314	UniProtKB	Modified residue	144	144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q00711 1 640
+Q00711	UniProtKB	Transit peptide	1	28	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1518827,ECO:0000269|PubMed:8120006;Dbxref=PMID:1518827,PMID:8120006	
+Q00711	UniProtKB	Chain	29	640	.	.	.	ID=PRO_0000010342;Note=Succinate dehydrogenase [ubiquinone] flavoprotein subunit%2C mitochondrial	
+Q00711	UniProtKB	Nucleotide binding	59	64	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+Q00711	UniProtKB	Nucleotide binding	82	97	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+Q00711	UniProtKB	Nucleotide binding	449	450	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+Q00711	UniProtKB	Active site	331	331	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+Q00711	UniProtKB	Binding site	266	266	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+Q00711	UniProtKB	Binding site	287	287	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+Q00711	UniProtKB	Binding site	299	299	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+Q00711	UniProtKB	Binding site	398	398	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+Q00711	UniProtKB	Binding site	433	433	.	.	.	Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+Q00711	UniProtKB	Binding site	444	444	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+Q00711	UniProtKB	Modified residue	90	90	.	.	.	Note=Tele-8alpha-FAD histidine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1	
+Q00711	UniProtKB	Mutagenesis	90	90	.	.	.	Note=Abolishes covalent attachment of FAD. No effect on complex assembly. Abolishes succinate-dehydrogenase activity but no effect on fumarate reductase activity. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8026509;Dbxref=PMID:8026509	
+##sequence-region Q04491 1 297
+Q04491	UniProtKB	Chain	1	297	.	.	.	ID=PRO_0000051206;Note=Protein transport protein SEC13	
+Q04491	UniProtKB	Repeat	7	46	.	.	.	Note=WD 1	
+Q04491	UniProtKB	Repeat	51	92	.	.	.	Note=WD 2	
+Q04491	UniProtKB	Repeat	97	138	.	.	.	Note=WD 3	
+Q04491	UniProtKB	Repeat	143	195	.	.	.	Note=WD 4	
+Q04491	UniProtKB	Repeat	202	244	.	.	.	Note=WD 5	
+Q04491	UniProtKB	Repeat	252	291	.	.	.	Note=WD 6	
+Q04491	UniProtKB	Mutagenesis	176	176	.	.	.	Note=Leads to mislocalization of NPCs and overproliferation of the nuclear and ER membranes at 34 degree Celsius. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12215173;Dbxref=PMID:12215173	
+Q04491	UniProtKB	Mutagenesis	224	224	.	.	.	Note=Growth inhibited above 30 degrees Celsius. S->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8432727;Dbxref=PMID:8432727	
+Q04491	UniProtKB	Mutagenesis	262	262	.	.	.	Note=Growth inhibited above 30 degrees Celsius. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8432727;Dbxref=PMID:8432727	
+Q04491	UniProtKB	Mutagenesis	266	266	.	.	.	Note=Growth inhibited above 34 degrees Celsius. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8432727;Dbxref=PMID:8432727	
+Q04491	UniProtKB	Beta strand	2	4	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+Q04491	UniProtKB	Beta strand	5	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JRP	
+Q04491	UniProtKB	Beta strand	12	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	21	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	33	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	56	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Helix	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	68	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	79	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+Q04491	UniProtKB	Beta strand	102	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Helix	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	114	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	123	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	139	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	148	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	157	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+Q04491	UniProtKB	Turn	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+Q04491	UniProtKB	Beta strand	166	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK	
+Q04491	UniProtKB	Beta strand	172	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	182	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Turn	189	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	193	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	207	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	217	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	227	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO	
+Q04491	UniProtKB	Beta strand	231	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	244	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	257	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	264	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	269	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	274	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM6	
+Q04491	UniProtKB	Beta strand	278	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+Q04491	UniProtKB	Beta strand	285	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9	
+Q04491	UniProtKB	Beta strand	289	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7	
+##sequence-region P24280 1 304
+P24280	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2407740;Dbxref=PMID:2407740	
+P24280	UniProtKB	Chain	2	304	.	.	.	ID=PRO_0000210744;Note=SEC14 cytosolic factor	
+P24280	UniProtKB	Domain	99	272	.	.	.	Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056	
+P24280	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P24280	UniProtKB	Cross-link	42	42	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P24280	UniProtKB	Cross-link	84	84	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P24280	UniProtKB	Helix	6	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Turn	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	33	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	55	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Turn	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	69	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	91	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	100	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Beta strand	110	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Beta strand	120	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Turn	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	140	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	158	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Beta strand	173	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	184	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Beta strand	209	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	219	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	234	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Beta strand	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	248	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Turn	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Beta strand	257	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	272	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	284	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+P24280	UniProtKB	Helix	288	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA	
+##sequence-region P29478 1 273
+P29478	UniProtKB	Chain	1	273	.	.	.	ID=PRO_0000135212;Note=Signal recognition particle subunit SEC65	
+##sequence-region Q02825 1 467
+Q02825	UniProtKB	Chain	1	467	.	.	.	ID=PRO_0000194034;Note=tRNA-splicing endonuclease subunit SEN54	
+Q02825	UniProtKB	Compositional bias	19	27	.	.	.	Note=Poly-Glu	
+Q02825	UniProtKB	Compositional bias	353	356	.	.	.	Note=Poly-Asp	
+##sequence-region P40510 1 469
+P40510	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P40510	UniProtKB	Chain	2	469	.	.	.	ID=PRO_0000076019;Note=D-3-phosphoglycerate dehydrogenase 2	
+P40510	UniProtKB	Domain	399	469	.	.	.	Note=ACT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007	
+P40510	UniProtKB	Nucleotide binding	208	209	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0	
+P40510	UniProtKB	Nucleotide binding	285	287	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0	
+P40510	UniProtKB	Nucleotide binding	347	350	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0	
+P40510	UniProtKB	Active site	287	287	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40510	UniProtKB	Active site	316	316	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40510	UniProtKB	Active site	347	347	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40510	UniProtKB	Binding site	228	228	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0	
+P40510	UniProtKB	Binding site	311	311	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0	
+P40510	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P40510	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950	
+P40510	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40510	UniProtKB	Modified residue	33	33	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P46995 1 733
+P46995	UniProtKB	Chain	1	733	.	.	.	ID=PRO_0000186087;Note=Histone-lysine N-methyltransferase%2C H3 lysine-36 specific	
+P46995	UniProtKB	Domain	63	118	.	.	.	Note=AWS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00562	
+P46995	UniProtKB	Domain	120	237	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+P46995	UniProtKB	Domain	244	260	.	.	.	Note=Post-SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00155	
+P46995	UniProtKB	Domain	475	507	.	.	.	Note=WW	
+P46995	UniProtKB	Region	619	718	.	.	.	Note=Binding to RNA polymerase II CTD	
+P46995	UniProtKB	Coiled coil	548	630	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46995	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46995	UniProtKB	Modified residue	522	522	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46995	UniProtKB	Mutagenesis	195	195	.	.	.	Note=Reduces dramatically histone methyltransferase activity toward nucleosomes. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839797;Dbxref=PMID:11839797	
+P46995	UniProtKB	Mutagenesis	201	201	.	.	.	Note=Reduces dramatically histone methyltransferase activity toward nucleosomes. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839797;Dbxref=PMID:11839797	
+P46995	UniProtKB	Sequence conflict	594	594	.	.	.	Note=A->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46995	UniProtKB	Sequence conflict	605	605	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46995	UniProtKB	Sequence conflict	716	716	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46995	UniProtKB	Beta strand	481	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E0N	
+P46995	UniProtKB	Turn	495	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E0N	
+P46995	UniProtKB	Beta strand	499	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E0N	
+P46995	UniProtKB	Helix	624	645	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Z	
+P46995	UniProtKB	Turn	648	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Z	
+P46995	UniProtKB	Helix	655	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Z	
+P46995	UniProtKB	Helix	688	712	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Z	
+##sequence-region Q08446 1 395
+Q08446	UniProtKB	Chain	1	395	.	.	.	ID=PRO_0000185393;Note=Protein SGT1	
+Q08446	UniProtKB	Domain	182	277	.	.	.	Note=CS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00547	
+Q08446	UniProtKB	Domain	312	395	.	.	.	Note=SGS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00386	
+Q08446	UniProtKB	Modified residue	168	168	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08446	UniProtKB	Modified residue	171	171	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q08446	UniProtKB	Cross-link	32	32	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q08446	UniProtKB	Mutagenesis	31	31	.	.	.	Note=In sgt1-3%3B induces arrest of cell division in G2/M%3B when associated with L-99 and I-213. L->P	
+Q08446	UniProtKB	Mutagenesis	99	99	.	.	.	Note=In sgt1-3%3B induces arrest of cell division in G2/M%3B when associated with P-31 I-213. F->L	
+Q08446	UniProtKB	Mutagenesis	213	213	.	.	.	Note=In sgt1-3%3B induces arrest of cell division in G2/M%3B when associated with P-31 and L-99. N->I	
+Q08446	UniProtKB	Mutagenesis	220	220	.	.	.	Note=In sgt1-5%3B induces arrest of cell division in G2/M%3B when associated with K-364. D->V	
+Q08446	UniProtKB	Mutagenesis	364	364	.	.	.	Note=In sgt1-5%3B induces arrest of cell division in G2/M%3B when associated with V-220. E->K	
+Q08446	UniProtKB	Mutagenesis	371	371	.	.	.	Note=In A364a%3B suppressor of the cdc35-1 allele. S->N	
+Q08446	UniProtKB	Sequence conflict	13	13	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08446	UniProtKB	Helix	4	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3	
+Q08446	UniProtKB	Helix	20	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3	
+Q08446	UniProtKB	Helix	38	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3	
+Q08446	UniProtKB	Helix	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3	
+Q08446	UniProtKB	Helix	61	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3	
+Q08446	UniProtKB	Helix	84	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3	
+Q08446	UniProtKB	Helix	104	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3	
+Q08446	UniProtKB	Helix	124	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3	
+##sequence-region P53266 1 389
+P53266	UniProtKB	Chain	1	389	.	.	.	ID=PRO_0000215659;Note=Cytochrome oxidase assembly protein SHY1	
+P53266	UniProtKB	Topological domain	1	71	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53266	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53266	UniProtKB	Topological domain	93	341	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53266	UniProtKB	Transmembrane	342	362	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53266	UniProtKB	Topological domain	363	389	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38634 1 284
+P38634	UniProtKB	Chain	1	284	.	.	.	ID=PRO_0000097751;Note=Protein SIC1	
+P38634	UniProtKB	Compositional bias	124	135	.	.	.	Note=Asp/Glu-rich (acidic)	
+P38634	UniProtKB	Compositional bias	200	206	.	.	.	Note=Asp/Glu-rich (acidic)	
+P38634	UniProtKB	Modified residue	5	5	.	.	.	Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9725902;Dbxref=PMID:9725902	
+P38634	UniProtKB	Modified residue	33	33	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9725902;Dbxref=PMID:9725902	
+P38634	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9725902;Dbxref=PMID:9725902	
+P38634	UniProtKB	Modified residue	173	173	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000269|PubMed:15448699;Dbxref=PMID:17330950,PMID:15448699	
+P38634	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P38634	UniProtKB	Modified residue	201	201	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38634	UniProtKB	Modified residue	268	268	.	.	.	Note=Lysine derivative	
+P38634	UniProtKB	Modified residue	272	272	.	.	.	Note=Lysine derivative	
+P38634	UniProtKB	Modified residue	274	274	.	.	.	Note=Lysine derivative	
+P38634	UniProtKB	Mutagenesis	173	173	.	.	.	Note=Impairs the ability to arrest the cell cycle. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15448699;Dbxref=PMID:15448699	
+P38634	UniProtKB	Sequence conflict	167	167	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38262 1 535
+P38262	UniProtKB	Chain	1	535	.	.	.	ID=PRO_0000051216;Note=SIR4-interacting protein SIF2	
+P38262	UniProtKB	Domain	4	36	.	.	.	Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126	
+P38262	UniProtKB	Repeat	155	186	.	.	.	Note=WD 1	
+P38262	UniProtKB	Repeat	218	248	.	.	.	Note=WD 2	
+P38262	UniProtKB	Repeat	259	289	.	.	.	Note=WD 3	
+P38262	UniProtKB	Repeat	316	345	.	.	.	Note=WD 4	
+P38262	UniProtKB	Repeat	357	387	.	.	.	Note=WD 5	
+P38262	UniProtKB	Repeat	399	428	.	.	.	Note=WD 6	
+P38262	UniProtKB	Repeat	440	470	.	.	.	Note=WD 7	
+P38262	UniProtKB	Repeat	503	534	.	.	.	Note=WD 8	
+P38262	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38262	UniProtKB	Sequence conflict	396	396	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38262	UniProtKB	Beta strand	152	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	161	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	172	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	181	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	198	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	223	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	232	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	244	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	253	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	264	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	273	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	285	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Turn	290	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	294	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	325	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	331	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Helix	337	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	341	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	352	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	362	368	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Turn	369	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	373	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	383	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	388	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	394	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	404	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Turn	411	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	414	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	422	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Turn	429	432	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	433	439	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	445	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	454	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	466	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Helix	472	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	496	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	509	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	518	528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+P38262	UniProtKB	Beta strand	531	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M	
+##sequence-region Q12216 1 726
+Q12216	UniProtKB	Chain	1	726	.	.	.	ID=PRO_0000218985;Note=E3 SUMO-protein ligase SIZ2	
+Q12216	UniProtKB	Domain	43	77	.	.	.	Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186	
+Q12216	UniProtKB	Domain	139	291	.	.	.	Note=PINIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00799	
+Q12216	UniProtKB	Zinc finger	323	400	.	.	.	Note=SP-RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00452	
+Q12216	UniProtKB	Compositional bias	7	16	.	.	.	Note=Poly-Asn	
+##sequence-region Q06315 1 1026
+Q06315	UniProtKB	Chain	1	1026	.	.	.	ID=PRO_0000269649;Note=Protein SKG3	
+Q06315	UniProtKB	Domain	90	221	.	.	.	Note=PH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+Q06315	UniProtKB	Domain	254	433	.	.	.	Note=PH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+Q06315	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06315	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06315	UniProtKB	Modified residue	578	578	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06315	UniProtKB	Modified residue	580	580	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06315	UniProtKB	Modified residue	592	592	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q06315	UniProtKB	Modified residue	701	701	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06315	UniProtKB	Modified residue	954	954	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38314 1 527
+P38314	UniProtKB	Chain	1	527	.	.	.	ID=PRO_0000202512;Note=Protein SDS24	
+P38314	UniProtKB	Domain	114	175	.	.	.	Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P38314	UniProtKB	Domain	198	256	.	.	.	Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P38314	UniProtKB	Domain	283	342	.	.	.	Note=CBS 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P38314	UniProtKB	Domain	443	512	.	.	.	Note=CBS 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P38314	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38314	UniProtKB	Modified residue	458	458	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38314	UniProtKB	Modified residue	524	524	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+##sequence-region P38164 1 1038
+P38164	UniProtKB	Chain	1	1038	.	.	.	ID=PRO_0000051470;Note=SEH-associated protein 4	
+P38164	UniProtKB	Repeat	50	90	.	.	.	Note=WD 1	
+P38164	UniProtKB	Repeat	147	189	.	.	.	Note=WD 2	
+P38164	UniProtKB	Repeat	235	276	.	.	.	Note=WD 3	
+P38164	UniProtKB	Repeat	544	587	.	.	.	Note=WD 4	
+P38164	UniProtKB	Modified residue	123	123	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38164	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q12745 1 709
+Q12745	UniProtKB	Chain	1	709	.	.	.	ID=PRO_0000234109;Note=Protein transport protein SEC39	
+Q12745	UniProtKB	Helix	33	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	49	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	54	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	105	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Turn	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	120	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Turn	139	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	143	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	156	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	166	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	182	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	190	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	212	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	218	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	228	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Turn	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	246	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	270	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	294	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Beta strand	310	314	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Turn	315	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Beta strand	318	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	322	334	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	341	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	352	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	373	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Turn	383	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Beta strand	392	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	399	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	416	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	432	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	457	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	479	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	515	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Turn	521	523	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	526	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	539	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	543	556	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	565	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	586	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	605	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	631	633	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	637	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	656	658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+Q12745	UniProtKB	Helix	659	673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P	
+##sequence-region P33332 1 1336
+P33332	UniProtKB	Chain	1	1336	.	.	.	ID=PRO_0000118917;Note=Exocyst complex component SEC3	
+P33332	UniProtKB	Coiled coil	319	464	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33332	UniProtKB	Coiled coil	1309	1336	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33332	UniProtKB	Modified residue	290	290	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P33332	UniProtKB	Modified residue	606	606	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P33332	UniProtKB	Helix	76	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Beta strand	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y	
+P33332	UniProtKB	Beta strand	99	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P33332	UniProtKB	Beta strand	107	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Helix	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Beta strand	134	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Beta strand	151	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Helix	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P33332	UniProtKB	Beta strand	164	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Helix	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Beta strand	177	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Beta strand	187	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Helix	203	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Turn	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58	
+P33332	UniProtKB	Beta strand	229	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Beta strand	235	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE	
+P33332	UniProtKB	Helix	240	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y	
+##sequence-region P89102 1 971
+P89102	UniProtKB	Chain	1	971	.	.	.	ID=PRO_0000118924;Note=Exocyst complex component SEC5	
+P89102	UniProtKB	Coiled coil	123	182	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P89102	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P38890 1 526
+P38890	UniProtKB	Chain	1	526	.	.	.	ID=PRO_0000202942;Note=Putative protein lysine methyltransferase SET5	
+P38890	UniProtKB	Domain	112	403	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+P38890	UniProtKB	Modified residue	517	517	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q12507 1 346
+Q12507	UniProtKB	Chain	1	346	.	.	.	ID=PRO_0000269646;Note=Superficial pseudohyphal growth protein 1	
+##sequence-region P40363 1 299
+P40363	UniProtKB	Chain	1	299	.	.	.	ID=PRO_0000210342;Note=S-formylglutathione hydrolase	
+P40363	UniProtKB	Active site	161	161	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40363	UniProtKB	Active site	241	241	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40363	UniProtKB	Active site	276	276	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40363	UniProtKB	Beta strand	2	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Beta strand	12	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Turn	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Beta strand	25	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	36	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Beta strand	51	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	62	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	71	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Beta strand	81	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Beta strand	102	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	117	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	125	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	132	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Beta strand	151	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	162	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	175	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Beta strand	181	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	196	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Beta strand	233	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	244	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	251	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Turn	261	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Beta strand	266	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+P40363	UniProtKB	Helix	278	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL	
+##sequence-region P47166 1 707
+P47166	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P47166	UniProtKB	Chain	2	707	.	.	.	ID=PRO_0000203121;Note=Protein SGM1	
+P47166	UniProtKB	Coiled coil	122	473	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47166	UniProtKB	Coiled coil	594	706	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47166	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P47166	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P47166	UniProtKB	Modified residue	538	538	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47166	UniProtKB	Modified residue	549	549	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47166	UniProtKB	Modified residue	568	568	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47166	UniProtKB	Modified residue	571	571	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P47166	UniProtKB	Modified residue	576	576	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47166	UniProtKB	Modified residue	589	589	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32578 1 815
+P32578	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32578	UniProtKB	Chain	2	815	.	.	.	ID=PRO_0000204374;Note=SNF1 protein kinase subunit beta-1	
+P32578	UniProtKB	Region	473	716	.	.	.	Note=Kinase-interacting sequence (KIS)%3B required for interaction with SNF1	
+P32578	UniProtKB	Region	724	804	.	.	.	Note=Association with SNF1 kinase complex (ASC) domain%3B required for interaction with SNF4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9121458;Dbxref=PMID:9121458	
+P32578	UniProtKB	Modified residue	33	33	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32578	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32578	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32578	UniProtKB	Modified residue	200	200	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32578	UniProtKB	Modified residue	206	206	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32578	UniProtKB	Modified residue	209	209	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32578	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32578	UniProtKB	Modified residue	331	331	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32578	UniProtKB	Modified residue	494	494	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32578	UniProtKB	Modified residue	497	497	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32578	UniProtKB	Modified residue	643	643	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32578	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32578	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Prevents relocalization to the vacuolar membrane. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14966266;Dbxref=PMID:14966266	
+##sequence-region Q02793 1 397
+Q02793	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000051218;Note=Antiviral protein SKI8	
+Q02793	UniProtKB	Repeat	21	42	.	.	.	Note=WD 1	
+Q02793	UniProtKB	Repeat	67	101	.	.	.	Note=WD 2	
+Q02793	UniProtKB	Repeat	126	157	.	.	.	Note=WD 3	
+Q02793	UniProtKB	Repeat	191	213	.	.	.	Note=WD 4	
+Q02793	UniProtKB	Repeat	238	264	.	.	.	Note=WD 5	
+Q02793	UniProtKB	Repeat	296	319	.	.	.	Note=WD 6	
+Q02793	UniProtKB	Repeat	359	392	.	.	.	Note=WD 7	
+Q02793	UniProtKB	Beta strand	4	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	15	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	19	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	26	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	36	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Helix	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	55	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	65	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Turn	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	79	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	93	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Turn	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	107	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Helix	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	124	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	139	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	150	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Helix	161	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Turn	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	172	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	182	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	191	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	198	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	207	213	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Turn	214	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	218	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	236	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	247	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	257	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Turn	265	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	270	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	288	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	294	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	301	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	313	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Turn	320	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	324	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Helix	333	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Helix	339	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	357	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Turn	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	368	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	378	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Turn	384	386	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+Q02793	UniProtKB	Beta strand	387	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9	
+##sequence-region P33336 1 771
+P33336	UniProtKB	Chain	1	771	.	.	.	ID=PRO_0000097780;Note=Beta-glucan synthesis-associated protein SKN1	
+P33336	UniProtKB	Topological domain	1	289	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33336	UniProtKB	Transmembrane	290	310	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33336	UniProtKB	Topological domain	311	771	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33336	UniProtKB	Domain	353	716	.	.	.	Note=GH16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01098	
+P33336	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33336	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33336	UniProtKB	Modified residue	67	67	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33336	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32486	
+P33336	UniProtKB	Modified residue	103	103	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P33336	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32486	
+P33336	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32486	
+P33336	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32486	
+P33336	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32486	
+P33336	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P33336	UniProtKB	Glycosylation	337	337	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33336	UniProtKB	Glycosylation	426	426	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33336	UniProtKB	Glycosylation	513	513	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33336	UniProtKB	Glycosylation	590	590	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33336	UniProtKB	Glycosylation	615	615	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33336	UniProtKB	Glycosylation	743	743	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12505 1 502
+Q12505	UniProtKB	Chain	1	502	.	.	.	ID=PRO_0000086657;Note=Serine/threonine-protein kinase SKS1	
+Q12505	UniProtKB	Domain	10	338	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12505	UniProtKB	Nucleotide binding	16	24	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12505	UniProtKB	Active site	186	186	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q12505	UniProtKB	Binding site	39	39	.	.	.	Note=ATP	
+Q12505	UniProtKB	Mutagenesis	39	39	.	.	.	Note=Loss of activity. K->R	
+##sequence-region Q03656 1 742
+Q03656	UniProtKB	Chain	1	742	.	.	.	ID=PRO_0000086658;Note=Serine/threonine-protein kinase SKY1	
+Q03656	UniProtKB	Domain	158	706	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03656	UniProtKB	Nucleotide binding	164	172	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03656	UniProtKB	Active site	294	294	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q03656	UniProtKB	Binding site	187	187	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03656	UniProtKB	Modified residue	383	383	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03656	UniProtKB	Modified residue	386	386	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03656	UniProtKB	Modified residue	388	388	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03656	UniProtKB	Modified residue	393	393	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03656	UniProtKB	Modified residue	410	410	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03656	UniProtKB	Modified residue	427	427	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03656	UniProtKB	Modified residue	432	432	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03656	UniProtKB	Modified residue	445	445	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03656	UniProtKB	Modified residue	449	449	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03656	UniProtKB	Modified residue	453	453	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03656	UniProtKB	Turn	154	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Beta strand	158	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Beta strand	168	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Turn	178	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Beta strand	182	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	193	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	216	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Beta strand	230	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Beta strand	239	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	253	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Turn	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	267	286	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	297	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Beta strand	300	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Turn	539	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Beta strand	543	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	551	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HOW	
+Q03656	UniProtKB	Helix	568	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	573	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	584	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Beta strand	610	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	615	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	631	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	640	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Beta strand	650	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	661	667	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	673	683	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	684	687	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Turn	691	693	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	697	701	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Helix	704	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+Q03656	UniProtKB	Turn	710	714	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q99	
+Q03656	UniProtKB	Helix	726	728	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q99	
+Q03656	UniProtKB	Beta strand	732	734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y	
+##sequence-region Q03406 1 294
+Q03406	UniProtKB	Chain	1	294	.	.	.	ID=PRO_0000071955;Note=DNA replication complex GINS protein SLD5	
+Q03406	UniProtKB	Mutagenesis	21	21	.	.	.	Note=In sld5-8%3B temperature-sensitive mutant%3B in association with P-66. Defective in DNA replication. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134	
+Q03406	UniProtKB	Mutagenesis	66	66	.	.	.	Note=In sld5-8%3B temperature-sensitive mutant%3B in association with P-21. Defective in DNA replication. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134	
+Q03406	UniProtKB	Mutagenesis	67	67	.	.	.	Note=In sld5-12%3B temperature-sensitive mutant. Defective in DNA replication. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134	
+Q03406	UniProtKB	Mutagenesis	150	150	.	.	.	Note=In sld5-2%3B temperature-sensitive mutant. Defective in DNA replication. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134	
+Q03406	UniProtKB	Mutagenesis	293	293	.	.	.	Note=In sld5-13%3B temperature-sensitive mutant. Defective in DNA replication. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134	
+Q03406	UniProtKB	Sequence conflict	232	232	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03406	UniProtKB	Helix	6	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C95	
+##sequence-region P38283 1 698
+P38283	UniProtKB	Chain	1	698	.	.	.	ID=PRO_0000071956;Note=Inner centromere protein-related protein SLI15	
+P38283	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38283	UniProtKB	Modified residue	489	489	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P38345 1 138
+P38345	UniProtKB	Transit peptide	1	32	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38345	UniProtKB	Chain	33	138	.	.	.	ID=PRO_0000041936;Note=Succinate dehydrogenase assembly factor 4%2C mitochondrial	
+##sequence-region P38804 1 111
+P38804	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000202905;Note=Restriction of telomere capping protein 3	
+P38804	UniProtKB	Beta strand	5	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN	
+P38804	UniProtKB	Beta strand	12	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN	
+P38804	UniProtKB	Helix	23	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN	
+P38804	UniProtKB	Helix	35	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN	
+P38804	UniProtKB	Beta strand	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN	
+P38804	UniProtKB	Beta strand	56	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN	
+P38804	UniProtKB	Helix	65	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN	
+P38804	UniProtKB	Helix	79	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN	
+P38804	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN	
+##sequence-region Q07953 1 250
+Q07953	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000123764;Note=Ribosome maturation protein SDO1	
+Q07953	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Impairs protein folding and stability. Loss of function. C->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15701631;Dbxref=PMID:15701631	
+Q07953	UniProtKB	Mutagenesis	34	34	.	.	.	Note=Impairs protein folding and stability. Loss of function. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15701631;Dbxref=PMID:15701631	
+Q07953	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Impairs protein folding and stability. Loss of function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15701631;Dbxref=PMID:15701631	
+##sequence-region P40479 1 209
+P40479	UniProtKB	Chain	1	209	.	.	.	ID=PRO_0000094924;Note=Dual-specificity protein phosphatase SDP1	
+P40479	UniProtKB	Active site	140	140	.	.	.	Note=Phosphocysteine intermediate	
+P40479	UniProtKB	Binding site	111	111	.	.	.	Note=Phosphotyrosine	
+P40479	UniProtKB	Disulfide bond	47	142	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17495930;Dbxref=PMID:17495930	
+P40479	UniProtKB	Beta strand	58	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Turn	65	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Turn	76	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Beta strand	83	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Beta strand	103	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Helix	112	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Helix	119	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Beta strand	136	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Helix	146	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Helix	163	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+P40479	UniProtKB	Helix	181	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16	
+##sequence-region P53078 1 280
+P53078	UniProtKB	Chain	1	280	.	.	.	ID=PRO_0000072213;Note=Suppressor of disruption of TFIIS	
+P53078	UniProtKB	Helix	6	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Beta strand	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Turn	63	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	71	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	93	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	108	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	122	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Turn	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	143	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Beta strand	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Beta strand	159	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	169	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Beta strand	186	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	205	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Beta strand	223	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	230	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Beta strand	242	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Beta strand	249	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPX	
+P53078	UniProtKB	Helix	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONN	
+P53078	UniProtKB	Beta strand	264	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	269	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+P53078	UniProtKB	Helix	277	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ	
+##sequence-region P20048 1 519
+P20048	UniProtKB	Chain	1	519	.	.	.	ID=PRO_0000097662;Note=Dolichol kinase	
+P20048	UniProtKB	Topological domain	1	47	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	69	88	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	89	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	110	118	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	140	151	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	152	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	173	181	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	182	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	204	223	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	224	244	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	245	253	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	254	274	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	275	294	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	295	315	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	316	326	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	327	347	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	348	349	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	350	370	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	371	394	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	395	415	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	416	417	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	418	438	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	439	449	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	450	470	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	471	472	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Transmembrane	473	493	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P20048	UniProtKB	Topological domain	494	519	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P14906 1 663
+P14906	UniProtKB	Chain	1	663	.	.	.	ID=PRO_0000071095;Note=Protein translocation protein SEC63	
+P14906	UniProtKB	Topological domain	1	13	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14906	UniProtKB	Transmembrane	14	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14906	UniProtKB	Topological domain	42	92	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14906	UniProtKB	Transmembrane	93	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14906	UniProtKB	Topological domain	109	220	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14906	UniProtKB	Transmembrane	221	239	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14906	UniProtKB	Topological domain	240	663	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14906	UniProtKB	Domain	123	198	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P14906	UniProtKB	Domain	228	532	.	.	.	Note=SEC63	
+P14906	UniProtKB	Repeat	461	471	.	.	.	Note=1	
+P14906	UniProtKB	Repeat	493	503	.	.	.	Note=2	
+P14906	UniProtKB	Region	461	503	.	.	.	Note=2 X 11 AA repeats	
+P14906	UniProtKB	Compositional bias	612	663	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P14906	UniProtKB	Modified residue	512	512	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P14906	UniProtKB	Mutagenesis	179	179	.	.	.	Note=Temperature-sensitive. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8514125;Dbxref=PMID:8514125	
+P14906	UniProtKB	Mutagenesis	426	426	.	.	.	Note=Temperature-sensitive. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8514125;Dbxref=PMID:8514125	
+P14906	UniProtKB	Mutagenesis	431	431	.	.	.	Note=Temperature-sensitive. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8514125;Dbxref=PMID:8514125	
+P14906	UniProtKB	Mutagenesis	503	503	.	.	.	Note=Temperature-sensitive. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8514125;Dbxref=PMID:8514125	
+P14906	UniProtKB	Mutagenesis	511	511	.	.	.	Note=Temperature-sensitive. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8514125;Dbxref=PMID:8514125	
+P14906	UniProtKB	Mutagenesis	652	652	.	.	.	Note=Abolishes interaction with SEC62%3B defect in protein translocation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15671059;Dbxref=PMID:15671059	
+P14906	UniProtKB	Mutagenesis	654	654	.	.	.	Note=Abolishes interaction with SEC62%3B defect in protein translocation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15671059;Dbxref=PMID:15671059	
+P14906	UniProtKB	Sequence conflict	263	263	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P14906	UniProtKB	Sequence conflict	293	293	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04279 1 960
+Q04279	UniProtKB	Chain	1	960	.	.	.	ID=PRO_0000203284;Note=Eisosome protein SEG1	
+Q04279	UniProtKB	Compositional bias	941	960	.	.	.	Note=Lys-rich (basic%2C sufficient to bind lipids%2C important for targeting the protein to the plasma membrane in small buds)	
+Q04279	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q04279	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04279	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q04279	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q04279	UniProtKB	Modified residue	319	319	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04279	UniProtKB	Modified residue	339	339	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04279	UniProtKB	Modified residue	352	352	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04279	UniProtKB	Modified residue	434	434	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04279	UniProtKB	Modified residue	461	461	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q04279	UniProtKB	Modified residue	467	467	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04279	UniProtKB	Modified residue	630	630	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04279	UniProtKB	Modified residue	675	675	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+Q04279	UniProtKB	Modified residue	758	758	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q04279	UniProtKB	Modified residue	816	816	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04279	UniProtKB	Modified residue	818	818	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04279	UniProtKB	Modified residue	855	855	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04279	UniProtKB	Sequence conflict	167	167	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53011 1 349
+P53011	UniProtKB	Chain	1	349	.	.	.	ID=PRO_0000051215;Note=Nucleoporin SEH1	
+P53011	UniProtKB	Repeat	7	46	.	.	.	Note=WD 1	
+P53011	UniProtKB	Repeat	53	94	.	.	.	Note=WD 2	
+P53011	UniProtKB	Repeat	106	147	.	.	.	Note=WD 3	
+P53011	UniProtKB	Repeat	153	192	.	.	.	Note=WD 4	
+P53011	UniProtKB	Repeat	210	253	.	.	.	Note=WD 5	
+P53011	UniProtKB	Repeat	302	341	.	.	.	Note=WD 6	
+P53011	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53011	UniProtKB	Beta strand	12	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	19	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	31	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	40	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	45	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	58	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Helix	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	70	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	77	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3P	
+P53011	UniProtKB	Beta strand	81	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	97	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	111	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Helix	119	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	123	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	133	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	149	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3P	
+P53011	UniProtKB	Beta strand	169	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	182	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	190	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	202	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	215	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	227	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	240	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	291	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	307	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	314	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	319	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	328	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+P53011	UniProtKB	Beta strand	339	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F	
+##sequence-region O94742 1 89
+O94742	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+O94742	UniProtKB	Chain	2	89	.	.	.	ID=PRO_0000122970;Note=26S proteasome complex subunit SEM1	
+O94742	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+O94742	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+O94742	UniProtKB	Helix	28	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5UBP	
+O94742	UniProtKB	Beta strand	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5UBP	
+O94742	UniProtKB	Beta strand	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5UBP	
+O94742	UniProtKB	Helix	72	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5UBP	
+##sequence-region P53953 1 876
+P53953	UniProtKB	Chain	1	876	.	.	.	ID=PRO_0000205151;Note=SED5-binding protein 2	
+P53953	UniProtKB	Region	164	189	.	.	.	Note=Zinc finger-like	
+P53953	UniProtKB	Compositional bias	311	320	.	.	.	Note=Poly-Glu	
+P53953	UniProtKB	Modified residue	51	51	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+##sequence-region P43682 1 97
+P43682	UniProtKB	Chain	1	97	.	.	.	ID=PRO_0000097712;Note=Protein transport protein SFT1	
+P43682	UniProtKB	Topological domain	1	74	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43682	UniProtKB	Transmembrane	75	94	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43682	UniProtKB	Topological domain	95	97	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43682	UniProtKB	Domain	7	69	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+##sequence-region P38166 1 215
+P38166	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38166	UniProtKB	Chain	2	215	.	.	.	ID=PRO_0000097713;Note=Protein transport protein SFT2	
+P38166	UniProtKB	Topological domain	2	81	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38166	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38166	UniProtKB	Topological domain	103	111	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38166	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38166	UniProtKB	Topological domain	133	145	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38166	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38166	UniProtKB	Topological domain	167	172	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38166	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38166	UniProtKB	Topological domain	194	215	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38166	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38166	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P40561 1 250
+P40561	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000081956;Note=RNA-binding protein SGN1	
+P40561	UniProtKB	Domain	64	141	.	.	.	Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+##sequence-region Q08490 1 590
+Q08490	UniProtKB	Chain	1	590	.	.	.	ID=PRO_0000055450;Note=Shugoshin	
+Q08490	UniProtKB	Coiled coil	25	86	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08490	UniProtKB	Mutagenesis	379	379	.	.	.	Note=In sgo1-100%3B induces a lack of response when chromosomes that are not under tension. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637284;Dbxref=PMID:15637284	
+Q08490	UniProtKB	Mutagenesis	390	390	.	.	.	Note=In sgo1-700%3B induces a lack of response when chromosomes that are not under tension. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637284;Dbxref=PMID:15637284	
+##sequence-region P46954 1 829
+P46954	UniProtKB	Chain	1	829	.	.	.	ID=PRO_0000114979;Note=Protein SIP4	
+P46954	UniProtKB	DNA binding	46	73	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P46954	UniProtKB	Sequence conflict	656	656	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P21691 1 654
+P21691	UniProtKB	Chain	1	654	.	.	.	ID=PRO_0000097767;Note=Regulatory protein SIR1	
+P21691	UniProtKB	Region	322	654	.	.	.	Note=Sufficient for interaction with SIR4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Region	449	587	.	.	.	Note=ORC interacting region (OIR)	
+P21691	UniProtKB	Mutagenesis	462	464	.	.	.	Note=No effect. EEE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	466	466	.	.	.	Note=Abolishes interaction with ORC1. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	469	469	.	.	.	Note=Abolishes interaction with ORC1. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	470	470	.	.	.	Note=Abolishes interaction with ORC1 and SIR4. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	477	477	.	.	.	Note=Abolishes interaction with ORC1 and SIR4. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	479	479	.	.	.	Note=Abolishes interaction with ORC1. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	480	480	.	.	.	Note=Abolishes interaction with ORC1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	482	483	.	.	.	Note=No effect. EE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	489	490	.	.	.	Note=No effect. KD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	498	499	.	.	.	Note=No effect. KD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	513	513	.	.	.	Note=Abolishes interaction with ORC1 and SIR4. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	517	518	.	.	.	Note=No effect. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	534	534	.	.	.	Note=No effect. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	538	540	.	.	.	Note=Abolishes interaction with SIR4. KKK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	569	569	.	.	.	Note=No effect. C->A	
+P21691	UniProtKB	Mutagenesis	571	571	.	.	.	Note=Abolishes interaction with ORC1 and SIR4. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	572	572	.	.	.	Note=No effect. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	573	573	.	.	.	Note=No effect. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	577	578	.	.	.	Note=Abolishes interaction with SIR4. DD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	584	584	.	.	.	Note=Abolishes interaction with ORC1 and SIR4. L->P%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Mutagenesis	586	587	.	.	.	Note=Abolishes interaction with SIR4. DD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749	
+P21691	UniProtKB	Beta strand	464	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Beta strand	476	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Turn	480	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Beta strand	484	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Helix	493	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Helix	499	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Helix	513	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Beta strand	523	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Helix	530	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Beta strand	537	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Beta strand	547	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Beta strand	566	575	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+P21691	UniProtKB	Beta strand	577	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZBX	
+P21691	UniProtKB	Beta strand	581	586	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A	
+##sequence-region P39980 1 628
+P39980	UniProtKB	Chain	1	628	.	.	.	ID=PRO_0000084878;Note=Siderophore iron transporter 1	
+P39980	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	107	127	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	194	214	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	225	245	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	285	305	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	317	337	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	354	374	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	394	414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	420	440	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	448	468	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	488	508	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Transmembrane	559	579	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39980	UniProtKB	Sequence conflict	386	386	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53965 1 281
+P53965	UniProtKB	Chain	1	281	.	.	.	ID=PRO_0000094922;Note=Tyrosine-protein phosphatase SIW14	
+P53965	UniProtKB	Active site	214	214	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10044	
+P53965	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q04195 1 904
+Q04195	UniProtKB	Chain	1	904	.	.	.	ID=PRO_0000245783;Note=E3 SUMO-protein ligase SIZ1	
+Q04195	UniProtKB	Domain	34	68	.	.	.	Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186	
+Q04195	UniProtKB	Domain	162	314	.	.	.	Note=PINIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00799	
+Q04195	UniProtKB	Zinc finger	346	423	.	.	.	Note=SP-RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00452	
+Q04195	UniProtKB	Region	794	904	.	.	.	Note=Required for localization at the bud neck	
+Q04195	UniProtKB	Modified residue	132	132	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04195	UniProtKB	Modified residue	794	794	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04195	UniProtKB	Mutagenesis	361	361	.	.	.	Note=Reduces E3 activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11577116;Dbxref=PMID:11577116	
+Q04195	UniProtKB	Mutagenesis	377	377	.	.	.	Note=Strongly reduces E3 activity%2C but no effect on subcellular location. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11577116,ECO:0000269|PubMed:11587849,ECO:0000269|PubMed:12761287;Dbxref=PMID:11577116,PMID:11587849,PMID:12761287	
+Q04195	UniProtKB	Mutagenesis	400	400	.	.	.	Note=Reduces E3 activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11577116;Dbxref=PMID:11577116	
+Q04195	UniProtKB	Mutagenesis	460	460	.	.	.	Note=No effect on E3 activity. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11577116;Dbxref=PMID:11577116	
+Q04195	UniProtKB	Helix	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN	
+Q04195	UniProtKB	Beta strand	16	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN	
+Q04195	UniProtKB	Helix	21	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN	
+Q04195	UniProtKB	Helix	39	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN	
+Q04195	UniProtKB	Helix	57	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN	
+Q04195	UniProtKB	Helix	79	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN	
+Q04195	UniProtKB	Helix	101	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN	
+Q04195	UniProtKB	Beta strand	169	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	183	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	199	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Helix	213	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	226	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Helix	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	250	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	269	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE	
+Q04195	UniProtKB	Helix	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Helix	281	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	287	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	291	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	304	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Helix	316	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Helix	331	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	354	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Turn	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	369	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Helix	385	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Turn	401	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Helix	409	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	412	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Helix	416	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	431	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	440	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D	
+Q04195	UniProtKB	Beta strand	456	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE	
+Q04195	UniProtKB	Beta strand	467	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE	
+Q04195	UniProtKB	Helix	479	488	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE	
+Q04195	UniProtKB	Helix	504	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE	
+Q04195	UniProtKB	Beta strand	507	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE	
+Q04195	UniProtKB	Turn	540	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE	
+Q04195	UniProtKB	Beta strand	549	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE	
+##sequence-region Q3E784 1 85
+Q3E784	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q3E784	UniProtKB	Chain	2	85	.	.	.	ID=PRO_0000076321;Note=SCOCO-like protein 1	
+Q3E784	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+Q3E784	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q3E784	UniProtKB	Mutagenesis	72	72	.	.	.	Note=Disrupts interaction with ARL3. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12620189;Dbxref=PMID:12620189	
+##sequence-region Q02775 1 382
+Q02775	UniProtKB	Chain	1	382	.	.	.	ID=PRO_0000218554;Note=Pre-mRNA-splicing factor SLU7	
+Q02775	UniProtKB	Zinc finger	120	137	.	.	.	Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047	
+Q02775	UniProtKB	Region	200	224	.	.	.	Note=Interaction with PRP8	
+Q02775	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q02775	UniProtKB	Modified residue	212	212	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q02775	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Affects the ability to associate with the spliceosome. Loss of growth and in vitro splicing activity%3B when associated with 215-AAA-217. Cryo- and thermosensitivity%3B when associated with A-217. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850	
+Q02775	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Affects the ability to associate with the spliceosome. Loss of growth and in vitro splicing activity%3B when associated with 215-AAA-217. Cryo- and thermosensitivity%3B when associated with A-217. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850	
+Q02775	UniProtKB	Mutagenesis	135	135	.	.	.	Note=Affects the ability to associate with the spliceosome. Loss of growth%2C spliceosome binding%2C and in vitro splicing activity%3B when associated with 215-AAA-217. Cryo- and thermosensitivity%3B when associated with A-217. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850	
+Q02775	UniProtKB	Mutagenesis	215	217	.	.	.	Note=Abolishes the interaction with PRP18%2C and temperature sensitive growth defect. Loss of growth and in vitro splicing activity%3B when associated with A-122 or A-130 or A-135. EIE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850	
+Q02775	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Abolishes the interaction with PRP18. Cryo- and thermosensitivity%3B when associated with A-122 or A-130 or A-135. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850	
+Q02775	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Abolishes the interaction with PRP18%2C and temperature sensitive growth defect. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850	
+Q02775	UniProtKB	Mutagenesis	221	224	.	.	.	Note=Abolishes the interaction with PRP18%2C and temperature sensitive growth defect. LELY->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850	
+Q02775	UniProtKB	Sequence conflict	235	235	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40072 1 274
+P40072	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000056336;Note=E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX8	
+P40072	UniProtKB	Zinc finger	206	250	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P40072	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40072	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40072	UniProtKB	Modified residue	67	67	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q12334 1 223
+Q12334	UniProtKB	Chain	1	223	.	.	.	ID=PRO_0000252298;Note=Protein SCM3	
+Q12334	UniProtKB	Helix	94	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L5A	
+Q12334	UniProtKB	Beta strand	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L5A	
+Q12334	UniProtKB	Helix	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L5A	
+Q12334	UniProtKB	Helix	154	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L5A	
+##sequence-region P23833 1 295
+P23833	UniProtKB	Transmembrane	76	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23833	UniProtKB	Metal binding	148	148	.	.	.	Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23833	UniProtKB	Metal binding	152	152	.	.	.	Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23833	UniProtKB	Metal binding	239	239	.	.	.	Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P23833	UniProtKB	Beta strand	120	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Helix	131	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Beta strand	139	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Helix	151	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Beta strand	175	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Turn	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Helix	188	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Beta strand	203	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Helix	209	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Turn	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Beta strand	243	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Beta strand	252	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Helix	264	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K	
+P23833	UniProtKB	Beta strand	284	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7J	
+##sequence-region P38072 1 301
+P38072	UniProtKB	Transmembrane	82	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38072	UniProtKB	Domain	101	284	.	.	.	Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691	
+P38072	UniProtKB	Metal binding	154	154	.	.	.	Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38072	UniProtKB	Metal binding	158	158	.	.	.	Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38072	UniProtKB	Metal binding	245	245	.	.	.	Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P11655 1 471
+P11655	UniProtKB	Chain	1	471	.	.	.	ID=PRO_0000097657;Note=Guanine nucleotide-exchange factor SEC12	
+P11655	UniProtKB	Topological domain	1	354	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922074;Dbxref=PMID:1922074	
+P11655	UniProtKB	Transmembrane	355	373	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P11655	UniProtKB	Topological domain	374	471	.	.	.	Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922074;Dbxref=PMID:1922074	
+P11655	UniProtKB	Repeat	259	300	.	.	.	Note=WD 1	
+P11655	UniProtKB	Repeat	302	341	.	.	.	Note=WD 2	
+P11655	UniProtKB	Glycosylation	439	439	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P11655	UniProtKB	Glycosylation	462	462	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P11655	UniProtKB	Beta strand	5	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	14	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	24	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	33	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	40	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Helix	54	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	58	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	75	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	82	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Helix	91	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	103	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Turn	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	114	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	133	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	145	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	155	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Turn	161	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	165	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	178	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	185	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	196	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Turn	201	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	206	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	217	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	229	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	242	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	253	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	269	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	280	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	290	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Turn	295	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	299	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	307	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	312	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	323	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Beta strand	331	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+P11655	UniProtKB	Turn	340	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I	
+##sequence-region P22224 1 910
+P22224	UniProtKB	Chain	1	910	.	.	.	ID=PRO_0000118959;Note=Exocyst complex component SEC15	
+P22224	UniProtKB	Coiled coil	88	116	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22224	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P30619 1 724
+P30619	UniProtKB	Chain	1	724	.	.	.	ID=PRO_0000206297;Note=Protein transport protein SEC1	
+##sequence-region P22214 1 214
+P22214	UniProtKB	Chain	1	214	.	.	.	ID=PRO_0000206769;Note=Protein transport protein SEC22	
+P22214	UniProtKB	Topological domain	1	192	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22214	UniProtKB	Transmembrane	193	213	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22214	UniProtKB	Topological domain	214	214	.	.	.	Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22214	UniProtKB	Domain	6	117	.	.	.	Note=Longin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00231	
+P22214	UniProtKB	Domain	132	192	.	.	.	Note=v-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00290	
+P22214	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P07560 1 215
+P07560	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000121330;Note=Ras-related protein SEC4	
+P07560	UniProtKB	Nucleotide binding	27	34	.	.	.	Note=GTP	
+P07560	UniProtKB	Nucleotide binding	75	79	.	.	.	Note=GTP	
+P07560	UniProtKB	Nucleotide binding	133	136	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07560	UniProtKB	Motif	49	57	.	.	.	Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07560	UniProtKB	Modified residue	201	201	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P07560	UniProtKB	Modified residue	204	204	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P07560	UniProtKB	Lipidation	214	214	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07560	UniProtKB	Lipidation	215	215	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07560	UniProtKB	Beta strand	20	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EQB	
+P07560	UniProtKB	Helix	33	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Beta strand	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EQB	
+P07560	UniProtKB	Helix	49	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z8Y	
+P07560	UniProtKB	Beta strand	57	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Beta strand	68	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Helix	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Helix	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z8Y	
+P07560	UniProtKB	Helix	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Beta strand	93	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Helix	105	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Helix	111	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Turn	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPH	
+P07560	UniProtKB	Beta strand	127	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EQB	
+P07560	UniProtKB	Helix	144	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Beta strand	158	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Turn	163	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Helix	169	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16	
+P07560	UniProtKB	Turn	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EQB	
+##sequence-region P11075 1 2009
+P11075	UniProtKB	Chain	1	2009	.	.	.	ID=PRO_0000120214;Note=Protein transport protein SEC7	
+P11075	UniProtKB	Domain	824	1010	.	.	.	Note=SEC7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00189	
+P11075	UniProtKB	Compositional bias	89	213	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P11075	UniProtKB	Modified residue	212	212	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+P11075	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P11075	UniProtKB	Modified residue	334	334	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P11075	UniProtKB	Modified residue	447	447	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P11075	UniProtKB	Modified residue	452	452	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P11075	UniProtKB	Modified residue	455	455	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P11075	UniProtKB	Modified residue	807	807	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P11075	UniProtKB	Modified residue	1226	1226	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P11075	UniProtKB	Modified residue	1240	1240	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P11075	UniProtKB	Modified residue	1741	1741	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P11075	UniProtKB	Modified residue	1752	1752	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P11075	UniProtKB	Cross-link	797	797	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P11075	UniProtKB	Sequence conflict	188	188	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11075	UniProtKB	Sequence conflict	399	400	.	.	.	Note=FV->LL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11075	UniProtKB	Sequence conflict	402	402	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11075	UniProtKB	Sequence conflict	1031	1034	.	.	.	Note=QQSA->PAIC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11075	UniProtKB	Sequence conflict	1036	1037	.	.	.	Note=NF->QL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11075	UniProtKB	Helix	830	840	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Helix	842	851	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Beta strand	854	856	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Helix	860	869	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Helix	875	883	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Helix	887	898	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Helix	907	915	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Helix	924	941	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Helix	949	967	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Beta strand	970	972	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Helix	977	983	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Turn	984	987	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+P11075	UniProtKB	Helix	995	1007	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY	
+##sequence-region P32855 1 1065
+P32855	UniProtKB	Chain	1	1065	.	.	.	ID=PRO_0000118942;Note=Exocyst complex component SEC8	
+P32855	UniProtKB	Coiled coil	114	148	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32855	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32855	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P40316 1 373
+P40316	UniProtKB	Chain	1	373	.	.	.	ID=PRO_0000206366;Note=Securin	
+P40316	UniProtKB	Motif	85	88	.	.	.	Note=D-box	
+P40316	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40316	UniProtKB	Modified residue	186	186	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40316	UniProtKB	Modified residue	212	212	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40316	UniProtKB	Modified residue	213	213	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40316	UniProtKB	Modified residue	277	277	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40316	UniProtKB	Modified residue	292	292	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12050115;Dbxref=PMID:12050115	
+P40316	UniProtKB	Mutagenesis	85	88	.	.	.	Note=Abolishes ubiquitination and subsequent degradation. RLPL->ALPA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8985178;Dbxref=PMID:8985178	
+P40316	UniProtKB	Mutagenesis	277	277	.	.	.	Note=Affects phosphorylation and the interaction with ESP1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12050115;Dbxref=PMID:12050115	
+P40316	UniProtKB	Mutagenesis	292	292	.	.	.	Note=Affects phosphorylation and the interaction with ESP1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12050115;Dbxref=PMID:12050115	
+P40316	UniProtKB	Mutagenesis	304	304	.	.	.	Note=No effect. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12050115;Dbxref=PMID:12050115	
+P40316	UniProtKB	Helix	273	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+P40316	UniProtKB	Helix	281	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+P40316	UniProtKB	Helix	365	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T	
+##sequence-region P25365 1 1065
+P25365	UniProtKB	Chain	1	1065	.	.	.	ID=PRO_0000051211;Note=Putative guanine nucleotide-exchange factor SED4	
+P25365	UniProtKB	Topological domain	1	346	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25365	UniProtKB	Transmembrane	347	365	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P25365	UniProtKB	Topological domain	366	1065	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25365	UniProtKB	Repeat	259	298	.	.	.	Note=WD 1	
+P25365	UniProtKB	Repeat	302	341	.	.	.	Note=WD 2	
+P25365	UniProtKB	Repeat	824	833	.	.	.	Note=1	
+P25365	UniProtKB	Repeat	834	843	.	.	.	Note=2	
+P25365	UniProtKB	Repeat	844	853	.	.	.	Note=3	
+P25365	UniProtKB	Repeat	854	863	.	.	.	Note=4	
+P25365	UniProtKB	Region	824	863	.	.	.	Note=4 X 10 AA tandem repeats	
+P25365	UniProtKB	Motif	1062	1065	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138	
+P25365	UniProtKB	Compositional bias	467	476	.	.	.	Note=Poly-Ser	
+P25365	UniProtKB	Compositional bias	579	590	.	.	.	Note=Poly-Ser	
+P25365	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25365	UniProtKB	Glycosylation	388	388	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25365	UniProtKB	Glycosylation	620	620	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25365	UniProtKB	Glycosylation	1039	1039	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39707 1 275
+P39707	UniProtKB	Chain	1	275	.	.	.	ID=PRO_0000109468;Note=tRNA-splicing endonuclease subunit SEN34	
+P39707	UniProtKB	Active site	209	209	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39707	UniProtKB	Active site	217	217	.	.	.	.	
+P39707	UniProtKB	Active site	250	250	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39707	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Loss of function%3B induces a marked accumulation of 5' exon and intron-3' exon 2/3 molecule. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9200603;Dbxref=PMID:9200603	
+##sequence-region P40054 1 469
+P40054	UniProtKB	Chain	1	469	.	.	.	ID=PRO_0000076018;Note=D-3-phosphoglycerate dehydrogenase 1	
+P40054	UniProtKB	Domain	399	469	.	.	.	Note=ACT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007	
+P40054	UniProtKB	Nucleotide binding	208	209	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0	
+P40054	UniProtKB	Nucleotide binding	285	287	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0	
+P40054	UniProtKB	Nucleotide binding	347	350	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0	
+P40054	UniProtKB	Active site	287	287	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40054	UniProtKB	Active site	316	316	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40054	UniProtKB	Active site	347	347	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40054	UniProtKB	Binding site	228	228	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0	
+P40054	UniProtKB	Binding site	311	311	.	.	.	Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0	
+P40054	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40054	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P40510	
+P40054	UniProtKB	Modified residue	33	33	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P40510	
+##sequence-region P42941 1 309
+P42941	UniProtKB	Chain	1	309	.	.	.	ID=PRO_0000156885;Note=Phosphoserine phosphatase	
+P42941	UniProtKB	Region	186	187	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42941	UniProtKB	Active site	97	97	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42941	UniProtKB	Active site	99	99	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42941	UniProtKB	Metal binding	97	97	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42941	UniProtKB	Metal binding	99	99	.	.	.	Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42941	UniProtKB	Metal binding	255	255	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42941	UniProtKB	Binding site	106	106	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42941	UniProtKB	Binding site	142	142	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42941	UniProtKB	Binding site	232	232	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P42941	UniProtKB	Binding site	258	258	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P36124 1 751
+P36124	UniProtKB	Chain	1	751	.	.	.	ID=PRO_0000097696;Note=SET domain-containing protein 3	
+P36124	UniProtKB	Domain	313	456	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+P36124	UniProtKB	Zinc finger	117	166	.	.	.	Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+P36124	UniProtKB	Modified residue	236	236	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36124	UniProtKB	Modified residue	684	684	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36124	UniProtKB	Modified residue	718	718	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36124	UniProtKB	Modified residue	719	719	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36124	UniProtKB	Modified residue	741	741	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36124	UniProtKB	Beta strand	129	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR	
+P36124	UniProtKB	Turn	135	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR	
+P36124	UniProtKB	Beta strand	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR	
+P36124	UniProtKB	Helix	143	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR	
+P36124	UniProtKB	Helix	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR	
+P36124	UniProtKB	Turn	161	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR	
+P36124	UniProtKB	Helix	170	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR	
+##sequence-region Q12529 1 373
+Q12529	UniProtKB	Chain	1	373	.	.	.	ID=PRO_0000269653;Note=Potential protein lysine methyltransferase SET6	
+Q12529	UniProtKB	Domain	12	338	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+##sequence-region Q12314 1 213
+Q12314	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000237643;Note=Protein arginine N-methyltransferase SFM1	
+Q12314	UniProtKB	Modified residue	204	204	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12314	UniProtKB	Modified residue	207	207	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q12314	UniProtKB	Beta strand	2	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Beta strand	9	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Helix	14	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Helix	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Beta strand	32	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Helix	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Helix	48	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Helix	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Helix	65	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Beta strand	79	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Beta strand	88	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Helix	93	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Beta strand	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Turn	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C74	
+Q12314	UniProtKB	Helix	118	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Turn	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Beta strand	128	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Helix	140	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Helix	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Beta strand	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Beta strand	167	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Beta strand	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Beta strand	180	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+Q12314	UniProtKB	Helix	196	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F	
+##sequence-region P53313 1 767
+P53313	UniProtKB	Chain	1	767	.	.	.	ID=PRO_0000202858;Note=Protein SDA1	
+P53313	UniProtKB	Compositional bias	555	628	.	.	.	Note=Asp-rich	
+P53313	UniProtKB	Modified residue	278	278	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P33421 1 198
+P33421	UniProtKB	Transit peptide	1	50	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8195189;Dbxref=PMID:8195189	
+P33421	UniProtKB	Chain	51	198	.	.	.	ID=PRO_0000003638;Note=Succinate dehydrogenase [ubiquinone] cytochrome b subunit%2C mitochondrial	
+P33421	UniProtKB	Topological domain	51	99	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33421	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33421	UniProtKB	Topological domain	121	139	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33421	UniProtKB	Transmembrane	140	160	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33421	UniProtKB	Topological domain	161	175	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33421	UniProtKB	Transmembrane	176	196	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33421	UniProtKB	Topological domain	197	198	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33421	UniProtKB	Metal binding	156	156	.	.	.	Note=Iron (heme axial ligand)%3B shared with second transmembrane subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33421	UniProtKB	Binding site	93	93	.	.	.	Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33421	UniProtKB	Binding site	97	97	.	.	.	Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33421	UniProtKB	Mutagenesis	96	96	.	.	.	Note=Decreases quinone reductase activity. H->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14672930;Dbxref=PMID:14672930	
+P33421	UniProtKB	Mutagenesis	153	153	.	.	.	Note=Decreases quinone reductase activity. Little effect on complex assembly. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10446163;Dbxref=PMID:10446163	
+P33421	UniProtKB	Mutagenesis	156	156	.	.	.	Note=Decreases SDH cytochrome b content. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14672930;Dbxref=PMID:14672930	
+P33421	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Decreases quinone reductase activity. Little effect on complex assembly. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10446163;Dbxref=PMID:10446163	
+P33421	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Decreases quinone reductase activity. Little effect on complex assembly. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10446163;Dbxref=PMID:10446163	
+P33421	UniProtKB	Mutagenesis	167	167	.	.	.	Note=Reduces SDH FAD content. Probably impairs complex assembly. D->V	
+P33421	UniProtKB	Sequence conflict	10	10	.	.	.	Note=L->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32602 1 292
+P32602	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378	
+P32602	UniProtKB	Chain	2	292	.	.	.	ID=PRO_0000219076;Note=Alpha-soluble NSF attachment protein	
+P32602	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378	
+P32602	UniProtKB	Cross-link	261	261	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32602	UniProtKB	Sequence conflict	103	103	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32602	UniProtKB	Sequence conflict	219	219	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32602	UniProtKB	Helix	4	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	21	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	30	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	54	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	73	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	93	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	113	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	134	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	154	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	174	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Turn	192	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	195	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	198	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	215	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	238	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Turn	253	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	256	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+P32602	UniProtKB	Helix	271	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE	
+##sequence-region P40482 1 926
+P40482	UniProtKB	Chain	1	926	.	.	.	ID=PRO_0000205150;Note=Protein transport protein SEC24	
+P40482	UniProtKB	Region	231	256	.	.	.	Note=Zinc finger-like	
+P40482	UniProtKB	Compositional bias	110	114	.	.	.	Note=Poly-Gln	
+P40482	UniProtKB	Compositional bias	157	160	.	.	.	Note=Poly-Pro	
+P40482	UniProtKB	Metal binding	231	231	.	.	.	Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12239560,ECO:0000269|PubMed:12941276;Dbxref=PMID:12239560,PMID:12941276	
+P40482	UniProtKB	Metal binding	234	234	.	.	.	Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12239560,ECO:0000269|PubMed:12941276;Dbxref=PMID:12239560,PMID:12941276	
+P40482	UniProtKB	Metal binding	253	253	.	.	.	Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12239560,ECO:0000269|PubMed:12941276;Dbxref=PMID:12239560,PMID:12941276	
+P40482	UniProtKB	Metal binding	256	256	.	.	.	Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12239560,ECO:0000269|PubMed:12941276;Dbxref=PMID:12239560,PMID:12941276	
+P40482	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40482	UniProtKB	Mutagenesis	230	230	.	.	.	Note=Abolishes binding to and packaging of cargo protein BET1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941277;Dbxref=PMID:12941277	
+P40482	UniProtKB	Mutagenesis	231	231	.	.	.	Note=Lethal. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10097109;Dbxref=PMID:10097109	
+P40482	UniProtKB	Mutagenesis	235	235	.	.	.	Note=Abolishes binding to and packaging of cargo protein BET1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941277;Dbxref=PMID:12941277	
+P40482	UniProtKB	Mutagenesis	559	559	.	.	.	Note=Abolishes binding to and packaging of cargo protein BET1. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941277;Dbxref=PMID:12941277	
+P40482	UniProtKB	Mutagenesis	561	561	.	.	.	Note=Abolishes binding to and packaging of cargo protein BET1. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941277;Dbxref=PMID:12941277	
+P40482	UniProtKB	Mutagenesis	616	616	.	.	.	Note=Abolishes binding to and packaging of cargo protein BET1. L->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941277;Dbxref=PMID:12941277	
+P40482	UniProtKB	Helix	64	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V	
+P40482	UniProtKB	Beta strand	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	151	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	165	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	173	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	182	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	193	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	232	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	243	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	246	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	254	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	259	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	264	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	277	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	281	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	286	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	294	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	305	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	314	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	321	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	333	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	344	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	374	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	390	392	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	393	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	396	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	400	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	414	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	424	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	436	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	440	448	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	471	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V	
+P40482	UniProtKB	Helix	482	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	495	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	509	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	518	520	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	523	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	534	549	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	554	562	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	566	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	578	587	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	594	600	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	606	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	620	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V	
+P40482	UniProtKB	Beta strand	624	637	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	639	644	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	648	665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	668	689	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	696	699	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V	
+P40482	UniProtKB	Beta strand	702	704	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	705	707	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	710	718	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	721	723	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	730	742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	745	752	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	755	758	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Turn	759	761	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V	
+P40482	UniProtKB	Helix	791	793	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PD0	
+P40482	UniProtKB	Beta strand	799	803	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	805	812	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	818	825	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	830	832	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	847	860	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Beta strand	870	875	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	885	899	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+P40482	UniProtKB	Helix	913	923	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX	
+##sequence-region P32844 1 805
+P32844	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32844	UniProtKB	Chain	2	805	.	.	.	ID=PRO_0000118931;Note=Exocyst complex component SEC6	
+P32844	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32844	UniProtKB	Sequence conflict	1	91	.	.	.	Note=MSSDPLQQVCDLIKGDLSLERVRDIKEQLLKEKSVVEYQLNKESDKYYGEVEESLKLLNLSKNSVTSIKQQINEVNKLGNDNRFAINRYDI->MKLINWVMIIDLQLIVMIY;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32844	UniProtKB	Sequence conflict	501	501	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32844	UniProtKB	Sequence conflict	627	628	.	.	.	Note=QQ->HE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32844	UniProtKB	Helix	412	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	463	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	485	522	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Turn	523	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	527	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Turn	533	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	541	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	572	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	586	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	609	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Turn	613	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	618	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	625	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	641	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	646	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	667	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	677	679	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	680	699	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Turn	700	702	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	706	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	728	730	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	731	739	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	748	754	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	762	785	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+P32844	UniProtKB	Helix	794	797	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI	
+##sequence-region P34250 1 1132
+P34250	UniProtKB	Chain	1	1132	.	.	.	ID=PRO_0000203159;Note=Eisosome protein SEG2	
+P34250	UniProtKB	Compositional bias	594	643	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P34250	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34250	UniProtKB	Modified residue	280	280	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34250	UniProtKB	Modified residue	504	504	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34250	UniProtKB	Modified residue	507	507	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34250	UniProtKB	Modified residue	556	556	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34250	UniProtKB	Modified residue	980	980	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34250	UniProtKB	Modified residue	1022	1022	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34250	UniProtKB	Cross-link	526	526	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P34250	UniProtKB	Cross-link	743	743	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P49955 1 971
+P49955	UniProtKB	Chain	1	971	.	.	.	ID=PRO_0000174327;Note=U2 snRNP component HSH155	
+P49955	UniProtKB	Repeat	199	237	.	.	.	Note=HEAT 1	
+P49955	UniProtKB	Repeat	273	310	.	.	.	Note=HEAT 2	
+P49955	UniProtKB	Repeat	350	387	.	.	.	Note=HEAT 3	
+P49955	UniProtKB	Repeat	513	550	.	.	.	Note=HEAT 4	
+P49955	UniProtKB	Repeat	596	633	.	.	.	Note=HEAT 5	
+P49955	UniProtKB	Repeat	680	717	.	.	.	Note=HEAT 6	
+P49955	UniProtKB	Repeat	722	759	.	.	.	Note=HEAT 7	
+P49955	UniProtKB	Repeat	792	829	.	.	.	Note=HEAT 8	
+P49955	UniProtKB	Repeat	832	870	.	.	.	Note=HEAT 9	
+##sequence-region Q03067 1 99
+Q03067	UniProtKB	Chain	1	99	.	.	.	ID=PRO_0000227805;Note=SAGA-associated factor 11	
+Q03067	UniProtKB	Zinc finger	71	92	.	.	.	Note=SGF11-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03047	
+Q03067	UniProtKB	Mutagenesis	15	15	.	.	.	Note=Moerately decreases the affinity of SGF11 for SUS1. I->A	
+Q03067	UniProtKB	Mutagenesis	18	18	.	.	.	Note=Causes a dramatic decrease in the affinity of SGF11 for SUS1. N->NA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20007317;Dbxref=PMID:20007317	
+Q03067	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Causes a dramatic decrease in the affinity of SGF11 for SUS1. L->LA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20007317;Dbxref=PMID:20007317	
+Q03067	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Reduces deubiquitination activity of the SAGA DUB module%3B when associated with A-60. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206	
+Q03067	UniProtKB	Mutagenesis	60	60	.	.	.	Note=Reduces deubiquitination activity of the SAGA DUB module%3B when associated with A-57. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206	
+Q03067	UniProtKB	Mutagenesis	84	84	.	.	.	Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206	
+Q03067	UniProtKB	Mutagenesis	85	85	.	.	.	Note=Strongly reduces deubiquitination activity of the SAGA DUB module. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206	
+Q03067	UniProtKB	Mutagenesis	86	86	.	.	.	Note=Moderately impairs deubiquitination activity of the SAGA DUB module. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206	
+Q03067	UniProtKB	Mutagenesis	89	89	.	.	.	Note=Strongly reduces deubiquitination activity of the SAGA DUB module. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206	
+Q03067	UniProtKB	Mutagenesis	91	91	.	.	.	Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206	
+Q03067	UniProtKB	Helix	8	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+Q03067	UniProtKB	Helix	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FK5	
+Q03067	UniProtKB	Beta strand	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+Q03067	UniProtKB	Turn	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+Q03067	UniProtKB	Beta strand	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+Q03067	UniProtKB	Helix	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+Q03067	UniProtKB	Helix	85	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+##sequence-region P53075 1 577
+P53075	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53075	UniProtKB	Chain	24	577	.	.	.	ID=PRO_0000202713;Note=Outer spore wall assembly protein SHE10	
+P53075	UniProtKB	Coiled coil	379	416	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53075	UniProtKB	Coiled coil	513	562	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36068 1 246
+P36068	UniProtKB	Chain	1	246	.	.	.	ID=PRO_0000203151;Note=SWI5-dependent HO expression protein 2	
+P36068	UniProtKB	Motif	15	23	.	.	.	Note=Nuclear localization signal	
+P36068	UniProtKB	Mutagenesis	36	36	.	.	.	Note=Prevents association with ASH1 and IST2 mRNAs and leads to their mislocalization. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888	
+P36068	UniProtKB	Mutagenesis	43	43	.	.	.	Note=Prevents association with ASH1 and mRNA and leads to its mislocalization. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888	
+P36068	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Prevents association with ASH1 and mRNA and leads to its mislocalization. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888	
+P36068	UniProtKB	Mutagenesis	49	49	.	.	.	Note=Prevents association with ASH1 and mRNA and leads to its mislocalization. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888	
+P36068	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Prevents association with ASH1 and mRNA and leads to its mislocalization. R->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888	
+P36068	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Prevents association with ASH1 and IST2 mRNAs and leads to their mislocalization. R->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888	
+P36068	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Prevents dimerization and RNA-binding. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15537539;Dbxref=PMID:15537539	
+P36068	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Prevents dimerization and RNA-binding. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15537539;Dbxref=PMID:15537539	
+P36068	UniProtKB	Mutagenesis	130	130	.	.	.	Note=Prevents tetramerization. L->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19710186;Dbxref=PMID:19710186	
+P36068	UniProtKB	Helix	13	42	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+P36068	UniProtKB	Helix	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+P36068	UniProtKB	Helix	49	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+P36068	UniProtKB	Helix	74	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+P36068	UniProtKB	Turn	86	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+P36068	UniProtKB	Helix	92	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+P36068	UniProtKB	Helix	120	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+P36068	UniProtKB	Helix	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+P36068	UniProtKB	Helix	138	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+P36068	UniProtKB	Helix	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+P36068	UniProtKB	Helix	172	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+P36068	UniProtKB	Helix	194	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNL	
+P36068	UniProtKB	Beta strand	197	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNL	
+P36068	UniProtKB	Helix	205	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY	
+##sequence-region P38272 1 425
+P38272	UniProtKB	Chain	1	425	.	.	.	ID=PRO_0000202490;Note=SWI5-dependent HO expression protein 3	
+P38272	UniProtKB	Coiled coil	68	197	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38272	UniProtKB	Compositional bias	377	381	.	.	.	Note=Poly-Ser	
+P38272	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38272	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38272	UniProtKB	Mutagenesis	343	343	.	.	.	Note=Prevents correct localization of ASH1 mRNA%3B when associated with E-361. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19429778;Dbxref=PMID:19429778	
+P38272	UniProtKB	Mutagenesis	348	348	.	.	.	Note=Prevents correct localization of ASH1 mRNA. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19429778;Dbxref=PMID:19429778	
+P38272	UniProtKB	Mutagenesis	361	361	.	.	.	Note=Prevents correct localization of ASH1 mRNA%3B when associated with E-343. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19429778;Dbxref=PMID:19429778	
+P38272	UniProtKB	Helix	44	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LL7	
+P38272	UniProtKB	Helix	74	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LL7	
+##sequence-region Q04172 1 456
+Q04172	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04172	UniProtKB	Chain	31	456	.	.	.	ID=PRO_0000022344;Note=Sensitive to high expression protein 9%2C mitochondrial	
+Q04172	UniProtKB	Topological domain	31	296	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04172	UniProtKB	Transmembrane	297	317	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04172	UniProtKB	Topological domain	318	435	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04172	UniProtKB	Transmembrane	436	456	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04172	UniProtKB	Coiled coil	71	128	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04172	UniProtKB	Coiled coil	178	277	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P35179 1 80
+P35179	UniProtKB	Chain	1	80	.	.	.	ID=PRO_0000104211;Note=Protein transport protein SSS1	
+P35179	UniProtKB	Topological domain	1	46	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35179	UniProtKB	Transmembrane	47	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35179	UniProtKB	Topological domain	76	80	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35179	UniProtKB	Sequence conflict	58	58	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q6Q595 1 175
+Q6Q595	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000213468;Note=Vesicle-associated membrane protein-associated protein SCS22	
+Q6Q595	UniProtKB	Topological domain	1	154	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6Q595	UniProtKB	Transmembrane	155	175	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q6Q595	UniProtKB	Domain	1	125	.	.	.	Note=MSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00132	
+Q6Q595	UniProtKB	Sequence conflict	169	169	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53012 1 380
+P53012	UniProtKB	Chain	1	380	.	.	.	ID=PRO_0000097635;Note=FIT family protein SCS3	
+P53012	UniProtKB	Topological domain	1	7	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Topological domain	29	43	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Transmembrane	44	64	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Topological domain	65	88	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Transmembrane	89	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Topological domain	110	233	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Transmembrane	234	254	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Topological domain	255	325	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Transmembrane	326	346	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Topological domain	347	356	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Transmembrane	357	377	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Topological domain	378	380	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53012	UniProtKB	Sequence conflict	240	240	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53189 1 542
+P53189	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53189	UniProtKB	Chain	21	542	.	.	.	ID=PRO_0000011903;Note=Probable family 17 glucosidase SCW11	
+P53189	UniProtKB	Compositional bias	31	303	.	.	.	Note=Ser/Thr-rich	
+P53189	UniProtKB	Active site	478	478	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53189	UniProtKB	Active site	532	532	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P53334 1 386
+P53334	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53334	UniProtKB	Propeptide	20	30	.	.	.	ID=PRO_0000011899;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9748433;Dbxref=PMID:9748433	
+P53334	UniProtKB	Chain	31	386	.	.	.	ID=PRO_0000011900;Note=Probable family 17 glucosidase SCW4	
+P53334	UniProtKB	Compositional bias	71	155	.	.	.	Note=Ser-rich	
+P53334	UniProtKB	Active site	323	323	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53334	UniProtKB	Active site	377	377	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53334	UniProtKB	Glycosylation	89	89	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53334	UniProtKB	Sequence conflict	35	35	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53334	UniProtKB	Sequence conflict	40	40	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53009 1 804
+P53009	UniProtKB	Chain	1	804	.	.	.	ID=PRO_0000097636;Note=Protein kinase-like protein SCY1	
+P53009	UniProtKB	Domain	1	324	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53009	UniProtKB	Compositional bias	36	43	.	.	.	Note=Poly-Ser	
+##sequence-region Q06058 1 285
+Q06058	UniProtKB	Chain	1	285	.	.	.	ID=PRO_0000247216;Note=Seipin	
+Q06058	UniProtKB	Topological domain	1	16	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258	
+Q06058	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06058	UniProtKB	Topological domain	38	244	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258	
+Q06058	UniProtKB	Transmembrane	245	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06058	UniProtKB	Topological domain	266	285	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12524434,ECO:0000269|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258	
+##sequence-region P39709 1 593
+P39709	UniProtKB	Chain	1	593	.	.	.	ID=PRO_0000121368;Note=Probable transporter SEO1	
+P39709	UniProtKB	Topological domain	1	130	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	152	175	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	176	196	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	197	200	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	201	221	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	222	234	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	235	255	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	256	265	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	266	286	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	287	302	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	303	323	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	324	363	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	364	384	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	385	411	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	412	432	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	433	438	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	439	459	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	460	466	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	467	487	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	488	499	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	500	520	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	521	532	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Transmembrane	533	553	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39709	UniProtKB	Topological domain	554	593	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P33330 1 395
+P33330	UniProtKB	Chain	1	395	.	.	.	ID=PRO_0000150141;Note=Phosphoserine aminotransferase	
+P33330	UniProtKB	Region	80	81	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33330	UniProtKB	Region	271	272	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33330	UniProtKB	Binding site	46	46	.	.	.	Note=L-glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33330	UniProtKB	Binding site	113	113	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33330	UniProtKB	Binding site	170	170	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33330	UniProtKB	Binding site	194	194	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33330	UniProtKB	Binding site	217	217	.	.	.	Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33330	UniProtKB	Modified residue	20	20	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P33330	UniProtKB	Modified residue	112	112	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P33330	UniProtKB	Modified residue	218	218	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33330	UniProtKB	Sequence conflict	258	259	.	.	.	Note=FD->LH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38827 1 1080
+P38827	UniProtKB	Chain	1	1080	.	.	.	ID=PRO_0000186086;Note=Histone-lysine N-methyltransferase%2C H3 lysine-4 specific	
+P38827	UniProtKB	Domain	938	1055	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+P38827	UniProtKB	Domain	1064	1080	.	.	.	Note=Post-SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00155	
+P38827	UniProtKB	Modified residue	625	625	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P38827	UniProtKB	Modified residue	875	875	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38827	UniProtKB	Beta strand	249	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A	
+P38827	UniProtKB	Helix	265	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A	
+P38827	UniProtKB	Beta strand	279	285	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A	
+P38827	UniProtKB	Turn	287	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A	
+P38827	UniProtKB	Beta strand	292	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A	
+P38827	UniProtKB	Helix	310	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A	
+P38827	UniProtKB	Turn	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A	
+P38827	UniProtKB	Beta strand	326	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A	
+P38827	UniProtKB	Beta strand	331	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A	
+P38827	UniProtKB	Helix	342	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A	
+##sequence-region Q12369 1 946
+Q12369	UniProtKB	Chain	1	946	.	.	.	ID=PRO_0000269647;Note=Protein SFI1	
+Q12369	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12369	UniProtKB	Modified residue	855	855	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q12369	UniProtKB	Helix	222	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DOQ	
+Q12369	UniProtKB	Helix	241	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DOQ	
+Q12369	UniProtKB	Helix	247	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DOQ	
+Q12369	UniProtKB	Helix	643	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GV5	
+Q12369	UniProtKB	Helix	677	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GV5	
+Q12369	UniProtKB	Turn	707	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GV5	
+##sequence-region P35735 1 353
+P35735	UniProtKB	Chain	1	353	.	.	.	ID=PRO_0000203179;Note=Protein SFK1	
+P35735	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Topological domain	33	62	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Topological domain	84	130	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Transmembrane	131	151	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Topological domain	152	160	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Topological domain	182	231	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Transmembrane	232	253	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Topological domain	254	263	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Transmembrane	264	284	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Topological domain	285	353	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P35735	UniProtKB	Modified residue	208	208	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P20134 1 766
+P20134	UniProtKB	Chain	1	766	.	.	.	ID=PRO_0000124595;Note=Flocculation suppression protein	
+P20134	UniProtKB	DNA binding	64	186	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20134	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P20134	UniProtKB	Modified residue	556	556	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P20134	UniProtKB	Modified residue	733	733	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P20134	UniProtKB	Sequence conflict	446	454	.	.	.	Note=FVQYQPQSQ->LYNTNRSRN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20134	UniProtKB	Sequence conflict	446	454	.	.	.	Note=FVQYQPQSQ->LYNTNRSRN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20134	UniProtKB	Sequence conflict	461	462	.	.	.	Note=KQ->SE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P20134	UniProtKB	Sequence conflict	461	462	.	.	.	Note=KQ->SE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12234 1 484
+Q12234	UniProtKB	Chain	1	484	.	.	.	ID=PRO_0000268739;Note=GRIP domain-containing protein RUD3	
+Q12234	UniProtKB	Domain	401	452	.	.	.	Note=GRIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00250	
+Q12234	UniProtKB	Coiled coil	84	383	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12234	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12234	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12234	UniProtKB	Modified residue	468	468	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+##sequence-region Q07458 1 294
+Q07458	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q07458	UniProtKB	Chain	2	294	.	.	.	ID=PRO_0000234080;Note=Transcriptional regulatory protein RXT3	
+Q07458	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P34218 1 831
+P34218	UniProtKB	Chain	1	831	.	.	.	ID=PRO_0000051579;Note=Histone acetyltransferase SAS3	
+P34218	UniProtKB	Domain	267	573	.	.	.	Note=MYST-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063	
+P34218	UniProtKB	Zinc finger	300	325	.	.	.	Note=C2HC MYST-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063	
+P34218	UniProtKB	Region	419	421	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6	
+P34218	UniProtKB	Region	426	432	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6	
+P34218	UniProtKB	Compositional bias	736	831	.	.	.	Note=Asp/Glu-rich (acidic)	
+P34218	UniProtKB	Active site	452	452	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6	
+P34218	UniProtKB	Binding site	456	456	.	.	.	Note=Acetyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6	
+P34218	UniProtKB	Modified residue	367	367	.	.	.	Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6	
+P34218	UniProtKB	Mutagenesis	303	303	.	.	.	Note=Greatly diminishes HAT activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10600516,ECO:0000269|PubMed:10817755;Dbxref=PMID:10600516,PMID:10817755	
+P34218	UniProtKB	Mutagenesis	306	306	.	.	.	Note=Greatly diminishes HAT activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10600516,ECO:0000269|PubMed:10817755;Dbxref=PMID:10600516,PMID:10817755	
+P34218	UniProtKB	Mutagenesis	319	319	.	.	.	Note=Greatly diminishes HAT activity. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10600516,ECO:0000269|PubMed:10817755;Dbxref=PMID:10600516,PMID:10817755	
+P34218	UniProtKB	Mutagenesis	323	323	.	.	.	Note=Abolishes HAT activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10600516,ECO:0000269|PubMed:10817755;Dbxref=PMID:10600516,PMID:10817755	
+P34218	UniProtKB	Mutagenesis	426	427	.	.	.	Note=Loss of function. QR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10817755;Dbxref=PMID:10817755	
+P34218	UniProtKB	Mutagenesis	429	431	.	.	.	Note=Loss of function. GYG->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10817755;Dbxref=PMID:10817755	
+P34218	UniProtKB	Mutagenesis	434	435	.	.	.	Note=No effect. LM->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10817755;Dbxref=PMID:10817755	
+##sequence-region P40963 1 338
+P40963	UniProtKB	Chain	1	338	.	.	.	ID=PRO_0000051578;Note=Histone acetyltransferase SAS2	
+P40963	UniProtKB	Domain	45	338	.	.	.	Note=MYST-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063	
+P40963	UniProtKB	Zinc finger	100	126	.	.	.	Note=C2HC MYST-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063	
+P40963	UniProtKB	Region	209	211	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6	
+P40963	UniProtKB	Region	216	222	.	.	.	Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6	
+P40963	UniProtKB	Active site	242	242	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6	
+P40963	UniProtKB	Binding site	246	246	.	.	.	Note=Acetyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6	
+P40963	UniProtKB	Binding site	323	323	.	.	.	Note=Acetyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6	
+P40963	UniProtKB	Modified residue	168	168	.	.	.	Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:22020126;Dbxref=PMID:22020126	
+P40963	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Loss of function. C->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11731479,ECO:0000269|PubMed:11731480;Dbxref=PMID:11731479,PMID:11731480	
+P40963	UniProtKB	Mutagenesis	168	168	.	.	.	Note=Abolishes catalytic activity. K->A%2CQ%2CR	
+P40963	UniProtKB	Mutagenesis	213	214	.	.	.	Note=Loss of function. PP->AV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11731480;Dbxref=PMID:11731480	
+P40963	UniProtKB	Mutagenesis	216	217	.	.	.	Note=Abolishes silencing activity. QR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11731479;Dbxref=PMID:11731479	
+P40963	UniProtKB	Mutagenesis	219	221	.	.	.	Note=Does not affect silencing activity. GLG->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11731479;Dbxref=PMID:11731479	
+P40963	UniProtKB	Mutagenesis	224	225	.	.	.	Note=Does not affect silencing activity. LI->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11731479;Dbxref=PMID:11731479	
+##sequence-region P39735 1 261
+P39735	UniProtKB	Chain	1	261	.	.	.	ID=PRO_0000202414;Note=Single-strand annealing weakened protein 1	
+##sequence-region Q9ZZX1 1 630
+Q9ZZX1	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZX1	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZX1	UniProtKB	Transmembrane	101	121	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZX1	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZX1	UniProtKB	Transmembrane	182	202	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZX1	UniProtKB	Transmembrane	235	255	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZX1	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZX1	UniProtKB	Transmembrane	305	325	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZX1	UniProtKB	Transmembrane	417	437	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZX1	UniProtKB	Transmembrane	464	483	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZX1	UniProtKB	Region	1	324	.	.	.	Note=COX1 exons encoded;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q9ZZX1	UniProtKB	Region	325	630	.	.	.	Note=COX1 intron aI5_alpha encoded	
+Q9ZZX1	UniProtKB	Compositional bias	333	390	.	.	.	Note=Asn-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36048 1 1008
+P36048	UniProtKB	Chain	1	1008	.	.	.	ID=PRO_0000091565;Note=Pre-mRNA-splicing factor SNU114	
+P36048	UniProtKB	Domain	131	338	.	.	.	Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P36048	UniProtKB	Nucleotide binding	140	147	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36048	UniProtKB	Nucleotide binding	214	218	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36048	UniProtKB	Nucleotide binding	268	271	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36048	UniProtKB	Region	140	147	.	.	.	Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P36048	UniProtKB	Region	188	192	.	.	.	Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P36048	UniProtKB	Region	214	217	.	.	.	Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P36048	UniProtKB	Region	268	271	.	.	.	Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P36048	UniProtKB	Region	315	317	.	.	.	Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059	
+P36048	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36048	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P36048	UniProtKB	Turn	68	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	75	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Turn	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	110	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	120	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Turn	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	134	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	146	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	166	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	182	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	194	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	207	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	222	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	233	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Turn	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	247	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	262	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	271	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Turn	275	277	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	281	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	306	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	311	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Turn	316	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	324	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	332	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	338	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	341	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	349	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	356	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	362	364	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	372	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	378	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	393	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Turn	410	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	417	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	433	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	445	455	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	465	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	483	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	499	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	504	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	541	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	547	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	561	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	568	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	575	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	583	588	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	603	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	612	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	615	628	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	633	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	642	648	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	649	661	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	668	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	678	681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	708	714	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	717	723	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	737	739	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	744	755	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	759	764	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	772	776	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	779	783	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	785	803	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	807	810	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	815	823	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	833	836	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	838	851	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	855	869	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	870	872	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	873	883	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	887	893	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	897	908	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	909	911	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	914	921	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Turn	922	924	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	928	931	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	937	939	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Beta strand	953	955	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	959	961	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P36048	UniProtKB	Helix	963	974	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P10870 1 884
+P10870	UniProtKB	Chain	1	884	.	.	.	ID=PRO_0000050390;Note=High-affinity glucose transporter SNF3	
+P10870	UniProtKB	Topological domain	1	97	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	119	143	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	144	164	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	165	178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	200	202	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	203	223	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	224	229	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	230	250	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	251	264	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	265	285	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	286	358	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	359	379	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	380	391	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	392	412	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	413	419	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	420	440	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	441	451	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	452	472	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	473	488	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	489	509	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	510	521	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Transmembrane	522	542	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Topological domain	543	884	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Glycosylation	383	383	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P10870	UniProtKB	Mutagenesis	112	112	.	.	.	Note=In SNF3-142. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406560;Dbxref=PMID:2406560	
+P10870	UniProtKB	Mutagenesis	153	153	.	.	.	Note=In SNF3-72. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406560;Dbxref=PMID:2406560	
+P10870	UniProtKB	Mutagenesis	229	229	.	.	.	Note=In SNF3-1%3B constitutively signaling glucose receptor. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406560;Dbxref=PMID:2406560	
+P10870	UniProtKB	Mutagenesis	402	402	.	.	.	Note=In SNF3-39. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406560;Dbxref=PMID:2406560	
+##sequence-region P18888 1 332
+P18888	UniProtKB	Chain	1	332	.	.	.	ID=PRO_0000072006;Note=Transcription regulatory protein SNF6	
+P18888	UniProtKB	Motif	2	8	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18888	UniProtKB	Compositional bias	264	276	.	.	.	Note=Gln-rich	
+P18888	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P39929 1 240
+P39929	UniProtKB	Chain	1	240	.	.	.	ID=PRO_0000211446;Note=Vacuolar-sorting protein SNF7	
+P39929	UniProtKB	Compositional bias	68	71	.	.	.	Note=Poly-Lys	
+P39929	UniProtKB	Compositional bias	216	228	.	.	.	Note=Asp/Glu-rich (acidic)	
+P39929	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P39929	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39929	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39929	UniProtKB	Cross-link	229	229	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P39929	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Impairs binding to membrane. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24139821;Dbxref=PMID:24139821	
+P39929	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Impairs binding to membrane. F->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24139821;Dbxref=PMID:24139821	
+P39929	UniProtKB	Mutagenesis	8	8	.	.	.	Note=Impairs binding to membrane. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24139821;Dbxref=PMID:24139821	
+P39929	UniProtKB	Mutagenesis	25	25	.	.	.	Note=Leads to severe sorting defects%3B when associated with E-29 and E-36. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Leads to severe sorting defects%3B when associated with E-25 and E-36. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	36	36	.	.	.	Note=Leads to severe sorting defects%3B when associated with E-25 and E-29. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Impairs the formation of protofilaments%3B when associated with K-90. Also impairs the formation of protofilaments%3B when associated with E-94. Also impairs the formation of protofilaments%3B when associated with E-107. Also impairs the formation of protofilaments%3B when associated with E-114. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Leads to severe sorting defects. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Leads to severe sorting defects. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	90	90	.	.	.	Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	94	94	.	.	.	Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Leads to severe sorting defects%3B when associated with K-102 and K-109. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Leads to severe sorting defects. A->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Leads to severe sorting defects. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Leads to severe sorting defects. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Leads to severe sorting defects%3B when associated with K-95 and K-109. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Leads to severe sorting defects. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Leads to severe sorting defects. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	107	107	.	.	.	Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Leads to severe sorting defects%3B when associated with K-95 and K-102. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Leads to severe sorting defects. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Mutagenesis	121	121	.	.	.	Note=Leads to severe sorting defects. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
+P39929	UniProtKB	Sequence conflict	173	173	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39929	UniProtKB	Helix	19	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FD9	
+P39929	UniProtKB	Helix	60	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FD9	
+P39929	UniProtKB	Turn	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FD7	
+P39929	UniProtKB	Helix	127	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FD9	
+P39929	UniProtKB	Turn	139	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FD9	
+##sequence-region P00445 1 154
+P00445	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6993479,ECO:0000269|Ref.6,ECO:0000269|Ref.8;Dbxref=PMID:6993479	
+P00445	UniProtKB	Chain	2	154	.	.	.	ID=PRO_0000164129;Note=Superoxide dismutase [Cu-Zn]	
+P00445	UniProtKB	Metal binding	43	43	.	.	.	Note=Zinc 2%3B shared with CCS1%3B in apo form;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:11524675;Dbxref=PMID:10026301,PMID:11524675	
+P00445	UniProtKB	Metal binding	47	47	.	.	.	Note=Copper%3B catalytic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:8652572;Dbxref=PMID:10026301,PMID:8652572	
+P00445	UniProtKB	Metal binding	49	49	.	.	.	Note=Copper%3B catalytic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:8652572;Dbxref=PMID:10026301,PMID:8652572	
+P00445	UniProtKB	Metal binding	64	64	.	.	.	Note=Copper%3B catalytic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:8652572;Dbxref=PMID:10026301,PMID:8652572	
+P00445	UniProtKB	Metal binding	64	64	.	.	.	Note=Zinc 1%3B structural;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:11524675;Dbxref=PMID:10026301,PMID:11524675	
+P00445	UniProtKB	Metal binding	72	72	.	.	.	Note=Zinc 1%3B structural;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:11524675;Dbxref=PMID:10026301,PMID:11524675	
+P00445	UniProtKB	Metal binding	81	81	.	.	.	Note=Zinc 1%3B structural;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:11524675;Dbxref=PMID:10026301,PMID:11524675	
+P00445	UniProtKB	Metal binding	84	84	.	.	.	Note=Zinc 1%3B structural;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:11524675;Dbxref=PMID:10026301,PMID:11524675	
+P00445	UniProtKB	Metal binding	121	121	.	.	.	Note=Copper%3B catalytic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:8652572;Dbxref=PMID:10026301,PMID:8652572	
+P00445	UniProtKB	Binding site	144	144	.	.	.	Note=Substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00445	UniProtKB	Modified residue	26	26	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P00445	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198	
+P00445	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P00445	UniProtKB	Modified residue	117	117	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00445	UniProtKB	Modified residue	132	132	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P00445	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P00445	UniProtKB	Disulfide bond	58	147	.	.	.	.	
+P00445	UniProtKB	Disulfide bond	58	58	.	.	.	Note=Interchain (with C-229 in CCS1)%3B in linked form	
+P00445	UniProtKB	Cross-link	19	19	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219	
+P00445	UniProtKB	Cross-link	70	70	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219	
+P00445	UniProtKB	Mutagenesis	123	123	.	.	.	Note=Does not enable copper chaperone-independent activation. G->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15069187;Dbxref=PMID:15069187	
+P00445	UniProtKB	Mutagenesis	131	132	.	.	.	Note=Does not enable copper chaperone-independent activation. DT->GN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15069187;Dbxref=PMID:15069187	
+P00445	UniProtKB	Mutagenesis	143	143	.	.	.	Note=Enables copper chaperone-independent activation%3B when associated with A-145 or with L-145. P->A%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15069187,ECO:0000269|PubMed:16234242;Dbxref=PMID:15069187,PMID:16234242	
+P00445	UniProtKB	Mutagenesis	145	145	.	.	.	Note=Enables copper chaperone-independent activation%3B when associated with A-143 or with S-143. P->A%2CL;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15069187,ECO:0000269|PubMed:16234242;Dbxref=PMID:15069187,PMID:16234242	
+P00445	UniProtKB	Sequence conflict	56	56	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00445	UniProtKB	Sequence conflict	93	93	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00445	UniProtKB	Beta strand	3	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	11	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	15	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	23	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SDY	
+P00445	UniProtKB	Beta strand	29	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	43	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Turn	55	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Helix	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	84	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	96	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	116	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	130	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Helix	135	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+P00445	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G	
+##sequence-region Q05676 1 74
+##sequence-region Q06411 1 708
+Q06411	UniProtKB	Chain	1	708	.	.	.	ID=PRO_0000270560;Note=Pre-mRNA-splicing factor SPP382	
+Q06411	UniProtKB	Domain	61	108	.	.	.	Note=G-patch;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00092	
+##sequence-region Q03954 1 165
+Q03954	UniProtKB	Chain	1	165	.	.	.	ID=PRO_0000142593;Note=DASH complex subunit SPC19	
+Q03954	UniProtKB	Coiled coil	74	104	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03954	UniProtKB	Coiled coil	132	165	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03954	UniProtKB	Modified residue	107	107	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:19779198,PMID:12408861	
+Q03954	UniProtKB	Modified residue	116	116	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:18407956,PMID:19779198,PMID:12408861	
+##sequence-region Q03868 1 1245
+Q03868	UniProtKB	Chain	1	1245	.	.	.	ID=PRO_0000072140;Note=Sporulation-specific protein 71	
+Q03868	UniProtKB	Domain	1030	1229	.	.	.	Note=PH	
+##sequence-region Q06134 1 477
+Q06134	UniProtKB	Chain	1	477	.	.	.	ID=PRO_0000072144;Note=Sporulation-specific protein 77	
+##sequence-region P09937 1 338
+P09937	UniProtKB	Chain	1	338	.	.	.	ID=PRO_0000072154;Note=Sporulation-specific protein 4	
+P09937	UniProtKB	Sequence conflict	107	107	.	.	.	Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09937	UniProtKB	Sequence conflict	180	180	.	.	.	Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12455 1 300
+Q12455	UniProtKB	Chain	1	300	.	.	.	ID=PRO_0000156540;Note=Spermine synthase	
+Q12455	UniProtKB	Domain	12	255	.	.	.	Note=PABS	
+Q12455	UniProtKB	Region	151	152	.	.	.	Note=S-adenosylmethioninamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12455	UniProtKB	Active site	174	174	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12455	UniProtKB	Binding site	44	44	.	.	.	Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12455	UniProtKB	Binding site	99	99	.	.	.	Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12455	UniProtKB	Binding site	119	119	.	.	.	Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12455	UniProtKB	Binding site	177	177	.	.	.	Note=Spermidine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12455	UniProtKB	Modified residue	5	5	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P06843 1 333
+P06843	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P06843	UniProtKB	Chain	2	333	.	.	.	ID=PRO_0000072163;Note=Protein SPT2	
+P06843	UniProtKB	Region	259	333	.	.	.	Note=Important for interaction with histones;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26109053;Dbxref=PMID:26109053	
+P06843	UniProtKB	Coiled coil	218	242	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06843	UniProtKB	Coiled coil	292	316	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06843	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P06843	UniProtKB	Modified residue	126	126	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P06843	UniProtKB	Mutagenesis	289	290	.	.	.	Note=Strongly reduces histone binding. ME->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26109053;Dbxref=PMID:26109053	
+P06843	UniProtKB	Mutagenesis	299	300	.	.	.	Note=Strongly reduces histone binding. EE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26109053;Dbxref=PMID:26109053	
+P06843	UniProtKB	Mutagenesis	310	311	.	.	.	Note=Strongly reduces histone binding. ED->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26109053;Dbxref=PMID:26109053	
+##sequence-region P35177 1 1332
+P35177	UniProtKB	Chain	1	1332	.	.	.	ID=PRO_0000211214;Note=Transcriptional activator SPT7	
+P35177	UniProtKB	Domain	458	528	.	.	.	Note=Bromo;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+P35177	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphothreonine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P35177	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P35177	UniProtKB	Modified residue	1293	1293	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38985 1 146
+P38985	UniProtKB	Chain	1	146	.	.	.	ID=PRO_0000135196;Note=Signal recognition particle subunit SRP14	
+P38985	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32342 1 167
+P32342	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:7925282;Dbxref=PMID:22814378,PMID:7925282	
+P32342	UniProtKB	Chain	2	167	.	.	.	ID=PRO_0000135239;Note=Signal recognition particle subunit SRP21	
+P32342	UniProtKB	Compositional bias	155	167	.	.	.	Note=Lys-rich (highly basic)	
+P32342	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:7925282;Dbxref=PMID:22814378,PMID:7925282	
+##sequence-region P38688 1 640
+P38688	UniProtKB	Chain	1	640	.	.	.	ID=PRO_0000135238;Note=Signal recognition particle subunit SRP72	
+P38688	UniProtKB	Repeat	188	221	.	.	.	Note=TPR	
+P38688	UniProtKB	Compositional bias	539	640	.	.	.	Note=Lys-rich	
+##sequence-region Q03529 1 384
+Q03529	UniProtKB	Chain	1	384	.	.	.	ID=PRO_0000185407;Note=Ceramide very long chain fatty acid hydroxylase SCS7	
+Q03529	UniProtKB	Topological domain	1	196	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03529	UniProtKB	Transmembrane	197	217	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03529	UniProtKB	Topological domain	218	222	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03529	UniProtKB	Transmembrane	223	243	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03529	UniProtKB	Topological domain	244	297	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03529	UniProtKB	Transmembrane	298	318	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03529	UniProtKB	Topological domain	319	352	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03529	UniProtKB	Transmembrane	353	373	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03529	UniProtKB	Topological domain	374	384	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03529	UniProtKB	Domain	9	90	.	.	.	Note=Cytochrome b5 heme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+Q03529	UniProtKB	Metal binding	45	45	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+Q03529	UniProtKB	Metal binding	72	72	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279	
+Q03529	UniProtKB	Helix	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	138	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	154	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	165	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	191	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	200	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	222	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Turn	247	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	251	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	258	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	269	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Beta strand	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	285	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	305	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	336	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Beta strand	353	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+Q03529	UniProtKB	Helix	363	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1	
+##sequence-region Q3E785 1 79
+Q3E785	UniProtKB	Chain	1	79	.	.	.	ID=PRO_0000253849;Note=Succinate dehydrogenase assembly factor 1%2C mitochondrial	
+Q3E785	UniProtKB	Mutagenesis	61	61	.	.	.	Note=Abolishes the ability to complement a yeast strain carrying a deletion for this gene. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19465911;Dbxref=PMID:19465911	
+Q3E785	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Abolishes the ability to complement a yeast strain carrying a deletion for this gene. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19465911;Dbxref=PMID:19465911	
+##sequence-region Q04401 1 133
+Q04401	UniProtKB	Transit peptide	1	12	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19837041;Dbxref=PMID:19837041	
+Q04401	UniProtKB	Chain	13	133	.	.	.	ID=PRO_0000042652;Note=Succinate dehydrogenase assembly factor 3%2C mitochondrial	
+Q04401	UniProtKB	Sequence conflict	13	13	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q04401	UniProtKB	Sequence conflict	17	17	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40505 1 327
+P40505	UniProtKB	Chain	1	327	.	.	.	ID=PRO_0000097654;Note=Transcriptional regulatory protein SDS3	
+P40505	UniProtKB	Coiled coil	61	135	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40505	UniProtKB	Modified residue	166	166	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40505	UniProtKB	Modified residue	211	211	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P15367 1 167
+P15367	UniProtKB	Chain	1	167	.	.	.	ID=PRO_0000109540;Note=Signal peptidase complex catalytic subunit SEC11	
+P15367	UniProtKB	Topological domain	1	9	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15367	UniProtKB	Transmembrane	10	31	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15367	UniProtKB	Topological domain	32	167	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15367	UniProtKB	Active site	44	44	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15367	UniProtKB	Glycosylation	121	121	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15367	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Nonviable. S->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957	
+P15367	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Nonviable%3B no protein expressed. H->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957	
+P15367	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Nonviable. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957	
+P15367	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Nonviable%3B no protein expressed. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957	
+P15367	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Nonviable. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957	
+P15367	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Nonviable. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957	
+P15367	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Nonviable%3B no protein expressed. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957	
+P15367	UniProtKB	Sequence conflict	162	162	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38810 1 929
+P38810	UniProtKB	Chain	1	929	.	.	.	ID=PRO_0000205152;Note=SED5-binding protein 3	
+P38810	UniProtKB	Region	220	244	.	.	.	Note=Zinc finger-like	
+P38810	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38810	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38810	UniProtKB	Modified residue	83	83	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38810	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38810	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38810	UniProtKB	Modified residue	101	101	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38810	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38810	UniProtKB	Modified residue	216	216	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P33303 1 322
+P33303	UniProtKB	Chain	1	322	.	.	.	ID=PRO_0000090679;Note=Succinate/fumarate mitochondrial transporter	
+P33303	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33303	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33303	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33303	UniProtKB	Transmembrane	177	193	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33303	UniProtKB	Transmembrane	219	235	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33303	UniProtKB	Transmembrane	278	295	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33303	UniProtKB	Repeat	8	99	.	.	.	Note=Solcar 1	
+P33303	UniProtKB	Repeat	111	202	.	.	.	Note=Solcar 2	
+P33303	UniProtKB	Repeat	212	303	.	.	.	Note=Solcar 3	
+P33303	UniProtKB	Sequence conflict	300	322	.	.	.	Note=VREHLENLGIFKKNDTPKPKPLK->RKGAFQKIWVYSRRMTHQSQSH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P51534 1 789
+P51534	UniProtKB	Chain	1	789	.	.	.	ID=PRO_0000097736;Note=SWI5-dependent HO expression protein 4	
+P51534	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P51534	UniProtKB	Sequence conflict	254	254	.	.	.	Note=L->LKL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P51534	UniProtKB	Sequence conflict	628	628	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P51534	UniProtKB	Sequence conflict	770	770	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P51534	UniProtKB	Beta strand	4	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	14	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	26	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	33	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	44	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	57	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Beta strand	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	65	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	83	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	97	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	112	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	122	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	126	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	144	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	163	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	167	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	179	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	223	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	235	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	239	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	248	250	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	251	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	265	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	282	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	303	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	306	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	318	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	327	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	338	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	361	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	377	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	386	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	404	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	449	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	464	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	469	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	477	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	482	496	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	499	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	502	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	510	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	527	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	545	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Beta strand	549	552	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	557	563	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Beta strand	568	570	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	584	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	603	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	616	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	625	627	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	631	645	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	648	650	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	652	654	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	661	672	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	673	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	679	695	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	697	703	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	707	719	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	720	722	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	724	738	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Turn	744	747	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	751	754	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	757	767	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Beta strand	768	772	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+P51534	UniProtKB	Helix	779	784	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB	
+##sequence-region P38337 1 142
+P38337	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000212515;Note=COMPASS component SHG1	
+##sequence-region P40073 1 367
+P40073	UniProtKB	Chain	1	367	.	.	.	ID=PRO_0000072231;Note=High osmolarity signaling protein SHO1	
+P40073	UniProtKB	Topological domain	1	32	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40073	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40073	UniProtKB	Topological domain	54	65	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40073	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40073	UniProtKB	Topological domain	87	93	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40073	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40073	UniProtKB	Topological domain	115	122	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40073	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40073	UniProtKB	Topological domain	144	367	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40073	UniProtKB	Domain	300	361	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P40073	UniProtKB	Modified residue	166	166	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17363249;Dbxref=PMID:17363249	
+P40073	UniProtKB	Glycosylation	59	59	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40073	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Diminishes the formation of oligomers%2C dampens activation of the HOG1 kinase%2C and impairs growth in high-salt or sorbitol conditions. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17363249;Dbxref=PMID:17363249	
+P40073	UniProtKB	Mutagenesis	309	309	.	.	.	Note=Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15200958;Dbxref=PMID:15200958	
+P40073	UniProtKB	Mutagenesis	317	317	.	.	.	Note=Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. D->I%2CH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15200958;Dbxref=PMID:15200958	
+P40073	UniProtKB	Mutagenesis	355	355	.	.	.	Note=Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. Y->A%2CF%2CI%2CM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15200958;Dbxref=PMID:15200958	
+P40073	UniProtKB	Beta strand	302	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN	
+P40073	UniProtKB	Beta strand	315	317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN	
+P40073	UniProtKB	Beta strand	328	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN	
+P40073	UniProtKB	Beta strand	336	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN	
+P40073	UniProtKB	Beta strand	348	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN	
+P40073	UniProtKB	Helix	353	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN	
+P40073	UniProtKB	Beta strand	356	363	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN	
+##sequence-region P25294 1 352
+P25294	UniProtKB	Chain	1	352	.	.	.	ID=PRO_0000071090;Note=Protein SIS1	
+P25294	UniProtKB	Domain	4	70	.	.	.	Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286	
+P25294	UniProtKB	Compositional bias	75	166	.	.	.	Note=Gly-rich	
+P25294	UniProtKB	Modified residue	275	275	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25294	UniProtKB	Helix	6	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RWU	
+P25294	UniProtKB	Helix	19	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RWU	
+P25294	UniProtKB	Helix	42	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RWU	
+P25294	UniProtKB	Helix	58	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RWU	
+P25294	UniProtKB	Helix	69	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RWU	
+P25294	UniProtKB	Beta strand	181	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Helix	190	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	198	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Turn	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	211	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	230	235	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	237	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	241	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	248	255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	259	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	267	272	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Helix	276	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	283	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	294	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	308	310	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Beta strand	319	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B26	
+P25294	UniProtKB	Beta strand	328	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+P25294	UniProtKB	Helix	344	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G	
+##sequence-region P52286 1 194
+P52286	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8670864;Dbxref=PMID:8670864	
+P52286	UniProtKB	Chain	2	194	.	.	.	ID=PRO_0000187257;Note=Suppressor of kinetochore protein 1	
+P52286	UniProtKB	Region	135	194	.	.	.	Note=Interaction with the F-box domain of F-box proteins;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P52286	UniProtKB	Compositional bias	66	74	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P52286	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P52286	UniProtKB	Sequence conflict	48	48	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P52286	UniProtKB	Beta strand	5	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P52286	UniProtKB	Beta strand	15	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P52286	UniProtKB	Helix	20	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P52286	UniProtKB	Helix	27	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P52286	UniProtKB	Beta strand	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P52286	UniProtKB	Helix	84	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P52286	UniProtKB	Turn	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P52286	UniProtKB	Helix	118	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P52286	UniProtKB	Helix	128	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P52286	UniProtKB	Helix	144	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P52286	UniProtKB	Helix	163	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+P52286	UniProtKB	Helix	178	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D	
+##sequence-region P33338 1 968
+P33338	UniProtKB	Chain	1	968	.	.	.	ID=PRO_0000071945;Note=Protein SLA2	
+P33338	UniProtKB	Transmembrane	772	791	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243	
+P33338	UniProtKB	Domain	1	127	.	.	.	Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243	
+P33338	UniProtKB	Domain	717	965	.	.	.	Note=I/LWEQ;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00292	
+P33338	UniProtKB	Modified residue	294	294	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P33338	UniProtKB	Modified residue	298	298	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33338	UniProtKB	Modified residue	308	308	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P33338	UniProtKB	Modified residue	555	555	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P33338	UniProtKB	Sequence conflict	52	52	.	.	.	Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33338	UniProtKB	Sequence conflict	344	344	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33338	UniProtKB	Sequence conflict	344	344	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33338	UniProtKB	Sequence conflict	560	560	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33338	UniProtKB	Sequence conflict	915	915	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P43321 1 101
+P43321	UniProtKB	Chain	1	101	.	.	.	ID=PRO_0000122220;Note=Small nuclear ribonucleoprotein Sm D3	
+P43321	UniProtKB	Sequence conflict	88	88	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P43321	UniProtKB	Helix	6	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P43321	UniProtKB	Beta strand	17	25	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P43321	UniProtKB	Beta strand	29	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P43321	UniProtKB	Beta strand	42	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P43321	UniProtKB	Beta strand	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P43321	UniProtKB	Beta strand	56	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P43321	UniProtKB	Helix	66	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P43321	UniProtKB	Beta strand	69	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P43321	UniProtKB	Helix	76	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P43321	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region Q12078 1 473
+Q12078	UniProtKB	Chain	1	473	.	.	.	ID=PRO_0000270538;Note=Iron transporter SMF3	
+Q12078	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12078	UniProtKB	Transmembrane	44	64	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12078	UniProtKB	Transmembrane	97	117	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12078	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12078	UniProtKB	Transmembrane	152	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12078	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12078	UniProtKB	Transmembrane	257	277	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12078	UniProtKB	Transmembrane	297	317	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12078	UniProtKB	Transmembrane	352	372	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12078	UniProtKB	Transmembrane	373	393	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12078	UniProtKB	Transmembrane	448	468	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12078	UniProtKB	Glycosylation	87	87	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P48232 1 102
+P48232	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000203445;Note=Biogenesis of lysosome-related organelles complex 1 subunit SNN1	
+P48232	UniProtKB	Coiled coil	71	102	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53823 1 222
+P53823	UniProtKB	Chain	1	222	.	.	.	ID=PRO_0000135620;Note=Probable pyridoxal 5'-phosphate synthase subunit SNO2	
+P53823	UniProtKB	Region	58	60	.	.	.	Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+P53823	UniProtKB	Region	151	152	.	.	.	Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+P53823	UniProtKB	Active site	91	91	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+P53823	UniProtKB	Active site	197	197	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+P53823	UniProtKB	Active site	199	199	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+P53823	UniProtKB	Binding site	120	120	.	.	.	Note=L-glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+##sequence-region P25357 1 1226
+P25357	UniProtKB	Chain	1	1226	.	.	.	ID=PRO_0000197122;Note=Probable DNA-binding protein SNT1	
+P25357	UniProtKB	Domain	668	720	.	.	.	Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624	
+P25357	UniProtKB	Domain	884	938	.	.	.	Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P25357	UniProtKB	DNA binding	911	934	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625	
+P25357	UniProtKB	Coiled coil	539	591	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25357	UniProtKB	Compositional bias	28	159	.	.	.	Note=Ser-rich	
+P25357	UniProtKB	Compositional bias	594	599	.	.	.	Note=Poly-Ser	
+P25357	UniProtKB	Modified residue	187	187	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25357	UniProtKB	Modified residue	395	395	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25357	UniProtKB	Modified residue	796	796	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P25357	UniProtKB	Modified residue	1037	1037	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25357	UniProtKB	Sequence conflict	305	305	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	375	375	.	.	.	Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	404	404	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	435	435	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	442	442	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	482	482	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	513	513	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	644	644	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	766	766	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	806	806	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	831	831	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	846	846	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	851	851	.	.	.	Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25357	UniProtKB	Sequence conflict	855	857	.	.	.	Note=AVQ->GVR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q03782 1 492
+Q03782	UniProtKB	Chain	1	492	.	.	.	ID=PRO_0000232634;Note=56 kDa U1 small nuclear ribonucleoprotein component	
+Q03782	UniProtKB	Mutagenesis	125	125	.	.	.	Note=Loss of function. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9630245;Dbxref=PMID:9630245	
+##sequence-region Q08826 1 162
+Q08826	UniProtKB	Chain	1	162	.	.	.	ID=PRO_0000213805;Note=Sorting nexin-3	
+Q08826	UniProtKB	Domain	38	161	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
+Q08826	UniProtKB	Binding site	81	81	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14514667;Dbxref=PMID:14514667	
+Q08826	UniProtKB	Binding site	83	83	.	.	.	Note=Phosphatidylinositol 3-phosphate%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14514667;Dbxref=PMID:14514667	
+Q08826	UniProtKB	Binding site	112	112	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14514667;Dbxref=PMID:14514667	
+Q08826	UniProtKB	Binding site	127	127	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14514667;Dbxref=PMID:14514667	
+Q08826	UniProtKB	Beta strand	36	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS	
+Q08826	UniProtKB	Beta strand	50	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCU	
+Q08826	UniProtKB	Beta strand	57	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS	
+Q08826	UniProtKB	Beta strand	74	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS	
+Q08826	UniProtKB	Helix	82	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS	
+Q08826	UniProtKB	Helix	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCU	
+Q08826	UniProtKB	Helix	121	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS	
+Q08826	UniProtKB	Helix	142	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS	
+Q08826	UniProtKB	Helix	149	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS	
+##sequence-region P43545 1 298
+P43545	UniProtKB	Chain	1	298	.	.	.	ID=PRO_0000109360;Note=Probable pyridoxal 5'-phosphate synthase subunit SNZ3	
+P43545	UniProtKB	Region	234	235	.	.	.	Note=D-ribose 5-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+P43545	UniProtKB	Active site	78	78	.	.	.	Note=Schiff-base intermediate with D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+P43545	UniProtKB	Binding site	21	21	.	.	.	Note=D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+P43545	UniProtKB	Binding site	150	150	.	.	.	Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+P43545	UniProtKB	Binding site	213	213	.	.	.	Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+##sequence-region P50278 1 321
+P50278	UniProtKB	Chain	1	321	.	.	.	ID=PRO_0000090082;Note=6-phosphogluconolactonase-like protein 1	
+P50278	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P50278	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P50278	UniProtKB	Modified residue	320	320	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P38858 1 249
+P38858	UniProtKB	Chain	1	249	.	.	.	ID=PRO_0000090084;Note=6-phosphogluconolactonase 3	
+##sequence-region P53165 1 657
+P53165	UniProtKB	Chain	1	657	.	.	.	ID=PRO_0000202764;Note=SAGA-associated factor 73	
+P53165	UniProtKB	Domain	220	286	.	.	.	Note=SCA7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00838	
+P53165	UniProtKB	Compositional bias	141	150	.	.	.	Note=Poly-Asp	
+P53165	UniProtKB	Compositional bias	153	162	.	.	.	Note=Poly-Asp	
+P53165	UniProtKB	Compositional bias	466	476	.	.	.	Note=Poly-Gln	
+P53165	UniProtKB	Compositional bias	517	526	.	.	.	Note=Poly-Gln	
+P53165	UniProtKB	Beta strand	7	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FK5	
+P53165	UniProtKB	Helix	13	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P53165	UniProtKB	Turn	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FJC	
+P53165	UniProtKB	Beta strand	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FJC	
+P53165	UniProtKB	Helix	32	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P53165	UniProtKB	Helix	36	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P53165	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P53165	UniProtKB	Helix	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P53165	UniProtKB	Beta strand	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P53165	UniProtKB	Beta strand	76	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P53165	UniProtKB	Turn	79	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P53165	UniProtKB	Beta strand	84	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FK5	
+P53165	UniProtKB	Helix	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+P53165	UniProtKB	Turn	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+##sequence-region Q12212 1 622
+Q12212	UniProtKB	Signal peptide	1	27	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12212	UniProtKB	Chain	28	622	.	.	.	ID=PRO_0000042719;Note=Protein SIA1	
+##sequence-region Q08199 1 421
+Q08199	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08199	UniProtKB	Chain	20	421	.	.	.	ID=PRO_0000223364;Note=Nucleotide exchange factor SIL1	
+Q08199	UniProtKB	Motif	418	421	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138	
+Q08199	UniProtKB	Glycosylation	105	105	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08199	UniProtKB	Glycosylation	181	181	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08199	UniProtKB	Glycosylation	215	215	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08199	UniProtKB	Glycosylation	233	233	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08199	UniProtKB	Glycosylation	315	315	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08199	UniProtKB	Glycosylation	333	333	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08199	UniProtKB	Mutagenesis	365	369	.	.	.	Note=Abrogates interaction with KAR2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10958688;Dbxref=PMID:10958688	
+Q08199	UniProtKB	Sequence conflict	51	51	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08199	UniProtKB	Helix	127	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	145	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	165	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	190	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	208	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	221	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	241	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	266	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Turn	276	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	280	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	306	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	321	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	338	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	356	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	363	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Helix	389	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+Q08199	UniProtKB	Turn	403	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML	
+##sequence-region P40472 1 476
+P40472	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40472	UniProtKB	Chain	20	476	.	.	.	ID=PRO_0000033465;Note=Probable secreted beta-glucosidase SIM1	
+P40472	UniProtKB	Compositional bias	58	113	.	.	.	Note=Ala-rich	
+P40472	UniProtKB	Compositional bias	81	204	.	.	.	Note=Ser-rich	
+P40472	UniProtKB	Glycosylation	423	423	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40472	UniProtKB	Natural variant	60	66	.	.	.	Note=In strain: SK1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40472	UniProtKB	Natural variant	174	185	.	.	.	Note=In strain: SK1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P40472	UniProtKB	Sequence conflict	85	88	.	.	.	Note=ADSS->GIA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11978 1 1358
+P11978	UniProtKB	Chain	1	1358	.	.	.	ID=PRO_0000097769;Note=Regulatory protein SIR4	
+P11978	UniProtKB	Coiled coil	1271	1347	.	.	.	.	
+P11978	UniProtKB	Modified residue	692	692	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P11978	UniProtKB	Cross-link	1128	1128	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542864;Dbxref=PMID:15542864	
+P11978	UniProtKB	Natural variant	994	994	.	.	.	Note=P->L	
+P11978	UniProtKB	Helix	808	821	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P11978	UniProtKB	Helix	829	837	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P11978	UniProtKB	Turn	846	848	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P11978	UniProtKB	Turn	854	857	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P11978	UniProtKB	Turn	861	863	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P11978	UniProtKB	Helix	864	866	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P11978	UniProtKB	Helix	869	872	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P11978	UniProtKB	Beta strand	879	883	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO	
+P11978	UniProtKB	Helix	1273	1342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PL5	
+P11978	UniProtKB	Turn	1343	1345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PL5	
+##sequence-region P36169 1 355
+P36169	UniProtKB	Chain	1	355	.	.	.	ID=PRO_0000203230;Note=Suppressor of lethality of KEX2 GAS1 double null mutant protein 1	
+P36169	UniProtKB	Topological domain	1	8	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36169	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical%3B Signal-anchor for type III membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36169	UniProtKB	Topological domain	30	355	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36169	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36169	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956	
+##sequence-region P32790 1 1244
+P32790	UniProtKB	Chain	1	1244	.	.	.	ID=PRO_0000071943;Note=Actin cytoskeleton-regulatory complex protein SLA1	
+P32790	UniProtKB	Domain	8	69	.	.	.	Note=SH3 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P32790	UniProtKB	Domain	70	132	.	.	.	Note=SH3 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P32790	UniProtKB	Domain	353	415	.	.	.	Note=SH3 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
+P32790	UniProtKB	Repeat	868	874	.	.	.	Note=1	
+P32790	UniProtKB	Repeat	877	883	.	.	.	Note=2	
+P32790	UniProtKB	Repeat	887	893	.	.	.	Note=3	
+P32790	UniProtKB	Repeat	923	929	.	.	.	Note=4	
+P32790	UniProtKB	Repeat	945	951	.	.	.	Note=5	
+P32790	UniProtKB	Repeat	1003	1009	.	.	.	Note=6	
+P32790	UniProtKB	Repeat	1020	1026	.	.	.	Note=7	
+P32790	UniProtKB	Repeat	1031	1037	.	.	.	Note=8	
+P32790	UniProtKB	Repeat	1048	1054	.	.	.	Note=9	
+P32790	UniProtKB	Repeat	1065	1071	.	.	.	Note=10	
+P32790	UniProtKB	Repeat	1084	1090	.	.	.	Note=11	
+P32790	UniProtKB	Repeat	1129	1135	.	.	.	Note=12	
+P32790	UniProtKB	Repeat	1155	1161	.	.	.	Note=13	
+P32790	UniProtKB	Repeat	1170	1176	.	.	.	Note=14	
+P32790	UniProtKB	Repeat	1185	1191	.	.	.	Note=15	
+P32790	UniProtKB	Repeat	1200	1206	.	.	.	Note=16	
+P32790	UniProtKB	Region	868	1205	.	.	.	Note=16 X 7 AA approximate repeats of T-G-G-A-M-M-P	
+P32790	UniProtKB	Modified residue	447	447	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32790	UniProtKB	Modified residue	449	449	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32790	UniProtKB	Modified residue	454	454	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32790	UniProtKB	Modified residue	799	799	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32790	UniProtKB	Modified residue	831	831	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32790	UniProtKB	Modified residue	858	858	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32790	UniProtKB	Modified residue	887	887	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32790	UniProtKB	Modified residue	904	904	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32790	UniProtKB	Modified residue	984	984	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32790	UniProtKB	Modified residue	993	993	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32790	UniProtKB	Modified residue	996	996	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32790	UniProtKB	Modified residue	1075	1075	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32790	UniProtKB	Cross-link	471	471	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32790	UniProtKB	Cross-link	548	548	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32790	UniProtKB	Beta strand	357	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q	
+P32790	UniProtKB	Beta strand	379	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q	
+P32790	UniProtKB	Beta strand	389	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q	
+P32790	UniProtKB	Turn	397	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q	
+P32790	UniProtKB	Beta strand	402	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q	
+P32790	UniProtKB	Helix	407	409	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q	
+P32790	UniProtKB	Beta strand	410	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q	
+P32790	UniProtKB	Turn	413	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JT4	
+P32790	UniProtKB	Beta strand	497	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP	
+P32790	UniProtKB	Beta strand	508	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP	
+P32790	UniProtKB	Beta strand	520	524	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP	
+P32790	UniProtKB	Beta strand	530	534	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP	
+P32790	UniProtKB	Helix	540	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP	
+P32790	UniProtKB	Helix	555	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP	
+P32790	UniProtKB	Helix	657	663	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IDW	
+P32790	UniProtKB	Helix	668	680	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IDW	
+P32790	UniProtKB	Helix	685	690	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IDW	
+P32790	UniProtKB	Helix	693	698	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IDW	
+P32790	UniProtKB	Helix	703	716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IDW	
+##sequence-region P47037 1 1230
+P47037	UniProtKB	Chain	1	1230	.	.	.	ID=PRO_0000119015;Note=Structural maintenance of chromosomes protein 3	
+P47037	UniProtKB	Nucleotide binding	32	39	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47037	UniProtKB	Region	483	684	.	.	.	Note=Flexible hinge	
+P47037	UniProtKB	Coiled coil	172	482	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47037	UniProtKB	Coiled coil	685	1041	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47037	UniProtKB	Compositional bias	1126	1161	.	.	.	Note=Ala/Asp-rich (DA-box)	
+P47037	UniProtKB	Modified residue	112	112	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18614053;Dbxref=PMID:18614053	
+P47037	UniProtKB	Modified residue	113	113	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18614053;Dbxref=PMID:18614053	
+P47037	UniProtKB	Beta strand	6	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	14	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	25	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	38	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	58	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	68	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Turn	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Turn	118	121	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	125	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	142	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	152	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	159	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	172	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	239	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	976	980	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	982	988	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	998	1059	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	1065	1069	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	1109	1113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	1121	1123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	1128	1143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	1149	1153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Turn	1154	1159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	1162	1176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	1179	1184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	1188	1190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Turn	1191	1193	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	1198	1203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Beta strand	1206	1210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+P47037	UniProtKB	Helix	1214	1221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3	
+##sequence-region Q02260 1 146
+Q02260	UniProtKB	Chain	1	146	.	.	.	ID=PRO_0000122206;Note=Small nuclear ribonucleoprotein Sm D1	
+Q02260	UniProtKB	Motif	128	144	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02260	UniProtKB	Helix	3	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q02260	UniProtKB	Beta strand	12	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q02260	UniProtKB	Beta strand	24	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q02260	UniProtKB	Beta strand	38	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q02260	UniProtKB	Beta strand	80	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q02260	UniProtKB	Turn	89	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q02260	UniProtKB	Beta strand	92	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q02260	UniProtKB	Helix	103	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P38925 1 575
+P38925	UniProtKB	Chain	1	575	.	.	.	ID=PRO_0000212605;Note=Manganese transporter SMF1	
+P38925	UniProtKB	Topological domain	1	70	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Transmembrane	71	91	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Topological domain	92	108	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Topological domain	130	156	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Topological domain	178	179	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Transmembrane	180	200	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Topological domain	201	218	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Transmembrane	219	239	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Topological domain	240	266	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Topological domain	288	344	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Transmembrane	345	365	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Topological domain	366	396	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Transmembrane	397	417	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Topological domain	418	463	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Transmembrane	464	484	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Topological domain	485	543	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Transmembrane	544	564	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Topological domain	565	575	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38925	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P38925	UniProtKB	Cross-link	33	33	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38925	UniProtKB	Cross-link	34	34	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P38925	UniProtKB	Sequence conflict	305	305	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38925	UniProtKB	Sequence conflict	416	416	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04007 1 877
+Q04007	UniProtKB	Chain	1	877	.	.	.	ID=PRO_0000253835;Note=SRP-independent targeting protein 1	
+Q04007	UniProtKB	Coiled coil	412	441	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04007	UniProtKB	Compositional bias	482	495	.	.	.	Note=Poly-Asp	
+Q04007	UniProtKB	Compositional bias	690	823	.	.	.	Note=Asn-rich	
+Q04007	UniProtKB	Modified residue	309	309	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04007	UniProtKB	Modified residue	310	310	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04007	UniProtKB	Modified residue	311	311	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04007	UniProtKB	Modified residue	332	332	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q04007	UniProtKB	Modified residue	334	334	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q04007	UniProtKB	Modified residue	692	692	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q04007	UniProtKB	Modified residue	694	694	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04007	UniProtKB	Modified residue	706	706	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+Q04007	UniProtKB	Modified residue	841	841	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q04007	UniProtKB	Cross-link	668	668	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q04007	UniProtKB	Cross-link	670	670	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P38956 1 169
+P38956	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38956	UniProtKB	Chain	2	169	.	.	.	ID=PRO_0000072004;Note=Transcription regulatory protein SNF11	
+P38956	UniProtKB	Repeat	28	31	.	.	.	Note=1-1	
+P38956	UniProtKB	Repeat	32	35	.	.	.	Note=1-2	
+P38956	UniProtKB	Repeat	36	39	.	.	.	Note=1-3	
+P38956	UniProtKB	Repeat	40	43	.	.	.	Note=1-4	
+P38956	UniProtKB	Repeat	44	47	.	.	.	Note=1-5	
+P38956	UniProtKB	Repeat	48	51	.	.	.	Note=1-6	
+P38956	UniProtKB	Repeat	76	80	.	.	.	Note=2-1	
+P38956	UniProtKB	Repeat	160	165	.	.	.	Note=2-2	
+P38956	UniProtKB	Region	28	51	.	.	.	Note=6 X 4 AA tandem repeats of N-[AT]-[NT]-A	
+P38956	UniProtKB	Region	76	165	.	.	.	Note=2 X 5 AA repeats of L-L-A-R-V	
+P38956	UniProtKB	Compositional bias	93	102	.	.	.	Note=Poly-Asn	
+P38956	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P22082 1 1703
+P22082	UniProtKB	Chain	1	1703	.	.	.	ID=PRO_0000074358;Note=Transcription regulatory protein SNF2	
+P22082	UniProtKB	Domain	247	282	.	.	.	Note=QLQ;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01001	
+P22082	UniProtKB	Domain	588	661	.	.	.	Note=HSA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00549	
+P22082	UniProtKB	Domain	779	944	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P22082	UniProtKB	Domain	1091	1254	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P22082	UniProtKB	Domain	1568	1638	.	.	.	Note=Bromo;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+P22082	UniProtKB	Nucleotide binding	792	799	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P22082	UniProtKB	DNA binding	1446	1456	.	.	.	Note=A.T hook 1	
+P22082	UniProtKB	DNA binding	1502	1513	.	.	.	Note=A.T hook 2	
+P22082	UniProtKB	DNA binding	1516	1526	.	.	.	Note=A.T hook 3	
+P22082	UniProtKB	Motif	894	897	.	.	.	Note=DEGH box	
+P22082	UniProtKB	Compositional bias	55	68	.	.	.	Note=Gln-rich	
+P22082	UniProtKB	Compositional bias	207	239	.	.	.	Note=Ala/Gln-rich	
+P22082	UniProtKB	Modified residue	358	358	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P22082	UniProtKB	Modified residue	383	383	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22082	UniProtKB	Modified residue	716	716	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P22082	UniProtKB	Modified residue	1340	1340	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22082	UniProtKB	Cross-link	543	543	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P22082	UniProtKB	Helix	593	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M	
+##sequence-region P46950 1 547
+P46950	UniProtKB	Chain	1	547	.	.	.	ID=PRO_0000072007;Note=Nitrosoguanidine resistance protein SNG1	
+P46950	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46950	UniProtKB	Transmembrane	159	179	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46950	UniProtKB	Transmembrane	318	338	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46950	UniProtKB	Transmembrane	363	383	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46950	UniProtKB	Transmembrane	394	414	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46950	UniProtKB	Transmembrane	418	438	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46950	UniProtKB	Transmembrane	457	477	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46950	UniProtKB	Transmembrane	488	508	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46950	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P46950	UniProtKB	Sequence conflict	117	117	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53127 1 1403
+P53127	UniProtKB	Chain	1	1403	.	.	.	ID=PRO_0000202742;Note=E3 ubiquitin-protein ligase SNT2	
+P53127	UniProtKB	Domain	121	258	.	.	.	Note=BAH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370	
+P53127	UniProtKB	Domain	555	606	.	.	.	Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624	
+P53127	UniProtKB	Zinc finger	317	369	.	.	.	Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+P53127	UniProtKB	Zinc finger	1038	1097	.	.	.	Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+P53127	UniProtKB	Zinc finger	1041	1095	.	.	.	Note=RING-type%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
+P53127	UniProtKB	Zinc finger	1105	1153	.	.	.	Note=C2HC pre-PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146	
+P53127	UniProtKB	Zinc finger	1177	1231	.	.	.	Note=PHD-type 3%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146	
+##sequence-region P39990 1 126
+P39990	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000136777;Note=13 kDa ribonucleoprotein-associated protein	
+P39990	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Impairs binding to U4 snRNA%2C but not U3 snoRNA. Causes pre-mRNA splicing and pre-rRNA processing defects. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730029;Dbxref=PMID:14730029	
+P39990	UniProtKB	Mutagenesis	81	81	.	.	.	Note=Impairs binding to U4 snRNA%2C but not U3 snoRNA%2C and causes pre rRNA processing defects and an accumulation of unspliced U3 snoRNA%3B when associated with A-84. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730029;Dbxref=PMID:14730029	
+P39990	UniProtKB	Mutagenesis	84	84	.	.	.	Note=Impairs binding to U4 snRNA%2C but not U3 snoRNA%2C and causes pre rRNA processing defects and an accumulation of unspliced U3 snoRNA%3B when associated with L-81. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730029;Dbxref=PMID:14730029	
+P39990	UniProtKB	Helix	14	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+P39990	UniProtKB	Beta strand	33	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+P39990	UniProtKB	Helix	37	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+P39990	UniProtKB	Beta strand	49	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+P39990	UniProtKB	Helix	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+P39990	UniProtKB	Helix	66	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+P39990	UniProtKB	Beta strand	78	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+P39990	UniProtKB	Helix	84	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+P39990	UniProtKB	Beta strand	98	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+P39990	UniProtKB	Helix	110	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT	
+##sequence-region Q04053 1 625
+Q04053	UniProtKB	Chain	1	625	.	.	.	ID=PRO_0000213834;Note=Sorting nexin-41	
+Q04053	UniProtKB	Domain	98	235	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
+Q04053	UniProtKB	Coiled coil	437	469	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04053	UniProtKB	Coiled coil	539	563	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04053	UniProtKB	Compositional bias	54	84	.	.	.	Note=Ser-rich	
+Q04053	UniProtKB	Compositional bias	497	508	.	.	.	Note=Ser-rich	
+Q04053	UniProtKB	Binding site	153	153	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04053	UniProtKB	Binding site	155	155	.	.	.	Note=Phosphatidylinositol 3-phosphate%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04053	UniProtKB	Binding site	179	179	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04053	UniProtKB	Binding site	202	202	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03148 1 297
+Q03148	UniProtKB	Chain	1	297	.	.	.	ID=PRO_0000109358;Note=Pyridoxal 5'-phosphate synthase subunit SNZ1	
+Q03148	UniProtKB	Region	235	236	.	.	.	Note=D-ribose 5-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+Q03148	UniProtKB	Active site	80	80	.	.	.	Note=Schiff-base intermediate with D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+Q03148	UniProtKB	Binding site	23	23	.	.	.	Note=D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+Q03148	UniProtKB	Binding site	152	152	.	.	.	Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+Q03148	UniProtKB	Binding site	164	164	.	.	.	Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991	
+Q03148	UniProtKB	Binding site	214	214	.	.	.	Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+Q03148	UniProtKB	Mutagenesis	116	116	.	.	.	Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991	
+Q03148	UniProtKB	Mutagenesis	117	117	.	.	.	Note=No activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991	
+Q03148	UniProtKB	Mutagenesis	136	137	.	.	.	Note=No pyridoxal 5'-phosphate synthesis activity. Retains ability to isomerize dihydroxyacetone phosphate to glyceraldehyde 3-phosphate. RR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991	
+Q03148	UniProtKB	Mutagenesis	148	148	.	.	.	Note=No activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991	
+Q03148	UniProtKB	Mutagenesis	164	164	.	.	.	Note=No pyridoxal 5'-phosphate synthesis activity. Retains ability to isomerize dihydroxyacetone phosphate to glyceraldehyde 3-phosphate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991	
+Q03148	UniProtKB	Mutagenesis	240	240	.	.	.	Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991	
+Q03148	UniProtKB	Helix	4	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FEM	
+Q03148	UniProtKB	Turn	15	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FEM	
+Q03148	UniProtKB	Beta strand	20	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	27	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Beta strand	39	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	48	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Turn	53	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	63	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Beta strand	77	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	86	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Beta strand	98	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Beta strand	124	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	131	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Beta strand	143	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O06	
+Q03148	UniProtKB	Helix	157	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	179	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	193	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Beta strand	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	218	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Beta strand	232	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	236	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Beta strand	241	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FEM	
+Q03148	UniProtKB	Helix	244	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Turn	257	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	261	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07	
+Q03148	UniProtKB	Helix	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FEM	
+##sequence-region P53438 1 785
+P53438	UniProtKB	Chain	1	785	.	.	.	ID=PRO_0000072036;Note=Protein SOK2	
+P53438	UniProtKB	Domain	414	520	.	.	.	Note=HTH APSES-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630	
+P53438	UniProtKB	DNA binding	448	469	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630	
+P53438	UniProtKB	Compositional bias	38	45	.	.	.	Note=Poly-Gln	
+P53438	UniProtKB	Compositional bias	148	151	.	.	.	Note=Poly-Tyr	
+P53438	UniProtKB	Compositional bias	169	172	.	.	.	Note=Poly-Tyr	
+P53438	UniProtKB	Compositional bias	206	217	.	.	.	Note=Poly-Gln	
+P53438	UniProtKB	Compositional bias	331	335	.	.	.	Note=Poly-Gln	
+P53438	UniProtKB	Compositional bias	526	532	.	.	.	Note=Poly-Ser	
+P53438	UniProtKB	Modified residue	771	771	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P37262 1 315
+P37262	UniProtKB	Chain	1	315	.	.	.	ID=PRO_0000090083;Note=6-phosphogluconolactonase-like protein 2	
+P37262	UniProtKB	Modified residue	42	42	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P37262	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50278	
+##sequence-region P38128 1 452
+P38128	UniProtKB	Chain	1	452	.	.	.	ID=PRO_0000199441;Note=Transcription factor SMP1	
+P38128	UniProtKB	Domain	3	57	.	.	.	Note=MADS-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00251	
+P38128	UniProtKB	DNA binding	58	87	.	.	.	Note=Mef2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38128	UniProtKB	Compositional bias	99	105	.	.	.	Note=Poly-Arg	
+##sequence-region P31109 1 117
+P31109	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000206744;Note=Synaptobrevin homolog 1	
+P31109	UniProtKB	Topological domain	1	94	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31109	UniProtKB	Transmembrane	95	111	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31109	UniProtKB	Topological domain	112	117	.	.	.	Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31109	UniProtKB	Domain	28	88	.	.	.	Note=v-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00290	
+P31109	UniProtKB	Lipidation	95	95	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15973437;Dbxref=PMID:15973437	
+P31109	UniProtKB	Cross-link	63	63	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P31109	UniProtKB	Helix	27	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B5N	
+##sequence-region P33328 1 115
+P33328	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000206745;Note=Synaptobrevin homolog 2	
+P33328	UniProtKB	Topological domain	1	93	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33328	UniProtKB	Transmembrane	94	112	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33328	UniProtKB	Topological domain	113	115	.	.	.	Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33328	UniProtKB	Domain	27	87	.	.	.	Note=v-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00290	
+P33328	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P33328	UniProtKB	Lipidation	94	94	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33328	UniProtKB	Cross-link	62	62	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P33328	UniProtKB	Sequence conflict	115	115	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53628 1 566
+P53628	UniProtKB	Chain	1	566	.	.	.	ID=PRO_0000072005;Note=Transcription regulatory protein SNF12	
+##sequence-region Q12420 1 587
+Q12420	UniProtKB	Chain	1	587	.	.	.	ID=PRO_0000232635;Note=66 kDa U4/U6.U5 small nuclear ribonucleoprotein component	
+Q12420	UniProtKB	Compositional bias	218	224	.	.	.	Note=Poly-Glu	
+Q12420	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q12420	UniProtKB	Helix	9	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU	
+Q12420	UniProtKB	Helix	40	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLV	
+##sequence-region P40317 1 901
+P40317	UniProtKB	Chain	1	901	.	.	.	ID=PRO_0000072035;Note=Protein SOK1	
+P40317	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40317	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40317	UniProtKB	Modified residue	191	191	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40317	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40317	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40317	UniProtKB	Sequence conflict	645	645	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25808 1 606
+P25808	UniProtKB	Chain	1	606	.	.	.	ID=PRO_0000055065;Note=ATP-dependent rRNA helicase SPB4	
+P25808	UniProtKB	Domain	38	224	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P25808	UniProtKB	Domain	248	404	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P25808	UniProtKB	Nucleotide binding	51	58	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P25808	UniProtKB	Coiled coil	539	582	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25808	UniProtKB	Motif	7	35	.	.	.	Note=Q motif;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25808	UniProtKB	Motif	172	175	.	.	.	Note=DEAD box;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25808	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P25808	UniProtKB	Mutagenesis	360	360	.	.	.	Note=Leads to accumulation of 35S and 27SB pre-rRNAs and a net 40S ribosomal subunit defect. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21825077;Dbxref=PMID:21825077	
+##sequence-region P46965 1 94
+P46965	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P46965	UniProtKB	Chain	2	94	.	.	.	ID=PRO_0000215162;Note=Signal peptidase complex subunit SPC1	
+P46965	UniProtKB	Topological domain	2	28	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46965	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46965	UniProtKB	Topological domain	50	50	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46965	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46965	UniProtKB	Topological domain	72	94	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46965	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P38915 1 602
+P38915	UniProtKB	Chain	1	602	.	.	.	ID=PRO_0000051226;Note=Transcription factor SPT8	
+P38915	UniProtKB	Repeat	173	212	.	.	.	Note=WD 1	
+P38915	UniProtKB	Repeat	305	346	.	.	.	Note=WD 2	
+P38915	UniProtKB	Repeat	415	454	.	.	.	Note=WD 3	
+P38915	UniProtKB	Repeat	506	544	.	.	.	Note=WD 4	
+P38915	UniProtKB	Repeat	560	600	.	.	.	Note=WD 5	
+P38915	UniProtKB	Compositional bias	1	76	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P38915	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38915	UniProtKB	Modified residue	108	108	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38915	UniProtKB	Modified residue	123	123	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38915	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38915	UniProtKB	Modified residue	451	451	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q03707 1 834
+Q03707	UniProtKB	Chain	1	834	.	.	.	ID=PRO_0000072188;Note=Inner nuclear membrane protein SRC1	
+Q03707	UniProtKB	Transmembrane	455	475	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03707	UniProtKB	Transmembrane	708	728	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03707	UniProtKB	Compositional bias	117	129	.	.	.	Note=Poly-Asp	
+Q03707	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03707	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03707	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03707	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03707	UniProtKB	Modified residue	203	203	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03707	UniProtKB	Modified residue	204	204	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03707	UniProtKB	Modified residue	206	206	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03707	UniProtKB	Modified residue	301	301	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03707	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03707	UniProtKB	Modified residue	427	427	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q99176 1 213
+Q99176	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000072191;Note=Protein SRN2	
+Q99176	UniProtKB	Domain	128	213	.	.	.	Note=VPS37 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00646	
+Q99176	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Defective in ESCRT-I cargo sorting. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+Q99176	UniProtKB	Mutagenesis	75	75	.	.	.	Note=Defective in ESCRT-I cargo sorting. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+Q99176	UniProtKB	Mutagenesis	79	79	.	.	.	Note=Defective in ESCRT-I cargo sorting. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+Q99176	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Defective in ESCRT-I cargo sorting%3B when associated with D-99. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+Q99176	UniProtKB	Mutagenesis	92	92	.	.	.	Note=Defective in ESCRT-I cargo sorting%3B when associated with D-102. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+Q99176	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Defective in ESCRT-I cargo sorting%3B when associated with D-99. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+Q99176	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Defective in ESCRT-I cargo sorting%3B when associated with D-88. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+Q99176	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Defective in ESCRT-I cargo sorting%3B when associated with D-95. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+Q99176	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Defective in ESCRT-I cargo sorting%3B when associated with D-92. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+Q99176	UniProtKB	Mutagenesis	181	181	.	.	.	Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVB)%3B when associated with R-185. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894	
+Q99176	UniProtKB	Mutagenesis	185	185	.	.	.	Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVB)%3B when associated with R-181. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894	
+Q99176	UniProtKB	Sequence conflict	90	90	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q99176	UniProtKB	Sequence conflict	140	140	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q99176	UniProtKB	Sequence conflict	143	143	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q99176	UniProtKB	Helix	23	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+Q99176	UniProtKB	Helix	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+Q99176	UniProtKB	Helix	62	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+Q99176	UniProtKB	Helix	72	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+Q99176	UniProtKB	Helix	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+Q99176	UniProtKB	Helix	86	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+Q99176	UniProtKB	Beta strand	144	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+Q99176	UniProtKB	Helix	147	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+Q99176	UniProtKB	Helix	178	205	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+##sequence-region P36057 1 244
+P36057	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000101230;Note=Signal recognition particle receptor subunit beta	
+P36057	UniProtKB	Transmembrane	7	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36057	UniProtKB	Nucleotide binding	45	53	.	.	.	Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654246;Dbxref=PMID:12654246	
+P36057	UniProtKB	Nucleotide binding	66	69	.	.	.	Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654246;Dbxref=PMID:12654246	
+P36057	UniProtKB	Nucleotide binding	154	157	.	.	.	Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654246;Dbxref=PMID:12654246	
+P36057	UniProtKB	Binding site	90	90	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654246;Dbxref=PMID:12654246	
+P36057	UniProtKB	Beta strand	40	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Helix	51	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Beta strand	73	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Helix	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Beta strand	84	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Helix	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Helix	96	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Helix	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Beta strand	109	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Helix	126	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Beta strand	149	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Helix	164	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Helix	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Beta strand	217	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Beta strand	221	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Turn	228	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P36057	UniProtKB	Helix	234	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+##sequence-region Q06688 1 274
+Q06688	UniProtKB	Chain	1	274	.	.	.	ID=PRO_0000186127;Note=SRR1-like protein BER1	
+##sequence-region Q03175 1 343
+Q03175	UniProtKB	Chain	1	343	.	.	.	ID=PRO_0000123760;Note=Dehydrodolichyl diphosphate synthase complex subunit SRT1	
+##sequence-region P39931 1 234
+P39931	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39931	UniProtKB	Chain	23	234	.	.	.	ID=PRO_0000022420;Note=Protein SSP120	
+P39931	UniProtKB	Domain	52	87	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P39931	UniProtKB	Domain	108	143	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
+P39931	UniProtKB	Modified residue	212	212	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38353 1 490
+P38353	UniProtKB	Chain	1	490	.	.	.	ID=PRO_0000131811;Note=Sec sixty-one protein homolog	
+P38353	UniProtKB	Topological domain	1	32	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Topological domain	54	121	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Topological domain	143	146	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Topological domain	168	174	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Topological domain	196	242	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Topological domain	264	293	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Transmembrane	294	314	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Topological domain	315	339	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Transmembrane	340	360	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Topological domain	361	361	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Transmembrane	362	382	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Topological domain	383	421	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Transmembrane	422	442	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Topological domain	443	449	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Transmembrane	450	470	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38353	UniProtKB	Topological domain	471	490	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53172 1 527
+P53172	UniProtKB	Chain	1	527	.	.	.	ID=PRO_0000202767;Note=Protein SDS23	
+P53172	UniProtKB	Domain	101	162	.	.	.	Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P53172	UniProtKB	Domain	185	243	.	.	.	Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P53172	UniProtKB	Domain	272	330	.	.	.	Note=CBS 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P53172	UniProtKB	Domain	335	391	.	.	.	Note=CBS 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703	
+P53172	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53172	UniProtKB	Modified residue	42	42	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P53172	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P53172	UniProtKB	Modified residue	430	430	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P53172	UniProtKB	Sequence conflict	180	180	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53172	UniProtKB	Sequence conflict	180	180	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53172	UniProtKB	Sequence conflict	180	180	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12118 1 346
+Q12118	UniProtKB	Chain	1	346	.	.	.	ID=PRO_0000106370;Note=Small glutamine-rich tetratricopeptide repeat-containing protein 2	
+Q12118	UniProtKB	Repeat	102	135	.	.	.	Note=TPR 1	
+Q12118	UniProtKB	Repeat	136	169	.	.	.	Note=TPR 2	
+Q12118	UniProtKB	Repeat	170	203	.	.	.	Note=TPR 3	
+Q12118	UniProtKB	Repeat	205	229	.	.	.	Note=TPR 4	
+Q12118	UniProtKB	Modified residue	308	308	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12118	UniProtKB	Helix	5	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM	
+Q12118	UniProtKB	Helix	27	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM	
+Q12118	UniProtKB	Helix	48	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM	
+Q12118	UniProtKB	Helix	51	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM	
+Q12118	UniProtKB	Helix	58	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM	
+Q12118	UniProtKB	Helix	69	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LXB	
+##sequence-region P38200 1 338
+P38200	UniProtKB	Chain	1	338	.	.	.	ID=PRO_0000202460;Note=Mitotic spindle-associated protein SHE1	
+P38200	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40486 1 507
+P40486	UniProtKB	Chain	1	507	.	.	.	ID=PRO_0000202966;Note=Protein SHQ1	
+P40486	UniProtKB	Domain	1	91	.	.	.	Note=CS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00547	
+P40486	UniProtKB	Beta strand	6	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD	
+P40486	UniProtKB	Beta strand	12	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD	
+P40486	UniProtKB	Beta strand	28	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD	
+P40486	UniProtKB	Beta strand	32	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD	
+P40486	UniProtKB	Beta strand	39	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD	
+P40486	UniProtKB	Beta strand	47	52	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD	
+P40486	UniProtKB	Beta strand	64	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD	
+P40486	UniProtKB	Turn	69	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD	
+P40486	UniProtKB	Beta strand	73	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD	
+P40486	UniProtKB	Helix	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD	
+P40486	UniProtKB	Helix	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	179	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Turn	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	201	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	218	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	233	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	241	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	250	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	275	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	296	315	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Turn	316	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	324	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	333	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	364	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Beta strand	379	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	385	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	403	418	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Turn	421	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	425	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	431	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	444	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	463	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Beta strand	467	471	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Turn	476	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZV0	
+P40486	UniProtKB	Beta strand	483	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+P40486	UniProtKB	Helix	488	504	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ	
+##sequence-region P36024 1 562
+P36024	UniProtKB	Chain	1	562	.	.	.	ID=PRO_0000182037;Note=Phosphopantothenoylcysteine decarboxylase subunit SIS2	
+P36024	UniProtKB	Compositional bias	496	553	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P36024	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P36024	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36024	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36024	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198	
+P36024	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36024	UniProtKB	Mutagenesis	378	378	.	.	.	Note=Abolishes PPCDC activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19915539;Dbxref=PMID:19915539	
+##sequence-region Q12469 1 655
+Q12469	UniProtKB	Chain	1	655	.	.	.	ID=PRO_0000086656;Note=Serine/threonine-protein kinase SKM1	
+Q12469	UniProtKB	Domain	3	118	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+Q12469	UniProtKB	Domain	123	136	.	.	.	Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057	
+Q12469	UniProtKB	Domain	360	639	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12469	UniProtKB	Nucleotide binding	366	374	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12469	UniProtKB	Active site	507	507	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q12469	UniProtKB	Binding site	406	406	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q12469	UniProtKB	Sequence conflict	150	150	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12469	UniProtKB	Sequence conflict	303	303	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12469	UniProtKB	Sequence conflict	306	306	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12469	UniProtKB	Sequence conflict	320	320	.	.	.	Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12469	UniProtKB	Sequence conflict	322	322	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12469	UniProtKB	Sequence conflict	452	452	.	.	.	Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12469	UniProtKB	Sequence conflict	468	468	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38889 1 622
+P38889	UniProtKB	Chain	1	622	.	.	.	ID=PRO_0000081404;Note=Transcription factor SKN7	
+P38889	UniProtKB	Domain	378	492	.	.	.	Note=Response regulatory;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00169	
+P38889	UniProtKB	DNA binding	86	190	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38889	UniProtKB	Modified residue	427	427	.	.	.	Note=4-aspartylphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00169,ECO:0000269|PubMed:9843501;Dbxref=PMID:9843501	
+P38889	UniProtKB	Mutagenesis	427	427	.	.	.	Note=No activity. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7957083,ECO:0000269|PubMed:8598053;Dbxref=PMID:7957083,PMID:8598053	
+P38889	UniProtKB	Mutagenesis	427	427	.	.	.	Note=Augments activity. D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7957083,ECO:0000269|PubMed:8598053;Dbxref=PMID:7957083,PMID:8598053	
+P38889	UniProtKB	Mutagenesis	427	427	.	.	.	Note=Diminishes activity. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7957083,ECO:0000269|PubMed:8598053;Dbxref=PMID:7957083,PMID:8598053	
+P38889	UniProtKB	Mutagenesis	427	427	.	.	.	Note=No activity. D->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7957083,ECO:0000269|PubMed:8598053;Dbxref=PMID:7957083,PMID:8598053	
+P38889	UniProtKB	Sequence conflict	45	45	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02100 1 647
+Q02100	UniProtKB	Chain	1	647	.	.	.	ID=PRO_0000076517;Note=CRE-binding bZIP protein SKO1	
+Q02100	UniProtKB	Domain	429	492	.	.	.	Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+Q02100	UniProtKB	Region	430	451	.	.	.	Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+Q02100	UniProtKB	Region	454	461	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+Q02100	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02100	UniProtKB	Modified residue	113	113	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q02100	UniProtKB	Modified residue	399	399	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q02100	UniProtKB	Modified residue	558	558	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P34252 1 453
+P34252	UniProtKB	Chain	1	453	.	.	.	ID=PRO_0000071952;Note=DNA replication regulator SLD2	
+P34252	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16619031;Dbxref=PMID:16619031	
+P34252	UniProtKB	Mutagenesis	84	84	.	.	.	Note=No interaction with DPB11. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16619031;Dbxref=PMID:16619031	
+P34252	UniProtKB	Mutagenesis	100	100	.	.	.	Note=No interaction with DPB11. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16619031;Dbxref=PMID:16619031	
+P34252	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Normal interaction with DPB11. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16619031;Dbxref=PMID:16619031	
+P34252	UniProtKB	Mutagenesis	241	241	.	.	.	Note=Reduced interaction with DPB11. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16619031;Dbxref=PMID:16619031	
+##sequence-region P53251 1 210
+P53251	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000202808;Note=Ribosome biogenesis protein SLX9	
+##sequence-region Q04964 1 104
+Q04964	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000071974;Note=Ribonucleotide reductase inhibitor protein SML1	
+Q04964	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04964	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine%3B by DUN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14684746;Dbxref=PMID:14684746	
+Q04964	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine%3B by DUN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14684746;Dbxref=PMID:14684746	
+Q04964	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine%3B by DUN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14684746;Dbxref=PMID:14684746	
+Q04964	UniProtKB	Disulfide bond	14	14	.	.	.	Note=Interchain	
+Q04964	UniProtKB	Mutagenesis	56	61	.	.	.	Note=Increased stability following gamma-irradiation and loss of phosphorylation by DUN1. Causes lethality in rnr1-W688G strain which has a mutation in RNR1. SASASS->AAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20566477;Dbxref=PMID:20566477	
+##sequence-region Q12306 1 101
+Q12306	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q12306	UniProtKB	Chain	2	98	.	.	.	ID=PRO_0000035963;Note=Ubiquitin-like protein SMT3	
+Q12306	UniProtKB	Propeptide	99	101	.	.	.	ID=PRO_0000035964	
+Q12306	UniProtKB	Domain	22	98	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
+Q12306	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q12306	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+Q12306	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q12306	UniProtKB	Cross-link	98	98	.	.	.	Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)	
+Q12306	UniProtKB	Beta strand	22	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8	
+Q12306	UniProtKB	Beta strand	34	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8	
+Q12306	UniProtKB	Helix	46	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8	
+Q12306	UniProtKB	Helix	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8	
+Q12306	UniProtKB	Beta strand	64	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8	
+Q12306	UniProtKB	Beta strand	70	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V60	
+Q12306	UniProtKB	Turn	78	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8	
+Q12306	UniProtKB	Beta strand	87	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8	
+##sequence-region P32364 1 656
+P32364	UniProtKB	Chain	1	656	.	.	.	ID=PRO_0000125454;Note=Kinesin-related protein SMY1	
+P32364	UniProtKB	Domain	27	364	.	.	.	Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P32364	UniProtKB	Nucleotide binding	114	121	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283	
+P32364	UniProtKB	Modified residue	583	583	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P32909 1 740
+P32909	UniProtKB	Chain	1	740	.	.	.	ID=PRO_0000071996;Note=Protein SMY2	
+P32909	UniProtKB	Domain	205	261	.	.	.	Note=GYF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00101	
+P32909	UniProtKB	Coiled coil	369	440	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32909	UniProtKB	Compositional bias	576	627	.	.	.	Note=Thr-rich	
+P32909	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32909	UniProtKB	Modified residue	96	96	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32909	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32909	UniProtKB	Modified residue	311	311	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32909	UniProtKB	Modified residue	545	545	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32909	UniProtKB	Modified residue	602	602	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32909	UniProtKB	Beta strand	207	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V	
+P32909	UniProtKB	Beta strand	217	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V	
+P32909	UniProtKB	Helix	223	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V	
+P32909	UniProtKB	Beta strand	240	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V	
+P32909	UniProtKB	Beta strand	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V	
+P32909	UniProtKB	Helix	260	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V	
+P32909	UniProtKB	Helix	274	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V	
+##sequence-region Q06091 1 175
+Q06091	UniProtKB	Chain	1	175	.	.	.	ID=PRO_0000071999;Note=Pre-mRNA-splicing factor SNT309	
+Q06091	UniProtKB	Turn	5	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06091	UniProtKB	Helix	14	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06091	UniProtKB	Helix	53	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06091	UniProtKB	Beta strand	74	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06091	UniProtKB	Helix	83	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06091	UniProtKB	Helix	104	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06091	UniProtKB	Helix	112	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P56508 1 79
+P56508	UniProtKB	Chain	1	79	.	.	.	ID=PRO_0000193989;Note=Protein SNA2	
+P56508	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P56508	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P56508	UniProtKB	Topological domain	28	32	.	.	.	Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P56508	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P56508	UniProtKB	Topological domain	54	79	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P56508	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P56508	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q03144 1 224
+Q03144	UniProtKB	Chain	1	224	.	.	.	ID=PRO_0000135619;Note=Pyridoxal 5'-phosphate synthase subunit SNO1	
+Q03144	UniProtKB	Region	67	69	.	.	.	Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+Q03144	UniProtKB	Region	160	161	.	.	.	Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+Q03144	UniProtKB	Active site	100	100	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+Q03144	UniProtKB	Active site	203	203	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+Q03144	UniProtKB	Active site	205	205	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+Q03144	UniProtKB	Binding site	129	129	.	.	.	Note=L-glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+##sequence-region Q04902 1 237
+Q04902	UniProtKB	Chain	1	237	.	.	.	ID=PRO_0000157853;Note=Probable glutathione-independent glyoxalase SNO4	
+Q04902	UniProtKB	Active site	138	138	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432	
+Q04902	UniProtKB	Active site	139	139	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432	
+Q04902	UniProtKB	Active site	170	170	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432	
+##sequence-region Q12368 1 194
+Q12368	UniProtKB	Chain	1	194	.	.	.	ID=PRO_0000232633;Note=23 kDa U4/U6.U5 small nuclear ribonucleoprotein component	
+Q12368	UniProtKB	Zinc finger	80	104	.	.	.	Note=C2H2-type	
+##sequence-region P00447 1 233
+P00447	UniProtKB	Transit peptide	1	26	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6	
+P00447	UniProtKB	Chain	27	233	.	.	.	ID=PRO_0000032888;Note=Superoxide dismutase [Mn]%2C mitochondrial	
+P00447	UniProtKB	Metal binding	52	52	.	.	.	Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00447	UniProtKB	Metal binding	107	107	.	.	.	Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00447	UniProtKB	Metal binding	194	194	.	.	.	Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00447	UniProtKB	Metal binding	198	198	.	.	.	Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00447	UniProtKB	Modified residue	147	147	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P00447	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666	
+P00447	UniProtKB	Helix	37	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Turn	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	46	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	56	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	84	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	117	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Turn	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	127	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	140	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Beta strand	156	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Beta strand	172	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Beta strand	187	194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	197	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	201	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	208	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	216	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+P00447	UniProtKB	Helix	221	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E	
+##sequence-region P53315 1 255
+P53315	UniProtKB	Chain	1	255	.	.	.	ID=PRO_0000090085;Note=6-phosphogluconolactonase 4	
+##sequence-region P23201 1 1466
+P23201	UniProtKB	Chain	1	1466	.	.	.	ID=PRO_0000072090;Note=Protein SPA2	
+P23201	UniProtKB	Repeat	818	825	.	.	.	Note=1	
+P23201	UniProtKB	Repeat	826	834	.	.	.	Note=2	
+P23201	UniProtKB	Repeat	835	843	.	.	.	Note=3	
+P23201	UniProtKB	Repeat	860	868	.	.	.	Note=4	
+P23201	UniProtKB	Repeat	875	883	.	.	.	Note=5	
+P23201	UniProtKB	Repeat	884	892	.	.	.	Note=6	
+P23201	UniProtKB	Repeat	893	901	.	.	.	Note=7	
+P23201	UniProtKB	Repeat	902	910	.	.	.	Note=8	
+P23201	UniProtKB	Repeat	911	919	.	.	.	Note=9	
+P23201	UniProtKB	Repeat	920	928	.	.	.	Note=10	
+P23201	UniProtKB	Repeat	929	937	.	.	.	Note=11	
+P23201	UniProtKB	Repeat	938	946	.	.	.	Note=12	
+P23201	UniProtKB	Repeat	947	953	.	.	.	Note=13	
+P23201	UniProtKB	Repeat	954	961	.	.	.	Note=14	
+P23201	UniProtKB	Repeat	962	970	.	.	.	Note=15	
+P23201	UniProtKB	Repeat	971	979	.	.	.	Note=16	
+P23201	UniProtKB	Repeat	980	988	.	.	.	Note=17	
+P23201	UniProtKB	Repeat	989	997	.	.	.	Note=18	
+P23201	UniProtKB	Repeat	998	1006	.	.	.	Note=19	
+P23201	UniProtKB	Repeat	1007	1015	.	.	.	Note=20	
+P23201	UniProtKB	Repeat	1036	1044	.	.	.	Note=21	
+P23201	UniProtKB	Repeat	1045	1053	.	.	.	Note=22	
+P23201	UniProtKB	Repeat	1054	1062	.	.	.	Note=23	
+P23201	UniProtKB	Repeat	1072	1080	.	.	.	Note=24	
+P23201	UniProtKB	Repeat	1081	1087	.	.	.	Note=25	
+P23201	UniProtKB	Region	818	1087	.	.	.	Note=25 X 9 AA approximate tandem repeats	
+P23201	UniProtKB	Coiled coil	286	388	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23201	UniProtKB	Coiled coil	1169	1189	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23201	UniProtKB	Coiled coil	1275	1302	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23201	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P23201	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P23201	UniProtKB	Modified residue	220	220	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P23201	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23201	UniProtKB	Modified residue	274	274	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P23201	UniProtKB	Modified residue	301	301	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P23201	UniProtKB	Modified residue	585	585	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23201	UniProtKB	Modified residue	599	599	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23201	UniProtKB	Modified residue	646	646	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P23201	UniProtKB	Modified residue	817	817	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P23201	UniProtKB	Modified residue	820	820	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P23201	UniProtKB	Modified residue	865	865	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P23201	UniProtKB	Modified residue	883	883	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23201	UniProtKB	Modified residue	910	910	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P23201	UniProtKB	Modified residue	937	937	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+P23201	UniProtKB	Modified residue	961	961	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P23201	UniProtKB	Modified residue	979	979	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23201	UniProtKB	Modified residue	1053	1053	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P23201	UniProtKB	Modified residue	1056	1056	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P23201	UniProtKB	Modified residue	1080	1080	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P23201	UniProtKB	Modified residue	1173	1173	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23201	UniProtKB	Modified residue	1179	1179	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23201	UniProtKB	Modified residue	1180	1180	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23201	UniProtKB	Modified residue	1251	1251	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23201	UniProtKB	Modified residue	1263	1263	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region Q04969 1 178
+Q04969	UniProtKB	Chain	1	178	.	.	.	ID=PRO_0000203253;Note=Signal peptidase complex subunit SPC2	
+Q04969	UniProtKB	Topological domain	1	37	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04969	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04969	UniProtKB	Topological domain	59	67	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04969	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04969	UniProtKB	Topological domain	89	178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36131 1 295
+P36131	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000211554;Note=DASH complex subunit SPC34	
+P36131	UniProtKB	Coiled coil	223	295	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36131	UniProtKB	Modified residue	199	199	.	.	.	Note=Phosphothreonine%3B by IPL1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000269|PubMed:12408861;Dbxref=PMID:17330950,PMID:12408861	
+##sequence-region Q08204 1 1093
+Q08204	UniProtKB	Chain	1	1093	.	.	.	ID=PRO_0000119020;Note=Structural maintenance of chromosomes protein 5	
+Q08204	UniProtKB	Nucleotide binding	69	76	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08204	UniProtKB	Region	442	650	.	.	.	Note=Flexible hinge	
+Q08204	UniProtKB	Coiled coil	208	354	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08204	UniProtKB	Coiled coil	404	441	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08204	UniProtKB	Coiled coil	651	757	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08204	UniProtKB	Coiled coil	884	926	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08204	UniProtKB	Compositional bias	986	1021	.	.	.	Note=Ala/Asp-rich (DA-box)	
+Q08204	UniProtKB	Helix	307	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+Q08204	UniProtKB	Turn	740	742	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+Q08204	UniProtKB	Helix	743	808	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK	
+##sequence-region Q12749 1 1114
+Q12749	UniProtKB	Chain	1	1114	.	.	.	ID=PRO_0000119022;Note=Structural maintenance of chromosomes protein 6	
+Q12749	UniProtKB	Nucleotide binding	109	116	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12749	UniProtKB	Region	530	695	.	.	.	Note=Flexible hinge	
+Q12749	UniProtKB	Coiled coil	259	529	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12749	UniProtKB	Coiled coil	696	969	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12749	UniProtKB	Motif	35	39	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12749	UniProtKB	Compositional bias	1019	1054	.	.	.	Note=Ala/Asp-rich (DA-box)	
+##sequence-region Q06217 1 110
+Q06217	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000122213;Note=Small nuclear ribonucleoprotein Sm D2	
+Q06217	UniProtKB	Helix	16	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06217	UniProtKB	Helix	32	40	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06217	UniProtKB	Beta strand	43	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06217	UniProtKB	Beta strand	53	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06217	UniProtKB	Beta strand	67	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06217	UniProtKB	Beta strand	87	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06217	UniProtKB	Turn	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q06217	UniProtKB	Beta strand	101	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P47057 1 423
+P47057	UniProtKB	Chain	1	423	.	.	.	ID=PRO_0000213818;Note=Sorting nexin-4	
+P47057	UniProtKB	Domain	29	157	.	.	.	Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147	
+P47057	UniProtKB	Coiled coil	217	252	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47057	UniProtKB	Coiled coil	346	381	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47057	UniProtKB	Binding site	78	78	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47057	UniProtKB	Binding site	80	80	.	.	.	Note=Phosphatidylinositol 3-phosphate%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47057	UniProtKB	Binding site	104	104	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47057	UniProtKB	Binding site	123	123	.	.	.	Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47057	UniProtKB	Mutagenesis	79	79	.	.	.	Note=Abolishes the intracellular punctate localization and decreases the cytoplasm to vacuole transport. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12048214;Dbxref=PMID:12048214	
+P47057	UniProtKB	Sequence conflict	292	304	.	.	.	Note=QLIKLKDQKQIDY->PDQIERPETDRL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38282 1 291
+P38282	UniProtKB	Chain	1	291	.	.	.	ID=PRO_0000202498;Note=Pre-mRNA-splicing factor SPP381	
+##sequence-region P53540 1 846
+P53540	UniProtKB	Chain	1	846	.	.	.	ID=PRO_0000078123;Note=Spindle pole body component SPC98	
+P53540	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53540	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P50088 1 95
+P50088	UniProtKB	Chain	1	95	.	.	.	ID=PRO_0000202853;Note=Stationary phase gene 1 protein	
+P50088	UniProtKB	Transmembrane	20	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40092 1 148
+P40092	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40092	UniProtKB	Chain	20	127	.	.	.	ID=PRO_0000014317;Note=Uncharacterized cell wall protein SPI1	
+P40092	UniProtKB	Propeptide	128	148	.	.	.	ID=PRO_0000372448;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40092	UniProtKB	Compositional bias	61	124	.	.	.	Note=Thr-rich	
+P40092	UniProtKB	Lipidation	127	127	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40092	UniProtKB	Glycosylation	41	41	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40092	UniProtKB	Glycosylation	59	59	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53541 1 631
+P53541	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53541	UniProtKB	Chain	18	631	.	.	.	ID=PRO_0000120569;Note=Putative meiotic phospholipase SPO1	
+P53541	UniProtKB	Transmembrane	376	396	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53541	UniProtKB	Domain	24	631	.	.	.	Note=PLA2c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00555	
+P53541	UniProtKB	Region	24	67	.	.	.	Note=Required for lipid-binding and function in meiosis	
+P53541	UniProtKB	Glycosylation	233	233	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53541	UniProtKB	Glycosylation	293	293	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53541	UniProtKB	Glycosylation	303	303	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53541	UniProtKB	Glycosylation	500	500	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53541	UniProtKB	Glycosylation	536	536	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53541	UniProtKB	Glycosylation	560	560	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53541	UniProtKB	Glycosylation	563	563	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53541	UniProtKB	Glycosylation	572	572	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53541	UniProtKB	Mutagenesis	103	103	.	.	.	Note=In SPO1-1%3B defective in sporulation at 34 degrees Celsius. I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10855497;Dbxref=PMID:10855497	
+P53541	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Loss of function. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10855497;Dbxref=PMID:10855497	
+##sequence-region P40031 1 143
+P40031	UniProtKB	Chain	1	143	.	.	.	ID=PRO_0000072141;Note=Sporulation-specific protein 73	
+##sequence-region P32572 1 300
+P32572	UniProtKB	Chain	1	300	.	.	.	ID=PRO_0000074227;Note=Sporulation protein SPS18	
+P32572	UniProtKB	Domain	11	130	.	.	.	Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+P32572	UniProtKB	Zinc finger	28	51	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288	
+P32572	UniProtKB	Sequence conflict	106	106	.	.	.	Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32572	UniProtKB	Sequence conflict	132	132	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32572	UniProtKB	Sequence conflict	201	201	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32572	UniProtKB	Sequence conflict	230	230	.	.	.	Note=Q->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35209 1 758
+P35209	UniProtKB	Chain	1	758	.	.	.	ID=PRO_0000072162;Note=Protein SPT21	
+P35209	UniProtKB	Compositional bias	127	144	.	.	.	Note=Asp/Glu-rich (acidic)	
+P35209	UniProtKB	Compositional bias	672	682	.	.	.	Note=Asp/Glu-rich (acidic)	
+P35209	UniProtKB	Modified residue	454	454	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P42948 1 560
+P42948	UniProtKB	Chain	1	560	.	.	.	ID=PRO_0000097697;Note=SET domain-containing protein 4	
+P42948	UniProtKB	Domain	346	475	.	.	.	Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190	
+P42948	UniProtKB	Zinc finger	160	210	.	.	.	Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+##sequence-region Q99287 1 776
+Q99287	UniProtKB	Chain	1	776	.	.	.	ID=PRO_0000155140;Note=Protein SEY1	
+Q99287	UniProtKB	Topological domain	1	681	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109	
+Q99287	UniProtKB	Transmembrane	682	702	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109	
+Q99287	UniProtKB	Topological domain	703	705	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109	
+Q99287	UniProtKB	Transmembrane	706	726	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109	
+Q99287	UniProtKB	Topological domain	727	776	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109	
+Q99287	UniProtKB	Domain	34	263	.	.	.	Note=GB1/RHD3-type G	
+Q99287	UniProtKB	Nucleotide binding	44	51	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109	
+Q99287	UniProtKB	Mutagenesis	50	50	.	.	.	Note=Abolishes GTP binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19665976;Dbxref=PMID:19665976	
+##sequence-region Q06168 1 426
+Q06168	UniProtKB	Chain	1	426	.	.	.	ID=PRO_0000205962;Note=Chromatin structure-remodeling complex subunit SFH1	
+Q06168	UniProtKB	Region	201	242	.	.	.	Note=Interaction with STH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9154831;Dbxref=PMID:9154831	
+Q06168	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32432 1 683
+P32432	UniProtKB	Chain	1	683	.	.	.	ID=PRO_0000046851;Note=Transcription factor SFP1	
+P32432	UniProtKB	Zinc finger	598	623	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P32432	UniProtKB	Zinc finger	659	683	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P32432	UniProtKB	Region	230	458	.	.	.	Note=Prion domain (PrD)	
+P32432	UniProtKB	Compositional bias	532	555	.	.	.	Note=Poly-Asp	
+##sequence-region P25554 1 259
+P25554	UniProtKB	Chain	1	259	.	.	.	ID=PRO_0000202539;Note=SAGA-associated factor 29	
+P25554	UniProtKB	Domain	121	255	.	.	.	Note=SGF29 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00851	
+P25554	UniProtKB	Region	163	165	.	.	.	Note=Histone H3K4me3 N-terminus binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874	
+P25554	UniProtKB	Region	207	210	.	.	.	Note=Histone H3K4me3 N-terminus binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874	
+P25554	UniProtKB	Region	229	232	.	.	.	Note=Histone H3K4me3 binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874	
+P25554	UniProtKB	Binding site	205	205	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874	
+P25554	UniProtKB	Binding site	212	212	.	.	.	Note=Histone H3K4me3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874	
+P25554	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P25554	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Reduces histone H3 acetylation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874	
+P25554	UniProtKB	Mutagenesis	165	165	.	.	.	Note=Reduces histone H3 acetylation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874	
+P25554	UniProtKB	Mutagenesis	205	205	.	.	.	Note=Reduces histone H3 acetylation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874	
+P25554	UniProtKB	Mutagenesis	210	210	.	.	.	Note=Reduces histone H3 acetylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874	
+P25554	UniProtKB	Mutagenesis	212	212	.	.	.	Note=Reduces histone H3 acetylation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874	
+P25554	UniProtKB	Mutagenesis	229	229	.	.	.	Note=Reduces histone H3 acetylation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874	
+P25554	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Beta strand	130	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Turn	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP8	
+P25554	UniProtKB	Beta strand	144	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Turn	154	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Beta strand	158	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Beta strand	174	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Helix	180	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Beta strand	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Beta strand	200	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Beta strand	209	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Beta strand	225	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Beta strand	232	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP8	
+P25554	UniProtKB	Beta strand	239	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Helix	243	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Beta strand	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+P25554	UniProtKB	Helix	250	253	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6	
+##sequence-region Q06236 1 168
+Q06236	UniProtKB	Transit peptide	1	23	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06236	UniProtKB	Chain	24	168	.	.	.	ID=PRO_0000268180;Note=Mitochondrial inner membrane protein SHH4	
+Q06236	UniProtKB	Topological domain	24	65	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08749	
+Q06236	UniProtKB	Transmembrane	66	86	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06236	UniProtKB	Topological domain	87	92	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08749	
+Q06236	UniProtKB	Transmembrane	93	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06236	UniProtKB	Topological domain	114	120	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08749	
+Q06236	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06236	UniProtKB	Topological domain	142	168	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08749	
+Q06236	UniProtKB	Metal binding	101	101	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37298	
+Q06236	UniProtKB	Binding site	112	112	.	.	.	Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37298	
+##sequence-region P38957 1 223
+P38957	UniProtKB	Chain	1	223	.	.	.	ID=PRO_0000202593;Note=Suppressor of hydroxyurea sensitivity protein 2	
+##sequence-region P22579 1 1536
+P22579	UniProtKB	Chain	1	1536	.	.	.	ID=PRO_0000121544;Note=Transcriptional regulatory protein SIN3	
+P22579	UniProtKB	Domain	217	287	.	.	.	Note=PAH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00810	
+P22579	UniProtKB	Domain	404	474	.	.	.	Note=PAH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00810	
+P22579	UniProtKB	Domain	656	727	.	.	.	Note=PAH 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00810	
+P22579	UniProtKB	Compositional bias	480	519	.	.	.	Note=Gln-rich	
+P22579	UniProtKB	Modified residue	137	137	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P22579	UniProtKB	Modified residue	303	303	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22579	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P22579	UniProtKB	Modified residue	316	316	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22579	UniProtKB	Modified residue	1046	1046	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P22579	UniProtKB	Sequence conflict	510	510	.	.	.	Note=Q->QAQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P34164 1 415
+P34164	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
+P34164	UniProtKB	Chain	2	415	.	.	.	ID=PRO_0000204375;Note=SNF1 protein kinase subunit beta-2	
+P34164	UniProtKB	Region	154	335	.	.	.	Note=Kinase-interacting sequence (KIS)%3B required for interaction with SNF1	
+P34164	UniProtKB	Region	336	415	.	.	.	Note=Association with SNF1 kinase complex (ASC) domain%3B required for interaction with SNF4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9121458;Dbxref=PMID:9121458	
+P34164	UniProtKB	Modified residue	66	66	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34164	UniProtKB	Modified residue	298	298	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34164	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12562756;Dbxref=PMID:12562756	
+P34164	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Changes protein distribution from the plasma membrane to the cytoplasm and nucleus and alters the cellular life span. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12562756;Dbxref=PMID:12562756	
+P34164	UniProtKB	Beta strand	164	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV	
+P34164	UniProtKB	Beta strand	177	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV	
+P34164	UniProtKB	Helix	182	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV	
+P34164	UniProtKB	Beta strand	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV	
+P34164	UniProtKB	Beta strand	202	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV	
+P34164	UniProtKB	Beta strand	210	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV	
+P34164	UniProtKB	Beta strand	222	224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV	
+P34164	UniProtKB	Beta strand	231	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV	
+P34164	UniProtKB	Beta strand	240	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV	
+P34164	UniProtKB	Beta strand	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P34164	UniProtKB	Helix	311	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P34164	UniProtKB	Helix	316	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P34164	UniProtKB	Helix	336	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P34164	UniProtKB	Helix	345	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P34164	UniProtKB	Helix	349	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P34164	UniProtKB	Helix	375	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P34164	UniProtKB	Beta strand	380	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TDH	
+P34164	UniProtKB	Beta strand	390	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+P34164	UniProtKB	Beta strand	402	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N	
+##sequence-region P40210 1 489
+P40210	UniProtKB	Chain	1	489	.	.	.	ID=PRO_0000203303;Note=Protein SIP5	
+P40210	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40210	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40210	UniProtKB	Modified residue	433	433	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40210	UniProtKB	Modified residue	436	436	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40210	UniProtKB	Modified residue	438	438	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P53955 1 656
+P53955	UniProtKB	Chain	1	656	.	.	.	ID=PRO_0000203453;Note=Phosphatidylinositol 4%2C5-bisphosphate-binding protein SLM2	
+P53955	UniProtKB	Domain	445	555	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P53955	UniProtKB	Motif	640	645	.	.	.	Note=PXIXIT-like%2C required for interaction with CNA1 and CNA2%2C and calcineurin-dependent dephosphorylation	
+P53955	UniProtKB	Modified residue	626	626	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53955	UniProtKB	Modified residue	649	649	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53955	UniProtKB	Modified residue	653	653	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q12098 1 748
+Q12098	UniProtKB	Chain	1	748	.	.	.	ID=PRO_0000270574;Note=Structure-specific endonuclease subunit SLX4	
+Q12098	UniProtKB	Compositional bias	568	573	.	.	.	Note=Poly-Glu	
+Q12098	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphothreonine%3B by ATR and ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17636031;Dbxref=PMID:17636031	
+Q12098	UniProtKB	Modified residue	113	113	.	.	.	Note=Phosphothreonine%3B by ATR and ATM;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12098	UniProtKB	Modified residue	289	289	.	.	.	Note=Phosphoserine%3B by ATR and ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17636031;Dbxref=PMID:17636031	
+Q12098	UniProtKB	Modified residue	319	319	.	.	.	Note=Phosphothreonine%3B by ATR and ATM;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12098	UniProtKB	Modified residue	329	329	.	.	.	Note=Phosphoserine%3B by ATR and ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17636031;Dbxref=PMID:17636031	
+Q12098	UniProtKB	Modified residue	355	355	.	.	.	Note=Phosphoserine%3B by ATR and ATM;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P22215 1 453
+P22215	UniProtKB	Chain	1	453	.	.	.	ID=PRO_0000206785;Note=Uncharacterized transporter SLY41	
+P22215	UniProtKB	Topological domain	1	110	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Topological domain	132	172	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Topological domain	194	201	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Topological domain	223	234	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Transmembrane	235	255	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Topological domain	256	269	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Transmembrane	270	290	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Topological domain	291	332	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Transmembrane	333	353	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Topological domain	354	371	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Topological domain	393	413	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Transmembrane	414	434	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Topological domain	435	453	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P22215	UniProtKB	Sequence conflict	34	34	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P22215	UniProtKB	Sequence conflict	339	339	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40167 1 298
+P40167	UniProtKB	Chain	1	298	.	.	.	ID=PRO_0000203397;Note=Sporulation-specific with a leucine zipper motif protein 1	
+##sequence-region P40548 1 159
+P40548	UniProtKB	Chain	1	159	.	.	.	ID=PRO_0000088881;Note=HSP70 co-chaperone SNL1	
+P40548	UniProtKB	Topological domain	1	12	.	.	.	Note=Perinuclear space	
+P40548	UniProtKB	Transmembrane	13	35	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40548	UniProtKB	Topological domain	36	159	.	.	.	Note=Cytoplasmic	
+P40548	UniProtKB	Domain	73	159	.	.	.	Note=BAG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00369	
+P40548	UniProtKB	Compositional bias	42	63	.	.	.	Note=Lys-rich	
+P40548	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Strongly reduces interaction with HSP70 family members. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105220;Dbxref=PMID:12105220	
+P40548	UniProtKB	Mutagenesis	141	141	.	.	.	Note=Strongly reduces interaction with HSP70 family members. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105220;Dbxref=PMID:12105220	
+##sequence-region Q12034 1 447
+Q12034	UniProtKB	Chain	1	447	.	.	.	ID=PRO_0000207614;Note=Protein SLF1	
+Q12034	UniProtKB	Domain	265	368	.	.	.	Note=HTH La-type RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00332	
+Q12034	UniProtKB	Sequence conflict	118	118	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P54867 1 378
+P54867	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54867	UniProtKB	Chain	22	378	.	.	.	ID=PRO_0000041483;Note=Protein SLG1	
+P54867	UniProtKB	Topological domain	22	264	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54867	UniProtKB	Transmembrane	265	285	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54867	UniProtKB	Topological domain	286	378	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54867	UniProtKB	Domain	22	110	.	.	.	Note=WSC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00558	
+P54867	UniProtKB	Compositional bias	125	255	.	.	.	Note=Thr-rich	
+P54867	UniProtKB	Modified residue	331	331	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P54867	UniProtKB	Modified residue	353	353	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+P54867	UniProtKB	Glycosylation	65	65	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54867	UniProtKB	Mutagenesis	303	303	.	.	.	Note=Sensitive to alkali. Fails to restore normal levels of SLT2 phosphorylation upon alkaline stress. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17088254;Dbxref=PMID:17088254	
+P54867	UniProtKB	Mutagenesis	319	319	.	.	.	Note=No phosphorylation%3B when associated with A-320. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15470108;Dbxref=PMID:15470108	
+P54867	UniProtKB	Mutagenesis	320	320	.	.	.	Note=No phosphorylation%3B when associated with A-319. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15470108;Dbxref=PMID:15470108	
+P54867	UniProtKB	Mutagenesis	322	322	.	.	.	Note=No phosphorylation%3B when associated with A-323. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15470108;Dbxref=PMID:15470108	
+P54867	UniProtKB	Mutagenesis	323	323	.	.	.	Note=No phosphorylation%3B when associated with A-322. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15470108;Dbxref=PMID:15470108	
+##sequence-region P40485 1 686
+P40485	UniProtKB	Chain	1	686	.	.	.	ID=PRO_0000202965;Note=Phosphatidylinositol 4%2C5-bisphosphate-binding protein SLM1	
+P40485	UniProtKB	Domain	468	581	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
+P40485	UniProtKB	Coiled coil	296	381	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40485	UniProtKB	Motif	673	678	.	.	.	Note=PXIXIT-like%2C required for interaction with CNA1 and CNA2%2C and calcineurin-dependent dephosphorylation	
+P40485	UniProtKB	Compositional bias	45	63	.	.	.	Note=Poly-Gln	
+P40485	UniProtKB	Compositional bias	133	136	.	.	.	Note=Poly-Asn	
+P40485	UniProtKB	Compositional bias	166	172	.	.	.	Note=Poly-Gln	
+P40485	UniProtKB	Modified residue	145	145	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40485	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40485	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40485	UniProtKB	Mutagenesis	477	478	.	.	.	Note=In SLM1-PHM2%3B reduces phosphoinositide binding by 95%25%3B when associated with A-487. RR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15689497;Dbxref=PMID:15689497	
+P40485	UniProtKB	Mutagenesis	483	483	.	.	.	Note=In SLM1-PHM1%3B reduces phosphoinositide binding by 80%25 and causes mislocalization to the cytoplasm%3B when associated with A-487. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15372071,ECO:0000269|PubMed:15689497;Dbxref=PMID:15372071,PMID:15689497	
+P40485	UniProtKB	Mutagenesis	487	487	.	.	.	Note=In SLM1-PHM1%3B reduces phosphoinositide binding by 80%25 and causes mislocalization to the cytoplasm%3B when associated with A-483. In SLM1-PHM2%3B reduces phosphoinositide binding by 95%25%3B when associated with 477-AA-478. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15372071,ECO:0000269|PubMed:15689497;Dbxref=PMID:15372071,PMID:15689497	
+P40485	UniProtKB	Beta strand	470	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H	
+P40485	UniProtKB	Turn	480	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H	
+P40485	UniProtKB	Beta strand	484	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H	
+P40485	UniProtKB	Beta strand	494	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H	
+P40485	UniProtKB	Turn	505	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H	
+P40485	UniProtKB	Beta strand	512	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H	
+P40485	UniProtKB	Helix	517	519	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H	
+P40485	UniProtKB	Beta strand	520	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H	
+P40485	UniProtKB	Beta strand	530	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NSU	
+P40485	UniProtKB	Beta strand	542	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H	
+P40485	UniProtKB	Beta strand	558	562	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H	
+P40485	UniProtKB	Helix	566	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H	
+##sequence-region P39928 1 1220
+P39928	UniProtKB	Chain	1	1220	.	.	.	ID=PRO_0000081405;Note=Osmosensing histidine protein kinase SLN1	
+P39928	UniProtKB	Topological domain	1	22	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39928	UniProtKB	Transmembrane	23	46	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39928	UniProtKB	Topological domain	47	333	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39928	UniProtKB	Transmembrane	334	354	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39928	UniProtKB	Topological domain	355	1220	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39928	UniProtKB	Domain	573	928	.	.	.	Note=Histidine kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00107	
+P39928	UniProtKB	Domain	1089	1210	.	.	.	Note=Response regulatory;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00169	
+P39928	UniProtKB	Metal binding	1094	1094	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39928	UniProtKB	Metal binding	1095	1095	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39928	UniProtKB	Metal binding	1144	1144	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39928	UniProtKB	Metal binding	1195	1195	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P39928	UniProtKB	Modified residue	502	502	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39928	UniProtKB	Modified residue	576	576	.	.	.	Note=Phosphohistidine%3B by autocatalysis;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00107,ECO:0000269|PubMed:8808622;Dbxref=PMID:8808622	
+P39928	UniProtKB	Modified residue	758	758	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39928	UniProtKB	Modified residue	833	833	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39928	UniProtKB	Modified residue	1041	1041	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39928	UniProtKB	Modified residue	1044	1044	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P39928	UniProtKB	Modified residue	1144	1144	.	.	.	Note=4-aspartylphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00169,ECO:0000269|PubMed:8808622;Dbxref=PMID:8808622	
+P39928	UniProtKB	Glycosylation	100	100	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39928	UniProtKB	Glycosylation	138	138	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39928	UniProtKB	Glycosylation	142	142	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39928	UniProtKB	Glycosylation	181	181	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39928	UniProtKB	Glycosylation	224	224	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39928	UniProtKB	Glycosylation	272	272	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39928	UniProtKB	Mutagenesis	576	576	.	.	.	Note=Inactive. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183345;Dbxref=PMID:8183345	
+P39928	UniProtKB	Mutagenesis	891	891	.	.	.	Note=In SLN1-1%3B slow growth. G->D	
+P39928	UniProtKB	Mutagenesis	1144	1144	.	.	.	Note=Inactive. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183345;Dbxref=PMID:8183345	
+P39928	UniProtKB	Beta strand	1090	1093	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+P39928	UniProtKB	Helix	1097	1109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+P39928	UniProtKB	Beta strand	1115	1120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+P39928	UniProtKB	Helix	1121	1134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+P39928	UniProtKB	Beta strand	1139	1143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+P39928	UniProtKB	Beta strand	1148	1150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+P39928	UniProtKB	Helix	1152	1162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+P39928	UniProtKB	Beta strand	1169	1174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+P39928	UniProtKB	Helix	1178	1186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+P39928	UniProtKB	Beta strand	1190	1196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+P39928	UniProtKB	Helix	1199	1209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25	
+##sequence-region P42900 1 643
+P42900	UniProtKB	Sequence conflict	103	103	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38241 1 364
+P38241	UniProtKB	Chain	1	364	.	.	.	ID=PRO_0000212432;Note=Pre-mRNA-splicing factor SLT11	
+P38241	UniProtKB	Turn	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Beta strand	24	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Beta strand	35	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Beta strand	48	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Helix	63	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Turn	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Turn	78	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Helix	84	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Beta strand	94	97	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Helix	108	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Helix	121	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Beta strand	204	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Beta strand	212	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Helix	216	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Beta strand	240	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Turn	244	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Beta strand	248	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P38241	UniProtKB	Helix	256	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P38324 1 304
+P38324	UniProtKB	Chain	1	304	.	.	.	ID=PRO_0000202517;Note=Structure-specific endonuclease subunit SLX1	
+P38324	UniProtKB	Domain	12	95	.	.	.	Note=GIY-YIG;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03100	
+P38324	UniProtKB	Zinc finger	218	282	.	.	.	Note=SLX1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03100	
+##sequence-region Q12267 1 1418
+Q12267	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12267	UniProtKB	Chain	2	1418	.	.	.	ID=PRO_0000119018;Note=Structural maintenance of chromosomes protein 4	
+Q12267	UniProtKB	Nucleotide binding	185	192	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12267	UniProtKB	Region	674	848	.	.	.	Note=Flexible hinge	
+Q12267	UniProtKB	Coiled coil	345	673	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12267	UniProtKB	Coiled coil	849	1172	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12267	UniProtKB	Coiled coil	1224	1263	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12267	UniProtKB	Compositional bias	1323	1358	.	.	.	Note=Ala/Asp-rich (DA-box)	
+Q12267	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q12267	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12267	UniProtKB	Modified residue	113	113	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12267	UniProtKB	Helix	562	681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Beta strand	688	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	692	694	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Beta strand	695	698	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	700	702	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	703	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	711	714	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Beta strand	715	719	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	721	734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Beta strand	738	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	758	760	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Turn	764	767	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Beta strand	768	772	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	773	775	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	778	782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Beta strand	784	787	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	794	797	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Beta strand	800	803	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Beta strand	806	808	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Beta strand	821	823	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Beta strand	832	834	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	850	883	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	886	910	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Turn	911	913	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	914	925	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+Q12267	UniProtKB	Helix	929	947	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+##sequence-region P41808 1 388
+P41808	UniProtKB	Chain	1	388	.	.	.	ID=PRO_0000186339;Note=Sporulation-specific mitogen-activated protein kinase SMK1	
+P41808	UniProtKB	Domain	38	337	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P41808	UniProtKB	Nucleotide binding	44	52	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P41808	UniProtKB	Motif	207	209	.	.	.	Note=TXY	
+P41808	UniProtKB	Compositional bias	384	387	.	.	.	Note=Poly-Ser	
+P41808	UniProtKB	Active site	166	166	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P41808	UniProtKB	Binding site	69	69	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region P18480 1 905
+P18480	UniProtKB	Chain	1	905	.	.	.	ID=PRO_0000205955;Note=SWI/SNF chromatin-remodeling complex subunit SNF5	
+P18480	UniProtKB	Compositional bias	31	270	.	.	.	Note=Gln-rich	
+P18480	UniProtKB	Compositional bias	72	132	.	.	.	Note=Pro-rich	
+P18480	UniProtKB	Compositional bias	272	324	.	.	.	Note=Pro-rich	
+P18480	UniProtKB	Compositional bias	489	588	.	.	.	Note=Asp/Glu-rich (acidic)	
+P18480	UniProtKB	Compositional bias	714	882	.	.	.	Note=Pro-rich	
+P18480	UniProtKB	Compositional bias	755	798	.	.	.	Note=Arg/Lys-rich (basic)	
+P18480	UniProtKB	Modified residue	818	818	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P18480	UniProtKB	Sequence conflict	564	564	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P18480	UniProtKB	Sequence conflict	564	564	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12483 1 233
+Q12483	UniProtKB	Chain	1	233	.	.	.	ID=PRO_0000215214;Note=Vacuolar-sorting protein SNF8	
+Q12483	UniProtKB	Coiled coil	23	46	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P43544 1 222
+P43544	UniProtKB	Chain	1	222	.	.	.	ID=PRO_0000135621;Note=Probable pyridoxal 5'-phosphate synthase subunit SNO3	
+P43544	UniProtKB	Region	58	60	.	.	.	Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+P43544	UniProtKB	Region	151	152	.	.	.	Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+P43544	UniProtKB	Active site	91	91	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+P43544	UniProtKB	Active site	197	197	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+P43544	UniProtKB	Active site	199	199	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+P43544	UniProtKB	Binding site	120	120	.	.	.	Note=L-glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528	
+##sequence-region P32568 1 1501
+P32568	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32568	UniProtKB	Chain	2	1501	.	.	.	ID=PRO_0000093441;Note=Protein SNQ2	
+P32568	UniProtKB	Transmembrane	521	541	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Transmembrane	554	574	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Transmembrane	600	620	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Transmembrane	628	648	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Transmembrane	664	680	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Transmembrane	771	789	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Transmembrane	1190	1212	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Transmembrane	1216	1236	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Transmembrane	1277	1296	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Transmembrane	1333	1352	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Transmembrane	1455	1475	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Domain	161	410	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P32568	UniProtKB	Domain	853	1095	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P32568	UniProtKB	Nucleotide binding	889	896	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P32568	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32568	UniProtKB	Modified residue	26	26	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32568	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32568	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P32568	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32568	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P32568	UniProtKB	Modified residue	1153	1153	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32568	UniProtKB	Glycosylation	273	273	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Glycosylation	334	334	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Glycosylation	518	518	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Glycosylation	730	730	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Glycosylation	874	874	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Glycosylation	1401	1401	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32568	UniProtKB	Sequence conflict	78	78	.	.	.	Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53207 1 620
+P53207	UniProtKB	Chain	1	620	.	.	.	ID=PRO_0000202781;Note=U1 small nuclear ribonucleoprotein component SNU71	
+P53207	UniProtKB	Coiled coil	296	385	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53207	UniProtKB	Modified residue	512	512	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P53207	UniProtKB	Modified residue	514	514	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region P53824 1 298
+P53824	UniProtKB	Chain	1	298	.	.	.	ID=PRO_0000109359;Note=Probable pyridoxal 5'-phosphate synthase subunit SNZ2	
+P53824	UniProtKB	Region	234	235	.	.	.	Note=D-ribose 5-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+P53824	UniProtKB	Active site	78	78	.	.	.	Note=Schiff-base intermediate with D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+P53824	UniProtKB	Binding site	21	21	.	.	.	Note=D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+P53824	UniProtKB	Binding site	150	150	.	.	.	Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+P53824	UniProtKB	Binding site	213	213	.	.	.	Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080	
+##sequence-region Q04748 1 898
+Q04748	UniProtKB	Transit peptide	1	31	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q04748	UniProtKB	Chain	32	898	.	.	.	ID=PRO_0000203280;Note=Protein SOV1%2C mitochondrial	
+##sequence-region Q12133 1 184
+Q12133	UniProtKB	Chain	1	184	.	.	.	ID=PRO_0000218951;Note=Signal peptidase complex subunit SPC3	
+Q12133	UniProtKB	Topological domain	1	14	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12133	UniProtKB	Transmembrane	15	35	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12133	UniProtKB	Topological domain	36	184	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12133	UniProtKB	Glycosylation	102	102	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12133	UniProtKB	Glycosylation	173	173	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P36094 1 363
+P36094	UniProtKB	Chain	1	363	.	.	.	ID=PRO_0000072109;Note=Spindle pole body component SPC42	
+P36094	UniProtKB	Coiled coil	60	137	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36094	UniProtKB	Coiled coil	249	298	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36094	UniProtKB	Modified residue	213	213	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36094	UniProtKB	Modified residue	217	217	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P36094	UniProtKB	Modified residue	284	284	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36094	UniProtKB	Modified residue	329	329	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36094	UniProtKB	Helix	68	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Q6Q	
+##sequence-region Q12074 1 293
+Q12074	UniProtKB	Chain	1	293	.	.	.	ID=PRO_0000156462;Note=Spermidine synthase	
+Q12074	UniProtKB	Domain	12	248	.	.	.	Note=PABS	
+Q12074	UniProtKB	Region	150	151	.	.	.	Note=S-adenosylmethioninamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12074	UniProtKB	Region	168	171	.	.	.	Note=Putrescine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12074	UniProtKB	Active site	168	168	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12074	UniProtKB	Binding site	44	44	.	.	.	Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12074	UniProtKB	Binding site	74	74	.	.	.	Note=Putrescine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12074	UniProtKB	Binding site	75	75	.	.	.	Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12074	UniProtKB	Binding site	99	99	.	.	.	Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12074	UniProtKB	Binding site	119	119	.	.	.	Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12074	UniProtKB	Binding site	168	168	.	.	.	Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12074	UniProtKB	Binding site	236	236	.	.	.	Note=Putrescine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q04438 1 115
+Q04438	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000203290;Note=Stationary phase protein 4	
+##sequence-region P17123 1 173
+P17123	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P17123	UniProtKB	Chain	2	173	.	.	.	ID=PRO_0000072133;Note=Sporulation-specific protein 12	
+P17123	UniProtKB	Region	159	173	.	.	.	Note=Negative-charged tail	
+P17123	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P17123	UniProtKB	Modified residue	118	118	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P17123	UniProtKB	Modified residue	125	125	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q04359 1 397
+Q04359	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000213614;Note=Sporulation-specific protein 20	
+Q04359	UniProtKB	Domain	330	392	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+Q04359	UniProtKB	Region	4	50	.	.	.	Note=Inhibitory region	
+Q04359	UniProtKB	Region	51	95	.	.	.	Note=Positive regulatory region	
+Q04359	UniProtKB	Mutagenesis	66	66	.	.	.	Note=Strong decrease of the sporulation rate and loss of lipid binding%3B when associated with E-68%3B E-71 and E-73. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704	
+Q04359	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Strong decrease of the sporulation rate. L->P%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704	
+Q04359	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Strong decrease of the sporulation rate and loss of lipid binding%3B when associated with E-66%3B E-71 and E-73. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704	
+Q04359	UniProtKB	Mutagenesis	70	70	.	.	.	Note=Strong decrease of the sporulation rate. L->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704	
+Q04359	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Strong decrease of the sporulation rate and loss of lipid binding%3B when associated with E-66%3B E-68 and E-73. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704	
+Q04359	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Strong decrease of the sporulation rate and loss of lipid binding%3B when associated with E-66%3B E-68 and E-71. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704	
+Q04359	UniProtKB	Sequence conflict	59	59	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02521 1 185
+Q02521	UniProtKB	Chain	1	185	.	.	.	ID=PRO_0000218529;Note=Pre-mRNA-splicing factor SPP2	
+Q02521	UniProtKB	Domain	100	149	.	.	.	Note=G-patch	
+Q02521	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Loss of the interaction with PRP2. L->E%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542821;Dbxref=PMID:15542821	
+Q02521	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Restores interactions with PRP2 mutants. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542821;Dbxref=PMID:15542821	
+Q02521	UniProtKB	Sequence conflict	68	69	.	.	.	Note=KK->GG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02521	UniProtKB	Sequence conflict	143	143	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q02521	UniProtKB	Sequence conflict	149	149	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P50875 1 604
+P50875	UniProtKB	Chain	1	604	.	.	.	ID=PRO_0000072161;Note=Transcription factor SPT20	
+P50875	UniProtKB	Compositional bias	157	162	.	.	.	Note=Poly-Gln	
+P50875	UniProtKB	Compositional bias	235	240	.	.	.	Note=Poly-Ser	
+P50875	UniProtKB	Compositional bias	422	425	.	.	.	Note=Poly-Ser	
+P50875	UniProtKB	Compositional bias	454	463	.	.	.	Note=Poly-Ala	
+P50875	UniProtKB	Compositional bias	552	559	.	.	.	Note=Poly-Asn	
+P50875	UniProtKB	Modified residue	446	446	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P50875	UniProtKB	Modified residue	516	516	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P50875	UniProtKB	Sequence conflict	293	293	.	.	.	Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06132 1 899
+Q06132	UniProtKB	Chain	1	899	.	.	.	ID=PRO_0000269652;Note=Suppressor of glycerol defect protein 1	
+Q06132	UniProtKB	Domain	335	540	.	.	.	Note=MIF4G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00698	
+Q06132	UniProtKB	Domain	644	781	.	.	.	Note=MI;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00698	
+Q06132	UniProtKB	Modified residue	736	736	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P33335 1 543
+P33335	UniProtKB	Chain	1	543	.	.	.	ID=PRO_0000173422;Note=Protein SGE1	
+P33335	UniProtKB	Topological domain	1	8	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	30	41	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	63	79	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	101	103	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	104	124	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	125	131	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	153	162	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	163	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	184	227	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	228	248	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	249	255	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	256	276	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	277	300	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	301	321	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	322	341	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	342	362	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	363	373	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	374	394	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	395	399	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	400	420	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	421	443	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	444	464	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	465	508	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Transmembrane	509	529	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Topological domain	530	543	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33335	UniProtKB	Sequence conflict	429	429	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P33335	UniProtKB	Sequence conflict	447	486	.	.	.	Note=KSLGFAFGGNMGAMIFTASLKNQMRSSQLNIPQFTSVETL->NPWALRLEGYGGNDIHCITQKPDALFPIKHTTIYVCRNT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35187 1 1447
+P35187	UniProtKB	Chain	1	1447	.	.	.	ID=PRO_0000205057;Note=ATP-dependent helicase SGS1	
+P35187	UniProtKB	Domain	687	864	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P35187	UniProtKB	Domain	886	1035	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P35187	UniProtKB	Domain	1272	1351	.	.	.	Note=HRDC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00328	
+P35187	UniProtKB	Nucleotide binding	714	721	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P35187	UniProtKB	Motif	808	811	.	.	.	Note=DEAH box	
+P35187	UniProtKB	Compositional bias	631	639	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P35187	UniProtKB	Mutagenesis	31	31	.	.	.	Note=In allele sgs1-34%3B temperature-sensitive. Q->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12228808;Dbxref=PMID:12228808	
+P35187	UniProtKB	Mutagenesis	980	980	.	.	.	Note=In allele sgs1-35%3B temperature-sensitive. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12228808;Dbxref=PMID:12228808	
+P35187	UniProtKB	Mutagenesis	987	987	.	.	.	Note=In allele sgs1-36%3B temperature-sensitive. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12228808;Dbxref=PMID:12228808	
+P35187	UniProtKB	Helix	1274	1291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B	
+P35187	UniProtKB	Beta strand	1292	1295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B	
+P35187	UniProtKB	Helix	1303	1312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B	
+P35187	UniProtKB	Helix	1317	1320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B	
+P35187	UniProtKB	Helix	1321	1323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B	
+P35187	UniProtKB	Helix	1328	1333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B	
+P35187	UniProtKB	Helix	1334	1336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B	
+P35187	UniProtKB	Helix	1338	1347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B	
+P35187	UniProtKB	Turn	1348	1350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B	
+##sequence-region Q04487 1 196
+Q04487	UniProtKB	Transit peptide	1	53	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04487	UniProtKB	Chain	54	196	.	.	.	ID=PRO_0000003639;Note=Mitochondrial inner membrane protein SHH3	
+Q04487	UniProtKB	Topological domain	54	97	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421	
+Q04487	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04487	UniProtKB	Topological domain	119	137	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421	
+Q04487	UniProtKB	Transmembrane	138	160	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04487	UniProtKB	Topological domain	161	174	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421	
+Q04487	UniProtKB	Transmembrane	175	195	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04487	UniProtKB	Topological domain	196	196	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421	
+Q04487	UniProtKB	Metal binding	154	154	.	.	.	Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421	
+Q04487	UniProtKB	Binding site	91	91	.	.	.	Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421	
+Q04487	UniProtKB	Binding site	95	95	.	.	.	Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421	
+##sequence-region P06701 1 978
+P06701	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564	
+P06701	UniProtKB	Chain	2	978	.	.	.	ID=PRO_0000097768;Note=Regulatory protein SIR3	
+P06701	UniProtKB	Domain	48	188	.	.	.	Note=BAH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370	
+P06701	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564	
+P06701	UniProtKB	Mutagenesis	2	2	.	.	.	Note=No acetylation%2C reduced silencing activity. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564	
+P06701	UniProtKB	Mutagenesis	2	2	.	.	.	Note=No acetylation%2C No silencing activity. A->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564	
+P06701	UniProtKB	Mutagenesis	2	2	.	.	.	Note=No effect. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564	
+P06701	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Reduced silencing activity. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564	
+P06701	UniProtKB	Sequence conflict	74	74	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	331	331	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	335	335	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	405	405	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	421	421	.	.	.	Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	429	430	.	.	.	Note=NE->KK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	497	497	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	587	587	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	597	597	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	669	669	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	704	704	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	712	712	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	726	726	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	828	828	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	830	830	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Sequence conflict	925	925	.	.	.	Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P06701	UniProtKB	Beta strand	2	4	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FVU	
+P06701	UniProtKB	Helix	5	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KUI	
+P06701	UniProtKB	Beta strand	11	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Beta strand	18	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Beta strand	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KUI	
+P06701	UniProtKB	Beta strand	27	30	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TU4	
+P06701	UniProtKB	Turn	31	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TU4	
+P06701	UniProtKB	Beta strand	37	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Turn	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KUI	
+P06701	UniProtKB	Beta strand	55	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Turn	61	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Beta strand	65	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Beta strand	79	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TU4	
+P06701	UniProtKB	Beta strand	84	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Helix	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Helix	98	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Helix	107	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Helix	116	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Beta strand	131	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Helix	143	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Beta strand	146	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Beta strand	151	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Turn	155	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Beta strand	159	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN	
+P06701	UniProtKB	Turn	167	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Beta strand	170	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Turn	179	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KUD	
+P06701	UniProtKB	Beta strand	184	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KUI	
+P06701	UniProtKB	Helix	189	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Helix	201	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7	
+P06701	UniProtKB	Helix	465	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OWT	
+P06701	UniProtKB	Helix	535	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Beta strand	574	578	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	583	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Turn	599	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Beta strand	608	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	622	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	643	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	655	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Beta strand	660	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Beta strand	669	671	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	675	685	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Beta strand	691	696	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	704	708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	711	714	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Beta strand	717	721	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	727	741	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Beta strand	745	749	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Beta strand	755	757	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Beta strand	773	776	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	782	796	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	799	820	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Beta strand	831	833	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	837	843	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6	
+P06701	UniProtKB	Helix	851	856	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Helix	860	873	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Beta strand	874	876	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Beta strand	880	882	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Helix	883	896	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Helix	901	910	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Helix	920	923	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Helix	928	937	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Beta strand	940	945	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Beta strand	947	949	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Beta strand	952	956	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Helix	959	968	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+P06701	UniProtKB	Helix	970	972	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO	
+##sequence-region P34226 1 696
+P34226	UniProtKB	Chain	1	693	.	.	.	ID=PRO_0000071940;Note=Protein SKT5	
+P34226	UniProtKB	Propeptide	694	696	.	.	.	ID=PRO_0000396725;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34226	UniProtKB	Repeat	271	306	.	.	.	Note=Sel1-like 1	
+P34226	UniProtKB	Repeat	307	342	.	.	.	Note=Sel1-like 2	
+P34226	UniProtKB	Repeat	343	382	.	.	.	Note=Sel1-like 3	
+P34226	UniProtKB	Repeat	386	423	.	.	.	Note=Sel1-like 4	
+P34226	UniProtKB	Repeat	424	460	.	.	.	Note=Sel1-like 5	
+P34226	UniProtKB	Repeat	461	498	.	.	.	Note=Sel1-like 6	
+P34226	UniProtKB	Repeat	499	534	.	.	.	Note=Sel1-like 7	
+P34226	UniProtKB	Modified residue	148	148	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34226	UniProtKB	Modified residue	561	561	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P34226	UniProtKB	Modified residue	563	563	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34226	UniProtKB	Modified residue	564	564	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34226	UniProtKB	Modified residue	693	693	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34226	UniProtKB	Lipidation	693	693	.	.	.	Note=S-farnesyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34226	UniProtKB	Sequence conflict	350	350	.	.	.	Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P34226	UniProtKB	Sequence conflict	643	643	.	.	.	Note=Q->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q08457 1 257
+Q08457	UniProtKB	Chain	1	257	.	.	.	ID=PRO_0000237650;Note=Mitochondrial morphogenesis protein SLD7	
+Q08457	UniProtKB	Helix	182	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3X38	
+Q08457	UniProtKB	Helix	208	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3X38	
+Q08457	UniProtKB	Helix	224	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3X38	
+Q08457	UniProtKB	Helix	240	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3X38	
+##sequence-region P53304 1 468
+P53304	UniProtKB	Chain	1	468	.	.	.	ID=PRO_0000202846;Note=N-acetyltransferase SLI1	
+##sequence-region Q08581 1 821
+Q08581	UniProtKB	Chain	1	821	.	.	.	ID=PRO_0000270573;Note=Kinetochore protein SLK19	
+Q08581	UniProtKB	Coiled coil	310	821	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08581	UniProtKB	Site	77	78	.	.	.	Note=Cleavage%3B by ESP1	
+Q08581	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q08581	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08581	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08581	UniProtKB	Modified residue	201	201	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08581	UniProtKB	Modified residue	216	216	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q08581	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q08581	UniProtKB	Modified residue	283	283	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q08581	UniProtKB	Mutagenesis	77	77	.	.	.	Note=No cleavage by ESP1. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11533655;Dbxref=PMID:11533655	
+Q08581	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Destabilizes%3B not detectable in anaphase cells%3B spindle becomes thin and fragile. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11533655;Dbxref=PMID:11533655	
+##sequence-region Q12232 1 587
+Q12232	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12232	UniProtKB	Chain	22	587	.	.	.	ID=PRO_0000237659;Note=Uncharacterized protein SLP1	
+Q12232	UniProtKB	Topological domain	22	541	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23275891;Dbxref=PMID:23275891	
+Q12232	UniProtKB	Transmembrane	542	562	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12232	UniProtKB	Topological domain	563	587	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23275891;Dbxref=PMID:23275891	
+Q12232	UniProtKB	Domain	163	331	.	.	.	Note=SUN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00802	
+Q12232	UniProtKB	Glycosylation	25	25	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q12232	UniProtKB	Glycosylation	378	378	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q12232	UniProtKB	Glycosylation	381	381	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q12232	UniProtKB	Glycosylation	408	408	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q12232	UniProtKB	Glycosylation	448	448	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+Q12232	UniProtKB	Glycosylation	486	486	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+##sequence-region P32380 1 944
+P32380	UniProtKB	Chain	1	944	.	.	.	ID=PRO_0000057993;Note=Spindle pole body component 110	
+P32380	UniProtKB	Region	900	927	.	.	.	Note=Calmodulin-binding	
+P32380	UniProtKB	Coiled coil	164	791	.	.	.	.	
+P32380	UniProtKB	Motif	54	59	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32380	UniProtKB	Motif	726	731	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32380	UniProtKB	Motif	742	747	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32380	UniProtKB	Compositional bias	731	944	.	.	.	Note=Arg/Tyr-rich	
+P32380	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32380	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine%3B by MPS1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:11278681;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:11278681	
+P32380	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphothreonine%3B by MPS1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278681;Dbxref=PMID:11278681	
+P32380	UniProtKB	Modified residue	68	68	.	.	.	Note=Phosphothreonine%3B by MPS1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278681;Dbxref=PMID:11278681	
+P32380	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32380	UniProtKB	Modified residue	529	529	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32380	UniProtKB	Mutagenesis	91	91	.	.	.	Note=Leads to a mild increase in the proportion of preanaphase spindles at the expense of elongated spindles. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17213332;Dbxref=PMID:17213332	
+P32380	UniProtKB	Helix	901	933	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS7	
+##sequence-region P25582 1 841
+P25582	UniProtKB	Chain	1	841	.	.	.	ID=PRO_0000155604;Note=27S pre-rRNA (guanosine(2922)-2'-O)-methyltransferase	
+P25582	UniProtKB	Coiled coil	360	389	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163	
+P25582	UniProtKB	Compositional bias	704	841	.	.	.	Note=Lys-rich	
+P25582	UniProtKB	Active site	159	159	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163	
+P25582	UniProtKB	Binding site	58	58	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163	
+P25582	UniProtKB	Binding site	60	60	.	.	.	Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163	
+P25582	UniProtKB	Binding site	78	78	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163	
+P25582	UniProtKB	Binding site	94	94	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163	
+P25582	UniProtKB	Binding site	119	119	.	.	.	Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163	
+P25582	UniProtKB	Modified residue	455	455	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25582	UniProtKB	Modified residue	464	464	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25582	UniProtKB	Modified residue	529	529	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25582	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Abolishes methyltransferase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14636587;Dbxref=PMID:14636587	
+##sequence-region P38863 1 823
+P38863	UniProtKB	Chain	1	823	.	.	.	ID=PRO_0000078117;Note=Spindle pole body component SPC97	
+##sequence-region Q04398 1 127
+Q04398	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000072121;Note=Stationary phase protein 3	
+Q04398	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04398	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04398	UniProtKB	Compositional bias	23	87	.	.	.	Note=Phe-rich	
+Q04398	UniProtKB	Glycosylation	86	86	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P33419 1 253
+P33419	UniProtKB	Chain	1	253	.	.	.	ID=PRO_0000096846;Note=Spindle pole component 29	
+P33419	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P33419	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P33419	UniProtKB	Modified residue	240	240	.	.	.	Note=Phosphothreonine%3B by MPS1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19269975;Dbxref=PMID:19269975	
+P33419	UniProtKB	Mutagenesis	240	240	.	.	.	Note=Lead to defects in spindle pole body assembly. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19269975;Dbxref=PMID:19269975	
+##sequence-region Q06160 1 661
+Q06160	UniProtKB	Chain	1	661	.	.	.	ID=PRO_0000233011;Note=Protein SPH1	
+Q06160	UniProtKB	Sequence conflict	141	141	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06160	UniProtKB	Sequence conflict	281	281	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06160	UniProtKB	Sequence conflict	316	316	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06160	UniProtKB	Sequence conflict	377	378	.	.	.	Note=AS->TF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06160	UniProtKB	Sequence conflict	400	400	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06160	UniProtKB	Sequence conflict	431	431	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06160	UniProtKB	Sequence conflict	541	541	.	.	.	Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06160	UniProtKB	Sequence conflict	576	576	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06160	UniProtKB	Sequence conflict	580	580	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q06160	UniProtKB	Sequence conflict	651	651	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P23179 1 398
+P23179	UniProtKB	Chain	1	398	.	.	.	ID=PRO_0000145473;Note=Meiosis-specific protein SPO11	
+P23179	UniProtKB	Active site	135	135	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9121560;Dbxref=PMID:9121560	
+P23179	UniProtKB	Metal binding	233	233	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q57815	
+P23179	UniProtKB	Metal binding	288	288	.	.	.	Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q57815	
+P23179	UniProtKB	Mutagenesis	135	135	.	.	.	Note=Loss of activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9121560;Dbxref=PMID:9121560	
+##sequence-region P23624 1 291
+P23624	UniProtKB	Chain	1	291	.	.	.	ID=PRO_0000072134;Note=Meiosis-specific protein SPO13	
+P23624	UniProtKB	Motif	3	6	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03029 1 223
+Q03029	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03029	UniProtKB	Chain	21	198	.	.	.	ID=PRO_0000019590;Note=Sporulation-specific protein 19	
+Q03029	UniProtKB	Propeptide	199	223	.	.	.	ID=PRO_0000372457;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03029	UniProtKB	Compositional bias	116	121	.	.	.	Note=Poly-Glu	
+Q03029	UniProtKB	Lipidation	198	198	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40511 1 975
+P40511	UniProtKB	Chain	1	975	.	.	.	ID=PRO_0000072137;Note=Sporulation-specific protein 22	
+##sequence-region P45819 1 413
+P45819	UniProtKB	Chain	1	413	.	.	.	ID=PRO_0000072142;Note=Sporulation-specific protein 74	
+P45819	UniProtKB	Sequence conflict	328	328	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P18410 1 259
+P18410	UniProtKB	Chain	1	259	.	.	.	ID=PRO_0000072145;Note=Sporulation-specific protein SPO7	
+P18410	UniProtKB	Topological domain	1	72	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18410	UniProtKB	Transmembrane	73	93	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18410	UniProtKB	Topological domain	94	106	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18410	UniProtKB	Transmembrane	107	127	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P18410	UniProtKB	Topological domain	128	259	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38904 1 1435
+P38904	UniProtKB	Chain	1	1435	.	.	.	ID=PRO_0000072147;Note=Protein SPP41	
+P38904	UniProtKB	Domain	171	190	.	.	.	Note=UIM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213	
+P38904	UniProtKB	Motif	683	699	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38904	UniProtKB	Modified residue	1014	1014	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38904	UniProtKB	Modified residue	1067	1067	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38904	UniProtKB	Cross-link	981	981	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219	
+P38904	UniProtKB	Cross-link	1154	1154	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219	
+##sequence-region P32603 1 445
+P32603	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32603	UniProtKB	Chain	22	445	.	.	.	ID=PRO_0000007898;Note=Sporulation-specific glucan 1%2C3-beta-glucosidase	
+P32603	UniProtKB	Active site	233	233	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32603	UniProtKB	Active site	335	335	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32603	UniProtKB	Glycosylation	201	201	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P41901 1 512
+P41901	UniProtKB	Chain	1	512	.	.	.	ID=PRO_0000173502;Note=Sporulation-regulated protein 3	
+P41901	UniProtKB	Domain	106	365	.	.	.	Note=Septin-type G	
+P41901	UniProtKB	Nucleotide binding	116	123	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41901	UniProtKB	Nucleotide binding	247	255	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41901	UniProtKB	Coiled coil	376	406	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41901	UniProtKB	Coiled coil	451	496	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41901	UniProtKB	Binding site	168	168	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41901	UniProtKB	Binding site	315	315	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P41901	UniProtKB	Sequence conflict	26	26	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41901	UniProtKB	Sequence conflict	250	250	.	.	.	Note=L->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41901	UniProtKB	Sequence conflict	263	263	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41901	UniProtKB	Sequence conflict	317	317	.	.	.	Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P41901	UniProtKB	Sequence conflict	481	481	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32573 1 292
+P32573	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9268358;Dbxref=PMID:9268358	
+P32573	UniProtKB	Chain	2	292	.	.	.	ID=PRO_0000054565;Note=Peroxisomal 2%2C4-dienoyl-CoA reductase SPS19	
+P32573	UniProtKB	Nucleotide binding	29	53	.	.	.	Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32573	UniProtKB	Motif	290	292	.	.	.	Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32573	UniProtKB	Cross-link	188	188	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P08458 1 490
+P08458	UniProtKB	Chain	1	490	.	.	.	ID=PRO_0000086679;Note=Sporulation-specific protein 1	
+P08458	UniProtKB	Domain	18	272	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P08458	UniProtKB	Nucleotide binding	24	32	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P08458	UniProtKB	Active site	141	141	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P08458	UniProtKB	Binding site	47	47	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P08458	UniProtKB	Sequence conflict	454	454	.	.	.	Note=N->NVN;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08458	UniProtKB	Sequence conflict	469	469	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32558 1 1035
+P32558	UniProtKB	Chain	1	1035	.	.	.	ID=PRO_0000089448;Note=FACT complex subunit SPT16	
+P32558	UniProtKB	Coiled coil	208	234	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32558	UniProtKB	Coiled coil	636	666	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32558	UniProtKB	Coiled coil	959	983	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32558	UniProtKB	Compositional bias	958	1021	.	.	.	Note=Asp/Glu-rich (acidic)	
+P32558	UniProtKB	Modified residue	526	526	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32558	UniProtKB	Modified residue	765	765	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32558	UniProtKB	Mutagenesis	565	565	.	.	.	Note=In spt16-4%3B induces a spt phenotype characterized by depletion of many mRNAs%3B when associated with L-570. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11432837;Dbxref=PMID:11432837	
+P32558	UniProtKB	Mutagenesis	570	570	.	.	.	Note=In spt16-4%3B induces a spt phenotype characterized by depletion of many mRNAs%3B when associated with S-565. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11432837;Dbxref=PMID:11432837	
+P32558	UniProtKB	Mutagenesis	836	836	.	.	.	Note=In cdc68-1%3B induces a spt phenotype characterized by depletion of many mRNAs. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9832518;Dbxref=PMID:9832518	
+P32558	UniProtKB	Mutagenesis	848	850	.	.	.	Note=In spt16-7%3B induces a spt phenotype characterized by depletion of many mRNAs. TTD->IIY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11432837;Dbxref=PMID:11432837	
+P32558	UniProtKB	Mutagenesis	920	920	.	.	.	Note=In spt16-6%3B induces a spt phenotype characterized by depletion of many mRNAs. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11432837;Dbxref=PMID:11432837	
+P32558	UniProtKB	Helix	8	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	30	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	47	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	61	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	71	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	78	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	85	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIP	
+P32558	UniProtKB	Beta strand	99	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	110	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	129	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	142	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	161	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	166	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	178	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	214	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	224	226	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	228	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	250	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	253	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	277	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	283	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	292	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	301	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	311	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	338	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	354	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	365	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	369	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	375	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	378	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	393	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Turn	406	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIT	
+P32558	UniProtKB	Beta strand	412	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	431	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Helix	440	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ	
+P32558	UniProtKB	Beta strand	679	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	689	691	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	696	700	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	702	707	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Helix	712	714	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	717	720	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Helix	721	723	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	724	730	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	735	750	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	753	763	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Helix	790	818	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Turn	819	821	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	825	827	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Helix	830	832	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	834	841	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	843	847	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	849	854	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	856	859	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	861	864	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Helix	865	867	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	868	874	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	881	891	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	897	903	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Helix	904	906	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Helix	907	916	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Beta strand	921	923	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+P32558	UniProtKB	Helix	931	939	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY	
+##sequence-region P35210 1 1082
+P35210	UniProtKB	Chain	1	1082	.	.	.	ID=PRO_0000067076;Note=Protein SPT23	
+P35210	UniProtKB	Domain	508	585	.	.	.	Note=IPT/TIG	
+P35210	UniProtKB	Repeat	709	738	.	.	.	Note=ANK 1	
+P35210	UniProtKB	Repeat	742	771	.	.	.	Note=ANK 2	
+P35210	UniProtKB	Modified residue	468	468	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P35210	UniProtKB	Sequence conflict	715	715	.	.	.	Note=H->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32914 1 102
+P32914	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000210338;Note=Transcription elongation factor SPT4	
+P32914	UniProtKB	Zinc finger	7	27	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32914	UniProtKB	Mutagenesis	10	10	.	.	.	Note=Loss of function. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8649393;Dbxref=PMID:8649393	
+P32914	UniProtKB	Beta strand	4	7	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Turn	8	10	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Beta strand	12	15	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Helix	16	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Turn	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Helix	28	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Helix	39	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Beta strand	42	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Beta strand	46	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Turn	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Helix	59	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Beta strand	71	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+P32914	UniProtKB	Helix	84	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU	
+##sequence-region P53866 1 767
+P53866	UniProtKB	Chain	1	767	.	.	.	ID=PRO_0000203388;Note=Protein SQS1	
+P53866	UniProtKB	Domain	594	656	.	.	.	Note=R3H	
+P53866	UniProtKB	Domain	720	767	.	.	.	Note=G-patch;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00092	
+P53866	UniProtKB	Modified residue	105	105	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53866	UniProtKB	Modified residue	217	217	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53866	UniProtKB	Modified residue	255	255	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53866	UniProtKB	Modified residue	334	334	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53866	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53866	UniProtKB	Modified residue	345	345	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P25648 1 1427
+P25648	UniProtKB	Chain	1	1427	.	.	.	ID=PRO_0000072183;Note=Mediator of RNA polymerase II transcription subunit 12	
+##sequence-region P24276 1 1250
+P24276	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P24276	UniProtKB	Chain	2	1250	.	.	.	ID=PRO_0000166424;Note=Protein SSD1	
+P24276	UniProtKB	Compositional bias	60	67	.	.	.	Note=Poly-Gln	
+P24276	UniProtKB	Compositional bias	71	74	.	.	.	Note=Poly-Gln	
+P24276	UniProtKB	Compositional bias	135	141	.	.	.	Note=Poly-Asn	
+P24276	UniProtKB	Compositional bias	214	217	.	.	.	Note=Poly-Pro	
+P24276	UniProtKB	Compositional bias	527	530	.	.	.	Note=Poly-Glu	
+P24276	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P24276	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P24276	UniProtKB	Modified residue	164	164	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P24276	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P24276	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P24276	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P24276	UniProtKB	Modified residue	322	322	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P24276	UniProtKB	Modified residue	491	491	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P24276	UniProtKB	Modified residue	492	492	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P24276	UniProtKB	Modified residue	688	688	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P32343 1 579
+P32343	UniProtKB	Chain	1	579	.	.	.	ID=PRO_0000203153;Note=Protein SSH4	
+P32343	UniProtKB	Topological domain	1	44	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32343	UniProtKB	Transmembrane	45	65	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32343	UniProtKB	Topological domain	66	579	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32343	UniProtKB	Domain	166	364	.	.	.	Note=B30.2/SPRY;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00548	
+P32343	UniProtKB	Compositional bias	490	557	.	.	.	Note=Asn-rich	
+P32343	UniProtKB	Modified residue	358	358	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P32343	UniProtKB	Glycosylation	212	212	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32343	UniProtKB	Glycosylation	356	356	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32343	UniProtKB	Glycosylation	430	430	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32343	UniProtKB	Glycosylation	507	507	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32343	UniProtKB	Glycosylation	557	557	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32343	UniProtKB	Glycosylation	575	575	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32343	UniProtKB	Cross-link	367	367	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q02794 1 444
+Q02794	UniProtKB	Chain	1	444	.	.	.	ID=PRO_0000072260;Note=Protein STD1	
+Q02794	UniProtKB	Compositional bias	26	78	.	.	.	Note=Asn-rich	
+Q02794	UniProtKB	Sequence conflict	139	139	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06010 1 1027
+Q06010	UniProtKB	Chain	1	1027	.	.	.	ID=PRO_0000074418;Note=A-factor-processing enzyme	
+Q06010	UniProtKB	Active site	121	121	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096	
+Q06010	UniProtKB	Metal binding	118	118	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096	
+Q06010	UniProtKB	Metal binding	122	122	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096	
+Q06010	UniProtKB	Metal binding	199	199	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096	
+##sequence-region P15705 1 589
+P15705	UniProtKB	Chain	1	589	.	.	.	ID=PRO_0000106341;Note=Heat shock protein STI1	
+P15705	UniProtKB	Repeat	5	38	.	.	.	Note=TPR 1	
+P15705	UniProtKB	Repeat	40	73	.	.	.	Note=TPR 2	
+P15705	UniProtKB	Repeat	74	107	.	.	.	Note=TPR 3	
+P15705	UniProtKB	Domain	138	177	.	.	.	Note=STI1 1	
+P15705	UniProtKB	Repeat	262	295	.	.	.	Note=TPR 4	
+P15705	UniProtKB	Repeat	297	328	.	.	.	Note=TPR 5	
+P15705	UniProtKB	Repeat	336	369	.	.	.	Note=TPR 6	
+P15705	UniProtKB	Repeat	396	429	.	.	.	Note=TPR 7	
+P15705	UniProtKB	Repeat	430	463	.	.	.	Note=TPR 8	
+P15705	UniProtKB	Repeat	465	492	.	.	.	Note=TPR 9	
+P15705	UniProtKB	Domain	537	576	.	.	.	Note=STI1 2	
+P15705	UniProtKB	Modified residue	227	227	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P15705	UniProtKB	Cross-link	99	99	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P15705	UniProtKB	Cross-link	168	168	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P15705	UniProtKB	Cross-link	384	384	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P15705	UniProtKB	Helix	133	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV	
+P15705	UniProtKB	Beta strand	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV	
+P15705	UniProtKB	Helix	142	147	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV	
+P15705	UniProtKB	Helix	152	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV	
+P15705	UniProtKB	Helix	160	169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV	
+P15705	UniProtKB	Helix	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV	
+P15705	UniProtKB	Turn	178	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV	
+P15705	UniProtKB	Helix	182	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV	
+P15705	UniProtKB	Turn	193	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV	
+P15705	UniProtKB	Helix	262	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3	
+P15705	UniProtKB	Helix	278	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3	
+P15705	UniProtKB	Helix	296	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3	
+P15705	UniProtKB	Helix	311	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3	
+P15705	UniProtKB	Helix	332	348	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3	
+P15705	UniProtKB	Helix	352	365	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3	
+P15705	UniProtKB	Helix	369	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3	
+P15705	UniProtKB	Helix	395	408	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV	
+P15705	UniProtKB	Helix	412	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV	
+P15705	UniProtKB	Helix	430	442	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV	
+P15705	UniProtKB	Helix	446	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV	
+P15705	UniProtKB	Helix	464	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV	
+P15705	UniProtKB	Helix	480	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV	
+P15705	UniProtKB	Turn	499	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV	
+P15705	UniProtKB	Helix	503	516	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV	
+P15705	UniProtKB	Helix	527	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLW	
+P15705	UniProtKB	Helix	538	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLW	
+P15705	UniProtKB	Helix	548	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLW	
+P15705	UniProtKB	Helix	560	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLW	
+P15705	UniProtKB	Helix	570	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLW	
+##sequence-region P38960 1 494
+P38960	UniProtKB	Chain	1	494	.	.	.	ID=PRO_0000072279;Note=Protein STN1	
+P38960	UniProtKB	DNA binding	62	159	.	.	.	Note=OB	
+P38960	UniProtKB	Region	311	397	.	.	.	Note=Winged helix-turn-helix (wHTH) 1	
+P38960	UniProtKB	Region	396	494	.	.	.	Note=Winged helix-turn-helix (wHTH) 2	
+P38960	UniProtKB	Mutagenesis	397	397	.	.	.	Note=Modest telomere elongation phenotype. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20008938;Dbxref=PMID:20008938	
+P38960	UniProtKB	Mutagenesis	466	466	.	.	.	Note=Elongated telomeres. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20008938;Dbxref=PMID:20008938	
+P38960	UniProtKB	Mutagenesis	466	466	.	.	.	Note=Elongated telomeres and severe growth defects. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20008938;Dbxref=PMID:20008938	
+P38960	UniProtKB	Helix	315	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Beta strand	326	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Helix	333	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Helix	340	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Helix	365	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Beta strand	385	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Turn	391	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Beta strand	395	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Helix	399	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Beta strand	421	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Helix	427	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Helix	441	458	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Turn	460	462	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Beta strand	463	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Beta strand	482	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+P38960	UniProtKB	Turn	491	493	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY	
+##sequence-region Q00947 1 519
+Q00947	UniProtKB	Zinc finger	160	182	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q00947	UniProtKB	Zinc finger	188	223	.	.	.	Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q00947	UniProtKB	Zinc finger	240	265	.	.	.	Note=C2H2-type 3%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q00947	UniProtKB	Region	16	35	.	.	.	Note=I	
+Q00947	UniProtKB	Region	65	97	.	.	.	Note=II	
+Q00947	UniProtKB	Mutagenesis	9	66	.	.	.	Note=In ASI13-1%3B dominant active and constitutively nuclear localized transcription factor. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502738;Dbxref=PMID:12502738	
+Q00947	UniProtKB	Mutagenesis	27	32	.	.	.	Note=In STP1-133%3B impairs cytoplasmic retention%2C resulting in a dominant active transcription factor. Activates transcription also in its unprocessed form%3B when associated with A-66. LVSGVI->AASGAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15314160;Dbxref=PMID:15314160	
+Q00947	UniProtKB	Mutagenesis	65	65	.	.	.	Note=No effect. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15314160;Dbxref=PMID:15314160	
+Q00947	UniProtKB	Mutagenesis	66	66	.	.	.	Note=In STP1-102%3B prevents proteolytic processing. Activates transcription also in its unprocessed form%3B when associated with 27-AASGAA-32. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15314160;Dbxref=PMID:15314160	
+Q00947	UniProtKB	Mutagenesis	67	67	.	.	.	Note=No effect. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15314160;Dbxref=PMID:15314160	
+##sequence-region P38989 1 1170
+P38989	UniProtKB	Chain	1	1170	.	.	.	ID=PRO_0000119013;Note=Structural maintenance of chromosomes protein 2	
+P38989	UniProtKB	Nucleotide binding	32	39	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38989	UniProtKB	Region	470	677	.	.	.	Note=Flexible hinge	
+P38989	UniProtKB	Coiled coil	172	469	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38989	UniProtKB	Coiled coil	678	1027	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38989	UniProtKB	Compositional bias	1084	1119	.	.	.	Note=Ala/Asp-rich (DA-box)	
+P38989	UniProtKB	Helix	455	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	473	495	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	498	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Beta strand	523	526	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	527	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	536	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	541	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	549	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Beta strand	555	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	560	568	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Beta strand	576	580	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Turn	581	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	591	600	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Beta strand	604	607	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	608	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	616	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	619	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Beta strand	629	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	635	642	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Beta strand	650	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Turn	654	656	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Beta strand	657	660	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Turn	661	663	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Beta strand	664	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	676	705	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Turn	706	711	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	714	721	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Turn	722	726	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+P38989	UniProtKB	Helix	727	734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI	
+##sequence-region P14359 1 133
+P14359	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000193990;Note=Protein SNA3	
+P14359	UniProtKB	Topological domain	1	16	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14359	UniProtKB	Transmembrane	17	37	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14359	UniProtKB	Topological domain	38	48	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14359	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14359	UniProtKB	Topological domain	70	133	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P14359	UniProtKB	Cross-link	125	125	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P38839 1 148
+P38839	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000202920;Note=Putative cyclin-dependent kinase inhibitor SPL2	
+P38839	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38839	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P38839	UniProtKB	Sequence conflict	58	58	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P35184 1 431
+P35184	UniProtKB	Chain	1	431	.	.	.	ID=PRO_0000051227;Note=Ribosome assembly protein SQT1	
+P35184	UniProtKB	Repeat	63	102	.	.	.	Note=WD 1	
+P35184	UniProtKB	Repeat	107	146	.	.	.	Note=WD 2	
+P35184	UniProtKB	Repeat	149	192	.	.	.	Note=WD 3	
+P35184	UniProtKB	Repeat	199	243	.	.	.	Note=WD 4	
+P35184	UniProtKB	Repeat	309	348	.	.	.	Note=WD 5	
+P35184	UniProtKB	Repeat	350	387	.	.	.	Note=WD 6	
+P35184	UniProtKB	Beta strand	58	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	68	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	75	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	89	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	101	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	112	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	121	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	131	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Helix	140	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	144	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	157	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	164	166	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	169	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	179	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Turn	186	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	191	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	204	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	220	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	230	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Turn	235	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	240	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Helix	246	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Turn	249	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	256	261	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Helix	264	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Turn	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	273	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	281	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Turn	288	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	294	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AMS	
+P35184	UniProtKB	Helix	309	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	314	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Turn	321	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	325	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	333	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Turn	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	345	350	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	355	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	364	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	374	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Turn	379	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	384	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	395	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	413	419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+P35184	UniProtKB	Beta strand	424	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX	
+##sequence-region Q12516 1 437
+Q12516	UniProtKB	Chain	1	437	.	.	.	ID=PRO_0000240873;Note=Regulator of phospholipase D SRF1	
+Q12516	UniProtKB	Topological domain	1	267	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12516	UniProtKB	Transmembrane	268	288	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12516	UniProtKB	Topological domain	289	308	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12516	UniProtKB	Transmembrane	309	329	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12516	UniProtKB	Topological domain	330	348	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12516	UniProtKB	Transmembrane	349	369	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12516	UniProtKB	Topological domain	370	403	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12516	UniProtKB	Transmembrane	404	424	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12516	UniProtKB	Topological domain	425	437	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12516	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q12516	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12516	UniProtKB	Glycosylation	297	297	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12516	UniProtKB	Glycosylation	385	385	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12020 1 392
+Q12020	UniProtKB	Chain	1	392	.	.	.	ID=PRO_0000270577;Note=Protein SRL2	
+Q12020	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12020	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P36167 1 246
+P36167	UniProtKB	Chain	1	246	.	.	.	ID=PRO_0000203228;Note=Protein SRL3	
+P36167	UniProtKB	Modified residue	212	212	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P25567 1 434
+P25567	UniProtKB	Chain	1	434	.	.	.	ID=PRO_0000207615;Note=RNA-binding protein SRO9	
+P25567	UniProtKB	Domain	255	351	.	.	.	Note=HTH La-type RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00332	
+P25567	UniProtKB	Compositional bias	168	171	.	.	.	Note=Poly-Gln	
+P25567	UniProtKB	Compositional bias	174	184	.	.	.	Note=His-rich	
+P25567	UniProtKB	Compositional bias	222	226	.	.	.	Note=Poly-Asn	
+P25567	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25567	UniProtKB	Modified residue	148	148	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25567	UniProtKB	Modified residue	422	422	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P25567	UniProtKB	Cross-link	156	156	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25567	UniProtKB	Cross-link	301	301	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25567	UniProtKB	Cross-link	342	342	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P25567	UniProtKB	Cross-link	352	352	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P20424 1 541
+P20424	UniProtKB	Chain	1	541	.	.	.	ID=PRO_0000101203;Note=Signal recognition particle subunit SRP54	
+P20424	UniProtKB	Nucleotide binding	116	123	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20424	UniProtKB	Nucleotide binding	198	202	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20424	UniProtKB	Nucleotide binding	256	259	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P20424	UniProtKB	Region	1	303	.	.	.	Note=G-domain	
+P20424	UniProtKB	Region	304	541	.	.	.	Note=M-domain	
+P20424	UniProtKB	Sequence conflict	136	136	.	.	.	Note=R->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36077 1 127
+P36077	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000211435;Note=Sulfiredoxin	
+P36077	UniProtKB	Disulfide bond	84	84	.	.	.	Note=Interchain (with C-48 in TSA1)%3B transient;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14586471;Dbxref=PMID:14586471	
+P36077	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Minor effect on formation of disulfide bond with TSA1 and reduction of cysteine-sulfinic acid. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14586471;Dbxref=PMID:14586471	
+P36077	UniProtKB	Mutagenesis	84	84	.	.	.	Note=Abolishes formation of disulfide bond with TSA1 and reduction of cysteine-sulfinic acid. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14586471;Dbxref=PMID:14586471	
+P36077	UniProtKB	Mutagenesis	106	106	.	.	.	Note=No effect on formation of disulfide bond with TSA1 and reduction of cysteine-sulfinic acid. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14586471;Dbxref=PMID:14586471	
+##sequence-region Q08646 1 371
+Q08646	UniProtKB	Chain	1	371	.	.	.	ID=PRO_0000072217;Note=Sporulation-specific protein 2	
+Q08646	UniProtKB	Natural variant	62	62	.	.	.	Note=In strain: SK1. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12073037;Dbxref=PMID:12073037	
+Q08646	UniProtKB	Natural variant	88	88	.	.	.	Note=In strain: SK1. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12073037;Dbxref=PMID:12073037	
+##sequence-region P42845 1 420
+P42845	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P42845	UniProtKB	Chain	2	420	.	.	.	ID=PRO_0000072251;Note=Protein STB1	
+P42845	UniProtKB	Region	2	70	.	.	.	Note=Interaction with SWI6	
+P42845	UniProtKB	Compositional bias	156	159	.	.	.	Note=Poly-Asn	
+P42845	UniProtKB	Compositional bias	165	169	.	.	.	Note=Poly-Asn	
+P42845	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P42845	UniProtKB	Modified residue	7	7	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P42845	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P42845	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P42845	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P42845	UniProtKB	Modified residue	419	419	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P38699 1 743
+P38699	UniProtKB	Chain	1	743	.	.	.	ID=PRO_0000114978;Note=Protein STB5	
+P38699	UniProtKB	DNA binding	22	49	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P32584 1 239
+P32584	UniProtKB	Chain	1	239	.	.	.	ID=PRO_0000209899;Note=Protein-S-isoprenylcysteine O-methyltransferase	
+P32584	UniProtKB	Topological domain	1	23	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32584	UniProtKB	Transmembrane	24	44	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32584	UniProtKB	Topological domain	45	47	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32584	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32584	UniProtKB	Topological domain	69	88	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32584	UniProtKB	Transmembrane	89	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32584	UniProtKB	Topological domain	110	110	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32584	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32584	UniProtKB	Topological domain	132	182	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32584	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32584	UniProtKB	Topological domain	204	239	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03497 1 939
+Q03497	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03497	UniProtKB	Chain	2	939	.	.	.	ID=PRO_0000086686;Note=Serine/threonine-protein kinase STE20	
+Q03497	UniProtKB	Domain	337	350	.	.	.	Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057	
+Q03497	UniProtKB	Domain	620	871	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03497	UniProtKB	Nucleotide binding	626	634	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03497	UniProtKB	Region	434	499	.	.	.	Note=BEM1-binding	
+Q03497	UniProtKB	Active site	739	739	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q03497	UniProtKB	Binding site	649	649	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03497	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03497	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03497	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03497	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03497	UniProtKB	Modified residue	169	169	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:16428446;Dbxref=PMID:17330950,PMID:19779198,PMID:16428446	
+Q03497	UniProtKB	Modified residue	203	203	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03497	UniProtKB	Modified residue	418	418	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16428446;Dbxref=PMID:16428446	
+Q03497	UniProtKB	Modified residue	502	502	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03497	UniProtKB	Modified residue	547	547	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10359756;Dbxref=PMID:19779198,PMID:10359756	
+Q03497	UniProtKB	Modified residue	562	562	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10359756;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198,PMID:10359756	
+Q03497	UniProtKB	Modified residue	573	573	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10359756;Dbxref=PMID:10359756	
+Q03497	UniProtKB	Modified residue	585	585	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000269|PubMed:10359756,ECO:0000269|PubMed:16428446;Dbxref=PMID:17330950,PMID:10359756,PMID:16428446	
+Q03497	UniProtKB	Modified residue	773	773	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10359756;Dbxref=PMID:10359756	
+Q03497	UniProtKB	Modified residue	924	924	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03497	UniProtKB	Modified residue	927	927	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03497	UniProtKB	Mutagenesis	338	338	.	.	.	Note=Reduces interaction with CDC42. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11940652;Dbxref=PMID:11940652	
+Q03497	UniProtKB	Mutagenesis	345	345	.	.	.	Note=Reduces interaction with CDC42. H->A%2CD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11940652,ECO:0000269|PubMed:12586692;Dbxref=PMID:11940652,PMID:12586692	
+Q03497	UniProtKB	Mutagenesis	348	348	.	.	.	Note=Reduces interaction with CDC42. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12586692;Dbxref=PMID:12586692	
+Q03497	UniProtKB	Mutagenesis	475	475	.	.	.	Note=Impairs interaction with BEM1%3B when associated with A-477. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15743816;Dbxref=PMID:15743816	
+Q03497	UniProtKB	Mutagenesis	477	477	.	.	.	Note=Impairs interaction with BEM1%3B when associated with G-475. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15743816;Dbxref=PMID:15743816	
+Q03497	UniProtKB	Mutagenesis	649	649	.	.	.	Note=Impairs phosphorylation of STE11 and histone H2B and mating efficiency. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15652479,ECO:0000269|PubMed:7608157;Dbxref=PMID:15652479,PMID:7608157	
+Q03497	UniProtKB	Mutagenesis	777	777	.	.	.	Note=Impairs autophosphorylation and mating efficiency. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7608157;Dbxref=PMID:7608157	
+Q03497	UniProtKB	Sequence conflict	19	19	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03497	UniProtKB	Sequence conflict	134	134	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q03497	UniProtKB	Sequence conflict	271	271	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P06783 1 470
+P06783	UniProtKB	Chain	1	470	.	.	.	ID=PRO_0000195079;Note=Pheromone a factor receptor	
+P06783	UniProtKB	Topological domain	1	5	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Transmembrane	6	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Topological domain	24	29	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Transmembrane	30	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Topological domain	54	70	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Transmembrane	71	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Topological domain	99	116	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Transmembrane	117	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Topological domain	135	155	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Transmembrane	156	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Topological domain	184	205	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Transmembrane	206	228	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Topological domain	229	266	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Transmembrane	267	285	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Topological domain	286	470	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P06783	UniProtKB	Region	300	470	.	.	.	Note=Hydrophilic	
+##sequence-region P32917 1 917
+P32917	UniProtKB	Chain	1	917	.	.	.	ID=PRO_0000072266;Note=Protein STE5	
+P32917	UniProtKB	Compositional bias	775	876	.	.	.	Note=Asp/Glu-rich (acidic)	
+P32917	UniProtKB	Modified residue	329	329	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P32917	UniProtKB	Sequence conflict	331	332	.	.	.	Note=LG->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32917	UniProtKB	Sequence conflict	341	343	.	.	.	Note=NSI->TLS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32917	UniProtKB	Sequence conflict	821	821	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32917	UniProtKB	Helix	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN	
+P32917	UniProtKB	Helix	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN	
+P32917	UniProtKB	Turn	52	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN	
+P32917	UniProtKB	Helix	55	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN	
+P32917	UniProtKB	Helix	59	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN	
+P32917	UniProtKB	Turn	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN	
+P32917	UniProtKB	Helix	593	604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Beta strand	608	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Helix	618	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Beta strand	622	624	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F2H	
+P32917	UniProtKB	Helix	625	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Beta strand	645	650	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Beta strand	653	660	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Helix	661	664	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Helix	668	672	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Helix	673	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Helix	685	692	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Beta strand	701	707	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Turn	713	715	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Helix	717	719	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Helix	723	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Beta strand	735	741	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Turn	748	750	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F2H	
+P32917	UniProtKB	Beta strand	755	758	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+P32917	UniProtKB	Helix	760	770	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE	
+##sequence-region P12866 1 1290
+P12866	UniProtKB	Chain	1	1290	.	.	.	ID=PRO_0000093370;Note=Alpha-factor-transporting ATPase	
+P12866	UniProtKB	Topological domain	1	25	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	26	46	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	47	75	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	97	150	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	151	171	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	172	173	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	195	262	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	263	283	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	284	296	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	297	317	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	318	715	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	716	736	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	737	763	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	764	784	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	785	838	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	839	859	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	860	865	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	866	886	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	887	945	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	946	966	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	967	981	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Transmembrane	982	1002	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Topological domain	1003	1290	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12866	UniProtKB	Domain	27	319	.	.	.	Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P12866	UniProtKB	Domain	357	603	.	.	.	Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P12866	UniProtKB	Domain	717	1007	.	.	.	Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441	
+P12866	UniProtKB	Domain	1052	1287	.	.	.	Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P12866	UniProtKB	Nucleotide binding	392	399	.	.	.	Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P12866	UniProtKB	Nucleotide binding	1087	1094	.	.	.	Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434	
+P12866	UniProtKB	Glycosylation	61	61	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P12866	UniProtKB	Cross-link	1022	1022	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+P12866	UniProtKB	Mutagenesis	392	392	.	.	.	Note=0.8%25 mating activity. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899	
+P12866	UniProtKB	Mutagenesis	398	398	.	.	.	Note=25%25 mating activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899	
+P12866	UniProtKB	Mutagenesis	398	398	.	.	.	Note=1%25 mating activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899	
+P12866	UniProtKB	Mutagenesis	509	509	.	.	.	Note=0.5%25 mating activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899	
+P12866	UniProtKB	Mutagenesis	1087	1087	.	.	.	Note=0.3%25 mating activity. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899	
+P12866	UniProtKB	Mutagenesis	1093	1093	.	.	.	Note=26%25 mating activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899	
+P12866	UniProtKB	Mutagenesis	1093	1093	.	.	.	Note=15%25 mating activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899	
+P12866	UniProtKB	Mutagenesis	1193	1193	.	.	.	Note=6%25 mating activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899	
+##sequence-region P06784 1 515
+P06784	UniProtKB	Chain	1	515	.	.	.	ID=PRO_0000086688;Note=Serine/threonine-protein kinase STE7	
+P06784	UniProtKB	Domain	191	466	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06784	UniProtKB	Nucleotide binding	197	205	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06784	UniProtKB	Active site	331	331	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P06784	UniProtKB	Binding site	220	220	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P06784	UniProtKB	Modified residue	359	359	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8131746;Dbxref=PMID:8131746	
+P06784	UniProtKB	Modified residue	363	363	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8131746;Dbxref=PMID:8131746	
+P06784	UniProtKB	Mutagenesis	353	353	.	.	.	Note=No loss of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8131746;Dbxref=PMID:8131746	
+P06784	UniProtKB	Mutagenesis	359	359	.	.	.	Note=Inactivation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8131746;Dbxref=PMID:8131746	
+P06784	UniProtKB	Mutagenesis	363	363	.	.	.	Note=Inactivation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8131746;Dbxref=PMID:8131746	
+##sequence-region P39932 1 569
+P39932	UniProtKB	Chain	1	569	.	.	.	ID=PRO_0000050461;Note=Sugar transporter STL1	
+P39932	UniProtKB	Topological domain	1	29	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	30	50	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	51	79	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	101	107	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	108	128	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	129	129	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	130	150	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	151	168	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	169	189	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	190	203	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	204	224	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	225	291	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	292	312	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	313	330	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	331	351	.	.	.	Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	352	358	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	359	379	.	.	.	Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	380	389	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	390	410	.	.	.	Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	411	426	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	427	447	.	.	.	Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	448	453	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Transmembrane	454	474	.	.	.	Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Topological domain	475	569	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Glycosylation	197	197	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Glycosylation	319	319	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39932	UniProtKB	Sequence conflict	237	237	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P09959 1 803
+P09959	UniProtKB	Chain	1	803	.	.	.	ID=PRO_0000067071;Note=Regulatory protein SWI6	
+P09959	UniProtKB	Repeat	318	346	.	.	.	Note=ANK 1	
+P09959	UniProtKB	Repeat	347	383	.	.	.	Note=ANK 2	
+P09959	UniProtKB	Repeat	384	469	.	.	.	Note=ANK 3	
+P09959	UniProtKB	Repeat	470	498	.	.	.	Note=ANK 4	
+P09959	UniProtKB	Repeat	499	514	.	.	.	Note=ANK 5	
+P09959	UniProtKB	Compositional bias	631	640	.	.	.	Note=Glu-rich (acidic)	
+P09959	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P09959	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000269|PubMed:14993267;Dbxref=PMID:17287358,PMID:14993267	
+P09959	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P09959	UniProtKB	Modified residue	179	179	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P09959	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P09959	UniProtKB	Modified residue	547	547	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P09959	UniProtKB	Beta strand	3	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Beta strand	16	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Turn	24	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Beta strand	29	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Helix	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Helix	35	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Helix	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Helix	58	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Beta strand	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Helix	84	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Turn	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Helix	101	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Beta strand	104	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV	
+P09959	UniProtKB	Beta strand	214	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Turn	225	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	244	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	292	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	321	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	331	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	354	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	363	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	370	377	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	378	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	391	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	405	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	422	424	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Beta strand	427	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	448	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	455	461	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Turn	462	464	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	473	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	483	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+P09959	UniProtKB	Helix	506	509	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6	
+##sequence-region P46655 1 708
+P46655	UniProtKB	Chain	1	708	.	.	.	ID=PRO_0000119739;Note=Glutamate--tRNA ligase%2C cytoplasmic	
+P46655	UniProtKB	Nucleotide binding	437	441	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46655	UniProtKB	Region	106	115	.	.	.	Note=Interaction with ARC1	
+P46655	UniProtKB	Region	141	157	.	.	.	Note=Interaction with ARC1	
+P46655	UniProtKB	Region	205	207	.	.	.	Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46655	UniProtKB	Region	382	386	.	.	.	Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46655	UniProtKB	Motif	210	219	.	.	.	Note="HIGH" region	
+P46655	UniProtKB	Motif	437	441	.	.	.	Note="KMSKS" region	
+P46655	UniProtKB	Binding site	215	215	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46655	UniProtKB	Binding site	241	241	.	.	.	Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46655	UniProtKB	Binding site	400	400	.	.	.	Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46655	UniProtKB	Binding site	403	403	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P46655	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46655	UniProtKB	Mutagenesis	148	148	.	.	.	Note=Abolishes interaction with ARC1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16914447;Dbxref=PMID:16914447	
+P46655	UniProtKB	Sequence conflict	209	209	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46655	UniProtKB	Sequence conflict	473	473	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46655	UniProtKB	Sequence conflict	510	510	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46655	UniProtKB	Sequence conflict	546	546	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46655	UniProtKB	Beta strand	3	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Helix	16	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Beta strand	32	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Beta strand	41	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSM	
+P46655	UniProtKB	Beta strand	45	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Helix	55	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Turn	63	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Helix	72	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Turn	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Helix	91	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Turn	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRK	
+P46655	UniProtKB	Helix	119	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Helix	134	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Helix	144	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Helix	157	160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+P46655	UniProtKB	Helix	162	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA	
+##sequence-region P53277 1 215
+P53277	UniProtKB	Chain	1	215	.	.	.	ID=PRO_0000072381;Note=Pre-mRNA-splicing factor SYF2	
+P53277	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53277	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53277	UniProtKB	Modified residue	125	125	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53277	UniProtKB	Helix	97	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53277	UniProtKB	Beta strand	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53277	UniProtKB	Helix	161	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+P53277	UniProtKB	Helix	198	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P11972 1 698
+P11972	UniProtKB	Chain	1	698	.	.	.	ID=PRO_0000204173;Note=Protein SST2	
+P11972	UniProtKB	Domain	273	358	.	.	.	Note=DEP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00066	
+P11972	UniProtKB	Domain	420	689	.	.	.	Note=RGS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00171	
+P11972	UniProtKB	Region	10	203	.	.	.	Note=Fungal-DR	
+P11972	UniProtKB	Modified residue	252	252	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P11972	UniProtKB	Modified residue	408	408	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P11972	UniProtKB	Modified residue	539	539	.	.	.	Note=Phosphoserine%3B by MAPK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10593933;Dbxref=PMID:10593933	
+P11972	UniProtKB	Modified residue	587	587	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P11972	UniProtKB	Sequence conflict	616	616	.	.	.	Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11972	UniProtKB	Sequence conflict	644	644	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P41930 1 458
+P41930	UniProtKB	Chain	1	458	.	.	.	ID=PRO_0000072229;Note=Sulfite efflux pump SSU1	
+P41930	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Topological domain	33	48	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Transmembrane	49	69	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Topological domain	70	89	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Topological domain	111	135	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Topological domain	157	176	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Transmembrane	177	197	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Topological domain	198	220	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Transmembrane	221	241	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Topological domain	242	252	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Transmembrane	253	275	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Topological domain	276	309	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Transmembrane	310	330	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Topological domain	331	350	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Transmembrane	351	371	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Topological domain	372	387	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Transmembrane	388	408	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Topological domain	409	458	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41930	UniProtKB	Modified residue	444	444	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P41930	UniProtKB	Modified residue	448	448	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P41930	UniProtKB	Modified residue	450	450	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P41930	UniProtKB	Natural variant	19	19	.	.	.	Note=In strain: Ba194%2C CECT 10233%2C M5-7A%2C M5-7B%2C M7-8D%2C MMR2-1%2C MMR2-3%2C MMW1-12%2C ORM1-1%2C Sgu52E%2C Y-9%2C YPS396%2C YPS400%2C YPS598%2C YPS600%2C YPS602%2C YPS604%2C YPS606%2C YPS608 and YPS610. M->V	
+P41930	UniProtKB	Natural variant	52	52	.	.	.	Note=In strain: ATCC 76625 / YPH499%2C Ba194%2C Bb32%2C M1-2A%2C M2-8%2C M5-7A%2C M5-7B%2C M7-8D%2C MMR2-1%2C MMR2-3%2C MMR2-5%2C MMW1-15%2C MMW1-15h2%2C MMW1-2%2C MMW1-2h2%2C MMW1-12%2C ORM1-1%2C S288c/ YPH1%2C Sgu52E%2C Sgu52F%2C Y-9%2C YPS396%2C YPS400%2C YPS598%2C YPS600%2C YPS602%2C YPS604%2C YPS606%2C YPS608 and YPS610. A->T	
+P41930	UniProtKB	Natural variant	90	90	.	.	.	Note=In strain: Ba194%2C Bb32%2C M1-2A%2C M2-8%2C M5-7A%2C M5-7B%2C M7-8D%2C MMR2-5%2C MMW1-15h2%2C MMW1-2h2%2C Sgu52E%2C Sgu52F and Y-9. N->S	
+P41930	UniProtKB	Natural variant	122	122	.	.	.	Note=In strain: Bb32%2C M1-2A%2C M2-8%2C MMR2-5%2C MMW1-15h2%2C MMW1-2h2 and Sgu52F. A->S	
+P41930	UniProtKB	Natural variant	157	157	.	.	.	Note=In strain: Ba194%2C Bb32%2C M1-2A%2C M2-8%2C M5-7A%2C M5-7B%2C M7-8D%2C MMR2-1%2C MMR2-3%2C MMR2-5%2C MMW1-12%2C MMW1-15h2%2C MMW1-2h2%2C ORM1-1%2C Sgu52E%2C Sgu52F%2C Y-9%2C YPS396%2C YPS400%2C YPS598%2C YPS600%2C YPS602%2C YPS604%2C YPS606%2C YPS608 and YPS610. P->S	
+P41930	UniProtKB	Natural variant	164	164	.	.	.	Note=In strain: Bb32%2C M1-2A%2C M2-8%2C MMR2-5%2C MMW1-15h2%2C MMW1-2h2 and Sgu52F. Y->H	
+P41930	UniProtKB	Natural variant	191	191	.	.	.	Note=In strain: ATCC 76625 / YPH499%2CMMW1-15%2C MMW1-2 and S288c / YPH1. A->T	
+P41930	UniProtKB	Natural variant	344	344	.	.	.	Note=In strain: Sgu52F. G->E	
+P41930	UniProtKB	Natural variant	345	345	.	.	.	Note=In strain: ATCC 76625 / YPH499%2C MMW1-15 and MMW1-2. K->R	
+##sequence-region P50104 1 949
+P50104	UniProtKB	Chain	1	949	.	.	.	ID=PRO_0000114980;Note=Probable transcriptional regulatory protein STB4	
+P50104	UniProtKB	DNA binding	87	113	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+##sequence-region P53394 1 754
+P53394	UniProtKB	Chain	1	754	.	.	.	ID=PRO_0000080192;Note=Putative sulfate transporter YPR003C	
+P53394	UniProtKB	Topological domain	1	118	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	140	146	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	147	167	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	168	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	194	199	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	200	220	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	221	232	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	233	253	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	254	282	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	283	303	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	304	317	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	318	338	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	339	370	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	371	391	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	392	410	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	411	431	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	432	450	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	451	471	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	472	474	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	475	495	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	496	517	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Transmembrane	518	538	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Topological domain	539	754	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53394	UniProtKB	Domain	574	725	.	.	.	Note=STAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00198	
+##sequence-region P08153 1 709
+P08153	UniProtKB	Chain	1	709	.	.	.	ID=PRO_0000046855;Note=Transcriptional factor SWI5	
+P08153	UniProtKB	Zinc finger	550	574	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P08153	UniProtKB	Zinc finger	580	604	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P08153	UniProtKB	Zinc finger	609	632	.	.	.	Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P08153	UniProtKB	DNA binding	647	659	.	.	.	Note=A.T hook	
+P08153	UniProtKB	Motif	635	659	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08153	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08153	UniProtKB	Modified residue	278	278	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08153	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08153	UniProtKB	Modified residue	339	339	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08153	UniProtKB	Modified residue	376	376	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08153	UniProtKB	Modified residue	488	488	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P08153	UniProtKB	Modified residue	492	492	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P08153	UniProtKB	Modified residue	505	505	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956	
+P08153	UniProtKB	Modified residue	522	522	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:1652372;Dbxref=PMID:19779198,PMID:1652372	
+P08153	UniProtKB	Modified residue	646	646	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000269|PubMed:1652372;Dbxref=PMID:17287358,PMID:1652372	
+P08153	UniProtKB	Modified residue	664	664	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1652372;Dbxref=PMID:1652372	
+P08153	UniProtKB	Mutagenesis	522	522	.	.	.	Note=Constitutive nuclear entry%3B when associated with A-646 and A-664. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1652372;Dbxref=PMID:1652372	
+P08153	UniProtKB	Mutagenesis	646	646	.	.	.	Note=Constitutive nuclear entry%3B when associated with A-522 and A-664. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1652372;Dbxref=PMID:1652372	
+P08153	UniProtKB	Mutagenesis	664	664	.	.	.	Note=Constitutive nuclear entry%3B when associated with A-522 and A-646. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1652372;Dbxref=PMID:1652372	
+P08153	UniProtKB	Sequence conflict	514	514	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08153	UniProtKB	Helix	538	540	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS	
+P08153	UniProtKB	Beta strand	543	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS	
+P08153	UniProtKB	Turn	546	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS	
+P08153	UniProtKB	Beta strand	549	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS	
+P08153	UniProtKB	Beta strand	563	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS	
+P08153	UniProtKB	Helix	567	574	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS	
+P08153	UniProtKB	Turn	575	577	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS	
+P08153	UniProtKB	Beta strand	591	594	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZFD	
+P08153	UniProtKB	Helix	595	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZFD	
+P08153	UniProtKB	Helix	602	604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZFD	
+##sequence-region Q12379 1 170
+Q12379	UniProtKB	Chain	1	170	.	.	.	ID=PRO_0000072352;Note=Anaphase-promoting complex subunit SWM1	
+Q12379	UniProtKB	Compositional bias	2	5	.	.	.	Note=Poly-Ser	
+##sequence-region P43554 1 623
+P43554	UniProtKB	Chain	1	623	.	.	.	ID=PRO_0000076350;Note=SWI/SNF global transcription activator complex subunit SWP82	
+##sequence-region Q05471 1 1514
+Q05471	UniProtKB	Chain	1	1514	.	.	.	ID=PRO_0000074375;Note=Helicase SWR1	
+Q05471	UniProtKB	Domain	339	411	.	.	.	Note=HSA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00549	
+Q05471	UniProtKB	Domain	708	873	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q05471	UniProtKB	Domain	1247	1400	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q05471	UniProtKB	Nucleotide binding	721	728	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q05471	UniProtKB	Motif	824	827	.	.	.	Note=DEAH box	
+Q05471	UniProtKB	Helix	353	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E	
+Q05471	UniProtKB	Helix	602	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B	
+##sequence-region P53852 1 767
+P53852	UniProtKB	Chain	1	767	.	.	.	ID=PRO_0000159553;Note=Cysteine--tRNA ligase	
+P53852	UniProtKB	Motif	65	75	.	.	.	Note="HIGH" region	
+P53852	UniProtKB	Motif	427	431	.	.	.	Note="KMSKS" region	
+P53852	UniProtKB	Metal binding	63	63	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53852	UniProtKB	Metal binding	369	369	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53852	UniProtKB	Metal binding	394	394	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53852	UniProtKB	Metal binding	398	398	.	.	.	Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53852	UniProtKB	Binding site	430	430	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53852	UniProtKB	Modified residue	326	326	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+##sequence-region P15179 1 658
+P15179	UniProtKB	Chain	1	658	.	.	.	ID=PRO_0000111015;Note=Aspartate--tRNA ligase%2C mitochondrial	
+P15179	UniProtKB	Nucleotide binding	248	250	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15179	UniProtKB	Nucleotide binding	604	607	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15179	UniProtKB	Region	226	229	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15179	UniProtKB	Binding site	198	198	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15179	UniProtKB	Binding site	248	248	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15179	UniProtKB	Binding site	553	553	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P15179	UniProtKB	Binding site	560	560	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P23615 1 1451
+P23615	UniProtKB	Chain	1	1451	.	.	.	ID=PRO_0000072173;Note=Transcription elongation factor SPT6	
+P23615	UniProtKB	Domain	1257	1354	.	.	.	Note=SH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00191	
+P23615	UniProtKB	Motif	8	12	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23615	UniProtKB	Motif	77	85	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23615	UniProtKB	Motif	120	125	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23615	UniProtKB	Compositional bias	1	484	.	.	.	Note=Asp/Glu-rich (acidic)	
+P23615	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P23615	UniProtKB	Modified residue	134	134	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23615	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23615	UniProtKB	Modified residue	148	148	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23615	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23615	UniProtKB	Modified residue	206	206	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P23615	UniProtKB	Modified residue	295	295	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23615	UniProtKB	Helix	239	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OAK	
+P23615	UniProtKB	Helix	256	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OAK	
+P23615	UniProtKB	Helix	301	308	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	312	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Beta strand	320	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	324	329	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	330	332	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Turn	334	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	341	359	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	368	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	388	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	396	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Beta strand	402	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Helix	411	441	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	446	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	465	476	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	478	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	502	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	511	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	521	530	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Beta strand	541	543	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Helix	545	554	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Turn	555	559	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	568	583	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	586	598	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Beta strand	599	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	608	613	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Turn	615	617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Turn	619	625	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	633	636	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	639	649	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Beta strand	652	659	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	662	673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	681	733	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Beta strand	740	744	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Beta strand	750	754	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Turn	760	762	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Beta strand	765	770	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Beta strand	776	782	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	793	806	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Beta strand	809	813	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	819	833	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Beta strand	839	841	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Beta strand	846	848	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	854	858	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	861	866	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	872	885	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	887	892	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	896	900	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	908	910	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	913	931	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	935	939	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	942	945	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	946	950	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	956	968	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	978	981	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	987	993	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Turn	994	996	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	1015	1018	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	1023	1025	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	1026	1036	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	1041	1050	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	1055	1062	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	1066	1070	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	1075	1086	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	1091	1102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Beta strand	1103	1105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Helix	1117	1125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Turn	1129	1131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Beta strand	1137	1145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Beta strand	1150	1153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Beta strand	1159	1162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Beta strand	1166	1169	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Turn	1177	1179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Beta strand	1185	1194	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Helix	1195	1197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Beta strand	1199	1203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Helix	1206	1209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI	
+P23615	UniProtKB	Turn	1222	1224	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Helix	1227	1246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF	
+P23615	UniProtKB	Turn	1247	1249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Beta strand	1253	1255	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L3T	
+P23615	UniProtKB	Helix	1264	1271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Beta strand	1279	1283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Turn	1285	1287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L3T	
+P23615	UniProtKB	Beta strand	1288	1298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Beta strand	1301	1311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Beta strand	1313	1317	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSJ	
+P23615	UniProtKB	Beta strand	1320	1324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Beta strand	1327	1331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Helix	1332	1338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Helix	1340	1351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Helix	1361	1372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Beta strand	1380	1385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Beta strand	1387	1389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Beta strand	1392	1400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Beta strand	1406	1412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Beta strand	1414	1419	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Beta strand	1422	1426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+P23615	UniProtKB	Helix	1427	1437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK	
+##sequence-region Q08673 1 210
+Q08673	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08673	UniProtKB	Chain	20	210	.	.	.	ID=PRO_0000270576;Note=Cell wall protein SRL1	
+Q08673	UniProtKB	Compositional bias	25	208	.	.	.	Note=Thr-rich	
+Q08673	UniProtKB	Glycosylation	23	23	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08673	UniProtKB	Glycosylation	174	174	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08673	UniProtKB	Glycosylation	200	200	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08673	UniProtKB	Glycosylation	206	206	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03085 1 281
+Q03085	UniProtKB	Chain	1	281	.	.	.	ID=PRO_0000269762;Note=Oxidoreductase-like protein SRL4	
+##sequence-region P10080 1 294
+P10080	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P10080	UniProtKB	Chain	2	294	.	.	.	ID=PRO_0000081964;Note=Single-stranded nucleic acid-binding protein	
+P10080	UniProtKB	Domain	37	119	.	.	.	Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P10080	UniProtKB	Domain	186	274	.	.	.	Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176	
+P10080	UniProtKB	Region	131	151	.	.	.	Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P10080	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P10080	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P10080	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P10080	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P10080	UniProtKB	Modified residue	244	244	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P10080	UniProtKB	Sequence conflict	162	162	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53599 1 1579
+P53599	UniProtKB	Chain	1	1579	.	.	.	ID=PRO_0000086682;Note=MAP kinase kinase kinase SSK2	
+P53599	UniProtKB	Domain	1266	1558	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53599	UniProtKB	Nucleotide binding	1272	1280	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53599	UniProtKB	Active site	1390	1390	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P53599	UniProtKB	Binding site	1295	1295	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P53599	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53599	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53599	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53599	UniProtKB	Modified residue	118	118	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53599	UniProtKB	Modified residue	290	290	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53599	UniProtKB	Modified residue	1424	1424	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q07084 1 712
+Q07084	UniProtKB	Chain	1	712	.	.	.	ID=PRO_0000081406;Note=Osmolarity two-component system protein SSK1	
+Q07084	UniProtKB	Domain	505	647	.	.	.	Note=Response regulatory;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00169	
+Q07084	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q07084	UniProtKB	Modified residue	195	195	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q07084	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q07084	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07084	UniProtKB	Modified residue	368	368	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q07084	UniProtKB	Modified residue	380	380	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q07084	UniProtKB	Modified residue	554	554	.	.	.	Note=4-aspartylphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00169,ECO:0000269|PubMed:8808622;Dbxref=PMID:8808622	
+Q07084	UniProtKB	Modified residue	673	673	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
+Q07084	UniProtKB	Modified residue	693	693	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q07084	UniProtKB	Modified residue	703	703	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q07084	UniProtKB	Modified residue	706	706	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07084	UniProtKB	Mutagenesis	554	554	.	.	.	Note=Activates. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183345;Dbxref=PMID:8183345	
+Q07084	UniProtKB	Sequence conflict	181	181	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32867 1 290
+P32867	UniProtKB	Chain	1	290	.	.	.	ID=PRO_0000210274;Note=Protein SSO1	
+P32867	UniProtKB	Topological domain	1	265	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32867	UniProtKB	Transmembrane	266	287	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32867	UniProtKB	Topological domain	288	290	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32867	UniProtKB	Domain	190	252	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+P32867	UniProtKB	Sequence conflict	97	97	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32867	UniProtKB	Sequence conflict	105	105	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32867	UniProtKB	Helix	31	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO	
+P32867	UniProtKB	Helix	70	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO	
+P32867	UniProtKB	Turn	105	107	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO	
+P32867	UniProtKB	Helix	109	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO	
+P32867	UniProtKB	Helix	157	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO	
+P32867	UniProtKB	Helix	166	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO	
+P32867	UniProtKB	Helix	190	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B5N	
+##sequence-region Q12427 1 513
+Q12427	UniProtKB	Chain	1	513	.	.	.	ID=PRO_0000072254;Note=Protein STB3	
+Q12427	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P36085 1 766
+P36085	UniProtKB	Chain	1	766	.	.	.	ID=PRO_0000072255;Note=Protein STB6	
+P36085	UniProtKB	Modified residue	514	514	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region D6VTK4 1 431
+D6VTK4	UniProtKB	Chain	1	431	.	.	.	ID=PRO_0000195068;Note=Pheromone alpha factor receptor	
+D6VTK4	UniProtKB	Transmembrane	51	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6VTK4	UniProtKB	Transmembrane	80	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6VTK4	UniProtKB	Transmembrane	133	155	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6VTK4	UniProtKB	Transmembrane	162	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6VTK4	UniProtKB	Transmembrane	209	231	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6VTK4	UniProtKB	Transmembrane	244	266	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6VTK4	UniProtKB	Transmembrane	276	298	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+D6VTK4	UniProtKB	Modified residue	310	310	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+D6VTK4	UniProtKB	Modified residue	315	315	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+D6VTK4	UniProtKB	Modified residue	329	329	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+D6VTK4	UniProtKB	Modified residue	331	331	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+D6VTK4	UniProtKB	Modified residue	360	360	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+D6VTK4	UniProtKB	Modified residue	363	363	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+D6VTK4	UniProtKB	Modified residue	366	366	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198	
+D6VTK4	UniProtKB	Modified residue	382	382	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+D6VTK4	UniProtKB	Modified residue	385	385	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+D6VTK4	UniProtKB	Modified residue	386	386	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+D6VTK4	UniProtKB	Modified residue	411	411	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+D6VTK4	UniProtKB	Modified residue	414	414	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+D6VTK4	UniProtKB	Glycosylation	25	25	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11583169;Dbxref=PMID:11583169	
+D6VTK4	UniProtKB	Glycosylation	32	32	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11583169;Dbxref=PMID:11583169	
+D6VTK4	UniProtKB	Cross-link	374	374	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+D6VTK4	UniProtKB	Cross-link	400	400	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+D6VTK4	UniProtKB	Cross-link	422	422	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+D6VTK4	UniProtKB	Sequence conflict	269	269	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+D6VTK4	UniProtKB	Helix	39	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K9P	
+D6VTK4	UniProtKB	Helix	80	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K9P	
+D6VTK4	UniProtKB	Helix	256	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PJD	
+##sequence-region P25344 1 346
+P25344	UniProtKB	Chain	1	346	.	.	.	ID=PRO_0000072265;Note=Protein STE50	
+P25344	UniProtKB	Domain	24	108	.	.	.	Note=SAM	
+P25344	UniProtKB	Domain	233	327	.	.	.	Note=Ras-associating;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00166	
+P25344	UniProtKB	Modified residue	202	202	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P25344	UniProtKB	Modified residue	244	244	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25344	UniProtKB	Modified residue	248	248	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P25344	UniProtKB	Turn	32	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV	
+P25344	UniProtKB	Helix	37	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV	
+P25344	UniProtKB	Helix	56	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV	
+P25344	UniProtKB	Helix	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV	
+P25344	UniProtKB	Helix	70	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV	
+P25344	UniProtKB	Beta strand	82	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV	
+P25344	UniProtKB	Helix	86	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV	
+##sequence-region P16965 1 84
+P16965	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6	
+P16965	UniProtKB	Chain	2	84	.	.	.	ID=PRO_0000072269;Note=ATPase-stabilizing factor 15 kDa protein	
+P16965	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P16965	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P16965	UniProtKB	Sequence conflict	15	15	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16965	UniProtKB	Sequence conflict	27	27	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16965	UniProtKB	Sequence conflict	55	55	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P16965	UniProtKB	Sequence conflict	61	84	.	.	.	Note=VFKKDRRGSNLQSHEQKFENVQKE->SVQER;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53312 1 427
+P53312	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219	
+P53312	UniProtKB	Chain	31	427	.	.	.	ID=PRO_0000033365;Note=Succinate--CoA ligase [ADP-forming] subunit beta%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219	
+P53312	UniProtKB	Domain	39	284	.	.	.	Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219	
+P53312	UniProtKB	Nucleotide binding	83	85	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219	
+P53312	UniProtKB	Region	361	363	.	.	.	Note=Substrate binding%3B shared with subunit alpha;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219	
+P53312	UniProtKB	Metal binding	236	236	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219	
+P53312	UniProtKB	Metal binding	253	253	.	.	.	Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219	
+P53312	UniProtKB	Binding site	76	76	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219	
+P53312	UniProtKB	Binding site	144	144	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219	
+P53312	UniProtKB	Binding site	304	304	.	.	.	Note=Substrate%3B shared with subunit alpha;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219	
+P53312	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P53312	UniProtKB	Modified residue	263	263	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53312	UniProtKB	Modified residue	276	276	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q06524 1 206
+Q06524	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06524	UniProtKB	Chain	25	206	.	.	.	ID=PRO_0000270578;Note=Protein SUE1%2C mitochondrial	
+##sequence-region P38359 1 859
+P38359	UniProtKB	Chain	1	859	.	.	.	ID=PRO_0000080184;Note=Sulfate permease 1	
+P38359	UniProtKB	Transmembrane	94	114	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Transmembrane	116	136	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Transmembrane	148	168	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Transmembrane	206	226	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Transmembrane	234	254	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Transmembrane	292	312	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Transmembrane	332	352	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Transmembrane	395	415	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Transmembrane	428	448	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Transmembrane	468	488	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Transmembrane	525	545	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Domain	630	808	.	.	.	Note=STAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00198	
+P38359	UniProtKB	Glycosylation	51	51	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Glycosylation	93	93	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Glycosylation	358	358	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Glycosylation	391	391	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Glycosylation	630	630	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Glycosylation	653	653	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Glycosylation	718	718	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38359	UniProtKB	Sequence conflict	87	87	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38359	UniProtKB	Sequence conflict	457	457	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05515 1 481
+Q05515	UniProtKB	Chain	1	481	.	.	.	ID=PRO_0000072336;Note=Survival factor 1	
+Q05515	UniProtKB	Compositional bias	200	256	.	.	.	Note=Glu-rich	
+Q05515	UniProtKB	Compositional bias	359	395	.	.	.	Note=Glu-rich	
+##sequence-region Q03088 1 825
+Q03088	UniProtKB	Chain	1	825	.	.	.	ID=PRO_0000072340;Note=Styryl dye vacuolar localization protein 3	
+Q03088	UniProtKB	Coiled coil	366	423	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03088	UniProtKB	Compositional bias	629	755	.	.	.	Note=Asn-rich	
+Q03088	UniProtKB	Modified residue	471	471	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+Q03088	UniProtKB	Modified residue	496	496	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03088	UniProtKB	Modified residue	551	551	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q03088	UniProtKB	Modified residue	662	662	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03088	UniProtKB	Modified residue	739	739	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03088	UniProtKB	Modified residue	756	756	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03088	UniProtKB	Modified residue	757	757	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q06677 1 668
+Q06677	UniProtKB	Chain	1	668	.	.	.	ID=PRO_0000270621;Note=Auxilin-like clathrin uncoating factor SWA2	
+Q06677	UniProtKB	Domain	140	180	.	.	.	Note=UBA	
+Q06677	UniProtKB	Repeat	374	407	.	.	.	Note=TPR 1	
+Q06677	UniProtKB	Repeat	412	445	.	.	.	Note=TPR 2	
+Q06677	UniProtKB	Repeat	467	500	.	.	.	Note=TPR 3	
+Q06677	UniProtKB	Domain	603	668	.	.	.	Note=J	
+Q06677	UniProtKB	Region	1	100	.	.	.	Note=CB1	
+Q06677	UniProtKB	Region	238	302	.	.	.	Note=CB2	
+Q06677	UniProtKB	Region	303	362	.	.	.	Note=CB3	
+Q06677	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q06677	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06677	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06677	UniProtKB	Modified residue	308	308	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06677	UniProtKB	Modified residue	312	312	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q06677	UniProtKB	Mutagenesis	388	388	.	.	.	Note=In SWA2-1/SWA2-TPR%3B partial loss of clathrin disassembly function. In SWA2-TPR-J%3B complete loss of clathrin disassembly function%3B when associated with 631-AAA-633. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11084334,ECO:0000269|PubMed:16687570;Dbxref=PMID:11084334,PMID:16687570	
+Q06677	UniProtKB	Mutagenesis	631	633	.	.	.	Note=In SWA2-J%3B abolishes ATPase stimulation activity. In SWA2-TPR-J%3B complete loss of clathrin disassembly function%3B when associated with R-388. HPD->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16687570;Dbxref=PMID:16687570	
+Q06677	UniProtKB	Helix	140	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGY	
+Q06677	UniProtKB	Helix	158	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGY	
+Q06677	UniProtKB	Helix	171	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGY	
+##sequence-region Q12104 1 458
+Q12104	UniProtKB	Chain	1	458	.	.	.	ID=PRO_0000237661;Note=Transcriptional protein SWT1	
+Q12104	UniProtKB	Domain	130	262	.	.	.	Note=PINc	
+Q12104	UniProtKB	Mutagenesis	1	115	.	.	.	Note=Fully functional%3B when associated with deletion of 260-L--T-458. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17030511;Dbxref=PMID:17030511	
+Q12104	UniProtKB	Mutagenesis	260	458	.	.	.	Note=Fully functional%3B when associated with deletion of 1-M--K-115. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17030511;Dbxref=PMID:17030511	
+Q12104	UniProtKB	Helix	326	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+Q12104	UniProtKB	Helix	354	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+Q12104	UniProtKB	Turn	358	361	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+Q12104	UniProtKB	Helix	370	379	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+Q12104	UniProtKB	Turn	380	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+Q12104	UniProtKB	Helix	385	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+Q12104	UniProtKB	Turn	389	391	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+Q12104	UniProtKB	Helix	396	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+Q12104	UniProtKB	Helix	404	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+Q12104	UniProtKB	Helix	413	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+Q12104	UniProtKB	Turn	431	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+Q12104	UniProtKB	Helix	436	454	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ	
+##sequence-region P53135 1 668
+P53135	UniProtKB	Chain	1	668	.	.	.	ID=PRO_0000071954;Note=DNA replication regulator SLD3	
+P53135	UniProtKB	Compositional bias	276	279	.	.	.	Note=Poly-Leu	
+P53135	UniProtKB	Helix	157	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	176	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	183	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Turn	197	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	200	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	215	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	226	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	234	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	258	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	339	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	373	380	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	390	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	398	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Beta strand	403	406	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+P53135	UniProtKB	Helix	407	417	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3	
+##sequence-region P38343 1 150
+P38343	UniProtKB	Chain	1	150	.	.	.	ID=PRO_0000202528;Note=Protein SLM6	
+P38343	UniProtKB	Topological domain	1	76	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38343	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38343	UniProtKB	Topological domain	98	104	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38343	UniProtKB	Transmembrane	105	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38343	UniProtKB	Topological domain	126	150	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P32828 1 619
+P32828	UniProtKB	Chain	1	619	.	.	.	ID=PRO_0000083954;Note=E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5	
+P32828	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32828	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q02651 1 245
+Q02651	UniProtKB	Chain	1	245	.	.	.	ID=PRO_0000071964;Note=Spore membrane assembly protein 1	
+##sequence-region Q04658 1 369
+Q04658	UniProtKB	Chain	1	369	.	.	.	ID=PRO_0000203252;Note=Spore membrane assembly protein 2	
+Q04658	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04658	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04658	UniProtKB	Topological domain	28	220	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04658	UniProtKB	Transmembrane	221	241	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04658	UniProtKB	Topological domain	242	265	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04658	UniProtKB	Transmembrane	266	286	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04658	UniProtKB	Topological domain	287	319	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04658	UniProtKB	Transmembrane	320	340	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04658	UniProtKB	Topological domain	341	369	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q08817 1 791
+Q08817	UniProtKB	Chain	1	791	.	.	.	ID=PRO_0000270575;Note=Leucine-rich repeat-containing protein SOG2	
+Q08817	UniProtKB	Repeat	43	64	.	.	.	Note=LRR 1	
+Q08817	UniProtKB	Repeat	67	88	.	.	.	Note=LRR 2	
+Q08817	UniProtKB	Repeat	90	111	.	.	.	Note=LRR 3	
+Q08817	UniProtKB	Repeat	113	134	.	.	.	Note=LRR 4	
+Q08817	UniProtKB	Repeat	138	159	.	.	.	Note=LRR 5	
+Q08817	UniProtKB	Repeat	163	183	.	.	.	Note=LRR 6	
+Q08817	UniProtKB	Modified residue	214	214	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P39543 1 234
+P39543	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39543	UniProtKB	Chain	19	234	.	.	.	ID=PRO_0000014332;Note=Protein SOP4	
+P39543	UniProtKB	Topological domain	19	188	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39543	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39543	UniProtKB	Topological domain	210	234	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39543	UniProtKB	Glycosylation	35	35	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39543	UniProtKB	Glycosylation	53	53	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39543	UniProtKB	Glycosylation	85	85	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39543	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39543	UniProtKB	Glycosylation	170	170	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53148 1 917
+P53148	UniProtKB	Chain	1	917	.	.	.	ID=PRO_0000202755;Note=Spindle pole body component SPC105	
+P53148	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53148	UniProtKB	Modified residue	356	356	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P53148	UniProtKB	Modified residue	380	380	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P53148	UniProtKB	Beta strand	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BL0	
+##sequence-region Q01684 1 191
+Q01684	UniProtKB	Chain	1	191	.	.	.	ID=PRO_0000072148;Note=Sporulation-specific protein	
+Q01684	UniProtKB	Sequence conflict	4	4	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q01684	UniProtKB	Sequence conflict	4	4	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P06844 1 337
+P06844	UniProtKB	Chain	1	337	.	.	.	ID=PRO_0000072166;Note=Protein SPT3	
+P06844	UniProtKB	Modified residue	270	270	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P06844	UniProtKB	Natural variant	76	76	.	.	.	Note=In strain: CLIB 556 and CLIB 630. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P06844	UniProtKB	Natural variant	93	93	.	.	.	Note=In strain: CLIB 556 and CLIB 630. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P06844	UniProtKB	Natural variant	120	120	.	.	.	Note=In strain: CLIB 413 haplotype Ha2. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P06844	UniProtKB	Natural variant	134	134	.	.	.	Note=In strain: R13 haplotype Ha2. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+P06844	UniProtKB	Natural variant	318	318	.	.	.	Note=In strain: YIIc12 haplotype Ha2 and YIIc17. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486	
+##sequence-region P38687 1 599
+P38687	UniProtKB	Chain	1	599	.	.	.	ID=PRO_0000135232;Note=Signal recognition particle subunit SRP68	
+##sequence-region P32916 1 621
+P32916	UniProtKB	Chain	1	621	.	.	.	ID=PRO_0000101216;Note=Signal recognition particle receptor subunit alpha homolog	
+P32916	UniProtKB	Nucleotide binding	404	411	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32916	UniProtKB	Nucleotide binding	510	514	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32916	UniProtKB	Nucleotide binding	572	575	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32916	UniProtKB	Region	1	158	.	.	.	Note=SRX	
+P32916	UniProtKB	Modified residue	239	239	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32916	UniProtKB	Modified residue	523	523	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32916	UniProtKB	Sequence conflict	499	499	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32916	UniProtKB	Beta strand	4	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Beta strand	13	19	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Helix	27	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Helix	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Helix	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Beta strand	58	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Beta strand	74	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Turn	81	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Beta strand	85	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Helix	96	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Helix	118	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Beta strand	127	129	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Turn	140	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+P32916	UniProtKB	Helix	145	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ	
+##sequence-region P12954 1 1174
+P12954	UniProtKB	Chain	1	1174	.	.	.	ID=PRO_0000102071;Note=ATP-dependent DNA helicase SRS2	
+P12954	UniProtKB	Domain	14	316	.	.	.	Note=UvrD-like helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00560	
+P12954	UniProtKB	Domain	317	654	.	.	.	Note=UvrD-like helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00617	
+P12954	UniProtKB	Nucleotide binding	38	43	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00560	
+P12954	UniProtKB	Region	222	243	.	.	.	Note=Leucine-zipper	
+P12954	UniProtKB	Binding site	314	314	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P12954	UniProtKB	Modified residue	833	833	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P12954	UniProtKB	Sequence conflict	173	182	.	.	.	Note=IKKQISKLKS->TQETDIKAKI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12954	UniProtKB	Sequence conflict	534	548	.	.	.	Note=YEYLYKDGKKKNDQL->VRILGTRMVRKKMSQF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P12954	UniProtKB	Helix	1152	1160	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V62	
+P12954	UniProtKB	Beta strand	1170	1172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V62	
+##sequence-region P13130 1 326
+P13130	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Chain	19	326	.	.	.	ID=PRO_0000022419;Note=Sporulation-specific wall maturation protein	
+P13130	UniProtKB	Domain	19	324	.	.	.	Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068	
+P13130	UniProtKB	Glycosylation	26	26	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Glycosylation	50	50	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Glycosylation	58	58	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Glycosylation	64	64	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Glycosylation	76	76	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Glycosylation	108	108	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Glycosylation	181	181	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Glycosylation	190	190	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Glycosylation	199	199	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Glycosylation	205	205	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Glycosylation	248	248	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P13130	UniProtKB	Glycosylation	281	281	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39073 1 555
+P39073	UniProtKB	Chain	1	555	.	.	.	ID=PRO_0000086784;Note=Meiotic mRNA stability protein kinase SSN3	
+P39073	UniProtKB	Domain	75	463	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P39073	UniProtKB	Nucleotide binding	81	89	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P39073	UniProtKB	Active site	286	286	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P39073	UniProtKB	Binding site	183	183	.	.	.	Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39073	UniProtKB	Mutagenesis	183	183	.	.	.	Note=In UME5-4%3B loss of activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8164691;Dbxref=PMID:8164691	
+P39073	UniProtKB	Mutagenesis	304	304	.	.	.	Note=Abrogates kinase activity and transcriptional repression. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10360183,ECO:0000269|PubMed:11226276,ECO:0000269|PubMed:11331604,ECO:0000269|PubMed:12200444,ECO:0000269|PubMed:12520306,ECO:0000269|PubMed:15240822,ECO:0000269|PubMed:9702190;Dbxref=PMID:10360183,PMID:11226276,PMID:11331604,PMID:12200444,PMID:12520306,PMID:15240822,PMID:9702190	
+##sequence-region P47821 1 323
+P47821	UniProtKB	Chain	1	323	.	.	.	ID=PRO_0000080428;Note=RNA polymerase II holoenzyme cyclin-like subunit	
+P47821	UniProtKB	Domain	45	176	.	.	.	Note=Cyclin N-terminal	
+##sequence-region P22213 1 666
+P22213	UniProtKB	Chain	1	666	.	.	.	ID=PRO_0000206299;Note=Protein SLY1	
+P22213	UniProtKB	Repeat	106	142	.	.	.	Note=1	
+P22213	UniProtKB	Repeat	220	257	.	.	.	Note=2	
+P22213	UniProtKB	Repeat	436	474	.	.	.	Note=3	
+P22213	UniProtKB	Repeat	478	514	.	.	.	Note=4	
+P22213	UniProtKB	Region	106	514	.	.	.	Note=4 X approximate repeats	
+P22213	UniProtKB	Natural variant	532	532	.	.	.	Note=In SLY1-20 mutant. E->K	
+P22213	UniProtKB	Helix	14	26	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Turn	27	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	43	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	54	58	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	60	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Turn	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	72	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	80	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	93	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	106	118	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	121	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	134	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	150	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	153	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	163	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	170	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	178	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	191	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	215	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	220	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	223	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	260	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	266	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	271	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	280	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	295	297	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	317	319	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	328	331	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	332	335	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	336	360	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	388	412	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Turn	413	415	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	417	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	429	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	447	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	467	478	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Turn	479	481	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	486	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	529	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Turn	534	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	540	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	543	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	557	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	573	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	582	585	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	589	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	593	595	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	604	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	616	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Beta strand	635	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+P22213	UniProtKB	Helix	646	659	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS	
+##sequence-region P38778 1 549
+P38778	UniProtKB	Chain	1	549	.	.	.	ID=PRO_0000212606;Note=Manganese transporter SMF2	
+P38778	UniProtKB	Transmembrane	91	109	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38778	UniProtKB	Transmembrane	130	147	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38778	UniProtKB	Transmembrane	161	185	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38778	UniProtKB	Transmembrane	196	214	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38778	UniProtKB	Transmembrane	312	332	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38778	UniProtKB	Transmembrane	350	372	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38778	UniProtKB	Transmembrane	432	452	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38778	UniProtKB	Transmembrane	521	541	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07549 1 140
+Q07549	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000193988;Note=Protein SNA4	
+Q07549	UniProtKB	Topological domain	1	8	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07549	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07549	UniProtKB	Topological domain	30	41	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07549	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07549	UniProtKB	Topological domain	63	140	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07549	UniProtKB	Modified residue	134	134	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q07549	UniProtKB	Lipidation	2	2	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+Q07549	UniProtKB	Lipidation	3	3	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+Q07549	UniProtKB	Lipidation	5	5	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+Q07549	UniProtKB	Lipidation	7	7	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+Q07549	UniProtKB	Lipidation	8	8	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107	
+Q07549	UniProtKB	Cross-link	128	128	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q04477 1 213
+Q04477	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04477	UniProtKB	Chain	2	213	.	.	.	ID=PRO_0000203294;Note=Kinetochore protein SPC24	
+Q04477	UniProtKB	Coiled coil	54	123	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04477	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q04477	UniProtKB	Helix	11	20	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+Q04477	UniProtKB	Helix	24	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+Q04477	UniProtKB	Helix	157	167	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+Q04477	UniProtKB	Beta strand	170	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+Q04477	UniProtKB	Helix	174	176	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+Q04477	UniProtKB	Beta strand	178	181	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+Q04477	UniProtKB	Turn	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+Q04477	UniProtKB	Beta strand	190	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+Q04477	UniProtKB	Turn	197	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FV4	
+Q04477	UniProtKB	Helix	200	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+##sequence-region P40014 1 221
+P40014	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40014	UniProtKB	Chain	2	221	.	.	.	ID=PRO_0000202622;Note=Kinetochore protein SPC25	
+P40014	UniProtKB	Coiled coil	9	112	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40014	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40014	UniProtKB	Helix	4	6	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40014	UniProtKB	Helix	7	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS	
+P40014	UniProtKB	Helix	133	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+P40014	UniProtKB	Beta strand	147	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+P40014	UniProtKB	Beta strand	153	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+P40014	UniProtKB	Beta strand	158	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+P40014	UniProtKB	Beta strand	169	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+P40014	UniProtKB	Beta strand	175	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+P40014	UniProtKB	Beta strand	180	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+P40014	UniProtKB	Helix	190	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+P40014	UniProtKB	Helix	206	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J	
+##sequence-region P39723 1 622
+P39723	UniProtKB	Chain	1	622	.	.	.	ID=PRO_0000202421;Note=Spindle pole component SPC72	
+P39723	UniProtKB	Sequence conflict	302	302	.	.	.	Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P42933 1 373
+P42933	UniProtKB	Chain	1	373	.	.	.	ID=PRO_0000203324;Note=Stationary phase protein 5	
+P42933	UniProtKB	Sequence conflict	43	43	.	.	.	Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P42933	UniProtKB	Sequence conflict	47	50	.	.	.	Note=FVTW->LALG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P17122 1 198
+P17122	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000072136;Note=Sporulation-specific protein 16	
+##sequence-region Q03012 1 353
+Q03012	UniProtKB	Chain	1	353	.	.	.	ID=PRO_0000059338;Note=COMPASS component SPP1	
+Q03012	UniProtKB	Zinc finger	22	72	.	.	.	Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
+Q03012	UniProtKB	Compositional bias	246	251	.	.	.	Note=Poly-Lys	
+Q03012	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P25380 1 463
+P25380	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25380	UniProtKB	Chain	26	440	.	.	.	ID=PRO_0000202550;Note=Sporulation-specific protein 22	
+P25380	UniProtKB	Propeptide	441	463	.	.	.	ID=PRO_0000277472;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25380	UniProtKB	Repeat	127	147	.	.	.	Note=LRR 1	
+P25380	UniProtKB	Repeat	185	206	.	.	.	Note=LRR 2	
+P25380	UniProtKB	Repeat	207	233	.	.	.	Note=LRR 3	
+P25380	UniProtKB	Repeat	251	275	.	.	.	Note=LRR 4	
+P25380	UniProtKB	Repeat	302	325	.	.	.	Note=LRR 5	
+P25380	UniProtKB	Lipidation	440	440	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25380	UniProtKB	Glycosylation	256	256	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25380	UniProtKB	Glycosylation	314	314	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25380	UniProtKB	Glycosylation	327	327	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P35208 1 640
+P35208	UniProtKB	Chain	1	640	.	.	.	ID=PRO_0000072160;Note=Protein SPT10	
+P35208	UniProtKB	Domain	121	259	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
+P35208	UniProtKB	Mutagenesis	388	388	.	.	.	Note=Loss of complementation of the suppression phenotype. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138180;Dbxref=PMID:8138180	
+##sequence-region P27692 1 1063
+P27692	UniProtKB	Chain	1	1063	.	.	.	ID=PRO_0000208477;Note=Transcription elongation factor SPT5	
+P27692	UniProtKB	Domain	382	415	.	.	.	Note=KOW 1	
+P27692	UniProtKB	Domain	533	560	.	.	.	Note=KOW 2	
+P27692	UniProtKB	Domain	584	615	.	.	.	Note=KOW 3	
+P27692	UniProtKB	Domain	799	832	.	.	.	Note=KOW 4	
+P27692	UniProtKB	Repeat	931	936	.	.	.	Note=1	
+P27692	UniProtKB	Repeat	937	942	.	.	.	Note=2	
+P27692	UniProtKB	Repeat	948	953	.	.	.	Note=3	
+P27692	UniProtKB	Repeat	958	963	.	.	.	Note=4	
+P27692	UniProtKB	Repeat	969	974	.	.	.	Note=5	
+P27692	UniProtKB	Repeat	975	980	.	.	.	Note=6	
+P27692	UniProtKB	Repeat	981	986	.	.	.	Note=7	
+P27692	UniProtKB	Repeat	987	992	.	.	.	Note=8	
+P27692	UniProtKB	Repeat	1000	1005	.	.	.	Note=9	
+P27692	UniProtKB	Repeat	1009	1014	.	.	.	Note=10	
+P27692	UniProtKB	Repeat	1015	1020	.	.	.	Note=11	
+P27692	UniProtKB	Repeat	1032	1037	.	.	.	Note=12	
+P27692	UniProtKB	Repeat	1043	1048	.	.	.	Note=13	
+P27692	UniProtKB	Repeat	1052	1057	.	.	.	Note=14	
+P27692	UniProtKB	Repeat	1058	1063	.	.	.	Note=15	
+P27692	UniProtKB	Region	931	1063	.	.	.	Note=15 X 6 AA tandem repeats of S-[TA]-W-G-G-[AQ]	
+P27692	UniProtKB	Compositional bias	148	167	.	.	.	Note=Asp/Glu-rich (acidic)	
+P27692	UniProtKB	Compositional bias	189	199	.	.	.	Note=Asp/Glu-rich (acidic)	
+P27692	UniProtKB	Modified residue	35	35	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27692	UniProtKB	Modified residue	133	133	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P27692	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P27692	UniProtKB	Modified residue	188	188	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27692	UniProtKB	Modified residue	219	219	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P27692	UniProtKB	Beta strand	387	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Turn	394	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Beta strand	399	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Beta strand	409	416	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Turn	422	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Helix	442	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Helix	453	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Helix	461	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Beta strand	464	468	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Beta strand	471	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Beta strand	477	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Beta strand	483	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Helix	490	492	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Helix	502	507	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK	
+P27692	UniProtKB	Beta strand	539	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Turn	546	549	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Beta strand	551	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Beta strand	573	576	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Helix	577	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Beta strand	580	582	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Beta strand	589	592	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Turn	596	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Beta strand	601	608	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Beta strand	611	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Turn	617	619	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Beta strand	620	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+P27692	UniProtKB	Helix	627	629	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL	
+##sequence-region P39015 1 273
+P39015	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+P39015	UniProtKB	Chain	2	273	.	.	.	ID=PRO_0000072278;Note=Suppressor protein STM1	
+P39015	UniProtKB	Compositional bias	38	54	.	.	.	Note=Pro-rich	
+P39015	UniProtKB	Compositional bias	77	102	.	.	.	Note=Ser/Thr-rich	
+P39015	UniProtKB	Compositional bias	119	141	.	.	.	Note=Ala-rich	
+P39015	UniProtKB	Compositional bias	147	164	.	.	.	Note=Asn/Gln-rich	
+P39015	UniProtKB	Compositional bias	225	250	.	.	.	Note=Arg/Asn/Gly-rich	
+P39015	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+P39015	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39015	UniProtKB	Modified residue	118	118	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P39015	UniProtKB	Modified residue	229	229	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P39015	UniProtKB	Cross-link	46	46	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P39015	UniProtKB	Cross-link	121	121	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P39015	UniProtKB	Cross-link	171	171	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P39015	UniProtKB	Cross-link	184	184	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P39015	UniProtKB	Sequence conflict	133	133	.	.	.	Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39015	UniProtKB	Sequence conflict	171	171	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39015	UniProtKB	Sequence conflict	177	177	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39015	UniProtKB	Helix	44	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39015	UniProtKB	Helix	56	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39015	UniProtKB	Helix	67	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39015	UniProtKB	Helix	78	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39015	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39015	UniProtKB	Beta strand	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56	
+P39015	UniProtKB	Helix	103	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39015	UniProtKB	Helix	113	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39015	UniProtKB	Helix	116	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+P39015	UniProtKB	Turn	136	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U	
+P39015	UniProtKB	Helix	156	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R	
+##sequence-region Q05937 1 343
+Q05937	UniProtKB	Chain	1	343	.	.	.	ID=PRO_0000270565;Note=Zinc finger protein STP3	
+Q05937	UniProtKB	Zinc finger	169	191	.	.	.	Note=C2H2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q05937	UniProtKB	Compositional bias	36	111	.	.	.	Note=Ser-rich	
+Q05937	UniProtKB	Modified residue	71	71	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q05937	UniProtKB	Modified residue	111	111	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+##sequence-region Q07351 1 490
+Q07351	UniProtKB	Chain	1	490	.	.	.	ID=PRO_0000270566;Note=Zinc finger protein STP4	
+Q07351	UniProtKB	Zinc finger	304	326	.	.	.	Note=C2H2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q07351	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07351	UniProtKB	Modified residue	155	155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38163 1 1010
+P38163	UniProtKB	Chain	1	1010	.	.	.	ID=PRO_0000051221;Note=Lethal(2) giant larvae protein homolog SRO77	
+P38163	UniProtKB	Repeat	47	80	.	.	.	Note=WD 1	
+P38163	UniProtKB	Repeat	87	122	.	.	.	Note=WD 2	
+P38163	UniProtKB	Repeat	127	163	.	.	.	Note=WD 3	
+P38163	UniProtKB	Repeat	182	215	.	.	.	Note=WD 4	
+P38163	UniProtKB	Repeat	240	275	.	.	.	Note=WD 5	
+P38163	UniProtKB	Repeat	299	364	.	.	.	Note=WD 6	
+P38163	UniProtKB	Repeat	372	407	.	.	.	Note=WD 7	
+P38163	UniProtKB	Repeat	431	504	.	.	.	Note=WD 8	
+P38163	UniProtKB	Repeat	518	595	.	.	.	Note=WD 9	
+P38163	UniProtKB	Repeat	602	637	.	.	.	Note=WD 10	
+P38163	UniProtKB	Repeat	649	700	.	.	.	Note=WD 11	
+P38163	UniProtKB	Repeat	709	763	.	.	.	Note=WD 12	
+P38163	UniProtKB	Repeat	768	815	.	.	.	Note=WD 13	
+P38163	UniProtKB	Repeat	829	852	.	.	.	Note=WD 14	
+P38163	UniProtKB	Sequence conflict	130	130	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38163	UniProtKB	Sequence conflict	130	130	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38163	UniProtKB	Sequence conflict	135	135	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38163	UniProtKB	Sequence conflict	135	135	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38163	UniProtKB	Sequence conflict	260	260	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38163	UniProtKB	Sequence conflict	260	260	.	.	.	Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38163	UniProtKB	Sequence conflict	834	834	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38163	UniProtKB	Sequence conflict	834	834	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38163	UniProtKB	Sequence conflict	858	858	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38163	UniProtKB	Sequence conflict	858	858	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38163	UniProtKB	Sequence conflict	943	943	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38163	UniProtKB	Sequence conflict	943	943	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12038 1 1033
+Q12038	UniProtKB	Chain	1	1033	.	.	.	ID=PRO_0000072008;Note=Lethal(2) giant larvae protein homolog SRO7	
+Q12038	UniProtKB	Repeat	81	114	.	.	.	Note=WD 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	121	156	.	.	.	Note=WD 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	161	197	.	.	.	Note=WD 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	216	249	.	.	.	Note=WD 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	274	309	.	.	.	Note=WD 5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	333	397	.	.	.	Note=WD 6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	405	440	.	.	.	Note=WD 7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	464	538	.	.	.	Note=WD 8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	552	631	.	.	.	Note=WD 9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	638	673	.	.	.	Note=WD 10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	685	736	.	.	.	Note=WD 11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	745	799	.	.	.	Note=WD 12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	804	851	.	.	.	Note=WD 13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Repeat	865	888	.	.	.	Note=WD 14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788	
+Q12038	UniProtKB	Compositional bias	49	52	.	.	.	Note=Poly-Ser	
+Q12038	UniProtKB	Modified residue	591	591	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12038	UniProtKB	Modified residue	602	602	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12038	UniProtKB	Beta strand	66	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	80	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	87	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	91	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	99	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	110	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	121	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	128	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	131	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	140	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	150	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	161	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	171	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	182	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	187	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	191	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	200	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	207	209	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	216	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	223	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	235	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	240	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	244	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	274	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	283	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	295	299	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	300	302	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	305	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	333	341	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	347	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	365	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	376	378	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	381	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	392	397	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	400	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	405	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	417	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	425	431	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	436	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	441	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	450	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	455	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	461	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	464	473	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	474	482	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	505	514	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	517	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	528	532	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	535	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	539	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	546	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	551	557	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	558	561	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	562	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	572	579	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	603	605	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	609	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	614	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	622	631	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	637	643	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	647	653	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	656	662	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	663	666	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	667	673	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	674	676	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	685	694	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	698	709	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	712	721	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	723	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	727	736	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	745	750	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	751	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	761	765	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	766	769	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	775	780	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	782	788	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	795	799	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	804	815	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	817	819	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	821	831	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	834	840	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	841	843	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	846	851	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	858	861	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	872	875	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Beta strand	877	888	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Turn	915	917	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	927	935	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+Q12038	UniProtKB	Helix	945	949	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ	
+##sequence-region P32583 1 406
+P32583	UniProtKB	Chain	1	406	.	.	.	ID=PRO_0000072192;Note=Suppressor protein SRP40	
+P32583	UniProtKB	Compositional bias	25	314	.	.	.	Note=Asp/Ser-rich	
+P32583	UniProtKB	Modified residue	133	133	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P32583	UniProtKB	Modified residue	289	289	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P32583	UniProtKB	Modified residue	293	293	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32583	UniProtKB	Modified residue	394	394	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198	
+P32583	UniProtKB	Sequence conflict	400	400	.	.	.	Note=G->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38931 1 1420
+P38931	UniProtKB	Chain	1	1420	.	.	.	ID=PRO_0000072215;Note=Mediator of RNA polymerase II transcription subunit 13	
+P38931	UniProtKB	Compositional bias	526	529	.	.	.	Note=Poly-Asn	
+P38931	UniProtKB	Compositional bias	657	664	.	.	.	Note=Poly-Glu	
+P38931	UniProtKB	Compositional bias	813	816	.	.	.	Note=Poly-Ser	
+P38931	UniProtKB	Compositional bias	1005	1008	.	.	.	Note=Poly-Leu	
+P38931	UniProtKB	Compositional bias	1121	1136	.	.	.	Note=Poly-Gln	
+P38931	UniProtKB	Modified residue	370	370	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P38931	UniProtKB	Modified residue	375	375	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38931	UniProtKB	Modified residue	425	425	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38931	UniProtKB	Modified residue	601	601	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38931	UniProtKB	Modified residue	608	608	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15225552;Dbxref=PMID:19779198,PMID:15225552	
+P38931	UniProtKB	Modified residue	636	636	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38931	UniProtKB	Modified residue	748	748	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38931	UniProtKB	Mutagenesis	608	608	.	.	.	Note=Loss of function%3B when associated with A-1236. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15225552;Dbxref=PMID:15225552	
+P38931	UniProtKB	Mutagenesis	1236	1236	.	.	.	Note=Loss of function%3B when associated with A-608. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15225552;Dbxref=PMID:15225552	
+P38931	UniProtKB	Sequence conflict	38	38	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38931	UniProtKB	Sequence conflict	812	812	.	.	.	Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38931	UniProtKB	Sequence conflict	859	859	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38931	UniProtKB	Sequence conflict	877	878	.	.	.	Note=VK->GE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38931	UniProtKB	Sequence conflict	887	887	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38931	UniProtKB	Sequence conflict	1284	1284	.	.	.	Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38871 1 571
+P38871	UniProtKB	Chain	1	571	.	.	.	ID=PRO_0000072216;Note=Sporulation-specific protein 1	
+P38871	UniProtKB	Coiled coil	469	486	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38871	UniProtKB	Coiled coil	542	566	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P37296 1 890
+P37296	UniProtKB	Chain	1	890	.	.	.	ID=PRO_0000119225;Note=V-type proton ATPase subunit a%2C Golgi isoform	
+P37296	UniProtKB	Topological domain	1	450	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Transmembrane	451	469	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Topological domain	470	471	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Transmembrane	472	488	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Topological domain	489	502	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Transmembrane	503	532	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Topological domain	533	580	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Transmembrane	581	600	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Topological domain	601	618	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Transmembrane	619	639	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Topological domain	640	682	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Transmembrane	683	702	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Topological domain	703	779	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Transmembrane	780	804	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Topological domain	805	828	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Transmembrane	829	867	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Topological domain	868	890	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Coiled coil	113	154	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Coiled coil	297	347	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P37296	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P37296	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P37296	UniProtKB	Modified residue	228	228	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P37296	UniProtKB	Sequence conflict	805	805	.	.	.	Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P31377 1 255
+P31377	UniProtKB	Chain	1	255	.	.	.	ID=PRO_0000210281;Note=Syntaxin-8	
+P31377	UniProtKB	Topological domain	1	234	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31377	UniProtKB	Transmembrane	235	255	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P31377	UniProtKB	Domain	164	228	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+P31377	UniProtKB	Lipidation	238	238	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53598 1 329
+P53598	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222	
+P53598	UniProtKB	Chain	25	329	.	.	.	ID=PRO_0000033351;Note=Succinate--CoA ligase [ADP-forming] subunit alpha%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222	
+P53598	UniProtKB	Region	45	48	.	.	.	Note=Coenzyme A binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222	
+P53598	UniProtKB	Region	124	126	.	.	.	Note=Coenzyme A binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222	
+P53598	UniProtKB	Active site	284	284	.	.	.	Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222	
+P53598	UniProtKB	Binding site	71	71	.	.	.	Note=Coenzyme A;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222	
+P53598	UniProtKB	Binding site	189	189	.	.	.	Note=Substrate%3B shared with subunit beta;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222	
+##sequence-region P36126 1 1683
+P36126	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P36126	UniProtKB	Chain	2	1683	.	.	.	ID=PRO_0000218825;Note=Phospholipase D1	
+P36126	UniProtKB	Domain	291	487	.	.	.	Note=PX	
+P36126	UniProtKB	Domain	496	664	.	.	.	Note=PH	
+P36126	UniProtKB	Domain	791	818	.	.	.	Note=PLD phosphodiesterase 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P36126	UniProtKB	Domain	1091	1118	.	.	.	Note=PLD phosphodiesterase 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P36126	UniProtKB	Compositional bias	255	280	.	.	.	Note=Asn-rich	
+P36126	UniProtKB	Compositional bias	405	410	.	.	.	Note=Poly-Asn	
+P36126	UniProtKB	Compositional bias	628	633	.	.	.	Note=Poly-Leu	
+P36126	UniProtKB	Active site	796	796	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P36126	UniProtKB	Active site	798	798	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P36126	UniProtKB	Active site	803	803	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P36126	UniProtKB	Active site	1096	1096	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P36126	UniProtKB	Active site	1098	1098	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P36126	UniProtKB	Active site	1103	1103	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153	
+P36126	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378	
+P36126	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P36126	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P36126	UniProtKB	Modified residue	145	145	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36126	UniProtKB	Modified residue	1461	1461	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36126	UniProtKB	Modified residue	1462	1462	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P33757 1 523
+P33757	UniProtKB	Chain	1	523	.	.	.	ID=PRO_0000202524;Note=Sporulation protein 23	
+##sequence-region Q07798 1 868
+Q07798	UniProtKB	Chain	1	868	.	.	.	ID=PRO_0000072143;Note=Sporulation-specific protein 75	
+Q07798	UniProtKB	Topological domain	1	34	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Transmembrane	35	55	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Topological domain	56	127	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Topological domain	149	187	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Transmembrane	188	208	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Topological domain	209	481	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Transmembrane	482	502	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Topological domain	503	527	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Transmembrane	528	548	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Topological domain	549	569	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Transmembrane	570	590	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Topological domain	591	611	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Transmembrane	612	632	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Topological domain	633	660	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Transmembrane	661	683	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Topological domain	684	692	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Transmembrane	693	713	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Topological domain	714	730	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Transmembrane	731	751	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Topological domain	752	753	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Transmembrane	754	774	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Topological domain	775	868	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Glycosylation	2	2	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Glycosylation	184	184	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07798	UniProtKB	Glycosylation	503	503	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04921 1 423
+Q04921	UniProtKB	Chain	1	423	.	.	.	ID=PRO_0000173501;Note=Sporulation-regulated protein 28	
+Q04921	UniProtKB	Domain	28	342	.	.	.	Note=Septin-type G	
+Q04921	UniProtKB	Nucleotide binding	38	45	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04921	UniProtKB	Nucleotide binding	204	212	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04921	UniProtKB	Coiled coil	384	417	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04921	UniProtKB	Compositional bias	60	68	.	.	.	Note=Poly-Asp	
+Q04921	UniProtKB	Binding site	124	124	.	.	.	Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q04921	UniProtKB	Binding site	291	291	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P08459 1 502
+P08459	UniProtKB	Signal peptide	1	56	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08459	UniProtKB	Chain	57	475	.	.	.	ID=PRO_0000033195;Note=Sporulation-specific protein 2	
+P08459	UniProtKB	Propeptide	476	502	.	.	.	ID=PRO_0000277471;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08459	UniProtKB	Lipidation	475	475	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08459	UniProtKB	Glycosylation	77	77	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08459	UniProtKB	Glycosylation	135	135	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08459	UniProtKB	Glycosylation	285	285	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08459	UniProtKB	Glycosylation	303	303	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08459	UniProtKB	Glycosylation	340	340	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08459	UniProtKB	Glycosylation	343	343	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08459	UniProtKB	Glycosylation	355	355	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P08459	UniProtKB	Sequence conflict	203	203	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08459	UniProtKB	Sequence conflict	210	210	.	.	.	Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08459	UniProtKB	Sequence conflict	324	324	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P09007 1 221
+P09007	UniProtKB	Chain	1	221	.	.	.	ID=PRO_0000083482;Note=Pre-rRNA-processing protein SRD1	
+P09007	UniProtKB	Zinc finger	168	193	.	.	.	Note=GATA-type	
+P09007	UniProtKB	Sequence conflict	106	106	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09007	UniProtKB	Sequence conflict	192	192	.	.	.	Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38789 1 453
+P38789	UniProtKB	Chain	1	453	.	.	.	ID=PRO_0000120259;Note=Ribosome biogenesis protein SSF1	
+P38789	UniProtKB	Domain	26	348	.	.	.	Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034	
+P38789	UniProtKB	Modified residue	301	301	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P39926 1 295
+P39926	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000210275;Note=Protein SSO2	
+P39926	UniProtKB	Topological domain	1	269	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39926	UniProtKB	Transmembrane	270	291	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39926	UniProtKB	Topological domain	292	295	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39926	UniProtKB	Domain	194	256	.	.	.	Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202	
+P39926	UniProtKB	Coiled coil	39	100	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39926	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39926	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P39926	UniProtKB	Sequence conflict	222	222	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P39926	UniProtKB	Helix	36	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y	
+P39926	UniProtKB	Helix	74	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y	
+P39926	UniProtKB	Turn	109	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LG4	
+P39926	UniProtKB	Helix	113	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y	
+P39926	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LG4	
+P39926	UniProtKB	Helix	161	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y	
+P39926	UniProtKB	Beta strand	169	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y	
+P39926	UniProtKB	Turn	174	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LG4	
+P39926	UniProtKB	Helix	192	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y	
+##sequence-region Q03770 1 852
+Q03770	UniProtKB	Chain	1	852	.	.	.	ID=PRO_0000054164;Note=SPS-sensor component SSY1	
+Q03770	UniProtKB	Topological domain	1	285	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	286	306	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	307	329	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	330	350	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	351	357	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	358	378	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	379	400	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	401	421	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	422	422	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	423	443	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	444	500	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	501	521	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	522	540	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	541	561	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	562	623	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	624	644	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	645	673	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	674	694	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	695	703	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	704	724	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	725	755	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	756	776	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	777	784	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Transmembrane	785	805	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Topological domain	806	852	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03770	UniProtKB	Mutagenesis	382	382	.	.	.	Note=Constitutively active%2C up-regulates amino acid permease transcription in response to subthreshold concentrations of amino acids. T->H%2CL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555474;Dbxref=PMID:14555474	
+Q03770	UniProtKB	Mutagenesis	382	382	.	.	.	Note=In SSY1-102%3B constitutively active%2C up-regulates amino acid permease transcription in the absence of amino-acids. T->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555474;Dbxref=PMID:14555474	
+Q03770	UniProtKB	Mutagenesis	382	382	.	.	.	Note=Constitutively active%2C up-regulates amino acid permease transcription in the absence of amino acids. T->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555474;Dbxref=PMID:14555474	
+##sequence-region P38788 1 538
+P38788	UniProtKB	Chain	1	538	.	.	.	ID=PRO_0000078400;Note=Ribosome-associated complex subunit SSZ1	
+P38788	UniProtKB	Region	400	538	.	.	.	Note=Peptide-binding domain;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38788	UniProtKB	Modified residue	477	477	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P38788	UniProtKB	Modified residue	480	480	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P38788	UniProtKB	Mutagenesis	295	295	.	.	.	Note=Increases readthrough in translation termination. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15456889;Dbxref=PMID:15456889	
+P38788	UniProtKB	Sequence conflict	208	208	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25379 1 360
+P25379	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25379	UniProtKB	Chain	2	360	.	.	.	ID=PRO_0000185598;Note=Catabolic L-serine/threonine dehydratase	
+P25379	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25379	UniProtKB	Modified residue	37	37	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P25379	UniProtKB	Sequence conflict	34	34	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25379	UniProtKB	Sequence conflict	268	268	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25379	UniProtKB	Sequence conflict	317	318	.	.	.	Note=GG->AS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33894 1 931
+P33894	UniProtKB	Chain	1	931	.	.	.	ID=PRO_0000122420;Note=Dipeptidyl aminopeptidase A	
+P33894	UniProtKB	Topological domain	1	119	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33894	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein	
+P33894	UniProtKB	Topological domain	141	931	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33894	UniProtKB	Active site	785	785	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33894	UniProtKB	Active site	863	863	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33894	UniProtKB	Active site	896	896	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P33894	UniProtKB	Glycosylation	377	377	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33894	UniProtKB	Glycosylation	814	814	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53538 1 206
+P53538	UniProtKB	Chain	1	206	.	.	.	ID=PRO_0000072230;Note=RNA polymerase II subunit A C-terminal domain phosphatase SSU72	
+P53538	UniProtKB	Sequence conflict	199	199	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53101 1 465
+P53101	UniProtKB	Chain	1	465	.	.	.	ID=PRO_0000114764;Note=Cystathionine beta-lyase	
+P53101	UniProtKB	Modified residue	213	213	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q12325 1 893
+Q12325	UniProtKB	Chain	1	893	.	.	.	ID=PRO_0000080185;Note=Sulfate permease 2	
+Q12325	UniProtKB	Topological domain	1	131	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	132	152	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	153	163	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	185	188	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	210	221	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	222	242	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	243	244	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	245	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	266	305	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	306	326	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	327	350	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	351	371	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	372	399	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	400	420	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	421	443	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	444	464	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	465	483	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	484	504	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	505	532	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	533	551	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	552	559	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Transmembrane	560	580	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Topological domain	581	893	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12325	UniProtKB	Domain	676	854	.	.	.	Note=STAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00198	
+##sequence-region P46676 1 1062
+P46676	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P46676	UniProtKB	Chain	2	1062	.	.	.	ID=PRO_0000072311;Note=Suppressor of mar1-1 protein	
+P46676	UniProtKB	Compositional bias	464	467	.	.	.	Note=Poly-Asn	
+P46676	UniProtKB	Compositional bias	514	523	.	.	.	Note=Poly-Ala	
+P46676	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P46676	UniProtKB	Modified residue	378	378	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46676	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46676	UniProtKB	Modified residue	628	628	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46676	UniProtKB	Modified residue	681	681	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46676	UniProtKB	Modified residue	697	697	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P46676	UniProtKB	Modified residue	712	712	.	.	.	Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46676	UniProtKB	Modified residue	738	738	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46676	UniProtKB	Modified residue	817	817	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P46676	UniProtKB	Mutagenesis	988	988	.	.	.	Note=Loss of function. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8754829;Dbxref=PMID:8754829	
+P46676	UniProtKB	Sequence conflict	1	20	.	.	.	Note=MSENTTAPSDNITNEQRLPS->MNRDFRL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46676	UniProtKB	Sequence conflict	30	30	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46676	UniProtKB	Sequence conflict	408	408	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46676	UniProtKB	Sequence conflict	523	523	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46676	UniProtKB	Sequence conflict	826	826	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P36150 1 593
+P36150	UniProtKB	Chain	1	593	.	.	.	ID=PRO_0000150387;Note=Uroporphyrinogen-III C-methyltransferase	
+##sequence-region P53616 1 420
+P53616	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9748433;Dbxref=PMID:9748433	
+P53616	UniProtKB	Chain	25	420	.	.	.	ID=PRO_0000033466;Note=Probable secreted beta-glucosidase SUN4	
+P53616	UniProtKB	Compositional bias	31	148	.	.	.	Note=Ser/Thr-rich	
+P53616	UniProtKB	Compositional bias	336	339	.	.	.	Note=Poly-Ser	
+P53616	UniProtKB	Glycosylation	395	395	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53616	UniProtKB	Sequence conflict	299	299	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P33300 1 382
+P33300	UniProtKB	Chain	1	382	.	.	.	ID=PRO_0000072314;Note=Mannosyl phosphorylinositol ceramide synthase SUR1	
+P33300	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33300	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33300	UniProtKB	Topological domain	28	269	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33300	UniProtKB	Transmembrane	270	290	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33300	UniProtKB	Topological domain	291	382	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P33300	UniProtKB	Modified residue	349	349	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P54003 1 302
+P54003	UniProtKB	Chain	1	302	.	.	.	ID=PRO_0000072317;Note=Protein SUR7	
+P54003	UniProtKB	Topological domain	1	10	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54003	UniProtKB	Transmembrane	11	31	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54003	UniProtKB	Topological domain	32	114	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54003	UniProtKB	Transmembrane	115	135	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54003	UniProtKB	Topological domain	136	145	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54003	UniProtKB	Transmembrane	146	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54003	UniProtKB	Topological domain	167	189	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54003	UniProtKB	Transmembrane	190	210	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54003	UniProtKB	Topological domain	211	302	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P54003	UniProtKB	Modified residue	293	293	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P54003	UniProtKB	Modified residue	301	301	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198	
+P54003	UniProtKB	Glycosylation	47	47	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53937 1 143
+P53937	UniProtKB	Chain	1	143	.	.	.	ID=PRO_0000132210;Note=37S ribosomal protein SWS2%2C mitochondrial	
+##sequence-region Q08553 1 188
+Q08553	UniProtKB	Chain	1	188	.	.	.	ID=PRO_0000076351;Note=Protein SYC1	
+##sequence-region P04802 1 557
+P04802	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:3902099,ECO:0000269|PubMed:9298649;Dbxref=PMID:3902099,PMID:9298649	
+P04802	UniProtKB	Chain	2	557	.	.	.	ID=PRO_0000111014;Note=Aspartate--tRNA ligase%2C cytoplasmic	
+P04802	UniProtKB	Nucleotide binding	325	327	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04802	UniProtKB	Nucleotide binding	333	335	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04802	UniProtKB	Nucleotide binding	528	531	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04802	UniProtKB	Region	303	306	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04802	UniProtKB	Binding site	281	281	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04802	UniProtKB	Binding site	325	325	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04802	UniProtKB	Binding site	478	478	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04802	UniProtKB	Binding site	481	481	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04802	UniProtKB	Binding site	485	485	.	.	.	Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04802	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P04802	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04802	UniProtKB	Modified residue	301	301	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P04802	UniProtKB	Modified residue	502	502	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P04802	UniProtKB	Modified residue	546	546	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P04802	UniProtKB	Mutagenesis	273	273	.	.	.	Note=Loss of activity%3B important for dimerization. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8248175;Dbxref=PMID:8248175	
+P04802	UniProtKB	Beta strand	73	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Turn	101	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	108	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	122	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	135	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	145	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	151	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	165	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	182	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	208	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	215	220	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	228	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	235	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	242	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	274	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	280	284	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	294	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	303	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	316	324	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	331	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ASZ	
+P04802	UniProtKB	Beta strand	336	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	352	372	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	374	383	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	393	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ASY	
+P04802	UniProtKB	Beta strand	398	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	402	411	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	418	420	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ASY	
+P04802	UniProtKB	Helix	424	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	441	446	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	450	452	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	461	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ASZ	
+P04802	UniProtKB	Beta strand	466	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	477	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	489	498	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Turn	506	508	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	509	515	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	522	528	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	529	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Helix	542	545	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV	
+P04802	UniProtKB	Beta strand	546	548	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ASY	
+##sequence-region P48525 1 536
+P48525	UniProtKB	Chain	1	536	.	.	.	ID=PRO_0000119740;Note=Glutamate--tRNA ligase%2C mitochondrial	
+P48525	UniProtKB	Nucleotide binding	291	295	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48525	UniProtKB	Region	48	50	.	.	.	Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48525	UniProtKB	Region	235	239	.	.	.	Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48525	UniProtKB	Motif	53	61	.	.	.	Note="HIGH" region	
+P48525	UniProtKB	Motif	291	295	.	.	.	Note="KMSKS" region	
+P48525	UniProtKB	Binding site	58	58	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48525	UniProtKB	Binding site	84	84	.	.	.	Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48525	UniProtKB	Binding site	253	253	.	.	.	Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48525	UniProtKB	Binding site	256	256	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48525	UniProtKB	Sequence conflict	464	464	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q02875 1 849
+Q02875	UniProtKB	Chain	1	849	.	.	.	ID=PRO_0000238645;Note=SMY2 homolog 2	
+Q02875	UniProtKB	Domain	149	205	.	.	.	Note=GYF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00101	
+Q02875	UniProtKB	Coiled coil	410	484	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02875	UniProtKB	Compositional bias	637	720	.	.	.	Note=Ser-rich	
+Q02875	UniProtKB	Modified residue	350	350	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P39965 1 576
+P39965	UniProtKB	Chain	1	576	.	.	.	ID=PRO_0000139354;Note=Probable proline--tRNA ligase%2C mitochondrial	
+##sequence-region P54000 1 292
+P54000	UniProtKB	Chain	1	292	.	.	.	ID=PRO_0000215951;Note=RNA polymerase II transcriptional coactivator SUB1	
+P54000	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P54000	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P54000	UniProtKB	Modified residue	269	269	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P54000	UniProtKB	Modified residue	289	289	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q07478 1 446
+Q07478	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q07478	UniProtKB	Chain	2	446	.	.	.	ID=PRO_0000055082;Note=ATP-dependent RNA helicase SUB2	
+Q07478	UniProtKB	Domain	93	268	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+Q07478	UniProtKB	Domain	280	441	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+Q07478	UniProtKB	Nucleotide binding	106	113	.	.	.	Note=ATP	
+Q07478	UniProtKB	Motif	62	90	.	.	.	Note=Q motif	
+Q07478	UniProtKB	Motif	215	218	.	.	.	Note=DECD box	
+Q07478	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q07478	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q07478	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q07478	UniProtKB	Modified residue	169	169	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q07478	UniProtKB	Mutagenesis	8	8	.	.	.	Note=No growth at 37 degrees Celsius%3B when associated with DEL-135. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156603;Dbxref=PMID:11156603	
+Q07478	UniProtKB	Mutagenesis	22	22	.	.	.	Note=In SUB2-1%3B no growth at 16 and 37 degrees Celsius%3B when associated with G-83%3B M-142 and T-146. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156604;Dbxref=PMID:11156604	
+Q07478	UniProtKB	Mutagenesis	83	83	.	.	.	Note=In SUB2-1%3B no growth at 16 and 37 degrees Celsius%3B when associated with G-22%3B M-142 and T-146. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156604;Dbxref=PMID:11156604	
+Q07478	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Lethal. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156602;Dbxref=PMID:11156602	
+Q07478	UniProtKB	Mutagenesis	122	122	.	.	.	Note=In SUB2-201%3B no growth at 37 degrees Celsius%3B when associated with G-173 and F-403. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156603;Dbxref=PMID:11156603	
+Q07478	UniProtKB	Mutagenesis	135	135	.	.	.	Note=No growth at 37 degrees Celsius%3B when associated with G-8. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156603;Dbxref=PMID:11156603	
+Q07478	UniProtKB	Mutagenesis	142	142	.	.	.	Note=In SUB2-1%3B no growth at 16 and 37 degrees Celsius%3B when associated with G-22%3B G-83 and T-146. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156604;Dbxref=PMID:11156604	
+Q07478	UniProtKB	Mutagenesis	146	146	.	.	.	Note=In SUB2-1%3B no growth at 16 and 37 degrees Celsius%3B when associated with G-22%3B G-83 and M-142. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156604;Dbxref=PMID:11156604	
+Q07478	UniProtKB	Mutagenesis	173	173	.	.	.	Note=In SUB2-201%3B no growth at 37 degrees Celsius%3B when associated with R-122 and F-403. K->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156603;Dbxref=PMID:11156603	
+Q07478	UniProtKB	Mutagenesis	174	174	.	.	.	Note=In SUB2-100%3B no growth at 37 degrees Celsius. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156602;Dbxref=PMID:11156602	
+Q07478	UniProtKB	Mutagenesis	215	215	.	.	.	Note=Lethal. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156602;Dbxref=PMID:11156602	
+Q07478	UniProtKB	Mutagenesis	217	217	.	.	.	Note=Lethal. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156602;Dbxref=PMID:11156602	
+Q07478	UniProtKB	Mutagenesis	247	247	.	.	.	Note=Lethal. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156602;Dbxref=PMID:11156602	
+Q07478	UniProtKB	Mutagenesis	308	308	.	.	.	Note=In SUB2-5%3B no growth at 16 degrees Celsius. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156604;Dbxref=PMID:11156604	
+Q07478	UniProtKB	Mutagenesis	403	403	.	.	.	Note=In SUB2-201%3B no growth at 37 degrees Celsius%3B when associated with R-122 and G-173. K->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156603;Dbxref=PMID:11156603	
+Q07478	UniProtKB	Helix	63	67	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	71	79	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	87	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Turn	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	102	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	113	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	133	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	140	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Turn	154	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	162	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	171	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Turn	181	183	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	186	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	192	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Turn	200	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	211	215	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	217	222	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	224	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	239	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Turn	252	254	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	255	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	266	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	273	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	281	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	290	292	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	293	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	307	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	316	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	333	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	338	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	342	353	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	358	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	364	366	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	367	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	375	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	387	394	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	399	401	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Beta strand	404	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	413	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+Q07478	UniProtKB	Helix	441	443	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP	
+##sequence-region P31376 1 625
+P31376	UniProtKB	Chain	1	625	.	.	.	ID=PRO_0000072344;Note=SWR1-complex protein 3	
+P31376	UniProtKB	Compositional bias	34	56	.	.	.	Note=Asp-rich	
+P31376	UniProtKB	Compositional bias	175	262	.	.	.	Note=Lys-rich	
+##sequence-region P53201 1 476
+P53201	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53201	UniProtKB	Chain	2	476	.	.	.	ID=PRO_0000072345;Note=SWR1-complex protein 4	
+P53201	UniProtKB	Domain	156	209	.	.	.	Note=SANT	
+P53201	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P38326 1 303
+P38326	UniProtKB	Chain	1	303	.	.	.	ID=PRO_0000212513;Note=SWR1-complex protein 5	
+P38326	UniProtKB	Domain	217	294	.	.	.	Note=BCNT-C;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00610	
+P38326	UniProtKB	Modified residue	209	209	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q06707 1 132
+Q06707	UniProtKB	Chain	1	132	.	.	.	ID=PRO_0000072346;Note=SWR1-complex protein 7	
+##sequence-region P36104 1 329
+P36104	UniProtKB	Chain	1	329	.	.	.	ID=PRO_0000051253;Note=COMPASS component SWD2	
+P36104	UniProtKB	Repeat	25	64	.	.	.	Note=WD 1	
+P36104	UniProtKB	Repeat	111	150	.	.	.	Note=WD 2	
+P36104	UniProtKB	Repeat	152	191	.	.	.	Note=WD 3	
+P36104	UniProtKB	Repeat	199	238	.	.	.	Note=WD 4	
+P36104	UniProtKB	Repeat	246	287	.	.	.	Note=WD 5	
+P36104	UniProtKB	Repeat	298	328	.	.	.	Note=WD 6	
+##sequence-region Q04175 1 944
+Q04175	UniProtKB	Chain	1	944	.	.	.	ID=PRO_0000269756;Note=Importin beta SMX1	
+Q04175	UniProtKB	Domain	25	97	.	.	.	Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115	
+##sequence-region P15624 1 595
+P15624	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:338359;Dbxref=PMID:338359	
+P15624	UniProtKB	Chain	2	595	.	.	.	ID=PRO_0000127023;Note=Phenylalanine--tRNA ligase beta subunit	
+P15624	UniProtKB	Domain	292	370	.	.	.	Note=B5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00816	
+P15624	UniProtKB	Region	86	90	.	.	.	Note=CCA binding of tRNA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P15624	UniProtKB	Sequence conflict	18	18	.	.	.	Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15624	UniProtKB	Sequence conflict	426	426	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15624	UniProtKB	Sequence conflict	544	544	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06817 1 618
+Q06817	UniProtKB	Chain	1	618	.	.	.	ID=PRO_0000073006;Note=Glycine--tRNA ligase 2	
+Q06817	UniProtKB	Nucleotide binding	219	221	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06817	UniProtKB	Nucleotide binding	229	234	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06817	UniProtKB	Nucleotide binding	347	348	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06817	UniProtKB	Nucleotide binding	470	473	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06817	UniProtKB	Region	234	238	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06817	UniProtKB	Region	466	470	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06817	UniProtKB	Binding site	101	101	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06817	UniProtKB	Binding site	187	187	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06817	UniProtKB	Binding site	325	325	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q06817	UniProtKB	Binding site	325	325	.	.	.	Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38088 1 690
+P38088	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000244,ECO:0000255;evidence=ECO:0000244|PubMed:22814378,ECO:0000255;Dbxref=PMID:22814378	
+P38088	UniProtKB	Chain	25	690	.	.	.	ID=PRO_0000073005;Note=Glycine--tRNA ligase 1%2C mitochondrial	
+P38088	UniProtKB	Nucleotide binding	283	285	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38088	UniProtKB	Nucleotide binding	293	298	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38088	UniProtKB	Nucleotide binding	410	411	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38088	UniProtKB	Nucleotide binding	535	538	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38088	UniProtKB	Region	298	302	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38088	UniProtKB	Region	531	535	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38088	UniProtKB	Binding site	132	132	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38088	UniProtKB	Binding site	251	251	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38088	UniProtKB	Binding site	388	388	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38088	UniProtKB	Binding site	388	388	.	.	.	Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38088	UniProtKB	Modified residue	25	25	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P38088	UniProtKB	Modified residue	226	226	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198	
+P38088	UniProtKB	Modified residue	476	476	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38088	UniProtKB	Modified residue	528	528	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38088	UniProtKB	Modified residue	689	689	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38088	UniProtKB	Alternative sequence	1	23	.	.	.	ID=VSP_041147;Note=In isoform Cytoplasmic. Missing	
+P38088	UniProtKB	Sequence conflict	586	587	.	.	.	Note=TT->HH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38088	UniProtKB	Sequence conflict	586	587	.	.	.	Note=TT->HH;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q6WNK7 1 96
+Q6WNK7	UniProtKB	Chain	1	96	.	.	.	ID=PRO_0000227806;Note=Transcription and mRNA export factor SUS1	
+Q6WNK7	UniProtKB	Cross-link	68	68	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+Q6WNK7	UniProtKB	Helix	7	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+Q6WNK7	UniProtKB	Helix	21	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+Q6WNK7	UniProtKB	Helix	38	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+Q6WNK7	UniProtKB	Helix	58	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+Q6WNK7	UniProtKB	Helix	75	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS	
+Q6WNK7	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FK5	
+##sequence-region P38869 1 228
+P38869	UniProtKB	Chain	1	228	.	.	.	ID=PRO_0000202934;Note=Protein SVP26	
+P38869	UniProtKB	Topological domain	1	1	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38869	UniProtKB	Transmembrane	2	22	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38869	UniProtKB	Topological domain	23	42	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38869	UniProtKB	Transmembrane	43	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38869	UniProtKB	Topological domain	60	88	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38869	UniProtKB	Transmembrane	89	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38869	UniProtKB	Topological domain	106	142	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38869	UniProtKB	Transmembrane	143	166	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38869	UniProtKB	Topological domain	167	228	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38869	UniProtKB	Glycosylation	115	115	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39706 1 426
+P39706	UniProtKB	Chain	1	426	.	.	.	ID=PRO_0000051251;Note=COMPASS component SWD1	
+P39706	UniProtKB	Repeat	24	63	.	.	.	Note=WD 1	
+P39706	UniProtKB	Repeat	70	109	.	.	.	Note=WD 2	
+P39706	UniProtKB	Repeat	212	251	.	.	.	Note=WD 3	
+P39706	UniProtKB	Repeat	264	307	.	.	.	Note=WD 4	
+P39706	UniProtKB	Repeat	310	350	.	.	.	Note=WD 5	
+##sequence-region P38123 1 315
+P38123	UniProtKB	Chain	1	315	.	.	.	ID=PRO_0000051255;Note=COMPASS component SWD3	
+P38123	UniProtKB	Repeat	53	93	.	.	.	Note=WD 1	
+P38123	UniProtKB	Repeat	94	133	.	.	.	Note=WD 2	
+P38123	UniProtKB	Repeat	136	178	.	.	.	Note=WD 3	
+P38123	UniProtKB	Repeat	187	228	.	.	.	Note=WD 4	
+P38123	UniProtKB	Repeat	238	278	.	.	.	Note=WD 5	
+P38123	UniProtKB	Repeat	285	314	.	.	.	Note=WD 6	
+##sequence-region P09547 1 1314
+P09547	UniProtKB	Chain	1	1314	.	.	.	ID=PRO_0000200596;Note=SWI/SNF chromatin-remodeling complex subunit SWI1	
+P09547	UniProtKB	Domain	406	493	.	.	.	Note=ARID;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00355	
+P09547	UniProtKB	Zinc finger	1241	1258	.	.	.	Note=C4-type	
+P09547	UniProtKB	Region	1	323	.	.	.	Note=Prion domain (PrD)	
+P09547	UniProtKB	Compositional bias	337	524	.	.	.	Note=Gln-rich	
+P09547	UniProtKB	Beta strand	396	398	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LI6	
+P09547	UniProtKB	Beta strand	402	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LI6	
+P09547	UniProtKB	Helix	408	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX	
+P09547	UniProtKB	Beta strand	426	429	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX	
+P09547	UniProtKB	Beta strand	434	437	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX	
+P09547	UniProtKB	Helix	442	447	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX	
+P09547	UniProtKB	Turn	448	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX	
+P09547	UniProtKB	Helix	453	456	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX	
+P09547	UniProtKB	Helix	460	469	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX	
+P09547	UniProtKB	Helix	474	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX	
+P09547	UniProtKB	Turn	492	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KN5	
+P09547	UniProtKB	Beta strand	498	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KN5	
+##sequence-region P32591 1 825
+P32591	UniProtKB	Chain	1	825	.	.	.	ID=PRO_0000197123;Note=SWI/SNF complex subunit SWI3	
+P32591	UniProtKB	Domain	305	402	.	.	.	Note=SWIRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00247	
+P32591	UniProtKB	Domain	522	573	.	.	.	Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624	
+P32591	UniProtKB	Region	694	722	.	.	.	Note=Leucine-zipper	
+P32591	UniProtKB	Compositional bias	1	304	.	.	.	Note=Asp/Glu-rich (acidic)	
+P32591	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32591	UniProtKB	Modified residue	185	185	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32591	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P32591	UniProtKB	Modified residue	657	657	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32591	UniProtKB	Mutagenesis	374	374	.	.	.	Note=Loss of DNA-binding. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16461455;Dbxref=PMID:16461455	
+P32591	UniProtKB	Mutagenesis	383	383	.	.	.	Note=Loss of DNA-binding%3B when associated with D-387. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16461455;Dbxref=PMID:16461455	
+P32591	UniProtKB	Mutagenesis	387	387	.	.	.	Note=Loss of DNA-binding%3B when associated with D-383. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16461455;Dbxref=PMID:16461455	
+P32591	UniProtKB	Mutagenesis	392	392	.	.	.	Note=Loss of DNA-binding. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16461455;Dbxref=PMID:16461455	
+P32591	UniProtKB	Helix	321	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3	
+P32591	UniProtKB	Helix	328	330	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3	
+P32591	UniProtKB	Helix	340	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3	
+P32591	UniProtKB	Helix	364	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3	
+P32591	UniProtKB	Helix	375	387	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3	
+P32591	UniProtKB	Beta strand	390	393	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3	
+##sequence-region P40825 1 983
+P40825	UniProtKB	Transit peptide	1	24	.	.	.	Note=Mitochondrion	
+P40825	UniProtKB	Chain	25	983	.	.	.	ID=PRO_0000075287;Note=Alanine--tRNA ligase%2C mitochondrial	
+P40825	UniProtKB	Metal binding	625	625	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03133	
+P40825	UniProtKB	Metal binding	629	629	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03133	
+P40825	UniProtKB	Metal binding	744	744	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03133	
+P40825	UniProtKB	Metal binding	748	748	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03133	
+P40825	UniProtKB	Modified residue	504	504	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40825	UniProtKB	Modified residue	975	975	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40825	UniProtKB	Alternative sequence	1	25	.	.	.	ID=VSP_040236;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40825	UniProtKB	Sequence conflict	4	7	.	.	.	Note=TTGL->NYRI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40825	UniProtKB	Sequence conflict	16	16	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40825	UniProtKB	Sequence conflict	161	161	.	.	.	Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40825	UniProtKB	Sequence conflict	490	492	.	.	.	Note=KDQ->RTK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40825	UniProtKB	Sequence conflict	865	866	.	.	.	Note=FE->LQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40528 1 902
+P40528	UniProtKB	Chain	1	902	.	.	.	ID=PRO_0000072382;Note=Protein SYG1	
+P40528	UniProtKB	Topological domain	1	404	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Transmembrane	405	425	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Topological domain	426	435	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Transmembrane	436	456	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Topological domain	457	497	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Transmembrane	498	518	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Topological domain	519	522	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Transmembrane	523	543	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Topological domain	544	554	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Transmembrane	555	575	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Topological domain	576	576	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Transmembrane	577	599	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Topological domain	600	732	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Transmembrane	733	753	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Topological domain	754	761	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Transmembrane	762	782	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Topological domain	783	902	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40528	UniProtKB	Domain	1	303	.	.	.	Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714	
+P40528	UniProtKB	Domain	606	815	.	.	.	Note=EXS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00712	
+P40528	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40528	UniProtKB	Modified residue	179	179	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40528	UniProtKB	Modified residue	859	859	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40528	UniProtKB	Modified residue	860	860	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P47002 1 699
+P47002	UniProtKB	Propeptide	1	381	.	.	.	ID=PRO_0000377374;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914	
+P47002	UniProtKB	Chain	382	699	.	.	.	ID=PRO_0000072232;Note=SPS-sensor serine protease component SSY5	
+P47002	UniProtKB	Region	459	699	.	.	.	Note=Serine protease	
+P47002	UniProtKB	Active site	465	465	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47002	UniProtKB	Active site	545	545	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47002	UniProtKB	Active site	640	640	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47002	UniProtKB	Mutagenesis	131	131	.	.	.	Note=In SSY5-13%3B constitutively active%2C confers 9.3%25 increased STP1 processing in the absence of amino acids. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914	
+P47002	UniProtKB	Mutagenesis	420	424	.	.	.	Note=Prevents maturation and amino-acid-induced STP1 cleavage. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15509782;Dbxref=PMID:15509782	
+P47002	UniProtKB	Mutagenesis	512	512	.	.	.	Note=In SSY5-6%3B constitutively active%2C confers 30%25 increased STP1 processing in the absence of amino acids. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15947203;Dbxref=PMID:15947203	
+P47002	UniProtKB	Mutagenesis	575	575	.	.	.	Note=In SSY5-14%3B constitutively active%2C confers 30%25 increased STP1 processing in the absence of amino acids. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914	
+P47002	UniProtKB	Mutagenesis	576	576	.	.	.	Note=In SSY5-15%3B constitutively active%2C confers 30%25 increased STP1 processing in the absence of amino acids. Q->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914	
+P47002	UniProtKB	Mutagenesis	581	581	.	.	.	Note=In SSY5-18%3B constitutively active%2C confers 15.5%25 increased STP1 processing in the absence of amino acids%3B when associated with H-632. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914	
+P47002	UniProtKB	Mutagenesis	632	632	.	.	.	Note=In SSY5-18%3B constitutively active%2C confers 15.5%25 increased STP1 processing in the absence of amino acids%3B when associated with N-581. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914	
+P47002	UniProtKB	Mutagenesis	640	640	.	.	.	Note=Impairs maturation and amino acid-induced STP1 cleavage. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15509782;Dbxref=PMID:15509782	
+##sequence-region P46679 1 850
+P46679	UniProtKB	Chain	1	850	.	.	.	ID=PRO_0000072252;Note=Protein STB2	
+P46679	UniProtKB	Compositional bias	270	273	.	.	.	Note=Poly-Gln	
+P46679	UniProtKB	Compositional bias	541	544	.	.	.	Note=Poly-Ser	
+P46679	UniProtKB	Modified residue	594	594	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46679	UniProtKB	Modified residue	625	625	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P23561 1 717
+P23561	UniProtKB	Chain	1	717	.	.	.	ID=PRO_0000086684;Note=Serine/threonine-protein kinase STE11	
+P23561	UniProtKB	Domain	20	84	.	.	.	Note=SAM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00184	
+P23561	UniProtKB	Domain	415	712	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23561	UniProtKB	Nucleotide binding	421	429	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23561	UniProtKB	Active site	579	579	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P23561	UniProtKB	Binding site	444	444	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P23561	UniProtKB	Modified residue	323	323	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P23561	UniProtKB	Modified residue	465	465	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23561	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Disrupts interaction with STE50 and abolishes signal transduction. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15327964;Dbxref=PMID:15327964	
+P23561	UniProtKB	Helix	24	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OW5	
+P23561	UniProtKB	Helix	36	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OW5	
+P23561	UniProtKB	Helix	49	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OW5	
+P23561	UniProtKB	Helix	57	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OW5	
+P23561	UniProtKB	Helix	68	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OW5	
+##sequence-region P01098 1 86
+P01098	UniProtKB	Transit peptide	1	23	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6194151;Dbxref=PMID:6194151	
+P01098	UniProtKB	Chain	24	86	.	.	.	ID=PRO_0000002555;Note=ATPase-stabilizing factor 9 kDa%2C mitochondrial	
+P01098	UniProtKB	Modified residue	24	24	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P39007 1 718
+P39007	UniProtKB	Chain	1	718	.	.	.	ID=PRO_0000072293;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3	
+P39007	UniProtKB	Topological domain	1	8	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Topological domain	30	113	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Topological domain	135	168	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Transmembrane	169	189	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Topological domain	190	207	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Transmembrane	208	228	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Topological domain	229	240	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Transmembrane	241	261	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Topological domain	262	266	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Topological domain	288	296	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Transmembrane	297	316	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Topological domain	317	358	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Transmembrane	359	379	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Topological domain	380	385	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Transmembrane	386	403	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Topological domain	404	404	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Transmembrane	405	425	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Topological domain	426	443	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Transmembrane	444	464	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Topological domain	465	718	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Glycosylation	60	60	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Glycosylation	535	535	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Glycosylation	539	539	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39007	UniProtKB	Mutagenesis	159	159	.	.	.	Note=Temperature sensitive and staurosporine sensitive. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470	
+P39007	UniProtKB	Mutagenesis	160	160	.	.	.	Note=Temperature sensitive and staurosporine sensitive. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470	
+P39007	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Temperature sensitive and staurosporine sensitive. G->R	
+P39007	UniProtKB	Mutagenesis	164	164	.	.	.	Note=Temperature sensitive and staurosporine sensitive. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470	
+P39007	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Lethal%3B abolishes interaction with OST1 and WBP1. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470	
+P39007	UniProtKB	Mutagenesis	210	210	.	.	.	Note=Temperature sensitive and staurosporine sensitive. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470	
+P39007	UniProtKB	Mutagenesis	393	393	.	.	.	Note=Staurosporine sensitive. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470	
+P39007	UniProtKB	Mutagenesis	404	404	.	.	.	Note=Lethal%3B abolishes interaction with OST1 and WBP1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470	
+P39007	UniProtKB	Mutagenesis	516	519	.	.	.	Note=Lethal%3B greatly reduces amount of OST1 in complex. WWDY->AAAA	
+P39007	UniProtKB	Mutagenesis	516	516	.	.	.	Note=Temperature-sensitive. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722	
+P39007	UniProtKB	Mutagenesis	517	517	.	.	.	Note=Lethal. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722	
+P39007	UniProtKB	Mutagenesis	518	518	.	.	.	Note=Lethal. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722	
+P39007	UniProtKB	Mutagenesis	519	519	.	.	.	Note=Temperature-sensitive. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722	
+P39007	UniProtKB	Mutagenesis	520	520	.	.	.	Note=Temperature-sensitive. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722	
+P39007	UniProtKB	Mutagenesis	554	556	.	.	.	Note=Temperature-sensitive%3B reduces amount of OST1 in complex. EEK->AAA	
+P39007	UniProtKB	Mutagenesis	592	594	.	.	.	Note=Lethal%3B reduces glycosylation%3B greatly reduces amount of OST1 in complex. RIS->AAA	
+P39007	UniProtKB	Mutagenesis	593	593	.	.	.	Note=Temperature-sensitive. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722	
+P39007	UniProtKB	Helix	467	470	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	472	474	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Turn	481	483	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	491	503	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Beta strand	508	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	512	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Turn	525	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Turn	531	535	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	536	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Beta strand	552	555	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	560	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Beta strand	578	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	601	606	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Beta strand	611	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	621	635	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	646	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Turn	663	665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	666	670	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	675	686	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	692	695	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Helix	698	700	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Beta strand	705	708	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+P39007	UniProtKB	Beta strand	712	716	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ	
+##sequence-region P38198 1 1513
+P38198	UniProtKB	Chain	1	1513	.	.	.	ID=PRO_0000072294;Note=Protein STU1	
+P38198	UniProtKB	Region	461	716	.	.	.	Note=Interaction with microtubules	
+P38198	UniProtKB	Modified residue	997	997	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38198	UniProtKB	Modified residue	1018	1018	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38198	UniProtKB	Modified residue	1047	1047	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38198	UniProtKB	Modified residue	1063	1063	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38198	UniProtKB	Modified residue	1167	1167	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region P46675 1 888
+P46675	UniProtKB	Chain	1	888	.	.	.	ID=PRO_0000072295;Note=Protein STU2	
+P46675	UniProtKB	Repeat	51	88	.	.	.	Note=HEAT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46675	UniProtKB	Repeat	175	216	.	.	.	Note=HEAT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46675	UniProtKB	Repeat	411	448	.	.	.	Note=HEAT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46675	UniProtKB	Repeat	453	490	.	.	.	Note=HEAT 4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46675	UniProtKB	Repeat	503	541	.	.	.	Note=HEAT 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00103	
+P46675	UniProtKB	Region	8	280	.	.	.	Note=TOG 1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16567500;Dbxref=PMID:16567500	
+P46675	UniProtKB	Region	326	550	.	.	.	Note=TOG 1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16567500;Dbxref=PMID:16567500	
+P46675	UniProtKB	Coiled coil	654	762	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46675	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P46675	UniProtKB	Modified residue	277	277	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P46675	UniProtKB	Modified residue	813	813	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P46675	UniProtKB	Mutagenesis	23	23	.	.	.	Note=Disrupts interaction with tubulin heterodimer. Impairs polymerase activity under microtubule stress. W->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17355870,ECO:0000269|PubMed:22904013;Dbxref=PMID:17355870,PMID:22904013	
+P46675	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Impairs polymerase activity under microtubule stress. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22904013;Dbxref=PMID:22904013	
+P46675	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Decreases interaction with tubulin heterodimer. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17355870;Dbxref=PMID:17355870	
+P46675	UniProtKB	Mutagenesis	151	151	.	.	.	Note=Disrupts interaction with tubulin heterodimer. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17355870;Dbxref=PMID:17355870	
+P46675	UniProtKB	Mutagenesis	200	200	.	.	.	Note=No effect on polymerase activity under normal conditions but impairs polymerase activity under microtubule stress. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22904013,ECO:0000269|PubMed:25097237;Dbxref=PMID:22904013,PMID:25097237	
+P46675	UniProtKB	Mutagenesis	341	341	.	.	.	Note=Disrupts interaction with tubulin heterodimer. Impairs polymerase activity under microtubule stress. W->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22904013,ECO:0000269|PubMed:25097237;Dbxref=PMID:22904013,PMID:25097237	
+P46675	UniProtKB	Mutagenesis	519	519	.	.	.	Note=Disrupts interaction with tubulin heterodimer. No effect on polymerase activity under normal conditions but impairs polymerase activity under microtubule stress. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22904013,ECO:0000269|PubMed:25097237;Dbxref=PMID:22904013,PMID:25097237	
+P46675	UniProtKB	Helix	14	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	23	38	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	58	63	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	69	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	93	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	117	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Beta strand	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	138	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	145	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	153	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Turn	171	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	177	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	185	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	188	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	197	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	231	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	256	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P46675	UniProtKB	Helix	325	327	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	332	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	341	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	356	358	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	370	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	386	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Turn	405	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	410	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	423	425	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	429	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	456	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	471	487	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	493	499	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Turn	500	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	503	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	516	533	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	536	538	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	539	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+P46675	UniProtKB	Helix	547	558	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1	
+##sequence-region P32911 1 108
+P32911	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32911	UniProtKB	Chain	2	108	.	.	.	ID=PRO_0000130566;Note=Eukaryotic translation initiation factor eIF-1	
+P32911	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P32911	UniProtKB	Beta strand	26	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P32911	UniProtKB	Beta strand	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OGH	
+P32911	UniProtKB	Beta strand	38	44	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P32911	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P32911	UniProtKB	Helix	51	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P32911	UniProtKB	Beta strand	67	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P32911	UniProtKB	Turn	72	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P32911	UniProtKB	Beta strand	77	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P32911	UniProtKB	Helix	86	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+P32911	UniProtKB	Beta strand	100	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM	
+##sequence-region Q12286 1 268
+Q12286	UniProtKB	Chain	1	268	.	.	.	ID=PRO_0000115015;Note=Sterol uptake protein 2	
+##sequence-region P32580 1 737
+P32580	UniProtKB	Transit peptide	1	25	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32580	UniProtKB	Chain	26	737	.	.	.	ID=PRO_0000013306;Note=ATP-dependent RNA helicase SUV3%2C mitochondrial	
+P32580	UniProtKB	Domain	226	365	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32580	UniProtKB	Domain	390	546	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P32580	UniProtKB	Nucleotide binding	239	246	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32580	UniProtKB	Mutagenesis	272	272	.	.	.	Note=In suv3-1%3B probably excised introns are less efficiently released. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1379722;Dbxref=PMID:1379722	
+P32580	UniProtKB	Sequence conflict	165	165	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32580	UniProtKB	Sequence conflict	664	664	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12254 1 260
+Q12254	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12254	UniProtKB	Chain	20	260	.	.	.	ID=PRO_0000022450;Note=Protein SVS1	
+Q12254	UniProtKB	Glycosylation	23	23	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12254	UniProtKB	Glycosylation	249	249	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12254	UniProtKB	Glycosylation	256	256	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04629 1 336
+Q04629	UniProtKB	Chain	1	336	.	.	.	ID=PRO_0000212994;Note=Palmitoyltransferase SWF1	
+Q04629	UniProtKB	Topological domain	1	2	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04629	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04629	UniProtKB	Topological domain	24	50	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04629	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04629	UniProtKB	Topological domain	72	86	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04629	UniProtKB	Transmembrane	87	107	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04629	UniProtKB	Topological domain	108	179	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04629	UniProtKB	Transmembrane	180	200	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04629	UniProtKB	Topological domain	201	216	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04629	UniProtKB	Transmembrane	217	237	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04629	UniProtKB	Topological domain	238	336	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04629	UniProtKB	Domain	134	184	.	.	.	Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067	
+Q04629	UniProtKB	Mutagenesis	164	164	.	.	.	Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15973437;Dbxref=PMID:15973437	
+##sequence-region P08425 1 469
+P08425	UniProtKB	Transit peptide	1	17	.	.	.	Note=Mitochondrion	
+P08425	UniProtKB	Chain	18	469	.	.	.	ID=PRO_0000035817;Note=Phenylalanine--tRNA ligase%2C mitochondrial	
+P08425	UniProtKB	Domain	372	469	.	.	.	Note=FDX-ACB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00778	
+P08425	UniProtKB	Region	126	129	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08425	UniProtKB	Region	162	164	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08425	UniProtKB	Region	169	171	.	.	.	Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08425	UniProtKB	Binding site	155	155	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08425	UniProtKB	Binding site	302	302	.	.	.	Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08425	UniProtKB	Binding site	329	329	.	.	.	Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P08425	UniProtKB	Sequence conflict	86	86	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P08425	UniProtKB	Sequence conflict	233	233	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P15180 1 591
+P15180	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P15180	UniProtKB	Chain	2	591	.	.	.	ID=PRO_0000152771;Note=Lysine--tRNA ligase%2C cytoplasmic	
+P15180	UniProtKB	Compositional bias	33	61	.	.	.	Note=Lys-rich (basic)	
+P15180	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P15180	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P15180	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P15180	UniProtKB	Cross-link	308	308	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P15180	UniProtKB	Cross-link	577	577	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P15180	UniProtKB	Mutagenesis	488	488	.	.	.	Note=In GCD5-1%3B defects in lysine-binding. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1505029;Dbxref=PMID:1505029	
+P15180	UniProtKB	Sequence conflict	22	22	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15180	UniProtKB	Sequence conflict	51	51	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15180	UniProtKB	Sequence conflict	111	111	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15180	UniProtKB	Sequence conflict	162	162	.	.	.	Note=C->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15180	UniProtKB	Sequence conflict	165	165	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15180	UniProtKB	Sequence conflict	259	259	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15180	UniProtKB	Sequence conflict	430	432	.	.	.	Note=ILV->VLA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15180	UniProtKB	Sequence conflict	591	591	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q04048 1 859
+Q04048	UniProtKB	Chain	1	859	.	.	.	ID=PRO_0000205737;Note=Pre-mRNA-splicing factor SYF1	
+Q04048	UniProtKB	Repeat	17	49	.	.	.	Note=HAT 1	
+Q04048	UniProtKB	Repeat	52	84	.	.	.	Note=HAT 2	
+Q04048	UniProtKB	Repeat	88	108	.	.	.	Note=HAT 3	
+Q04048	UniProtKB	Repeat	123	157	.	.	.	Note=HAT 4	
+Q04048	UniProtKB	Repeat	177	219	.	.	.	Note=HAT 5	
+Q04048	UniProtKB	Repeat	238	271	.	.	.	Note=HAT 6	
+Q04048	UniProtKB	Repeat	427	459	.	.	.	Note=HAT 7	
+Q04048	UniProtKB	Repeat	461	482	.	.	.	Note=HAT 8	
+Q04048	UniProtKB	Repeat	520	554	.	.	.	Note=HAT 9	
+Q04048	UniProtKB	Repeat	599	633	.	.	.	Note=HAT 10	
+Q04048	UniProtKB	Repeat	639	675	.	.	.	Note=HAT 11	
+Q04048	UniProtKB	Repeat	685	718	.	.	.	Note=HAT 12	
+Q04048	UniProtKB	Repeat	720	754	.	.	.	Note=HAT 13	
+Q04048	UniProtKB	Repeat	756	790	.	.	.	Note=HAT 14	
+Q04048	UniProtKB	Helix	570	578	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q04048	UniProtKB	Helix	585	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q04048	UniProtKB	Helix	602	611	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q04048	UniProtKB	Turn	612	614	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q04048	UniProtKB	Helix	616	635	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q04048	UniProtKB	Helix	641	652	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q04048	UniProtKB	Helix	664	675	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q04048	UniProtKB	Helix	680	688	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q04048	UniProtKB	Helix	707	719	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+Q04048	UniProtKB	Helix	723	733	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK	
+##sequence-region P07263 1 546
+P07263	UniProtKB	Transit peptide	1	20	.	.	.	Note=Mitochondrion	
+P07263	UniProtKB	Chain	21	546	.	.	.	ID=PRO_0000035804;Note=Histidine--tRNA ligase%2C mitochondrial	
+P07263	UniProtKB	Alternative sequence	1	20	.	.	.	ID=VSP_018907;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07263	UniProtKB	Sequence conflict	476	478	.	.	.	Note=AAE->TTK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07263	UniProtKB	Sequence conflict	476	478	.	.	.	Note=AAE->TTK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06563 1 197
+Q06563	UniProtKB	Chain	1	197	.	.	.	ID=PRO_0000234417;Note=Protein SYM1	
+Q06563	UniProtKB	Transmembrane	20	40	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06563	UniProtKB	Transmembrane	55	75	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06563	UniProtKB	Transmembrane	97	117	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06563	UniProtKB	Transmembrane	137	157	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06563	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Almost abolishes function. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16582910;Dbxref=PMID:16582910	
+Q06563	UniProtKB	Mutagenesis	54	54	.	.	.	Note=Loss of function. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16582910;Dbxref=PMID:16582910	
+Q06563	UniProtKB	Mutagenesis	172	172	.	.	.	Note=Loss of function. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16582910;Dbxref=PMID:16582910	
+##sequence-region Q05506 1 607
+Q05506	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q05506	UniProtKB	Chain	2	607	.	.	.	ID=PRO_0000151664;Note=Arginine--tRNA ligase%2C cytoplasmic	
+Q05506	UniProtKB	Region	59	60	.	.	.	Note=Interaction with tRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11060012;Dbxref=PMID:11060012	
+Q05506	UniProtKB	Region	106	111	.	.	.	Note=Interaction with tRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11060012;Dbxref=PMID:11060012	
+Q05506	UniProtKB	Region	148	153	.	.	.	Note=L-arginine binding;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1BS2,ECO:0000244|PDB:1F7U,ECO:0000269|PubMed:11060012,ECO:0000269|PubMed:9736621;Dbxref=PMID:11060012,PMID:9736621	
+Q05506	UniProtKB	Region	484	498	.	.	.	Note=Interaction with tRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11060012;Dbxref=PMID:11060012	
+Q05506	UniProtKB	Motif	151	162	.	.	.	Note="HIGH" region	
+Q05506	UniProtKB	Binding site	162	162	.	.	.	Note=L-arginine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1BS2,ECO:0000269|PubMed:9736621;Dbxref=PMID:9736621	
+Q05506	UniProtKB	Binding site	347	347	.	.	.	Note=L-arginine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1BS2,ECO:0000244|PDB:1F7U,ECO:0000269|PubMed:11060012,ECO:0000269|PubMed:9736621;Dbxref=PMID:11060012,PMID:9736621	
+Q05506	UniProtKB	Binding site	351	351	.	.	.	Note=L-arginine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1BS2,ECO:0000244|PDB:1F7U,ECO:0000269|PubMed:11060012,ECO:0000269|PubMed:9736621;Dbxref=PMID:11060012,PMID:9736621	
+Q05506	UniProtKB	Binding site	375	375	.	.	.	Note=L-arginine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1BS2,ECO:0000244|PDB:1F7U,ECO:0000269|PubMed:11060012,ECO:0000269|PubMed:9736621;Dbxref=PMID:11060012,PMID:9736621	
+Q05506	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q05506	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q05506	UniProtKB	Helix	3	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	19	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Turn	27	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	31	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	51	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	55	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	64	66	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	68	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	83	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Turn	97	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	109	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	116	130	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	131	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	144	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	160	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	163	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	182	190	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	194	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	209	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	216	233	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	235	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BS2	
+Q05506	UniProtKB	Turn	240	242	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	243	245	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	246	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	260	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	289	293	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	294	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	299	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	315	318	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	321	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	326	328	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Turn	331	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	335	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Turn	341	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BS2	
+Q05506	UniProtKB	Helix	347	362	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	365	370	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	373	375	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	376	388	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	392	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	397	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	405	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Turn	410	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	418	434	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	437	440	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	446	463	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	475	479	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Beta strand	482	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	486	502	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Turn	503	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	508	511	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	516	518	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	522	531	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	534	544	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	547	567	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+Q05506	UniProtKB	Helix	575	599	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U	
+##sequence-region P07284 1 462
+P07284	UniProtKB	Chain	1	462	.	.	.	ID=PRO_0000122199;Note=Serine--tRNA ligase%2C cytoplasmic	
+P07284	UniProtKB	Nucleotide binding	279	281	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07284	UniProtKB	Nucleotide binding	366	369	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07284	UniProtKB	Region	246	248	.	.	.	Note=Serine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07284	UniProtKB	Binding site	295	295	.	.	.	Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07284	UniProtKB	Binding site	302	302	.	.	.	Note=Serine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07284	UniProtKB	Binding site	404	404	.	.	.	Note=Serine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07284	UniProtKB	Sequence conflict	224	224	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40150 1 613
+P40150	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P40150	UniProtKB	Chain	2	613	.	.	.	ID=PRO_0000078390;Note=Ribosome-associated molecular chaperone SSB2	
+P40150	UniProtKB	Nucleotide binding	16	18	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P40150	UniProtKB	Nucleotide binding	205	207	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P40150	UniProtKB	Nucleotide binding	271	278	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P40150	UniProtKB	Region	2	391	.	.	.	Note=Nucleotide binding domain (NBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P40150	UniProtKB	Region	392	402	.	.	.	Note=Inter-domain linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P40150	UniProtKB	Region	403	613	.	.	.	Note=Substrate binding domain (SBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P40150	UniProtKB	Region	516	612	.	.	.	Note=Lid domain (SBDalpha);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P40150	UniProtKB	Region	601	613	.	.	.	Note=Required for interaction with ribosomes;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27917864;Dbxref=PMID:27917864	
+P40150	UniProtKB	Motif	428	430	.	.	.	Note=Contributes to ribosome binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27917864;Dbxref=PMID:27917864	
+P40150	UniProtKB	Motif	574	582	.	.	.	Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11484	
+P40150	UniProtKB	Binding site	73	73	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P40150	UniProtKB	Binding site	342	342	.	.	.	Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5	
+P40150	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P40150	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956	
+P40150	UniProtKB	Modified residue	431	431	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11484	
+##sequence-region Q12153 1 453
+Q12153	UniProtKB	Chain	1	453	.	.	.	ID=PRO_0000120260;Note=Ribosome biogenesis protein SSF2	
+Q12153	UniProtKB	Domain	26	348	.	.	.	Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034	
+##sequence-region P25390 1 1331
+P25390	UniProtKB	Chain	1	1331	.	.	.	ID=PRO_0000086681;Note=Serine/threonine-protein kinase SSK22	
+P25390	UniProtKB	Domain	1034	1310	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P25390	UniProtKB	Nucleotide binding	1040	1048	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P25390	UniProtKB	Active site	1158	1158	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P25390	UniProtKB	Binding site	1063	1063	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+##sequence-region Q04673 1 461
+Q04673	UniProtKB	Chain	1	461	.	.	.	ID=PRO_0000046852;Note=Suppressor of stem-loop protein 1	
+Q04673	UniProtKB	Domain	125	304	.	.	.	Note=VWFA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00219	
+Q04673	UniProtKB	Zinc finger	349	366	.	.	.	Note=C4-type	
+Q04673	UniProtKB	Sequence conflict	131	131	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q04673	UniProtKB	Beta strand	125	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Helix	134	137	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Beta strand	139	143	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Helix	145	163	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Beta strand	168	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Beta strand	178	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Helix	189	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Helix	210	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Beta strand	231	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Helix	247	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Beta strand	260	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Helix	271	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Turn	280	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Beta strand	288	291	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+Q04673	UniProtKB	Helix	294	305	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ	
+##sequence-region P13574 1 688
+P13574	UniProtKB	Chain	1	688	.	.	.	ID=PRO_0000072262;Note=Protein STE12	
+P13574	UniProtKB	DNA binding	57	167	.	.	.	.	
+P13574	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P13574	UniProtKB	Modified residue	214	214	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13574	UniProtKB	Modified residue	226	226	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P13574	UniProtKB	Modified residue	289	289	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P13574	UniProtKB	Modified residue	400	400	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P47154 1 453
+P47154	UniProtKB	Chain	1	453	.	.	.	ID=PRO_0000138846;Note=CAAX prenyl protease 1	
+P47154	UniProtKB	Topological domain	1	12	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Transmembrane	13	33	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Topological domain	34	89	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Transmembrane	90	110	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Topological domain	111	121	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Transmembrane	122	142	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Topological domain	143	167	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Topological domain	189	197	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Topological domain	219	306	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Transmembrane	307	327	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Topological domain	328	357	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Transmembrane	358	378	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Topological domain	379	453	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47154	UniProtKB	Active site	298	298	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P47154	UniProtKB	Active site	394	394	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P47154	UniProtKB	Metal binding	297	297	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P47154	UniProtKB	Metal binding	301	301	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+P47154	UniProtKB	Metal binding	390	390	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
+##sequence-region P32597 1 1359
+P32597	UniProtKB	Chain	1	1359	.	.	.	ID=PRO_0000074361;Note=Nuclear protein STH1/NPS1	
+P32597	UniProtKB	Domain	307	383	.	.	.	Note=HSA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00549	
+P32597	UniProtKB	Domain	482	647	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
+P32597	UniProtKB	Domain	795	956	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
+P32597	UniProtKB	Domain	1270	1340	.	.	.	Note=Bromo;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035	
+P32597	UniProtKB	Nucleotide binding	495	502	.	.	.	Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32597	UniProtKB	Motif	597	600	.	.	.	Note=DEGH box	
+P32597	UniProtKB	Compositional bias	1198	1247	.	.	.	Note=Lys-rich	
+P32597	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32597	UniProtKB	Mutagenesis	505	505	.	.	.	Note=Temperature-sensitive. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9799253;Dbxref=PMID:9799253	
+P32597	UniProtKB	Mutagenesis	646	646	.	.	.	Note=Temperature-sensitive. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9799253;Dbxref=PMID:9799253	
+P32597	UniProtKB	Mutagenesis	763	763	.	.	.	Note=Temperature-sensitive. Reduced sporulation efficiency. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10320476;Dbxref=PMID:10320476	
+P32597	UniProtKB	Mutagenesis	792	792	.	.	.	Note=Complete inactivation. K->E	
+P32597	UniProtKB	Mutagenesis	806	806	.	.	.	Note=Temperature-sensitive%3B when associated with M-881. Altered cell cycle distribution. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9799253;Dbxref=PMID:9799253	
+P32597	UniProtKB	Mutagenesis	881	881	.	.	.	Note=Temperature-sensitive%3B when associated with L-806. Altered cell cycle distribution. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9799253;Dbxref=PMID:9799253	
+P32597	UniProtKB	Sequence conflict	105	106	.	.	.	Note=DK->NE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32597	UniProtKB	Sequence conflict	144	144	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32597	UniProtKB	Sequence conflict	227	227	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32597	UniProtKB	Sequence conflict	546	546	.	.	.	Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32597	UniProtKB	Sequence conflict	566	566	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32597	UniProtKB	Sequence conflict	1010	1010	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32597	UniProtKB	Sequence conflict	1074	1080	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32597	UniProtKB	Sequence conflict	1114	1114	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32597	UniProtKB	Sequence conflict	1157	1157	.	.	.	Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32597	UniProtKB	Sequence conflict	1221	1221	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32597	UniProtKB	Sequence conflict	1246	1246	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25604 1 385
+P25604	UniProtKB	Chain	1	385	.	.	.	ID=PRO_0000082605;Note=Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease	
+P25604	UniProtKB	Domain	12	161	.	.	.	Note=UEV;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00652	
+P25604	UniProtKB	Domain	322	385	.	.	.	Note=SB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00644	
+P25604	UniProtKB	Coiled coil	272	300	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25604	UniProtKB	Compositional bias	155	201	.	.	.	Note=Pro-rich	
+P25604	UniProtKB	Mutagenesis	85	85	.	.	.	Note=No interaction of the ESCRT-I complex with ubiquitin. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11511343;Dbxref=PMID:11511343	
+P25604	UniProtKB	Mutagenesis	254	254	.	.	.	Note=Defective in ESCRT-I cargo sorting%3B reduces MVB12 localization to MVBs%3B abolishes interaction with MVB12%3B reduces interaction with SRN2. M->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+P25604	UniProtKB	Mutagenesis	286	286	.	.	.	Note=Defective in ESCRT-I cargo sorting. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384	
+P25604	UniProtKB	Mutagenesis	345	345	.	.	.	Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVBs). L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894	
+P25604	UniProtKB	Mutagenesis	371	371	.	.	.	Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVBs). F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894	
+P25604	UniProtKB	Helix	11	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Turn	22	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Helix	28	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Beta strand	45	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Beta strand	59	70	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Beta strand	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R42	
+P25604	UniProtKB	Beta strand	80	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Turn	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Beta strand	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Helix	102	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Turn	107	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Helix	116	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Beta strand	124	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Helix	129	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Helix	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Helix	141	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q	
+P25604	UniProtKB	Helix	219	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+P25604	UniProtKB	Helix	248	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+P25604	UniProtKB	Helix	254	289	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+P25604	UniProtKB	Helix	291	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+P25604	UniProtKB	Helix	314	316	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22	
+P25604	UniProtKB	Helix	323	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M	
+P25604	UniProtKB	Helix	356	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M	
+P25604	UniProtKB	Turn	382	384	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M	
+##sequence-region P38704 1 541
+P38704	UniProtKB	Zinc finger	204	226	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P38704	UniProtKB	Zinc finger	232	267	.	.	.	Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P38704	UniProtKB	Zinc finger	284	309	.	.	.	Note=C2H2-type 3%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P38704	UniProtKB	Region	13	32	.	.	.	Note=I	
+P38704	UniProtKB	Region	73	105	.	.	.	Note=II	
+P38704	UniProtKB	Mutagenesis	2	74	.	.	.	Note=Dominant active transcription factor. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502738;Dbxref=PMID:12502738	
+P38704	UniProtKB	Sequence conflict	101	101	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38637 1 319
+P38637	UniProtKB	Chain	1	319	.	.	.	ID=PRO_0000079792;Note=Tethering factor for nuclear proteasome STS1	
+P38637	UniProtKB	Compositional bias	43	49	.	.	.	Note=Poly-Glu	
+P38637	UniProtKB	Compositional bias	303	308	.	.	.	Note=Poly-Asn	
+P38637	UniProtKB	Sequence conflict	231	231	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P37297 1 1900
+P37297	UniProtKB	Chain	1	1900	.	.	.	ID=PRO_0000088835;Note=Phosphatidylinositol 4-kinase STT4	
+P37297	UniProtKB	Domain	1345	1530	.	.	.	Note=PIK helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00878	
+P37297	UniProtKB	Domain	1643	1882	.	.	.	Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269	
+P37297	UniProtKB	Region	1531	1648	.	.	.	Note=Pleckstrin homology (PH) domain conferring phosphoinositide binding specificity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P37297	UniProtKB	Modified residue	459	459	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P32579 1 426
+P32579	UniProtKB	Chain	1	426	.	.	.	ID=PRO_0000202013;Note=Threonylcarbamoyl-AMP synthase	
+P32579	UniProtKB	Domain	49	252	.	.	.	Note=YrdC-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00518	
+P32579	UniProtKB	Compositional bias	225	313	.	.	.	Note=Gly-rich	
+P32579	UniProtKB	Binding site	72	72	.	.	.	Note=L-threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Binding site	95	95	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Binding site	99	99	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Binding site	104	104	.	.	.	Note=L-threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Binding site	170	170	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Binding site	174	174	.	.	.	Note=L-threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Binding site	194	194	.	.	.	Note=L-threonine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Binding site	196	196	.	.	.	Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Binding site	204	204	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Binding site	234	234	.	.	.	Note=L-threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Binding site	248	248	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Binding site	292	292	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32579	UniProtKB	Mutagenesis	70	70	.	.	.	Note=Reduces t(6)A37 formation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P32579	UniProtKB	Mutagenesis	93	93	.	.	.	Note=Severely impairs t(6)A37 formation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P32579	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Severely impairs t(6)A37 formation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P32579	UniProtKB	Mutagenesis	107	107	.	.	.	Note=In SUA5-1%3B suppresses a translation initiation defect in a CYC1 allele at an aberrant ATG codon. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1325384;Dbxref=PMID:1325384	
+P32579	UniProtKB	Mutagenesis	174	174	.	.	.	Note=Severely impairs t(6)A37 formation. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P32579	UniProtKB	Mutagenesis	196	196	.	.	.	Note=Severely impairs t(6)A37 formation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P32579	UniProtKB	Mutagenesis	198	198	.	.	.	Note=Severely impairs t(6)A37 formation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P32579	UniProtKB	Mutagenesis	234	234	.	.	.	Note=Severely impairs t(6)A37 formation. S->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299	
+P32579	UniProtKB	Mutagenesis	423	423	.	.	.	Note=No phenotypes. C->S	
+##sequence-region P53032 1 299
+P53032	UniProtKB	Chain	1	299	.	.	.	ID=PRO_0000115014;Note=Sterol uptake protein 1	
+##sequence-region P32944 1 819
+P32944	UniProtKB	Chain	1	819	.	.	.	ID=PRO_0000086727;Note=Mitosis inhibitor protein kinase SWE1	
+P32944	UniProtKB	Domain	444	794	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32944	UniProtKB	Nucleotide binding	450	458	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32944	UniProtKB	Compositional bias	88	96	.	.	.	Note=Poly-Glu	
+P32944	UniProtKB	Active site	579	579	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P32944	UniProtKB	Metal binding	584	584	.	.	.	Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32944	UniProtKB	Metal binding	597	597	.	.	.	Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32944	UniProtKB	Binding site	473	473	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P32944	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:15037762,PMID:16096060	
+P32944	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	105	105	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	111	111	.	.	.	Note=Phosphoserine%3B by CDC5%2C CDC28 and CLA4;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:15037762,PMID:16096060	
+P32944	UniProtKB	Modified residue	118	118	.	.	.	Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:15037762,PMID:16096060	
+P32944	UniProtKB	Modified residue	121	121	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphothreonine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	133	133	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	136	136	.	.	.	Note=Phosphoserine%3B by CDC28 and CLA4;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:15037762,PMID:16096060	
+P32944	UniProtKB	Modified residue	156	156	.	.	.	Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	169	169	.	.	.	Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	201	201	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	254	254	.	.	.	Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	262	262	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	263	263	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	266	266	.	.	.	Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	280	280	.	.	.	Note=Phosphothreonine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	284	284	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	294	294	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	312	312	.	.	.	Note=Phosphoserine%3B by CLA4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	345	345	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	373	373	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphoserine%3B by CDC5 and CLA4;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:19779198,PMID:15037762,PMID:16096060	
+P32944	UniProtKB	Modified residue	384	384	.	.	.	Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Modified residue	395	395	.	.	.	Note=Phosphoserine%3B by CDC5 and CLA4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	438	438	.	.	.	Note=Phosphoserine%3B by CDC5 and CLA4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	610	610	.	.	.	Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:15037762,PMID:16096060	
+P32944	UniProtKB	Modified residue	629	629	.	.	.	Note=Phosphothreonine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	688	688	.	.	.	Note=Phosphothreonine%3B by CDC5 and CLA4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762	
+P32944	UniProtKB	Modified residue	692	692	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060	
+P32944	UniProtKB	Cross-link	741	741	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P32944	UniProtKB	Mutagenesis	318	328	.	.	.	Note=Impairs interaction with HSL7 and prevents bud neck localization and degradation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757	
+P32944	UniProtKB	Mutagenesis	320	320	.	.	.	Note=Prevents degradation. L->P%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757	
+P32944	UniProtKB	Mutagenesis	324	324	.	.	.	Note=Prevents degradation. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757	
+P32944	UniProtKB	Mutagenesis	327	327	.	.	.	Note=Prevents degradation. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757	
+P32944	UniProtKB	Mutagenesis	328	328	.	.	.	Note=Prevents degradation. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757	
+P32944	UniProtKB	Mutagenesis	331	331	.	.	.	Note=Prevents degradation. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757	
+P32944	UniProtKB	Mutagenesis	332	332	.	.	.	Note=Prevents degradation. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757	
+P32944	UniProtKB	Mutagenesis	473	473	.	.	.	Note=Loss of catalytic activity. K->A%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10454545;Dbxref=PMID:10454545	
+P32944	UniProtKB	Mutagenesis	797	797	.	.	.	Note=Prevents degradation. E->K%2CV%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757	
+P32944	UniProtKB	Mutagenesis	806	806	.	.	.	Note=Prevents degradation. I->T%2CA%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757	
+P32944	UniProtKB	Mutagenesis	807	807	.	.	.	Note=Prevents degradation. Q->R%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757	
+##sequence-region P25302 1 1093
+P25302	UniProtKB	Chain	1	1093	.	.	.	ID=PRO_0000067069;Note=Regulatory protein SWI4	
+P25302	UniProtKB	Domain	37	147	.	.	.	Note=HTH APSES-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630	
+P25302	UniProtKB	Repeat	520	549	.	.	.	Note=ANK 1	
+P25302	UniProtKB	Repeat	641	670	.	.	.	Note=ANK 2	
+P25302	UniProtKB	DNA binding	71	92	.	.	.	Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630	
+P25302	UniProtKB	Compositional bias	201	727	.	.	.	Note=Asn/Gln-rich	
+P25302	UniProtKB	Modified residue	255	255	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25302	UniProtKB	Modified residue	806	806	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P25302	UniProtKB	Sequence conflict	175	175	.	.	.	Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25302	UniProtKB	Sequence conflict	431	431	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P25302	UniProtKB	Sequence conflict	1054	1054	.	.	.	Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P15625 1 503
+P15625	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P15625	UniProtKB	Chain	2	503	.	.	.	ID=PRO_0000126828;Note=Phenylalanine--tRNA ligase alpha subunit	
+P15625	UniProtKB	Region	2	173	.	.	.	Note=Contains the major tRNA-Phe binding sites	
+P15625	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P15625	UniProtKB	Sequence conflict	177	177	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P15625	UniProtKB	Sequence conflict	289	289	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P32048 1 576
+P32048	UniProtKB	Transit peptide	1	30	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32048	UniProtKB	Chain	31	576	.	.	.	ID=PRO_0000035812;Note=Lysine--tRNA ligase%2C mitochondrial	
+##sequence-region P11325 1 894
+P11325	UniProtKB	Transit peptide	1	9	.	.	.	Note=Mitochondrion	
+P11325	UniProtKB	Chain	10	894	.	.	.	ID=PRO_0000035810;Note=Leucine--tRNA ligase%2C mitochondrial	
+P11325	UniProtKB	Motif	56	66	.	.	.	Note="HIGH" region	
+P11325	UniProtKB	Motif	646	650	.	.	.	Note="KMSKS" region	
+P11325	UniProtKB	Binding site	649	649	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q07395 1 620
+Q07395	UniProtKB	Chain	1	620	.	.	.	ID=PRO_0000248459;Note=Synchronized import protein 1	
+Q07395	UniProtKB	Repeat	25	64	.	.	.	Note=ARM 1	
+Q07395	UniProtKB	Repeat	66	106	.	.	.	Note=ARM 2	
+Q07395	UniProtKB	Repeat	181	221	.	.	.	Note=ARM 3	
+Q07395	UniProtKB	Repeat	258	299	.	.	.	Note=ARM 4	
+Q07395	UniProtKB	Repeat	340	386	.	.	.	Note=ARM 5	
+Q07395	UniProtKB	Repeat	435	470	.	.	.	Note=ARM 6	
+Q07395	UniProtKB	Repeat	471	510	.	.	.	Note=ARM 7	
+Q07395	UniProtKB	Repeat	564	607	.	.	.	Note=ARM 8	
+##sequence-region P07806 1 1104
+P07806	UniProtKB	Transit peptide	1	47	.	.	.	Note=Mitochondrion	
+P07806	UniProtKB	Chain	48	1104	.	.	.	ID=PRO_0000035839;Note=Valine--tRNA ligase%2C mitochondrial	
+P07806	UniProtKB	Motif	190	200	.	.	.	Note="HIGH" region	
+P07806	UniProtKB	Motif	703	707	.	.	.	Note="KMSKS" region	
+P07806	UniProtKB	Binding site	706	706	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P07806	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07806	UniProtKB	Modified residue	294	294	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07806	UniProtKB	Modified residue	332	332	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07806	UniProtKB	Modified residue	707	707	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07806	UniProtKB	Modified residue	1003	1003	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P07806	UniProtKB	Alternative sequence	1	46	.	.	.	ID=VSP_018910;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07806	UniProtKB	Sequence conflict	147	147	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07806	UniProtKB	Sequence conflict	540	540	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P41895 1 735
+P41895	UniProtKB	Chain	1	735	.	.	.	ID=PRO_0000211234;Note=Transcription initiation factor IIF subunit alpha	
+P41895	UniProtKB	Compositional bias	455	580	.	.	.	Note=Asp/Glu-rich (acidic)	
+P41895	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P41895	UniProtKB	Modified residue	200	200	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P41895	UniProtKB	Modified residue	515	515	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P41895	UniProtKB	Modified residue	560	560	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41895	UniProtKB	Modified residue	562	562	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41895	UniProtKB	Modified residue	571	571	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P41895	UniProtKB	Modified residue	655	655	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956	
+P41895	UniProtKB	Sequence conflict	238	238	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12030 1 206
+Q12030	UniProtKB	Chain	1	206	.	.	.	ID=PRO_0000118901;Note=Transcription initiation factor TFIID subunit 10	
+Q12030	UniProtKB	Domain	47	194	.	.	.	Note=Histone-fold	
+Q12030	UniProtKB	Compositional bias	147	172	.	.	.	Note=Gln-rich	
+Q12030	UniProtKB	Modified residue	58	58	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12030	UniProtKB	Modified residue	146	146	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P35189 1 244
+P35189	UniProtKB	Chain	1	244	.	.	.	ID=PRO_0000211241;Note=Transcription initiation factor TFIID subunit 14	
+P35189	UniProtKB	Domain	8	115	.	.	.	Note=YEATS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00376	
+P35189	UniProtKB	Cross-link	181	181	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P35189	UniProtKB	Sequence conflict	116	116	.	.	.	Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P35189	UniProtKB	Beta strand	3	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+P35189	UniProtKB	Beta strand	30	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+P35189	UniProtKB	Beta strand	40	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L7E	
+P35189	UniProtKB	Beta strand	45	47	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D7E	
+P35189	UniProtKB	Beta strand	51	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+P35189	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+P35189	UniProtKB	Beta strand	66	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+P35189	UniProtKB	Beta strand	76	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+P35189	UniProtKB	Beta strand	86	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+P35189	UniProtKB	Helix	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+P35189	UniProtKB	Beta strand	97	103	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+P35189	UniProtKB	Beta strand	107	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+P35189	UniProtKB	Helix	125	131	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+P35189	UniProtKB	Turn	132	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL	
+##sequence-region P23255 1 1407
+P23255	UniProtKB	Chain	1	1407	.	.	.	ID=PRO_0000118867;Note=Transcription initiation factor TFIID subunit 2	
+P23255	UniProtKB	Region	1285	1350	.	.	.	Note=Highly charged	
+P23255	UniProtKB	Coiled coil	304	337	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P23255	UniProtKB	Compositional bias	52	55	.	.	.	Note=Poly-Ile	
+P23255	UniProtKB	Compositional bias	259	334	.	.	.	Note=Asp/Glu-rich (acidic)	
+P23255	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23255	UniProtKB	Modified residue	161	161	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P23255	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P23255	UniProtKB	Modified residue	318	318	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P23255	UniProtKB	Sequence conflict	323	323	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12297 1 353
+Q12297	UniProtKB	Chain	1	353	.	.	.	ID=PRO_0000118868;Note=Transcription initiation factor TFIID subunit 3	
+Q12297	UniProtKB	Domain	11	78	.	.	.	Note=Histone-fold	
+Q12297	UniProtKB	Coiled coil	289	309	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12297	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q12297	UniProtKB	Modified residue	310	310	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q12297	UniProtKB	Modified residue	346	346	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38992 1 349
+P38992	UniProtKB	Chain	1	349	.	.	.	ID=PRO_0000072316;Note=Sphingolipid C4-hydroxylase SUR2	
+P38992	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38992	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38992	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38992	UniProtKB	Transmembrane	148	168	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38992	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40342 1 146
+P40342	UniProtKB	Chain	1	146	.	.	.	ID=PRO_0000203468;Note=Nucleolar protein SWM2	
+##sequence-region P53873 1 357
+P53873	UniProtKB	Chain	1	357	.	.	.	ID=PRO_0000203403;Note=Protein SWT21	
+##sequence-region P09436 1 1072
+P09436	UniProtKB	Chain	1	1072	.	.	.	ID=PRO_0000098604;Note=Isoleucine--tRNA ligase%2C cytoplasmic	
+P09436	UniProtKB	Motif	47	57	.	.	.	Note="HIGH" region	
+P09436	UniProtKB	Motif	602	606	.	.	.	Note="KMSKS" region	
+P09436	UniProtKB	Binding site	605	605	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P09436	UniProtKB	Modified residue	829	829	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P09436	UniProtKB	Modified residue	1059	1059	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P09436	UniProtKB	Cross-link	486	486	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P09436	UniProtKB	Sequence conflict	551	551	.	.	.	Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09436	UniProtKB	Sequence conflict	588	588	.	.	.	Note=N->KS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09436	UniProtKB	Sequence conflict	693	695	.	.	.	Note=DRW->AEM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09436	UniProtKB	Sequence conflict	706	706	.	.	.	Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09436	UniProtKB	Sequence conflict	747	747	.	.	.	Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P48526 1 1002
+P48526	UniProtKB	Chain	1	1002	.	.	.	ID=PRO_0000098605;Note=Isoleucine--tRNA ligase%2C mitochondrial	
+P48526	UniProtKB	Motif	94	104	.	.	.	Note="HIGH" region	
+P48526	UniProtKB	Motif	668	672	.	.	.	Note="KMSKS" region	
+P48526	UniProtKB	Binding site	671	671	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48526	UniProtKB	Sequence conflict	437	437	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48526	UniProtKB	Sequence conflict	672	672	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P48526	UniProtKB	Sequence conflict	806	806	.	.	.	Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q06836 1 1226
+Q06836	UniProtKB	Chain	1	1226	.	.	.	ID=PRO_0000270620;Note=Arf guanine nucleotide exchange factor SYT1	
+Q06836	UniProtKB	Domain	405	620	.	.	.	Note=SEC7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00189	
+Q06836	UniProtKB	Domain	844	1074	.	.	.	Note=PH	
+Q06836	UniProtKB	Compositional bias	232	239	.	.	.	Note=Poly-Ser	
+Q06836	UniProtKB	Compositional bias	654	742	.	.	.	Note=Ser-rich	
+Q06836	UniProtKB	Modified residue	277	277	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+Q06836	UniProtKB	Modified residue	369	369	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P53040 1 516
+P53040	UniProtKB	Chain	1	516	.	.	.	ID=PRO_0000118878;Note=Transcription initiation factor TFIID subunit 6	
+P53040	UniProtKB	Domain	6	75	.	.	.	Note=Histone-fold	
+##sequence-region Q05027 1 157
+Q05027	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000118896;Note=Transcription initiation factor TFIID subunit 9	
+Q05027	UniProtKB	Domain	30	97	.	.	.	Note=Histone-fold	
+##sequence-region P25638 1 111
+P25638	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25638	UniProtKB	Chain	2	111	.	.	.	ID=PRO_0000106352;Note=TPR repeat-containing protein associated with Hsp90	
+P25638	UniProtKB	Repeat	4	37	.	.	.	Note=TPR 1	
+P25638	UniProtKB	Repeat	39	71	.	.	.	Note=TPR 2	
+P25638	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P25638	UniProtKB	Helix	3	16	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGQ	
+P25638	UniProtKB	Helix	20	33	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGQ	
+P25638	UniProtKB	Helix	38	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGQ	
+P25638	UniProtKB	Helix	54	65	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGQ	
+P25638	UniProtKB	Helix	71	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P25638	UniProtKB	Helix	76	90	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGQ	
+P25638	UniProtKB	Beta strand	92	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P25638	UniProtKB	Beta strand	98	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU	
+P25638	UniProtKB	Beta strand	105	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L6J	
+##sequence-region P15019 1 335
+P15019	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P15019	UniProtKB	Chain	2	335	.	.	.	ID=PRO_0000173574;Note=Transaldolase	
+P15019	UniProtKB	Active site	144	144	.	.	.	Note=Schiff-base intermediate with substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8109173;Dbxref=PMID:8109173	
+P15019	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649	
+P15019	UniProtKB	Sequence conflict	221	221	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P25345 1 492
+##sequence-region P13188 1 809
+P13188	UniProtKB	Chain	1	809	.	.	.	ID=PRO_0000195866;Note=Glutamine--tRNA ligase	
+P13188	UniProtKB	Nucleotide binding	259	261	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962	
+P13188	UniProtKB	Nucleotide binding	265	271	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962	
+P13188	UniProtKB	Nucleotide binding	488	489	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962	
+P13188	UniProtKB	Nucleotide binding	496	498	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962	
+P13188	UniProtKB	Motif	258	268	.	.	.	Note="HIGH" region	
+P13188	UniProtKB	Motif	495	499	.	.	.	Note="KMSKS" region	
+P13188	UniProtKB	Binding site	291	291	.	.	.	Note=L-glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962	
+P13188	UniProtKB	Binding site	440	440	.	.	.	Note=L-glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962	
+P13188	UniProtKB	Binding site	459	459	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962	
+P13188	UniProtKB	Modified residue	378	378	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P13188	UniProtKB	Sequence conflict	179	179	.	.	.	Note=G->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13188	UniProtKB	Helix	4	13	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	18	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	28	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	49	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	70	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	85	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	99	101	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	104	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Turn	110	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	119	132	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	134	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	141	144	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	145	153	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	156	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	166	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	183	185	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4	
+P13188	UniProtKB	Helix	222	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	241	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	253	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	260	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	267	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	285	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	300	312	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	318	322	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	323	326	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	327	339	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	343	346	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	350	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	373	376	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	379	390	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	400	403	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	412	414	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	418	422	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Turn	428	430	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	435	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	440	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	456	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	460	465	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	466	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	483	486	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	489	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	498	506	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	509	512	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	521	527	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	531	541	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	548	551	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	552	566	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	572	581	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	590	597	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	601	603	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	605	610	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	612	617	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	618	620	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	632	634	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	639	641	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	648	655	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	661	668	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	692	694	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	698	706	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	709	713	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	715	717	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	722	725	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	730	739	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	743	748	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	755	758	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Helix	771	773	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	776	778	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Turn	779	781	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	782	786	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	792	794	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+P13188	UniProtKB	Beta strand	796	801	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S	
+##sequence-region P32774 1 122
+P32774	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000194053;Note=Transcription initiation factor IIA subunit 2	
+P32774	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P32774	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32774	UniProtKB	Mutagenesis	27	27	.	.	.	Note=Decreases ability to interact with TAF11 and support growth on galactose-containing medium. Unable to support cell viability in a strain deleted for TOA2%3B when associated with A-69. I->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238911;Dbxref=PMID:11238911	
+P32774	UniProtKB	Mutagenesis	41	41	.	.	.	Note=Decreases ability to interact with Toa1 and TAF11%2C display mutant growth phenotypes and defects in transcription in vivo. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238911;Dbxref=PMID:11238911	
+P32774	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Unable to support cell viability in a strain deleted for TOA2%3B when associated with A-27 or K-27. Y->A	
+P32774	UniProtKB	Helix	9	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+P32774	UniProtKB	Helix	14	28	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+P32774	UniProtKB	Helix	34	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+P32774	UniProtKB	Beta strand	59	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+P32774	UniProtKB	Beta strand	75	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+P32774	UniProtKB	Beta strand	104	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2	
+##sequence-region P36421 1 394
+P36421	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+P36421	UniProtKB	Chain	2	394	.	.	.	ID=PRO_0000055676;Note=Tyrosine--tRNA ligase%2C cytoplasmic	
+P36421	UniProtKB	Motif	48	56	.	.	.	Note="HIGH" region	
+P36421	UniProtKB	Motif	227	231	.	.	.	Note="KMSKS" region	
+P36421	UniProtKB	Motif	360	378	.	.	.	Note=Nuclear localization signal	
+P36421	UniProtKB	Binding site	43	43	.	.	.	Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36421	UniProtKB	Binding site	170	170	.	.	.	Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36421	UniProtKB	Binding site	174	174	.	.	.	Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36421	UniProtKB	Binding site	177	177	.	.	.	Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36421	UniProtKB	Binding site	192	192	.	.	.	Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P36421	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7	
+P36421	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36421	UniProtKB	Modified residue	359	359	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36421	UniProtKB	Mutagenesis	43	43	.	.	.	Note=Decreases catalytic activity for L-tyrosine 400-fold%2C but allows the utilization of 3-iodo-L-tyrosine and other 3-modified tyrosines as substrates. Y->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11530018;Dbxref=PMID:11530018	
+P36421	UniProtKB	Mutagenesis	364	368	.	.	.	Note=Abolishes nuclear localization. KKAKK->EEAEE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359929;Dbxref=PMID:11359929	
+P36421	UniProtKB	Helix	9	17	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Beta strand	21	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	26	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Beta strand	41	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	57	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Beta strand	72	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	79	84	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Turn	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	93	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Beta strand	120	123	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	131	141	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	146	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Turn	153	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	166	180	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Beta strand	184	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	190	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	193	202	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	203	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Beta strand	212	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	243	252	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	264	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	273	278	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Beta strand	280	282	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Beta strand	288	290	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	294	296	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Beta strand	300	304	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	305	313	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	319	343	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+P36421	UniProtKB	Helix	345	354	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC	
+##sequence-region P36100 1 482
+P36100	UniProtKB	Chain	1	482	.	.	.	ID=PRO_0000211225;Note=Transcription initiation factor IIE subunit alpha	
+P36100	UniProtKB	Domain	9	99	.	.	.	Note=HTH TFE/IIEalpha-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00676	
+P36100	UniProtKB	Zinc finger	124	152	.	.	.	Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36100	UniProtKB	Compositional bias	374	482	.	.	.	Note=Asp/Glu-rich (highly acidic)	
+P36100	UniProtKB	Compositional bias	374	392	.	.	.	Note=Poly-Glu	
+##sequence-region Q9URQ3 1 322
+Q9URQ3	UniProtKB	Chain	1	322	.	.	.	ID=PRO_0000171741;Note=tRNA-specific adenosine deaminase subunit TAD3	
+Q9URQ3	UniProtKB	Domain	162	283	.	.	.	Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083	
+##sequence-region Q04226 1 346
+Q04226	UniProtKB	Chain	1	346	.	.	.	ID=PRO_0000118907;Note=Transcription initiation factor TFIID subunit 11	
+Q04226	UniProtKB	Domain	131	329	.	.	.	Note=Histone-fold	
+Q04226	UniProtKB	Modified residue	236	236	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q04226	UniProtKB	Modified residue	238	238	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38129 1 798
+P38129	UniProtKB	Chain	1	798	.	.	.	ID=PRO_0000051260;Note=Transcription initiation factor TFIID subunit 5	
+P38129	UniProtKB	Domain	56	88	.	.	.	Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126	
+P38129	UniProtKB	Repeat	464	503	.	.	.	Note=WD 1	
+P38129	UniProtKB	Repeat	523	562	.	.	.	Note=WD 2	
+P38129	UniProtKB	Repeat	565	604	.	.	.	Note=WD 3	
+P38129	UniProtKB	Repeat	607	646	.	.	.	Note=WD 4	
+P38129	UniProtKB	Repeat	649	688	.	.	.	Note=WD 5	
+P38129	UniProtKB	Repeat	692	731	.	.	.	Note=WD 6	
+P38129	UniProtKB	Coiled coil	329	349	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38129	UniProtKB	Compositional bias	3	48	.	.	.	Note=Gln-rich	
+P38129	UniProtKB	Modified residue	299	299	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38129	UniProtKB	Modified residue	411	411	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38129	UniProtKB	Modified residue	415	415	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38129	UniProtKB	Modified residue	787	787	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P38129	UniProtKB	Helix	152	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Turn	168	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Helix	171	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Helix	194	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Helix	205	208	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Helix	209	217	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Turn	218	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Helix	225	230	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Helix	232	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Beta strand	242	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Helix	248	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Helix	262	264	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Helix	266	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+P38129	UniProtKB	Beta strand	277	281	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49	
+##sequence-region Q03750 1 510
+Q03750	UniProtKB	Chain	1	510	.	.	.	ID=PRO_0000118887;Note=Transcription initiation factor TFIID subunit 8	
+Q03750	UniProtKB	Domain	37	103	.	.	.	Note=Histone-fold	
+Q03750	UniProtKB	Coiled coil	142	165	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03750	UniProtKB	Coiled coil	346	383	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03750	UniProtKB	Modified residue	269	269	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P09733 1 447
+P09733	UniProtKB	Chain	1	447	.	.	.	ID=PRO_0000048239;Note=Tubulin alpha-1 chain	
+P09733	UniProtKB	Nucleotide binding	143	149	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P09733	UniProtKB	Sequence conflict	94	94	.	.	.	Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09733	UniProtKB	Sequence conflict	327	327	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P09733	UniProtKB	Beta strand	4	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	10	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	34	36	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	47	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Turn	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	54	56	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	66	72	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	73	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Turn	83	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Turn	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	104	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	112	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	135	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Turn	146	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	149	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Turn	162	164	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	165	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	184	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	200	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	207	216	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	225	239	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	241	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	253	260	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	262	265	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P09733	UniProtKB	Beta strand	270	274	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	289	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	299	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	302	306	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	313	323	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	326	338	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	352	357	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	365	369	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Beta strand	373	382	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	383	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	386	400	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Turn	401	405	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	406	410	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Turn	411	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P09733	UniProtKB	Helix	417	436	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+##sequence-region P32613 1 152
+P32613	UniProtKB	Chain	1	152	.	.	.	ID=PRO_0000202605;Note=TRAPP-associated protein TCA17	
+P32613	UniProtKB	Sequence conflict	2	2	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P32613	UniProtKB	Beta strand	6	11	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Beta strand	17	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Helix	33	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Beta strand	57	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Beta strand	64	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Beta strand	72	78	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Turn	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Beta strand	85	91	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Helix	92	94	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Helix	99	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Helix	125	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Helix	130	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+P32613	UniProtKB	Helix	149	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6	
+##sequence-region P42943 1 550
+P42943	UniProtKB	Chain	1	550	.	.	.	ID=PRO_0000128372;Note=T-complex protein 1 subunit eta	
+##sequence-region Q6B2U8 1 126
+Q6B2U8	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000268622;Note=Topoisomerase I damage affected protein 8	
+Q6B2U8	UniProtKB	Domain	1	110	.	.	.	Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164	
+##sequence-region Q04545 1 1251
+Q04545	UniProtKB	Chain	1	1251	.	.	.	ID=PRO_0000046864;Note=Probable transcription factor TDA9	
+Q04545	UniProtKB	Zinc finger	61	83	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q04545	UniProtKB	Zinc finger	89	112	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+Q04545	UniProtKB	Modified residue	527	527	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+Q04545	UniProtKB	Modified residue	603	603	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P34163 1 548
+P34163	UniProtKB	Chain	1	548	.	.	.	ID=PRO_0000090379;Note=Sterol esterase TGL1	
+P34163	UniProtKB	Topological domain	1	13	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34163	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical%3B Signal-anchor for type III membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34163	UniProtKB	Topological domain	35	548	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34163	UniProtKB	Domain	107	402	.	.	.	Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P34163	UniProtKB	Active site	201	201	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34163	UniProtKB	Active site	369	369	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34163	UniProtKB	Active site	396	396	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34163	UniProtKB	Modified residue	462	462	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34163	UniProtKB	Modified residue	466	466	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34163	UniProtKB	Modified residue	521	521	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P34163	UniProtKB	Modified residue	538	538	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34163	UniProtKB	Modified residue	539	539	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P34163	UniProtKB	Cross-link	246	246	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region Q12043 1 749
+Q12043	UniProtKB	Chain	1	749	.	.	.	ID=PRO_0000270918;Note=Lipase 5	
+Q12043	UniProtKB	Transmembrane	183	203	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12043	UniProtKB	Domain	183	388	.	.	.	Note=PNPLA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+Q12043	UniProtKB	Motif	214	218	.	.	.	Note=GXSXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+Q12043	UniProtKB	Active site	216	216	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+Q12043	UniProtKB	Active site	375	375	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161	
+Q12043	UniProtKB	Modified residue	645	645	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q12043	UniProtKB	Glycosylation	270	270	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12043	UniProtKB	Glycosylation	289	289	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12043	UniProtKB	Glycosylation	297	297	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12043	UniProtKB	Glycosylation	304	304	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12043	UniProtKB	Glycosylation	321	321	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12043	UniProtKB	Glycosylation	474	474	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12043	UniProtKB	Glycosylation	589	589	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12043	UniProtKB	Glycosylation	680	680	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12043	UniProtKB	Glycosylation	714	714	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12043	UniProtKB	Glycosylation	742	742	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38714 1 643
+P38714	UniProtKB	Motif	188	198	.	.	.	Note="HIGH" region	
+P38714	UniProtKB	Sequence conflict	499	499	.	.	.	Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38705 1 446
+P38705	UniProtKB	Chain	1	446	.	.	.	ID=PRO_0000122200;Note=Serine--tRNA ligase%2C mitochondrial	
+P38705	UniProtKB	Nucleotide binding	284	286	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38705	UniProtKB	Nucleotide binding	371	374	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38705	UniProtKB	Region	251	253	.	.	.	Note=Serine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38705	UniProtKB	Binding site	300	300	.	.	.	Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38705	UniProtKB	Binding site	307	307	.	.	.	Note=Serine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38705	UniProtKB	Binding site	407	407	.	.	.	Note=Serine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P04801 1 734
+P04801	UniProtKB	Chain	1	734	.	.	.	ID=PRO_0000101125;Note=Threonine--tRNA ligase%2C cytoplasmic	
+P04801	UniProtKB	Modified residue	195	195	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04801	UniProtKB	Modified residue	289	289	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P04801	UniProtKB	Modified residue	297	297	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P04801	UniProtKB	Modified residue	381	381	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04801	UniProtKB	Modified residue	453	453	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P04801	UniProtKB	Modified residue	457	457	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P04801	UniProtKB	Modified residue	460	460	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04801	UniProtKB	Modified residue	605	605	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P04801	UniProtKB	Sequence conflict	9	9	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04801	UniProtKB	Sequence conflict	18	18	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04801	UniProtKB	Sequence conflict	502	502	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q12109 1 432
+Q12109	UniProtKB	Chain	1	432	.	.	.	ID=PRO_0000136744;Note=Tryptophan--tRNA ligase%2C cytoplasmic	
+Q12109	UniProtKB	Motif	111	120	.	.	.	Note="HIGH" region	
+Q12109	UniProtKB	Motif	295	299	.	.	.	Note="KMSKS" region	
+Q12109	UniProtKB	Sequence conflict	87	87	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q12109	UniProtKB	Helix	47	54	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	61	71	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	77	80	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Beta strand	83	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	90	99	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Beta strand	104	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Beta strand	112	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT3	
+Q12109	UniProtKB	Helix	118	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	121	134	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Beta strand	138	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	144	150	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	156	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Turn	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	177	179	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Beta strand	180	184	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	185	188	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	191	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	206	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	221	225	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	227	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	236	238	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Turn	240	243	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Beta strand	251	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	257	259	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	260	273	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Beta strand	279	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Beta strand	291	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT6	
+Q12109	UniProtKB	Helix	301	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	311	321	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	330	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Turn	340	342	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	344	352	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	356	367	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	373	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+Q12109	UniProtKB	Helix	400	407	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1	
+##sequence-region P38854 1 504
+P38854	UniProtKB	Chain	1	504	.	.	.	ID=PRO_0000202928;Note=Topoisomerase I damage affected protein 11	
+P38854	UniProtKB	Coiled coil	179	231	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38854	UniProtKB	Modified residue	236	236	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38854	UniProtKB	Modified residue	244	244	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P38854	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region Q03533 1 586
+Q03533	UniProtKB	Chain	1	586	.	.	.	ID=PRO_0000086153;Note=Serine/threonine-protein kinase TDA1	
+Q03533	UniProtKB	Domain	39	351	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03533	UniProtKB	Nucleotide binding	45	53	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03533	UniProtKB	Active site	180	180	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+Q03533	UniProtKB	Binding site	68	68	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+Q03533	UniProtKB	Modified residue	504	504	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03533	UniProtKB	Modified residue	509	509	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03533	UniProtKB	Modified residue	518	518	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+Q03533	UniProtKB	Modified residue	538	538	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+Q03533	UniProtKB	Modified residue	578	578	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40045 1 126
+P40045	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P40045	UniProtKB	Chain	2	126	.	.	.	ID=PRO_0000202634;Note=Topoisomerase I damage affected protein 2	
+P40045	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P47153 1 279
+P47153	UniProtKB	Chain	1	279	.	.	.	ID=PRO_0000185544;Note=Topoisomerase I damage affected protein 4	
+P47153	UniProtKB	Topological domain	1	32	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Topological domain	54	79	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Topological domain	101	110	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Transmembrane	111	131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Topological domain	132	135	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Topological domain	157	162	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Transmembrane	163	183	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Topological domain	184	192	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Transmembrane	193	213	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Topological domain	214	238	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Transmembrane	239	259	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Topological domain	260	279	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P47153	UniProtKB	Domain	70	271	.	.	.	Note=TLC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00205	
+##sequence-region P07236 1 462
+P07236	UniProtKB	Transit peptide	1	45	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P07236	UniProtKB	Chain	46	462	.	.	.	ID=PRO_0000035827;Note=Threonine--tRNA ligase%2C mitochondrial	
+P07236	UniProtKB	Sequence conflict	265	265	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P07236	UniProtKB	Helix	35	46	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	63	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	93	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	97	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Turn	106	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	110	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	113	117	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UGQ	
+P07236	UniProtKB	Beta strand	120	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UGQ	
+P07236	UniProtKB	Beta strand	126	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	133	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	147	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	151	156	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	159	161	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Turn	166	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Turn	171	173	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	176	187	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	189	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	192	207	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Turn	208	210	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	225	229	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	239	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	260	263	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	273	279	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	285	295	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	296	300	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	316	325	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	326	337	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	343	345	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	350	356	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	360	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	379	381	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EO4	
+P07236	UniProtKB	Beta strand	394	396	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	403	413	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	416	421	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	423	428	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	431	435	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	436	438	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Beta strand	443	445	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+P07236	UniProtKB	Helix	447	459	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0	
+##sequence-region P46677 1 1066
+P46677	UniProtKB	Chain	1	1066	.	.	.	ID=PRO_0000118862;Note=Transcription initiation factor TFIID subunit 1	
+P46677	UniProtKB	Coiled coil	409	425	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46677	UniProtKB	Coiled coil	944	1000	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P46677	UniProtKB	Compositional bias	65	69	.	.	.	Note=Poly-Asp	
+P46677	UniProtKB	Helix	15	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B0A	
+P46677	UniProtKB	Beta strand	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B0A	
+P46677	UniProtKB	Helix	28	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B0A	
+P46677	UniProtKB	Helix	471	475	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Turn	478	480	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	481	484	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	488	491	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Turn	492	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Turn	498	501	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	507	510	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	518	521	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	526	529	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	533	536	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	538	542	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	544	553	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	563	571	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	584	591	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Turn	598	601	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	610	615	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	617	626	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	632	640	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	643	650	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	653	658	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	662	665	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	673	694	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	702	705	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	713	720	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Turn	721	723	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	724	726	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Turn	731	734	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	735	738	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	747	750	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	751	753	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	756	778	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	782	790	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	793	804	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	820	824	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	859	882	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	888	891	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	900	903	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	914	922	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Beta strand	926	935	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+P46677	UniProtKB	Helix	938	951	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+##sequence-region P02557 1 457
+P02557	UniProtKB	Chain	1	457	.	.	.	ID=PRO_0000048443;Note=Tubulin beta chain	
+P02557	UniProtKB	Nucleotide binding	140	146	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P02557	UniProtKB	Modified residue	278	278	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P02557	UniProtKB	Modified residue	280	280	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P02557	UniProtKB	Mutagenesis	100	100	.	.	.	Note=Becomes sensitive to rhizoxin. V->N	
+P02557	UniProtKB	Mutagenesis	390	390	.	.	.	Note=Decreased microtubule stability. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28013290;Dbxref=PMID:28013290	
+P02557	UniProtKB	Mutagenesis	421	421	.	.	.	Note=Increased microtubule polymerization and depolymerization rates. Increased microtubule stability. Decreased kinesin KIP3 subcellular location at microtubule plus ends. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23001566;Dbxref=PMID:23001566	
+P02557	UniProtKB	Sequence conflict	9	9	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02557	UniProtKB	Sequence conflict	12	12	.	.	.	Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02557	UniProtKB	Sequence conflict	71	71	.	.	.	Note=G->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02557	UniProtKB	Sequence conflict	152	152	.	.	.	Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02557	UniProtKB	Sequence conflict	156	156	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02557	UniProtKB	Sequence conflict	159	159	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P02557	UniProtKB	Beta strand	4	9	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	10	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	46	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	59	61	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	63	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	70	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	80	82	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P02557	UniProtKB	Beta strand	83	85	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	101	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Turn	108	112	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	113	125	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	132	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	143	158	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	162	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	181	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	197	203	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	204	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	222	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	238	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	242	244	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB	
+P02557	UniProtKB	Beta strand	245	247	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	250	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	265	271	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	286	294	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	296	298	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	299	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	305	307	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	310	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	323	336	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	338	340	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	345	347	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	349	355	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Beta strand	362	371	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	372	374	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	375	389	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Turn	390	395	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	396	399	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Turn	400	402	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+P02557	UniProtKB	Helix	405	426	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J	
+##sequence-region P38114 1 1094
+P38114	UniProtKB	Chain	1	1094	.	.	.	ID=PRO_0000114992;Note=Uncharacterized transcriptional regulatory protein TBS1	
+P38114	UniProtKB	Transmembrane	755	775	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38114	UniProtKB	DNA binding	107	137	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P38114	UniProtKB	Compositional bias	935	991	.	.	.	Note=Asn-rich	
+P38114	UniProtKB	Compositional bias	985	1032	.	.	.	Note=Asp-rich	
+##sequence-region Q12466 1 1186
+Q12466	UniProtKB	Chain	1	1186	.	.	.	ID=PRO_0000252271;Note=Tricalbin-1	
+Q12466	UniProtKB	Topological domain	1	106	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12466	UniProtKB	Transmembrane	107	127	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12466	UniProtKB	Topological domain	128	128	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12466	UniProtKB	Transmembrane	129	149	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12466	UniProtKB	Topological domain	150	1186	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12466	UniProtKB	Domain	373	471	.	.	.	Note=C2 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+Q12466	UniProtKB	Domain	645	741	.	.	.	Note=C2 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+Q12466	UniProtKB	Domain	979	1078	.	.	.	Note=C2 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+Q12466	UniProtKB	Coiled coil	795	822	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12466	UniProtKB	Metal binding	1008	1008	.	.	.	Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12466	UniProtKB	Metal binding	1008	1008	.	.	.	Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12466	UniProtKB	Metal binding	1014	1014	.	.	.	Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12466	UniProtKB	Metal binding	1064	1064	.	.	.	Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12466	UniProtKB	Metal binding	1064	1064	.	.	.	Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12466	UniProtKB	Metal binding	1066	1066	.	.	.	Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12466	UniProtKB	Metal binding	1066	1066	.	.	.	Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12466	UniProtKB	Metal binding	1066	1066	.	.	.	Note=Calcium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12466	UniProtKB	Metal binding	1069	1069	.	.	.	Note=Calcium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12466	UniProtKB	Metal binding	1072	1072	.	.	.	Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12466	UniProtKB	Metal binding	1072	1072	.	.	.	Note=Calcium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12466	UniProtKB	Modified residue	1000	1000	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+##sequence-region Q03640 1 1545
+Q03640	UniProtKB	Chain	1	1545	.	.	.	ID=PRO_0000203249;Note=Tricalbin-3	
+Q03640	UniProtKB	Topological domain	1	206	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Transmembrane	207	227	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03640	UniProtKB	Topological domain	228	228	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Transmembrane	229	249	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03640	UniProtKB	Topological domain	250	1545	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Domain	478	580	.	.	.	Note=C2 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+Q03640	UniProtKB	Domain	785	881	.	.	.	Note=C2 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+Q03640	UniProtKB	Domain	1121	1218	.	.	.	Note=C2 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+Q03640	UniProtKB	Coiled coil	620	660	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03640	UniProtKB	Coiled coil	937	972	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03640	UniProtKB	Compositional bias	1316	1404	.	.	.	Note=Ser-rich	
+Q03640	UniProtKB	Metal binding	1150	1150	.	.	.	Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Metal binding	1150	1150	.	.	.	Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Metal binding	1156	1156	.	.	.	Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Metal binding	1204	1204	.	.	.	Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Metal binding	1204	1204	.	.	.	Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Metal binding	1206	1206	.	.	.	Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Metal binding	1206	1206	.	.	.	Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Metal binding	1206	1206	.	.	.	Note=Calcium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Metal binding	1212	1212	.	.	.	Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Metal binding	1212	1212	.	.	.	Note=Calcium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03640	UniProtKB	Modified residue	67	67	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03640	UniProtKB	Modified residue	112	112	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q03640	UniProtKB	Modified residue	1340	1340	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03640	UniProtKB	Modified residue	1342	1342	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03640	UniProtKB	Modified residue	1346	1346	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03640	UniProtKB	Modified residue	1350	1350	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198	
+Q03640	UniProtKB	Modified residue	1354	1354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q03640	UniProtKB	Modified residue	1400	1400	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P36101 1 447
+P36101	UniProtKB	Chain	1	447	.	.	.	ID=PRO_0000120586;Note=tRNA threonylcarbamoyladenosine dehydratase 2	
+P36101	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36101	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36101	UniProtKB	Transmembrane	294	314	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P36101	UniProtKB	Sequence conflict	41	41	.	.	.	Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q99190 1 310
+Q99190	UniProtKB	Chain	1	310	.	.	.	ID=PRO_0000262739;Note=Very-long-chain enoyl-CoA reductase	
+Q99190	UniProtKB	Topological domain	1	85	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Topological domain	107	141	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Transmembrane	142	162	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Topological domain	163	165	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Transmembrane	166	186	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Topological domain	187	201	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Topological domain	223	242	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Transmembrane	243	265	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Topological domain	266	268	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Transmembrane	269	291	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Topological domain	292	310	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q99190	UniProtKB	Mutagenesis	81	81	.	.	.	Note=In TSC13-1%3B reduces fatty acid elongation activity by 50%25. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11113186;Dbxref=PMID:11113186	
+##sequence-region P40533 1 473
+P40533	UniProtKB	Chain	1	473	.	.	.	ID=PRO_0000202993;Note=Protein TED1	
+P40533	UniProtKB	Topological domain	1	8	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40533	UniProtKB	Transmembrane	9	29	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40533	UniProtKB	Topological domain	30	451	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40533	UniProtKB	Transmembrane	452	472	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40533	UniProtKB	Topological domain	473	473	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40533	UniProtKB	Glycosylation	38	38	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40533	UniProtKB	Glycosylation	147	147	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40533	UniProtKB	Glycosylation	229	229	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40533	UniProtKB	Glycosylation	266	266	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40533	UniProtKB	Glycosylation	307	307	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07921 1 160
+Q07921	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000270926;Note=Telomere length regulation protein TEN1	
+##sequence-region P53065 1 400
+P53065	UniProtKB	Chain	1	400	.	.	.	ID=PRO_0000171777;Note=tRNA-specific adenosine deaminase 1	
+P53065	UniProtKB	Domain	76	400	.	.	.	Note=A to I editase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00240	
+P53065	UniProtKB	Active site	103	103	.	.	.	Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00240	
+P53065	UniProtKB	Metal binding	101	101	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00240	
+P53065	UniProtKB	Metal binding	157	157	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00240	
+P53065	UniProtKB	Metal binding	223	223	.	.	.	Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00240	
+P53065	UniProtKB	Binding site	108	108	.	.	.	Note=Inositol hexakisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53065	UniProtKB	Binding site	226	226	.	.	.	Note=Inositol hexakisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53065	UniProtKB	Binding site	232	232	.	.	.	Note=Inositol hexakisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53065	UniProtKB	Binding site	369	369	.	.	.	Note=Inositol hexakisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53065	UniProtKB	Binding site	375	375	.	.	.	Note=Inositol hexakisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P47058 1 250
+P47058	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000171740;Note=tRNA-specific adenosine deaminase subunit TAD2	
+P47058	UniProtKB	Domain	1	119	.	.	.	Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083	
+P47058	UniProtKB	Active site	56	56	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47058	UniProtKB	Metal binding	54	54	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47058	UniProtKB	Metal binding	88	88	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P47058	UniProtKB	Metal binding	91	91	.	.	.	Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q03761 1 539
+Q03761	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03761	UniProtKB	Chain	2	539	.	.	.	ID=PRO_0000118909;Note=Transcription initiation factor TFIID subunit 12	
+Q03761	UniProtKB	Domain	413	490	.	.	.	Note=Histone-fold	
+Q03761	UniProtKB	Coiled coil	153	202	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03761	UniProtKB	Coiled coil	239	285	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q03761	UniProtKB	Compositional bias	116	309	.	.	.	Note=Gln-rich	
+Q03761	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+Q03761	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q03761	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+##sequence-region P50105 1 388
+P50105	UniProtKB	Chain	1	388	.	.	.	ID=PRO_0000118871;Note=Transcription initiation factor TFIID subunit 4	
+P50105	UniProtKB	Domain	193	261	.	.	.	Note=Histone-fold	
+P50105	UniProtKB	Coiled coil	279	297	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P50105	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956	
+P50105	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P50105	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P53072 1 289
+P53072	UniProtKB	Chain	1	289	.	.	.	ID=PRO_0000072426;Note=tRNA acetyltransferase TAN1	
+P53072	UniProtKB	Domain	146	259	.	.	.	Note=THUMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00529	
+P53072	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+##sequence-region P39076 1 527
+P39076	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39076	UniProtKB	Chain	2	527	.	.	.	ID=PRO_0000128320;Note=T-complex protein 1 subunit beta	
+P39076	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P40413 1 562
+P40413	UniProtKB	Chain	1	562	.	.	.	ID=PRO_0000128354;Note=T-complex protein 1 subunit epsilon	
+P40413	UniProtKB	Sequence conflict	3	3	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40413	UniProtKB	Sequence conflict	27	27	.	.	.	Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40413	UniProtKB	Sequence conflict	58	58	.	.	.	Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40413	UniProtKB	Sequence conflict	92	92	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40413	UniProtKB	Sequence conflict	274	279	.	.	.	Note=CPFEPP->VHLNLL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40413	UniProtKB	Sequence conflict	336	336	.	.	.	Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P40413	UniProtKB	Sequence conflict	488	488	.	.	.	Note=G->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39079 1 546
+P39079	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39079	UniProtKB	Chain	2	546	.	.	.	ID=PRO_0000128362;Note=T-complex protein 1 subunit zeta	
+P39079	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P39079	UniProtKB	Modified residue	249	249	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+##sequence-region P42938 1 290
+P42938	UniProtKB	Chain	1	290	.	.	.	ID=PRO_0000214076;Note=Probable ATP-dependent kinase TDA10	
+P42938	UniProtKB	Nucleotide binding	38	45	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P42938	UniProtKB	Helix	8	24	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Turn	25	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Beta strand	32	37	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Helix	44	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Helix	60	62	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Beta strand	65	69	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Helix	70	73	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Helix	77	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Helix	91	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Beta strand	94	96	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Helix	104	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Beta strand	125	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Turn	133	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Helix	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Beta strand	147	152	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Beta strand	154	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Turn	172	174	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Beta strand	176	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Helix	182	195	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Turn	196	198	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Beta strand	204	212	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Helix	216	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Helix	238	246	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Helix	249	262	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Beta strand	265	275	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+P42938	UniProtKB	Beta strand	281	287	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF	
+##sequence-region P38758 1 523
+P38758	UniProtKB	Chain	1	523	.	.	.	ID=PRO_0000202886;Note=Putative oxidoreductase TDA3	
+P38758	UniProtKB	Compositional bias	156	212	.	.	.	Note=Ser-rich	
+P38758	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38758	UniProtKB	Modified residue	204	204	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38758	UniProtKB	Modified residue	306	306	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P53882 1 636
+P53882	UniProtKB	Chain	1	636	.	.	.	ID=PRO_0000203407;Note=Topoisomerase I damage affected protein 7	
+P53882	UniProtKB	Transmembrane	457	477	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53882	UniProtKB	Compositional bias	15	381	.	.	.	Note=Ser-rich	
+P53882	UniProtKB	Compositional bias	325	408	.	.	.	Note=Thr-rich	
+P53882	UniProtKB	Modified residue	628	628	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P53882	UniProtKB	Glycosylation	4	4	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53882	UniProtKB	Glycosylation	257	257	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53882	UniProtKB	Glycosylation	492	492	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53882	UniProtKB	Glycosylation	557	557	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53882	UniProtKB	Glycosylation	562	562	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53882	UniProtKB	Glycosylation	626	626	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P53882	UniProtKB	Cross-link	512	512	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+P53882	UniProtKB	Sequence conflict	251	251	.	.	.	Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P39933 1 429
+P39933	UniProtKB	Chain	1	429	.	.	.	ID=PRO_0000047086;Note=Transcription factor IIIA	
+P39933	UniProtKB	Zinc finger	49	74	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39933	UniProtKB	Zinc finger	80	102	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39933	UniProtKB	Zinc finger	108	130	.	.	.	Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39933	UniProtKB	Zinc finger	134	159	.	.	.	Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39933	UniProtKB	Zinc finger	163	186	.	.	.	Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39933	UniProtKB	Zinc finger	194	219	.	.	.	Note=C2H2-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39933	UniProtKB	Zinc finger	222	244	.	.	.	Note=C2H2-type 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39933	UniProtKB	Zinc finger	253	277	.	.	.	Note=C2H2-type 8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39933	UniProtKB	Zinc finger	365	389	.	.	.	Note=C2H2-type 9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
+P39933	UniProtKB	Compositional bias	24	43	.	.	.	Note=Ser-rich	
+P39933	UniProtKB	Compositional bias	321	327	.	.	.	Note=Arg/Lys-rich (basic)	
+##sequence-region Q02939 1 513
+Q02939	UniProtKB	Chain	1	513	.	.	.	ID=PRO_0000119268;Note=RNA polymerase II transcription factor B subunit 2	
+Q02939	UniProtKB	Helix	448	450	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q02939	UniProtKB	Beta strand	452	460	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q02939	UniProtKB	Helix	465	477	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q02939	UniProtKB	Beta strand	481	485	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q02939	UniProtKB	Turn	486	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q02939	UniProtKB	Beta strand	490	494	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q02939	UniProtKB	Helix	495	497	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+Q02939	UniProtKB	Helix	498	505	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP	
+##sequence-region Q12004 1 338
+Q12004	UniProtKB	Chain	1	338	.	.	.	ID=PRO_0000119275;Note=RNA polymerase II transcription factor B subunit 4	
+Q12004	UniProtKB	Zinc finger	289	308	.	.	.	Note=C4-type	
+Q12004	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region P34111 1 1160
+P34111	UniProtKB	Chain	1	1160	.	.	.	ID=PRO_0000072497;Note=Transcription factor tau 138 kDa subunit	
+P34111	UniProtKB	Modified residue	546	546	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P34111	UniProtKB	Mutagenesis	349	349	.	.	.	Note=In TSV115%3B thermosensitive. Level of TFIIIC and its affinity for tDNA reduced. tDNA binding activity very sensitive to mild heat treatments%2C and TFIIIC-DNA interaction inhibited at moderate salt concentrations. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8083243;Dbxref=PMID:8083243	
+P34111	UniProtKB	Helix	546	565	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM	
+P34111	UniProtKB	Beta strand	568	573	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM	
+P34111	UniProtKB	Helix	574	584	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM	
+P34111	UniProtKB	Helix	593	604	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM	
+P34111	UniProtKB	Beta strand	607	612	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM	
+P34111	UniProtKB	Turn	614	616	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM	
+P34111	UniProtKB	Beta strand	619	622	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM	
+P34111	UniProtKB	Helix	628	637	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM	
+##sequence-region Q04372 1 366
+Q04372	UniProtKB	Chain	1	366	.	.	.	ID=PRO_0000218623;Note=Type 2A phosphatase-associated protein 42	
+Q04372	UniProtKB	Helix	4	18	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P	
+Q04372	UniProtKB	Helix	29	50	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P	
+Q04372	UniProtKB	Helix	62	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P	
+Q04372	UniProtKB	Helix	67	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P	
+Q04372	UniProtKB	Helix	75	83	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P	
+Q04372	UniProtKB	Helix	93	120	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P	
+Q04372	UniProtKB	Helix	126	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P	
+Q04372	UniProtKB	Helix	143	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P	
+Q04372	UniProtKB	Helix	156	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P	
+Q04372	UniProtKB	Helix	199	231	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P	
+##sequence-region P40085 1 556
+P40085	UniProtKB	Chain	1	556	.	.	.	ID=PRO_0000202654;Note=Endoplasmic reticulum membrane protein 65	
+P40085	UniProtKB	Topological domain	1	87	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40085	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40085	UniProtKB	Topological domain	109	151	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40085	UniProtKB	Transmembrane	152	172	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40085	UniProtKB	Topological domain	173	224	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40085	UniProtKB	Transmembrane	225	245	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40085	UniProtKB	Topological domain	246	330	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40085	UniProtKB	Transmembrane	331	351	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40085	UniProtKB	Topological domain	352	391	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40085	UniProtKB	Transmembrane	392	412	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40085	UniProtKB	Topological domain	413	428	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258	
+P40085	UniProtKB	Transmembrane	429	449	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P40085	UniProtKB	Topological domain	450	556	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258	
+P40085	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P40085	UniProtKB	Glycosylation	318	318	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
+##sequence-region P13393 1 240
+P13393	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2677740;Dbxref=PMID:2677740	
+P13393	UniProtKB	Chain	2	240	.	.	.	ID=PRO_0000153990;Note=TATA-box-binding protein	
+P13393	UniProtKB	Repeat	67	143	.	.	.	Note=1	
+P13393	UniProtKB	Repeat	157	234	.	.	.	Note=2	
+P13393	UniProtKB	Sequence conflict	50	50	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P13393	UniProtKB	Beta strand	66	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Helix	82	88	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Beta strand	89	93	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Turn	96	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Beta strand	100	106	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Turn	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Beta strand	111	115	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Beta strand	119	128	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Helix	129	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Beta strand	153	165	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Helix	172	178	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Turn	179	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Beta strand	183	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RM1	
+P13393	UniProtKB	Turn	187	189	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Beta strand	191	196	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Beta strand	198	200	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Beta strand	203	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Beta strand	210	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+P13393	UniProtKB	Helix	220	236	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB	
+##sequence-region P38756 1 429
+P38756	UniProtKB	Chain	1	429	.	.	.	ID=PRO_0000120585;Note=tRNA threonylcarbamoyladenosine dehydratase 1	
+P38756	UniProtKB	Transmembrane	3	23	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38756	UniProtKB	Transmembrane	74	94	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38756	UniProtKB	Transmembrane	279	299	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38756	UniProtKB	Modified residue	259	259	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+##sequence-region Q06466 1 467
+Q06466	UniProtKB	Chain	1	467	.	.	.	ID=PRO_0000259482;Note=Putative vacuolar protein sorting-associated protein TDA6	
+Q06466	UniProtKB	Transmembrane	8	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06466	UniProtKB	Glycosylation	61	61	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06466	UniProtKB	Glycosylation	124	124	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q06466	UniProtKB	Glycosylation	141	141	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47988 1 759
+P47988	UniProtKB	Chain	1	759	.	.	.	ID=PRO_0000114982;Note=TY1 enhancer activator	
+P47988	UniProtKB	DNA binding	70	96	.	.	.	Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227	
+P47988	UniProtKB	Motif	744	752	.	.	.	Note=9aaTAD	
+P47988	UniProtKB	Modified residue	22	22	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47988	UniProtKB	Modified residue	755	755	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P47988	UniProtKB	Sequence conflict	501	502	.	.	.	Note=SV->RL;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P47988	UniProtKB	Sequence conflict	519	519	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P18412 1 486
+P18412	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P18412	UniProtKB	Chain	2	486	.	.	.	ID=PRO_0000205941;Note=Ty transcription activator TEC1	
+P18412	UniProtKB	DNA binding	125	199	.	.	.	Note=TEA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00505	
+P18412	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P18412	UniProtKB	Modified residue	325	325	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region P53038 1 688
+P53038	UniProtKB	Chain	1	688	.	.	.	ID=PRO_0000215561;Note=Telomere length regulation protein TEL2	
+P53038	UniProtKB	Modified residue	417	417	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53038	UniProtKB	Modified residue	419	419	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53038	UniProtKB	Natural variant	129	129	.	.	.	Note=In TEL2-1%3B short telomere length. S->R	
+P53038	UniProtKB	Mutagenesis	333	333	.	.	.	Note=Does not inhibit interaction with TTI1 or TTI2. Inhibits interaction with TTI1 or TTI2%3B when associated with E-345. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20801936;Dbxref=PMID:20801936	
+P53038	UniProtKB	Mutagenesis	345	345	.	.	.	Note=Does not inhibit weakly interaction with TTI1 or TTI2. Inhibits interaction with TTI1 or TTI2%3B when associated with Q-333. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20801936;Dbxref=PMID:20801936	
+P53038	UniProtKB	Sequence conflict	226	226	.	.	.	Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53038	UniProtKB	Helix	2	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Turn	6	8	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	12	23	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	32	41	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	43	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Turn	46	48	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	51	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	66	77	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	85	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	104	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	116	126	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	130	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Turn	136	138	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	141	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	166	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	179	186	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	187	191	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	195	206	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	210	218	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	221	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	231	241	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	246	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	252	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	261	268	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	273	288	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	293	309	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	313	320	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	323	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	338	351	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	382	385	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	430	433	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	437	444	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	456	467	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	476	489	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Turn	497	500	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	501	513	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	515	517	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	518	525	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	532	550	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	616	618	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	619	632	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	642	657	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Beta strand	659	663	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+P53038	UniProtKB	Helix	664	681	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z	
+##sequence-region Q06163 1 884
+Q06163	UniProtKB	Chain	1	884	.	.	.	ID=PRO_0000054932;Note=Telomerase reverse transcriptase	
+Q06163	UniProtKB	Domain	422	725	.	.	.	Note=Reverse transcriptase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405	
+Q06163	UniProtKB	Metal binding	530	530	.	.	.	Note=Magnesium%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405	
+Q06163	UniProtKB	Metal binding	670	670	.	.	.	Note=Magnesium%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405	
+Q06163	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405	
+Q06163	UniProtKB	Sequence conflict	162	162	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53851 1 422
+P53851	UniProtKB	Chain	1	422	.	.	.	ID=PRO_0000051482;Note=Protein TEX1	
+P53851	UniProtKB	Repeat	61	100	.	.	.	Note=WD 1	
+P53851	UniProtKB	Repeat	158	197	.	.	.	Note=WD 2	
+P53851	UniProtKB	Repeat	207	246	.	.	.	Note=WD 3	
+P53851	UniProtKB	Repeat	251	290	.	.	.	Note=WD 4	
+P53851	UniProtKB	Repeat	293	332	.	.	.	Note=WD 5	
+##sequence-region P32367 1 649
+P32367	UniProtKB	Chain	1	649	.	.	.	ID=PRO_0000209717;Note=Transcription factor tau 95 kDa subunit	
+P32367	UniProtKB	Repeat	221	239	.	.	.	Note=1	
+P32367	UniProtKB	Repeat	400	419	.	.	.	Note=2	
+P32367	UniProtKB	Region	221	419	.	.	.	Note=2 X repeats%2C Pro-rich	
+P32367	UniProtKB	Motif	296	300	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P32367	UniProtKB	Compositional bias	510	620	.	.	.	Note=Asp/Glu-rich (acidic)	
+P32367	UniProtKB	Modified residue	617	617	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P32367	UniProtKB	Mutagenesis	447	447	.	.	.	Note=Temperature-sensitive. TFCIII-DNA complexes present a shift in their 5' border%2C generate slow-migrating TFIIIB-DNA complexes upon stripping TFIIIC by heparin or heat treatment%2C and allow initiation at downstream sites. TFIIIC-DNA complexes highly unstable at high temperatures. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12533520;Dbxref=PMID:12533520	
+##sequence-region P53215 1 237
+P53215	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P53215	UniProtKB	Chain	2	237	.	.	.	ID=PRO_0000202788;Note=tRNA(His) guanylyltransferase	
+P53215	UniProtKB	Nucleotide binding	29	34	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53215	UniProtKB	Nucleotide binding	76	77	.	.	.	Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53215	UniProtKB	Metal binding	29	29	.	.	.	Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53215	UniProtKB	Metal binding	29	29	.	.	.	Note=Magnesium 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53215	UniProtKB	Metal binding	30	30	.	.	.	Note=Magnesium 1%3B via carbonyl oxygen%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53215	UniProtKB	Metal binding	77	77	.	.	.	Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53215	UniProtKB	Metal binding	77	77	.	.	.	Note=Magnesium 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P53215	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+##sequence-region Q07748 1 340
+Q07748	UniProtKB	Chain	1	340	.	.	.	ID=PRO_0000211621;Note=4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI13	
+Q07748	UniProtKB	Region	115	118	.	.	.	Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+Q07748	UniProtKB	Motif	195	199	.	.	.	Note=CCCFC%3B essential for catalytic activity%2C may be the site of iron coordination;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+Q07748	UniProtKB	Active site	66	66	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+Q07748	UniProtKB	Modified residue	62	62	.	.	.	Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534	
+##sequence-region Q08975 1 551
+Q08975	UniProtKB	Chain	1	551	.	.	.	ID=PRO_0000192042;Note=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21	
+Q08975	UniProtKB	Binding site	64	64	.	.	.	Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q08579 1 599
+Q08579	UniProtKB	Chain	1	599	.	.	.	ID=PRO_0000197928;Note=Thiamine transporter THI72	
+Q08579	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08579	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08579	UniProtKB	Transmembrane	112	132	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08579	UniProtKB	Transmembrane	174	194	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08579	UniProtKB	Transmembrane	197	217	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08579	UniProtKB	Transmembrane	280	300	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08579	UniProtKB	Transmembrane	333	353	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08579	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08579	UniProtKB	Transmembrane	395	415	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08579	UniProtKB	Transmembrane	447	467	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08579	UniProtKB	Transmembrane	484	504	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q08579	UniProtKB	Modified residue	560	560	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05998	
+Q08579	UniProtKB	Modified residue	572	572	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08485	
+##sequence-region P41544 1 203
+P41544	UniProtKB	Chain	1	203	.	.	.	ID=PRO_0000213942;Note=Protein SYS1	
+P41544	UniProtKB	Topological domain	1	29	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41544	UniProtKB	Transmembrane	30	52	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41544	UniProtKB	Topological domain	53	78	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41544	UniProtKB	Transmembrane	79	101	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41544	UniProtKB	Topological domain	102	105	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41544	UniProtKB	Transmembrane	106	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41544	UniProtKB	Topological domain	126	131	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41544	UniProtKB	Transmembrane	132	154	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41544	UniProtKB	Topological domain	155	203	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P41544	UniProtKB	Modified residue	192	192	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P41544	UniProtKB	Cross-link	15	15	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538	
+P41544	UniProtKB	Sequence conflict	149	203	.	.	.	Note=GTWTTRWRELRDTFFEGLVDPNEGEVGLVTPSQQHSNHSELEQSPIQLKDLESQI->ALT;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P41896 1 400
+P41896	UniProtKB	Chain	1	400	.	.	.	ID=PRO_0000211240;Note=Transcription initiation factor IIF subunit beta	
+P41896	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41896	UniProtKB	Modified residue	34	34	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P41896	UniProtKB	Modified residue	56	56	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P41896	UniProtKB	Sequence conflict	232	232	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q05021 1 590
+Q05021	UniProtKB	Chain	1	590	.	.	.	ID=PRO_0000118885;Note=Transcription initiation factor TFIID subunit 7	
+Q05021	UniProtKB	Coiled coil	427	549	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05021	UniProtKB	Compositional bias	7	90	.	.	.	Note=Lys-rich	
+Q05021	UniProtKB	Compositional bias	200	203	.	.	.	Note=Poly-Glu	
+Q05021	UniProtKB	Compositional bias	304	571	.	.	.	Note=Asp/Glu-rich	
+Q05021	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+Q05021	UniProtKB	Modified residue	101	101	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+Q05021	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+Q05021	UniProtKB	Beta strand	97	100	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Beta strand	112	119	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Helix	126	135	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Beta strand	141	145	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Beta strand	147	155	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Beta strand	158	175	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Beta strand	177	197	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Helix	201	204	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Turn	215	219	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Helix	221	223	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Helix	224	234	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Helix	238	240	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Helix	245	249	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Helix	251	256	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Helix	267	269	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Turn	270	276	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Helix	283	301	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+Q05021	UniProtKB	Beta strand	302	311	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2	
+##sequence-region P40468 1 2376
+P40468	UniProtKB	Chain	1	2376	.	.	.	ID=PRO_0000072430;Note=Cell morphogenesis protein PAG1	
+P40468	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40468	UniProtKB	Modified residue	1144	1144	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40468	UniProtKB	Modified residue	2264	2264	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198	
+P40468	UniProtKB	Modified residue	2267	2267	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40468	UniProtKB	Modified residue	2355	2355	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+##sequence-region Q8TGM6 1 124
+Q8TGM6	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000072432;Note=Protein TAR1	
+##sequence-region P38967 1 592
+P38967	UniProtKB	Chain	1	592	.	.	.	ID=PRO_0000054160;Note=Tryptophan permease	
+P38967	UniProtKB	Topological domain	1	87	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	88	108	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	109	113	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	114	134	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	135	160	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	161	181	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	182	192	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	193	213	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	214	226	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	227	247	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	248	266	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	267	287	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	288	306	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	307	327	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	328	358	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	359	379	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	380	404	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	405	425	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	426	428	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	429	449	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	450	472	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	473	493	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	494	514	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Transmembrane	515	535	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Topological domain	536	592	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38967	UniProtKB	Sequence conflict	187	187	.	.	.	Note=Q->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47030 1 604
+P47030	UniProtKB	Chain	1	604	.	.	.	ID=PRO_0000203050;Note=Protein TAX4	
+P47030	UniProtKB	Domain	469	559	.	.	.	Note=EH	
+P47030	UniProtKB	Compositional bias	182	239	.	.	.	Note=Ser-rich	
+P47030	UniProtKB	Compositional bias	397	422	.	.	.	Note=His-rich	
+##sequence-region P26637 1 1090
+P26637	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P26637	UniProtKB	Chain	2	1090	.	.	.	ID=PRO_0000152155;Note=Leucine--tRNA ligase%2C cytoplasmic	
+P26637	UniProtKB	Motif	66	76	.	.	.	Note="HIGH" region	
+P26637	UniProtKB	Motif	729	733	.	.	.	Note="KMSKS" region	
+P26637	UniProtKB	Binding site	732	732	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P26637	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P26637	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P00958 1 751
+P00958	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:3905796,ECO:0000269|PubMed:6371805;Dbxref=PMID:3905796,PMID:6371805	
+P00958	UniProtKB	Chain	2	751	.	.	.	ID=PRO_0000139269;Note=Methionine--tRNA ligase%2C cytoplasmic	
+P00958	UniProtKB	Region	36	92	.	.	.	Note=Interaction with ARC1	
+P00958	UniProtKB	Motif	205	215	.	.	.	Note="HIGH" region	
+P00958	UniProtKB	Motif	525	529	.	.	.	Note="KMSKS" region	
+P00958	UniProtKB	Binding site	411	411	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P00958	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:3905796,ECO:0000269|PubMed:6371805;Dbxref=PMID:3905796,PMID:6371805	
+P00958	UniProtKB	Mutagenesis	63	63	.	.	.	Note=Abolishes interaction with ARC1. A->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16914447;Dbxref=PMID:16914447	
+P00958	UniProtKB	Mutagenesis	502	502	.	.	.	Note=In mes1%3B renders the protein unstable in vitro%2C elevates the KM for methionine in vivo. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3312199;Dbxref=PMID:3312199	
+P00958	UniProtKB	Mutagenesis	584	584	.	.	.	Note=Abolishes aminoacylation activity. N->D%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1915850;Dbxref=PMID:1915850	
+P00958	UniProtKB	Mutagenesis	588	588	.	.	.	Note=Abolishes aminoacylation activity. R->A%2CK%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1915850;Dbxref=PMID:1915850	
+P00958	UniProtKB	Sequence conflict	122	122	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00958	UniProtKB	Sequence conflict	122	122	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P00958	UniProtKB	Beta strand	3	5	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Beta strand	10	12	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Helix	15	31	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Beta strand	49	51	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Helix	61	68	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Turn	73	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Helix	78	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Turn	87	89	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Helix	90	92	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Beta strand	93	95	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Helix	98	111	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Helix	122	142	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+P00958	UniProtKB	Helix	148	157	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN	
+##sequence-region P22438 1 575
+P22438	UniProtKB	Chain	1	575	.	.	.	ID=PRO_0000139272;Note=Methionine--tRNA ligase%2C mitochondrial	
+P22438	UniProtKB	Motif	20	32	.	.	.	Note="HIGH" region	
+P22438	UniProtKB	Motif	341	345	.	.	.	Note="KMSKS" region	
+P22438	UniProtKB	Binding site	344	344	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P22438	UniProtKB	Sequence conflict	14	14	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P04803 1 379
+P04803	UniProtKB	Chain	1	379	.	.	.	ID=PRO_0000136745;Note=Tryptophan--tRNA ligase%2C mitochondrial	
+P04803	UniProtKB	Nucleotide binding	48	51	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6	
+P04803	UniProtKB	Nucleotide binding	196	198	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6	
+P04803	UniProtKB	Nucleotide binding	244	248	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6	
+P04803	UniProtKB	Motif	43	51	.	.	.	Note="HIGH" region	
+P04803	UniProtKB	Motif	244	248	.	.	.	Note="KMSKS" region	
+P04803	UniProtKB	Binding site	42	42	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6	
+P04803	UniProtKB	Binding site	184	184	.	.	.	Note=L-tryptophan;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6	
+P04803	UniProtKB	Binding site	235	235	.	.	.	Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6	
+P04803	UniProtKB	Binding site	247	247	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P04803	UniProtKB	Sequence conflict	268	271	.	.	.	Note=KIRK->RLE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P04803	UniProtKB	Sequence conflict	371	379	.	.	.	Note=ADIHKIMGF->PTFIK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P48527 1 492
+P48527	UniProtKB	Motif	94	103	.	.	.	Note="HIGH" region	
+P48527	UniProtKB	Motif	303	307	.	.	.	Note="KMSKS" region	
+P48527	UniProtKB	Binding site	89	89	.	.	.	Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4	
+P48527	UniProtKB	Binding site	93	93	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4	
+P48527	UniProtKB	Binding site	133	133	.	.	.	Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4	
+P48527	UniProtKB	Binding site	239	239	.	.	.	Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4	
+P48527	UniProtKB	Binding site	243	243	.	.	.	Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4	
+P48527	UniProtKB	Binding site	246	246	.	.	.	Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4	
+P48527	UniProtKB	Binding site	265	265	.	.	.	Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4	
+P48527	UniProtKB	Binding site	306	306	.	.	.	Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P36145 1 328
+P36145	UniProtKB	Chain	1	328	.	.	.	ID=PRO_0000211230;Note=Transcription initiation factor IIE subunit beta	
+P36145	UniProtKB	DNA binding	113	187	.	.	.	Note=TFIIE beta;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00682	
+P36145	UniProtKB	Compositional bias	86	93	.	.	.	Note=Asp/Glu-rich (acidic)	
+P36145	UniProtKB	Compositional bias	294	311	.	.	.	Note=Arg/Lys-rich (basic)	
+P36145	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P36145	UniProtKB	Modified residue	97	97	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P36145	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P36145	UniProtKB	Sequence conflict	248	248	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P11747 1 167
+P11747	UniProtKB	Chain	1	167	.	.	.	ID=PRO_0000118912;Note=Transcription initiation factor TFIID subunit 13	
+P11747	UniProtKB	Domain	10	74	.	.	.	Note=Histone-fold	
+P11747	UniProtKB	Coiled coil	109	129	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P11747	UniProtKB	Compositional bias	113	136	.	.	.	Note=Asp/Glu-rich (acidic)	
+P11747	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P11747	UniProtKB	Sequence conflict	137	138	.	.	.	Note=AA->GV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P11747	UniProtKB	Sequence conflict	158	158	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P53228 1 333
+P53228	UniProtKB	Chain	1	333	.	.	.	ID=PRO_0000173575;Note=Transaldolase NQM1	
+P53228	UniProtKB	Active site	144	144	.	.	.	Note=Schiff-base intermediate with substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10019	
+P53228	UniProtKB	Sequence conflict	290	290	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P53228	UniProtKB	Helix	15	21	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Beta strand	25	29	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	33	35	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	37	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Beta strand	42	45	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	48	55	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	58	60	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	61	74	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	78	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Beta strand	105	108	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	111	113	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	117	133	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	138	140	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Beta strand	141	146	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	149	162	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Beta strand	166	171	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	174	182	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Beta strand	186	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	193	201	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Turn	209	211	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	213	228	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Beta strand	233	237	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	242	248	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Beta strand	251	257	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	258	266	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	277	280	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	281	283	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	294	303	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+P53228	UniProtKB	Helix	305	333	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0	
+##sequence-region P38085 1 619
+P38085	UniProtKB	Chain	1	619	.	.	.	ID=PRO_0000054162;Note=Valine/tyrosine/tryptophan amino-acid permease 1	
+P38085	UniProtKB	Topological domain	1	99	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	100	120	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	121	122	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	144	172	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	173	193	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	194	204	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	205	225	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	226	233	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	234	254	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	255	281	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	282	302	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	303	320	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	321	341	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	342	368	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	369	389	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	390	422	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	423	443	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	444	446	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	447	467	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	468	499	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	500	520	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	521	529	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Transmembrane	530	550	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Topological domain	551	619	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38085	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38085	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P38085	UniProtKB	Modified residue	84	84	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198	
+P38085	UniProtKB	Cross-link	39	39	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P48606 1 106
+P48606	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000080045;Note=Tubulin-specific chaperone A	
+P48606	UniProtKB	Modified residue	94	94	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198	
+P48606	UniProtKB	Helix	5	39	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSD	
+P48606	UniProtKB	Helix	45	81	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSD	
+P48606	UniProtKB	Beta strand	85	87	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSD	
+P48606	UniProtKB	Helix	90	104	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSD	
+##sequence-region P46670 1 268
+P46670	UniProtKB	Chain	1	268	.	.	.	ID=PRO_0000089762;Note=Tubulin-specific chaperone C	
+P46670	UniProtKB	Domain	98	255	.	.	.	Note=C-CAP/cofactor C-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00659	
+P46670	UniProtKB	Sequence conflict	66	66	.	.	.	Note=E->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46670	UniProtKB	Beta strand	103	105	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	107	110	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	116	122	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	124	127	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	136	148	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	150	154	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	157	170	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	172	177	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	184	192	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	194	199	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	208	214	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	216	221	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Helix	222	227	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	228	232	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Beta strand	248	251	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Helix	256	258	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+P46670	UniProtKB	Helix	260	267	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA	
+##sequence-region P38707 1 554
+P38707	UniProtKB	Chain	1	554	.	.	.	ID=PRO_0000176501;Note=Asparagine--tRNA ligase%2C cytoplasmic	
+##sequence-region P09734 1 445
+P09734	UniProtKB	Chain	1	445	.	.	.	ID=PRO_0000048240;Note=Tubulin alpha-3 chain	
+P09734	UniProtKB	Nucleotide binding	143	149	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53904 1 254
+P53904	UniProtKB	Chain	1	254	.	.	.	ID=PRO_0000083536;Note=Tubulin-specific chaperone B	
+P53904	UniProtKB	Domain	182	225	.	.	.	Note=CAP-Gly;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00045	
+##sequence-region P53378 1 473
+P53378	UniProtKB	Chain	1	473	.	.	.	ID=PRO_0000048481;Note=Tubulin gamma chain	
+P53378	UniProtKB	Nucleotide binding	143	149	.	.	.	Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P48231 1 1178
+P48231	UniProtKB	Chain	1	1178	.	.	.	ID=PRO_0000203444;Note=Tricalbin-2	
+P48231	UniProtKB	Topological domain	1	98	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48231	UniProtKB	Transmembrane	99	119	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48231	UniProtKB	Topological domain	120	120	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48231	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48231	UniProtKB	Topological domain	142	1178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P48231	UniProtKB	Domain	365	463	.	.	.	Note=C2 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+P48231	UniProtKB	Domain	637	733	.	.	.	Note=C2 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+P48231	UniProtKB	Domain	970	1070	.	.	.	Note=C2 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
+P48231	UniProtKB	Coiled coil	784	821	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P48231	UniProtKB	Modified residue	991	991	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12466	
+P48231	UniProtKB	Natural variant	11	13	.	.	.	Note=In strain: SK1. DQI->EQV	
+P48231	UniProtKB	Natural variant	121	121	.	.	.	Note=In strain: SK1. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P48231	UniProtKB	Natural variant	528	528	.	.	.	Note=In strain: SK1. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+P48231	UniProtKB	Natural variant	691	692	.	.	.	Note=In strain: SK1. IE->MK	
+P48231	UniProtKB	Natural variant	1159	1159	.	.	.	Note=In strain: SK1. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108	
+##sequence-region P12612 1 559
+P12612	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P12612	UniProtKB	Chain	2	559	.	.	.	ID=PRO_0000128315;Note=T-complex protein 1 subunit alpha	
+P12612	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378	
+P12612	UniProtKB	Mutagenesis	48	48	.	.	.	Note=Temperature-sensitive. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7908441;Dbxref=PMID:7908441	
+P12612	UniProtKB	Sequence conflict	530	530	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P47079 1 568
+P47079	UniProtKB	Chain	1	568	.	.	.	ID=PRO_0000128378;Note=T-complex protein 1 subunit theta	
+P47079	UniProtKB	Modified residue	505	505	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P47079	UniProtKB	Cross-link	15	15	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
+##sequence-region O13513 1 116
+O13513	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000299656;Note=Putative uncharacterized protein YAL056C-A	
+##sequence-region O13511 1 128
+O13511	UniProtKB	Chain	1	128	.	.	.	ID=PRO_0000248430;Note=Uncharacterized protein YAL065C	
+O13511	UniProtKB	Transmembrane	105	127	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39728 1 267
+P39728	UniProtKB	Chain	1	267	.	.	.	ID=PRO_0000202418;Note=Uncharacterized protein YAL037W	
+##sequence-region P39725 1 102
+P39725	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000202420;Note=Putative uncharacterized protein YAL045C	
+##sequence-region Q8TGU6 1 64
+Q8TGU6	UniProtKB	Chain	1	64	.	.	.	ID=PRO_0000248437;Note=Uncharacterized protein YBR182C-A	
+##sequence-region Q12260 1 438
+Q12260	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000279275;Note=Transposon Ty2-B Gag polyprotein	
+Q12260	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279276;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12260	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000279277;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12260	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12260	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q8TGU5 1 39
+Q8TGU5	UniProtKB	Chain	1	39	.	.	.	ID=PRO_0000248445;Note=Uncharacterized protein YBR296C-A	
+##sequence-region P38311 1 105
+P38311	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000202511;Note=Uncharacterized protein YBR209W	
+P38311	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38321 1 900
+P38321	UniProtKB	Chain	1	900	.	.	.	ID=PRO_0000202515;Note=Uncharacterized protein YBR225W	
+P38321	UniProtKB	Modified residue	105	105	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P38331 1 238
+P38331	UniProtKB	Chain	1	238	.	.	.	ID=PRO_0000202522;Note=HD domain-containing protein YBR242W	
+P38331	UniProtKB	Domain	77	183	.	.	.	Note=HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01175	
+##sequence-region P38178 1 141
+P38178	UniProtKB	Chain	1	141	.	.	.	ID=PRO_0000202446;Note=Putative uncharacterized protein YBL083C	
+##sequence-region P38168 1 104
+P38168	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000202440;Note=Putative uncharacterized protein YBL100C	
+P38168	UniProtKB	Transmembrane	77	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38240 1 142
+P38240	UniProtKB	Chain	1	142	.	.	.	ID=PRO_0000202477;Note=Putative uncharacterized membrane protein YBR064W	
+P38240	UniProtKB	Topological domain	1	9	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38240	UniProtKB	Transmembrane	10	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38240	UniProtKB	Topological domain	31	41	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38240	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38240	UniProtKB	Topological domain	63	101	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38240	UniProtKB	Transmembrane	102	122	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38240	UniProtKB	Topological domain	123	142	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38276 1 179
+P38276	UniProtKB	Chain	1	179	.	.	.	ID=PRO_0000208926;Note=UPF0303 protein YBR137W	
+P38276	UniProtKB	Sequence conflict	110	110	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38276	UniProtKB	Sequence conflict	110	110	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38276	UniProtKB	Helix	6	14	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Helix	19	27	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Beta strand	30	32	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Helix	36	53	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Beta strand	54	57	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Beta strand	60	64	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Beta strand	70	75	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Helix	82	98	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Helix	102	109	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Turn	114	116	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Turn	122	124	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Beta strand	131	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Turn	137	139	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Beta strand	143	151	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Helix	154	168	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+P38276	UniProtKB	Turn	169	172	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC	
+##sequence-region P25565 1 263
+P25565	UniProtKB	Chain	1	263	.	.	.	ID=PRO_0000202537;Note=Putative uncharacterized protein YCL002C	
+P25565	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25565	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25565	UniProtKB	Transmembrane	82	102	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25565	UniProtKB	Transmembrane	118	138	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25565	UniProtKB	Transmembrane	151	171	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25565	UniProtKB	Transmembrane	196	216	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25565	UniProtKB	Transmembrane	230	250	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25561 1 117
+P25561	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000202540;Note=Putative uncharacterized protein YCL021W	
+##sequence-region O13527 1 1196
+O13527	UniProtKB	Chain	1	1196	.	.	.	ID=PRO_0000278977;Note=Truncated transposon Ty1-A Gag-Pol polyprotein	
+O13527	UniProtKB	Chain	1	658	.	.	.	ID=PRO_0000278980;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O13527	UniProtKB	Chain	659	1196	.	.	.	ID=PRO_0000278981;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O13527	UniProtKB	Domain	101	276	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13527	UniProtKB	Domain	779	917	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+O13527	UniProtKB	Domain	1051	1193	.	.	.	Note=RNase H Ty1/copia-type	
+O13527	UniProtKB	Motif	619	653	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O13527	UniProtKB	Metal binding	112	112	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13527	UniProtKB	Metal binding	177	177	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13527	UniProtKB	Metal binding	787	787	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13527	UniProtKB	Metal binding	868	868	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13527	UniProtKB	Metal binding	869	869	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13527	UniProtKB	Metal binding	1051	1051	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13527	UniProtKB	Metal binding	1093	1093	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13527	UniProtKB	Metal binding	1126	1126	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+O13527	UniProtKB	Site	658	659	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P0C5L1 1 78
+P0C5L1	UniProtKB	Chain	1	78	.	.	.	ID=PRO_0000309009;Note=Putative uncharacterized protein YBL068W-A	
+##sequence-region Q7M4S9 1 792
+Q7M4S9	UniProtKB	Chain	1	792	.	.	.	ID=PRO_0000248431;Note=Uncharacterized protein YBL113C	
+Q7M4S9	UniProtKB	Repeat	91	102	.	.	.	Note=1	
+Q7M4S9	UniProtKB	Repeat	103	114	.	.	.	Note=2	
+Q7M4S9	UniProtKB	Repeat	115	126	.	.	.	Note=3	
+Q7M4S9	UniProtKB	Repeat	127	138	.	.	.	Note=4	
+Q7M4S9	UniProtKB	Repeat	139	150	.	.	.	Note=5	
+Q7M4S9	UniProtKB	Repeat	151	162	.	.	.	Note=6	
+Q7M4S9	UniProtKB	Repeat	163	174	.	.	.	Note=7	
+Q7M4S9	UniProtKB	Repeat	175	186	.	.	.	Note=8	
+Q7M4S9	UniProtKB	Repeat	187	198	.	.	.	Note=9	
+Q7M4S9	UniProtKB	Repeat	199	210	.	.	.	Note=10	
+Q7M4S9	UniProtKB	Repeat	211	222	.	.	.	Note=11	
+Q7M4S9	UniProtKB	Repeat	223	234	.	.	.	Note=12	
+Q7M4S9	UniProtKB	Repeat	235	246	.	.	.	Note=13	
+Q7M4S9	UniProtKB	Repeat	247	258	.	.	.	Note=14	
+Q7M4S9	UniProtKB	Repeat	259	270	.	.	.	Note=15	
+Q7M4S9	UniProtKB	Repeat	271	282	.	.	.	Note=16	
+Q7M4S9	UniProtKB	Repeat	283	294	.	.	.	Note=17	
+Q7M4S9	UniProtKB	Repeat	295	306	.	.	.	Note=18	
+Q7M4S9	UniProtKB	Repeat	307	318	.	.	.	Note=19	
+Q7M4S9	UniProtKB	Repeat	319	330	.	.	.	Note=20	
+Q7M4S9	UniProtKB	Repeat	331	342	.	.	.	Note=21	
+Q7M4S9	UniProtKB	Repeat	343	354	.	.	.	Note=22	
+Q7M4S9	UniProtKB	Repeat	355	366	.	.	.	Note=23	
+Q7M4S9	UniProtKB	Repeat	367	378	.	.	.	Note=24	
+Q7M4S9	UniProtKB	Repeat	379	390	.	.	.	Note=25	
+Q7M4S9	UniProtKB	Region	91	390	.	.	.	Note=25 X 12 AA tandem repeat of N-[SV]-[RS]-T-[NS]-A-T-T-T-[AE]-[ST]-[IT]	
+##sequence-region P0C5L4 1 52
+P0C5L4	UniProtKB	Chain	1	52	.	.	.	ID=PRO_0000309012;Note=Uncharacterized protein YBR121C-A	
+##sequence-region Q8TGK5 1 160
+Q8TGK5	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000299783;Note=Putative UPF0479 protein YBL113W-A	
+Q8TGK5	UniProtKB	Transmembrane	39	59	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q8TGK5	UniProtKB	Transmembrane	136	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E755 1 54
+Q3E755	UniProtKB	Signal peptide	1	13	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E755	UniProtKB	Chain	14	54	.	.	.	ID=PRO_0000248440;Note=Uncharacterized protein YBR200W-A	
+##sequence-region Q8TGQ3 1 39
+Q8TGQ3	UniProtKB	Chain	1	39	.	.	.	ID=PRO_0000299796;Note=Putative uncharacterized protein YBR223W-A	
+##sequence-region P38296 1 124
+P38296	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000202504;Note=Putative uncharacterized protein YBR178W	
+##sequence-region P38327 1 119
+P38327	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000202519;Note=Putative uncharacterized protein YBR232C	
+P38327	UniProtKB	Transmembrane	61	80	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38327	UniProtKB	Transmembrane	87	103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38354 1 144
+P38354	UniProtKB	Chain	1	144	.	.	.	ID=PRO_0000202534;Note=Putative uncharacterized protein YBR285W	
+P38354	UniProtKB	Sequence conflict	55	55	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38354	UniProtKB	Sequence conflict	55	55	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P38354	UniProtKB	Sequence conflict	55	55	.	.	.	Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38362 1 165
+P38362	UniProtKB	Chain	1	165	.	.	.	ID=PRO_0000202536;Note=Putative uncharacterized protein YBR300C	
+P38362	UniProtKB	Transmembrane	10	27	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E778 1 34
+Q3E778	UniProtKB	Chain	1	34	.	.	.	ID=PRO_0000248439;Note=Uncharacterized protein YBR196C-B	
+##sequence-region P32788 1 280
+P32788	UniProtKB	Chain	1	280	.	.	.	ID=PRO_0000076536;Note=Uncharacterized protein YBL010C	
+P32788	UniProtKB	Domain	225	264	.	.	.	Note=bZIP	
+P32788	UniProtKB	Region	225	240	.	.	.	Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P32788	UniProtKB	Region	250	264	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38177 1 466
+P38177	UniProtKB	Chain	1	466	.	.	.	ID=PRO_0000202445;Note=Uncharacterized protein YBL086C	
+P38177	UniProtKB	Domain	8	206	.	.	.	Note=NT-C2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38177	UniProtKB	Modified residue	433	433	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198	
+P38177	UniProtKB	Modified residue	439	439	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P38177	UniProtKB	Sequence conflict	318	318	.	.	.	Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38171 1 102
+P38171	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000014308;Note=Putative uncharacterized protein YBL096C	
+##sequence-region P38214 1 139
+P38214	UniProtKB	Chain	1	139	.	.	.	ID=PRO_0000202468;Note=Putative uncharacterized protein YBR012C	
+##sequence-region P38315 1 674
+P38315	UniProtKB	Chain	1	674	.	.	.	ID=PRO_0000066150;Note=YAP1-binding protein 1	
+P38315	UniProtKB	Compositional bias	613	616	.	.	.	Note=Poly-Leu	
+P38315	UniProtKB	Natural variant	7	7	.	.	.	Note=In strain: W303-1a. I->L	
+P38315	UniProtKB	Natural variant	328	328	.	.	.	Note=In strain: W303-1a. F->V	
+P38315	UniProtKB	Natural variant	343	343	.	.	.	Note=In strain: W303-1a. K->E	
+P38315	UniProtKB	Natural variant	570	570	.	.	.	Note=In strain: W303-1a. N->D	
+##sequence-region P38267 1 160
+P38267	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000202487;Note=Putative uncharacterized membrane protein YBR113W	
+P38267	UniProtKB	Topological domain	1	33	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38267	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38267	UniProtKB	Topological domain	55	68	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38267	UniProtKB	Transmembrane	69	89	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38267	UniProtKB	Topological domain	90	119	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38267	UniProtKB	Transmembrane	120	140	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38267	UniProtKB	Topological domain	141	160	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38275 1 133
+P38275	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000202492;Note=Putative uncharacterized protein YBR134W	
+##sequence-region P34215 1 104
+P34215	UniProtKB	Chain	1	104	.	.	.	ID=PRO_0000202495;Note=Uncharacterized protein YBR144C	
+##sequence-region Q96VH2 1 84
+Q96VH2	UniProtKB	Chain	1	84	.	.	.	ID=PRO_0000248412;Note=Putative pelota-like protein YCL001W-B	
+##sequence-region P25571 1 164
+P25571	UniProtKB	Chain	1	164	.	.	.	ID=PRO_0000202544;Note=Putative uncharacterized protein YCL041C	
+##sequence-region P25350 1 157
+P25350	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000202560;Note=Uncharacterized protein YCR006C	
+##sequence-region Q3E7Z7 1 40
+Q3E7Z7	UniProtKB	Chain	1	40	.	.	.	ID=PRO_0000242622;Note=Uncharacterized protein YDR003W-A	
+Q3E7Z7	UniProtKB	Compositional bias	14	17	.	.	.	Note=Poly-Lys	
+##sequence-region Q12281 1 103
+Q12281	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000299848;Note=Putative uncharacterized protein YDL032w	
+##sequence-region Q07793 1 1604
+Q07793	UniProtKB	Chain	1	1604	.	.	.	ID=PRO_0000279017;Note=Transposon Ty1-DR4 Gag-Pol polyprotein	
+Q07793	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279018;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07793	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279019;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07793	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279020;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07793	UniProtKB	Chain	1218	1604	.	.	.	ID=PRO_0000279021;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07793	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07793	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q07793	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07793	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q07793	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07793	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q07793	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07793	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07793	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07793	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07793	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07793	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07793	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07793	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07793	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region Q12082 1 118
+Q12082	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000240875;Note=Uncharacterized protein YDL157C%2C mitochondrial	
+##sequence-region Q12148 1 100
+Q12148	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000299861;Note=Putative uncharacterized protein YDL163W	
+##sequence-region Q03983 1 463
+Q03983	UniProtKB	Chain	1	463	.	.	.	ID=PRO_0000202588;Note=Uncharacterized protein YDR179W-A	
+##sequence-region P48568 1 277
+P48568	UniProtKB	Chain	1	277	.	.	.	ID=PRO_0000202589;Note=Uncharacterized protein YDL186W	
+P48568	UniProtKB	Compositional bias	51	54	.	.	.	Note=Poly-Arg	
+P48568	UniProtKB	Compositional bias	240	252	.	.	.	Note=Poly-Gln	
+P48568	UniProtKB	Sequence conflict	273	273	.	.	.	Note=F->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q2V2P9 1 66
+Q2V2P9	UniProtKB	Chain	1	66	.	.	.	ID=PRO_0000253829;Note=Uncharacterized protein YDR119W-A	
+Q2V2P9	UniProtKB	Transmembrane	39	61	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03787 1 373
+Q03787	UniProtKB	Chain	1	373	.	.	.	ID=PRO_0000253841;Note=Uncharacterized protein YDR249C	
+##sequence-region Q05612 1 105
+Q05612	UniProtKB	Chain	1	105	.	.	.	ID=PRO_0000299881;Note=Uncharacterized protein YDR278C	
+Q05612	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q05497 1 695
+Q05497	UniProtKB	Chain	1	695	.	.	.	ID=PRO_0000164255;Note=Uncharacterized transporter YDR338C	
+Q05497	UniProtKB	Transmembrane	237	257	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Transmembrane	265	285	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Transmembrane	313	333	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Transmembrane	344	364	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Transmembrane	380	400	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Transmembrane	408	428	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Transmembrane	457	477	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Transmembrane	488	508	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Transmembrane	531	551	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Transmembrane	565	585	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Transmembrane	604	624	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Transmembrane	633	653	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q05497	UniProtKB	Modified residue	113	113	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region Q3E6R5 1 114
+Q3E6R5	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000253850;Note=Uncharacterized mitochondrial outer membrane protein YDR381C-A	
+Q3E6R5	UniProtKB	Transmembrane	13	30	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P87266 1 191
+P87266	UniProtKB	Chain	1	191	.	.	.	ID=PRO_0000299890;Note=Putative uncharacterized protein YDR413C	
+P87266	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87266	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87266	UniProtKB	Transmembrane	92	112	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87266	UniProtKB	Transmembrane	168	188	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87266	UniProtKB	Compositional bias	57	185	.	.	.	Note=Ser-rich	
+##sequence-region Q8TGP5 1 62
+Q8TGP5	UniProtKB	Chain	1	62	.	.	.	ID=PRO_0000299897;Note=Putative uncharacterized protein YDR464C-A	
+##sequence-region P87274 1 156
+P87274	UniProtKB	Chain	1	156	.	.	.	ID=PRO_0000299903;Note=Putative uncharacterized protein YDR526C	
+P87274	UniProtKB	Transmembrane	21	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87274	UniProtKB	Transmembrane	54	74	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P87274	UniProtKB	Transmembrane	80	100	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P87261 1 201
+P87261	UniProtKB	Chain	1	201	.	.	.	ID=PRO_0000299905;Note=Putative uncharacterized protein YDR537C	
+##sequence-region P0CL37 1 159
+P0CL37	UniProtKB	Chain	1	159	.	.	.	ID=PRO_0000299784;Note=Putative UPF0479 protein YDR545C-A	
+P0CL37	UniProtKB	Transmembrane	38	58	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL37	UniProtKB	Transmembrane	135	155	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CL37	UniProtKB	Compositional bias	102	105	.	.	.	Note=Poly-Ser	
+##sequence-region Q02896 1 317
+Q02896	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000212465;Note=Alkaline ceramidase YDC1	
+Q02896	UniProtKB	Topological domain	1	42	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Transmembrane	43	60	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Topological domain	61	66	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Transmembrane	67	89	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Topological domain	90	98	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Transmembrane	99	121	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Topological domain	122	133	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Transmembrane	134	156	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Topological domain	157	159	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Transmembrane	160	182	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Topological domain	183	202	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Transmembrane	203	225	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Topological domain	226	239	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Transmembrane	240	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q02896	UniProtKB	Topological domain	263	317	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40057 1 128
+P40057	UniProtKB	Chain	1	128	.	.	.	ID=PRO_0000202638;Note=Uncharacterized protein YER084W	
+P40057	UniProtKB	Sequence conflict	57	57	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P40093 1 338
+P40093	UniProtKB	Chain	1	338	.	.	.	ID=PRO_0000213487;Note=UPF0160 protein YER156C	
+##sequence-region Q3E838 1 28
+Q3E838	UniProtKB	Chain	1	28	.	.	.	ID=PRO_0000245374;Note=Uncharacterized protein YFR012W-A	
+##sequence-region P43541 1 151
+P43541	UniProtKB	Chain	1	151	.	.	.	ID=PRO_0000211372;Note=Putative UPF0320 protein YFL063W	
+##sequence-region P43600 1 232
+P43600	UniProtKB	Chain	1	232	.	.	.	ID=PRO_0000202689;Note=Uncharacterized protein YFR020W	
+P43600	UniProtKB	Glycosylation	25	25	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43600	UniProtKB	Glycosylation	26	26	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43600	UniProtKB	Glycosylation	53	53	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43600	UniProtKB	Glycosylation	77	77	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P43600	UniProtKB	Glycosylation	163	163	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0C5N1 1 53
+P0C5N1	UniProtKB	Chain	1	53	.	.	.	ID=PRO_0000309029;Note=Uncharacterized protein YGL014C-A	
+##sequence-region P53185 1 909
+P53185	UniProtKB	Chain	1	909	.	.	.	ID=PRO_0000096613;Note=Uncharacterized protein YGL036W	
+P53185	UniProtKB	Compositional bias	377	387	.	.	.	Note=Poly-Asn	
+P53185	UniProtKB	Compositional bias	394	405	.	.	.	Note=Poly-Thr	
+P53185	UniProtKB	Compositional bias	406	413	.	.	.	Note=Poly-Asn	
+P53185	UniProtKB	Compositional bias	758	763	.	.	.	Note=Poly-Gln	
+P53185	UniProtKB	Modified residue	856	856	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P53185	UniProtKB	Modified residue	898	898	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region O13515 1 117
+O13515	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13515	UniProtKB	Chain	21	117	.	.	.	ID=PRO_0000299654;Note=Putative uncharacterized protein YAL034C-B	
+##sequence-region O13514 1 125
+O13514	UniProtKB	Chain	1	125	.	.	.	ID=PRO_0000299655;Note=Putative uncharacterized protein YAL042C-A	
+O13514	UniProtKB	Transmembrane	96	113	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PYD0 1 140
+A0A023PYD0	UniProtKB	Chain	1	140	.	.	.	ID=PRO_0000430974;Note=Putative uncharacterized membrane protein YAL059C-A	
+A0A023PYD0	UniProtKB	Transmembrane	42	62	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PYD0	UniProtKB	Transmembrane	65	85	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PYD0	UniProtKB	Transmembrane	96	116	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P0CX18 1 203
+P0CX18	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX18	UniProtKB	Chain	24	184	.	.	.	ID=PRO_0000202945;Note=Putative GPI-anchored protein YAR066W	
+P0CX18	UniProtKB	Propeptide	185	203	.	.	.	ID=PRO_0000409753;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX18	UniProtKB	Compositional bias	25	57	.	.	.	Note=Ser-rich	
+P0CX18	UniProtKB	Lipidation	184	184	.	.	.	Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX18	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX18	UniProtKB	Glycosylation	138	138	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P47118 1 141
+P47118	UniProtKB	Chain	1	141	.	.	.	ID=PRO_0000203099;Note=Uncharacterized protein YAE1	
+##sequence-region P0CX90 1 67
+P0CX90	UniProtKB	Chain	1	67	.	.	.	ID=PRO_0000202431;Note=Uncharacterized protein YAR061W	
+##sequence-region P0CX92 1 97
+P0CX92	UniProtKB	Chain	1	97	.	.	.	ID=PRO_0000202435;Note=Putative uncharacterized protein YAR069C	
+P0CX92	UniProtKB	Transmembrane	5	25	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX92	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P0CX92	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P40574 1 245
+P40574	UniProtKB	Chain	1	245	.	.	.	ID=PRO_0000076525;Note=AP-1-like transcription factor YAP5	
+P40574	UniProtKB	Domain	58	121	.	.	.	Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P40574	UniProtKB	Region	63	82	.	.	.	Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P40574	UniProtKB	Region	86	114	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
+P40574	UniProtKB	Sequence conflict	173	173	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region Q3E756 1 94
+Q3E756	UniProtKB	Chain	1	94	.	.	.	ID=PRO_0000248433;Note=UPF0768 protein YBL029C-A	
+##sequence-region P0C5L0 1 52
+P0C5L0	UniProtKB	Chain	1	52	.	.	.	ID=PRO_0000309008;Note=Putative uncharacterized protein YBR056C-B	
+P0C5L0	UniProtKB	Compositional bias	28	34	.	.	.	Note=Poly-Gln	
+##sequence-region P34220 1 418
+P34220	UniProtKB	Chain	1	418	.	.	.	ID=PRO_0000201994;Note=Deoxyribonuclease Tat-D	
+P34220	UniProtKB	Metal binding	185	185	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34220	UniProtKB	Metal binding	185	185	.	.	.	Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34220	UniProtKB	Metal binding	226	226	.	.	.	Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34220	UniProtKB	Metal binding	277	277	.	.	.	Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34220	UniProtKB	Metal binding	327	327	.	.	.	Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P34220	UniProtKB	Mutagenesis	185	185	.	.	.	Note=Reduces enzymatic activities by 50%25. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657035;Dbxref=PMID:15657035	
+P34220	UniProtKB	Mutagenesis	325	325	.	.	.	Note=Reduces enzymatic activities by 50%25. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657035;Dbxref=PMID:15657035	
+P34220	UniProtKB	Mutagenesis	327	327	.	.	.	Note=Reduces enzymatic activities by almost 95%25. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657035;Dbxref=PMID:15657035	
+P34220	UniProtKB	Sequence conflict	278	278	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region P38185 1 102
+P38185	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000202450;Note=Uncharacterized protein YBL071C	
+P38185	UniProtKB	Transmembrane	77	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38183 1 143
+P38183	UniProtKB	Chain	1	143	.	.	.	ID=PRO_0000202448;Note=Putative uncharacterized protein YBL077W	
+##sequence-region P38173 1 110
+P38173	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000202443;Note=Putative uncharacterized protein YBL094C	
+P38173	UniProtKB	Transmembrane	21	41	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38173	UniProtKB	Transmembrane	63	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P53169 1 641
+P53169	UniProtKB	Chain	1	641	.	.	.	ID=PRO_0000066151;Note=YAP1-binding protein 2	
+##sequence-region P38256 1 230
+P38256	UniProtKB	Chain	1	230	.	.	.	ID=PRO_0000202483;Note=Uncharacterized protein YBR096W	
+##sequence-region P25577 1 312
+P25577	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P25577	UniProtKB	Chain	20	312	.	.	.	ID=PRO_0000014312;Note=Uncharacterized protein YCL049C	
+P25577	UniProtKB	Compositional bias	286	292	.	.	.	Note=Poly-Glu	
+##sequence-region P25601 1 146
+P25601	UniProtKB	Chain	1	146	.	.	.	ID=PRO_0000203504;Note=Putative transposon Ty5-1 protein YCL075W	
+##sequence-region P25616 1 317
+P25616	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000202562;Note=UPF0655 protein YCR015C	
+##sequence-region P25629 1 148
+P25629	UniProtKB	Chain	1	148	.	.	.	ID=PRO_0000202570;Note=Putative uncharacterized protein YCR049C	
+##sequence-region P25630 1 102
+P25630	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000202571;Note=Uncharacterized protein YCR050C	
+##sequence-region P25608 1 368
+P25608	UniProtKB	Chain	1	368	.	.	.	ID=PRO_0000202585;Note=Uncharacterized protein YCR102C	
+##sequence-region Q2V2Q0 1 85
+Q2V2Q0	UniProtKB	Chain	1	85	.	.	.	ID=PRO_0000248455;Note=Putative uncharacterized protein YDL007C-A	
+##sequence-region Q12185 1 396
+Q12185	UniProtKB	Chain	1	396	.	.	.	ID=PRO_0000208208;Note=Uncharacterized acyltransferase YDR018C	
+Q12185	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12185	UniProtKB	Transmembrane	69	89	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12185	UniProtKB	Transmembrane	123	143	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12185	UniProtKB	Transmembrane	372	392	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12185	UniProtKB	Motif	117	122	.	.	.	Note=HXXXXD motif	
+##sequence-region Q12352 1 117
+Q12352	UniProtKB	Chain	1	117	.	.	.	ID=PRO_0000299850;Note=Putative uncharacterized protein YDL041W	
+Q12352	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q03831 1 136
+Q03831	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000299872;Note=Putative uncharacterized protein YDR095C	
+##sequence-region Q03856 1 440
+Q03856	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279006;Note=Transposon Ty1-DR1 Gag polyprotein	
+Q03856	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279007;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03856	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279008;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03856	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03856	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q03856	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03856	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q07541 1 149
+Q07541	UniProtKB	Chain	1	149	.	.	.	ID=PRO_0000240867;Note=Uncharacterized protein YDL121C	
+Q07541	UniProtKB	Topological domain	1	6	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07541	UniProtKB	Transmembrane	7	27	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07541	UniProtKB	Topological domain	28	149	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region O74302 1 440
+O74302	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279022;Note=Transposon Ty1-DR4 Gag polyprotein	
+O74302	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279023;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O74302	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279024;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O74302	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O74302	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+O74302	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+O74302	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region P0CX70 1 440
+P0CX70	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279037;Note=Transposon Ty1-DR6 Gag polyprotein	
+P0CX70	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279038;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX70	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279039;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX70	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX70	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+P0CX70	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P0CX70	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441	
+##sequence-region Q12027 1 708
+Q12027	UniProtKB	Chain	1	708	.	.	.	ID=PRO_0000240880;Note=Uncharacterized protein YDL176W	
+##sequence-region Q03964 1 440
+Q03964	UniProtKB	Chain	1	440	.	.	.	ID=PRO_0000279040;Note=Transposon Ty1-DR2 Gag polyprotein	
+Q03964	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279041;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03964	UniProtKB	Peptide	402	440	.	.	.	ID=PRO_0000279042;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03964	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03964	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q3E818 1 50
+Q3E818	UniProtKB	Chain	1	50	.	.	.	ID=PRO_0000253836;Note=Uncharacterized protein YDR194W-A	
+##sequence-region Q12424 1 762
+Q12424	UniProtKB	Signal peptide	1	26	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Chain	27	762	.	.	.	ID=PRO_0000242480;Note=Putative cation exchanger YDL206W	
+Q12424	UniProtKB	Topological domain	27	30	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Transmembrane	31	51	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Topological domain	52	102	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Transmembrane	103	123	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Topological domain	124	156	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Topological domain	178	178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Transmembrane	179	199	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Topological domain	200	501	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Transmembrane	502	522	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Topological domain	523	554	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Transmembrane	555	575	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Topological domain	576	589	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Transmembrane	590	610	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Topological domain	611	615	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Transmembrane	616	636	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Topological domain	637	650	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Transmembrane	651	671	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Topological domain	672	709	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Transmembrane	710	730	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Topological domain	731	738	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Transmembrane	739	759	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Topological domain	760	762	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Glycosylation	148	148	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Glycosylation	280	280	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Glycosylation	329	329	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12424	UniProtKB	Glycosylation	645	645	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q07629 1 317
+Q07629	UniProtKB	Chain	1	317	.	.	.	ID=PRO_0000242482;Note=Uncharacterized membrane protein YDL218W	
+Q07629	UniProtKB	Topological domain	1	13	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07629	UniProtKB	Transmembrane	14	34	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07629	UniProtKB	Topological domain	35	49	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07629	UniProtKB	Transmembrane	50	70	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07629	UniProtKB	Topological domain	71	71	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07629	UniProtKB	Transmembrane	72	92	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07629	UniProtKB	Topological domain	93	133	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07629	UniProtKB	Transmembrane	134	154	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07629	UniProtKB	Topological domain	155	317	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07629	UniProtKB	Compositional bias	239	259	.	.	.	Note=Thr-rich	
+Q07629	UniProtKB	Glycosylation	43	43	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q07629	UniProtKB	Glycosylation	129	129	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04923 1 97
+Q04923	UniProtKB	Chain	1	97	.	.	.	ID=PRO_0000299877;Note=Putative uncharacterized protein YDR220C	
+##sequence-region A0A023PZA9 1 115
+A0A023PZA9	UniProtKB	Chain	1	115	.	.	.	ID=PRO_0000430984;Note=Putative uncharacterized protein YDR230W	
+##sequence-region Q99303 1 438
+Q99303	UniProtKB	Chain	1	438	.	.	.	ID=PRO_0000279305;Note=Transposon Ty2-DR3 Gag polyprotein	
+Q99303	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279306;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99303	UniProtKB	Peptide	398	438	.	.	.	ID=PRO_0000279307;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99303	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q99303	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q07791 1 1770
+Q07791	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000279300;Note=Transposon Ty2-DR3 Gag-Pol polyprotein	
+Q07791	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279301;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07791	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000279302;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07791	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000279303;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07791	UniProtKB	Chain	1233	1770	.	.	.	ID=PRO_0000279304;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07791	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07791	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q07791	UniProtKB	Domain	1625	1767	.	.	.	Note=RNase H Ty1/copia-type	
+Q07791	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07791	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+Q07791	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07791	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07791	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07791	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07791	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07791	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07791	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07791	UniProtKB	Metal binding	1625	1625	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07791	UniProtKB	Metal binding	1667	1667	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07791	UniProtKB	Metal binding	1700	1700	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q07791	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07791	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q07791	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region Q05510 1 147
+Q05510	UniProtKB	Chain	1	147	.	.	.	ID=PRO_0000299885;Note=Uncharacterized protein YDR344C	
+##sequence-region P0C5M1 1 34
+P0C5M1	UniProtKB	Chain	1	34	.	.	.	ID=PRO_0000309019;Note=Uncharacterized protein YDR371C-A	
+##sequence-region Q04162 1 555
+Q04162	UniProtKB	Chain	1	555	.	.	.	ID=PRO_0000252274;Note=Probable metabolite transport protein YDR387C	
+Q04162	UniProtKB	Topological domain	1	39	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	40	60	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	61	83	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	84	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	105	118	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	140	140	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	141	161	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	162	168	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	169	189	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	190	200	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	201	221	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	222	356	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	357	377	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	378	384	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	385	405	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	406	413	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	414	434	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	435	440	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	441	461	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	462	474	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	475	497	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	498	506	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Transmembrane	507	527	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Topological domain	528	555	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q04162	UniProtKB	Compositional bias	315	318	.	.	.	Note=Poly-Ser	
+##sequence-region P87268 1 125
+P87268	UniProtKB	Chain	1	125	.	.	.	ID=PRO_0000299891;Note=Putative uncharacterized protein YDR426C	
+##sequence-region A0A023PYD7 1 172
+A0A023PYD7	UniProtKB	Chain	1	172	.	.	.	ID=PRO_0000430986;Note=Putative uncharacterized membrane protein YDR187C	
+A0A023PYD7	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q12187 1 109
+Q12187	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000299864;Note=Putative uncharacterized protein YDL196W	
+Q12187	UniProtKB	Transmembrane	19	39	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q12187	UniProtKB	Transmembrane	53	73	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q04597 1 100
+Q04597	UniProtKB	Chain	1	100	.	.	.	ID=PRO_0000277620;Note=Uncharacterized protein YDR114C	
+##sequence-region A0A023PZ94 1 102
+A0A023PZ94	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000430972;Note=Putative uncharacterized membrane protein YAL031W-A	
+A0A023PZ94	UniProtKB	Transmembrane	28	48	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZ94	UniProtKB	Transmembrane	81	101	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGV0 1 26
+Q8TGV0	UniProtKB	Chain	1	26	.	.	.	ID=PRO_0000248426;Note=Uncharacterized protein YAR035C-A	
+Q8TGV0	UniProtKB	Sequence conflict	24	24	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+Q8TGV0	UniProtKB	Sequence conflict	24	24	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+##sequence-region A0A023PZE2 1 109
+A0A023PZE2	UniProtKB	Chain	1	109	.	.	.	ID=PRO_0000430973;Note=Putative uncharacterized membrane protein YAL047W-A	
+A0A023PZE2	UniProtKB	Transmembrane	24	44	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PZE2	UniProtKB	Transmembrane	68	88	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGR8 1 324
+Q8TGR8	UniProtKB	Chain	1	324	.	.	.	ID=PRO_0000299746;Note=Putative uncharacterized protein YAL037C-B	
+##sequence-region O13512 1 126
+O13512	UniProtKB	Chain	1	126	.	.	.	ID=PRO_0000248429;Note=Uncharacterized membrane protein YAL064W-B	
+O13512	UniProtKB	Topological domain	1	28	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13512	UniProtKB	Transmembrane	29	49	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13512	UniProtKB	Topological domain	50	75	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13512	UniProtKB	Transmembrane	76	96	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13512	UniProtKB	Topological domain	97	97	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13512	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+O13512	UniProtKB	Topological domain	119	126	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39711 1 94
+P39711	UniProtKB	Chain	1	94	.	.	.	ID=PRO_0000202425;Note=Putative uncharacterized protein YAL064W	
+##sequence-region P14680 1 807
+P14680	UniProtKB	Chain	1	807	.	.	.	ID=PRO_0000086828;Note=Dual specificity protein kinase YAK1	
+P14680	UniProtKB	Domain	369	704	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P14680	UniProtKB	Nucleotide binding	375	383	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P14680	UniProtKB	Compositional bias	56	85	.	.	.	Note=Gln-rich	
+P14680	UniProtKB	Active site	496	496	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
+P14680	UniProtKB	Binding site	398	398	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
+P14680	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P14680	UniProtKB	Modified residue	115	115	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14680	UniProtKB	Modified residue	118	118	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14680	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
+P14680	UniProtKB	Modified residue	206	206	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14680	UniProtKB	Modified residue	240	240	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14680	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14680	UniProtKB	Modified residue	247	247	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P14680	UniProtKB	Modified residue	288	288	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P14680	UniProtKB	Modified residue	295	295	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358	
+P14680	UniProtKB	Modified residue	530	530	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10816418;Dbxref=PMID:17330950,PMID:19779198,PMID:10816418	
+##sequence-region P46683 1 200
+P46683	UniProtKB	Chain	1	200	.	.	.	ID=PRO_0000067079;Note=Ankyrin repeat-containing protein YAR1	
+P46683	UniProtKB	Repeat	49	78	.	.	.	Note=ANK 1	
+P46683	UniProtKB	Repeat	92	121	.	.	.	Note=ANK 2	
+P46683	UniProtKB	Modified residue	78	78	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P46683	UniProtKB	Sequence conflict	118	118	.	.	.	Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
+P46683	UniProtKB	Helix	10	22	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P46683	UniProtKB	Helix	25	34	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P46683	UniProtKB	Helix	38	43	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P46683	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P46683	UniProtKB	Helix	53	59	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P46683	UniProtKB	Helix	63	76	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P46683	UniProtKB	Helix	79	86	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P46683	UniProtKB	Helix	96	102	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P46683	UniProtKB	Helix	106	114	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P46683	UniProtKB	Helix	130	136	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+P46683	UniProtKB	Helix	140	149	.	.	.	Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ	
+##sequence-region Q3E794 1 53
+Q3E794	UniProtKB	Chain	1	53	.	.	.	ID=PRO_0000248435;Note=Uncharacterized protein YBR072C-A	
+##sequence-region P90471 1 74
+P90471	UniProtKB	Chain	1	74	.	.	.	ID=PRO_0000299793;Note=Putative uncharacterized protein YBR109W-A	
+P90471	UniProtKB	Transmembrane	15	32	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q6B113 1 34
+Q6B113	UniProtKB	Chain	1	34	.	.	.	ID=PRO_0000299791;Note=Putative uncharacterized protein YBL107W-A	
+##sequence-region Q12491 1 1770
+Q12491	UniProtKB	Chain	1	1770	.	.	.	ID=PRO_0000279270;Note=Transposon Ty2-B Gag-Pol polyprotein	
+Q12491	UniProtKB	Chain	1	397	.	.	.	ID=PRO_0000279271;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12491	UniProtKB	Chain	398	578	.	.	.	ID=PRO_0000279272;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12491	UniProtKB	Chain	579	1232	.	.	.	ID=PRO_0000279273;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12491	UniProtKB	Chain	1233	1770	.	.	.	ID=PRO_0000279274;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12491	UniProtKB	Domain	656	831	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12491	UniProtKB	Domain	1353	1491	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q12491	UniProtKB	Domain	1625	1767	.	.	.	Note=RNase H Ty1/copia-type	
+Q12491	UniProtKB	Region	295	397	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12491	UniProtKB	Region	579	636	.	.	.	Note=Integrase-type zinc finger-like	
+Q12491	UniProtKB	Motif	1193	1227	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12491	UniProtKB	Active site	457	457	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12491	UniProtKB	Metal binding	667	667	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12491	UniProtKB	Metal binding	732	732	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12491	UniProtKB	Metal binding	1361	1361	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12491	UniProtKB	Metal binding	1442	1442	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12491	UniProtKB	Metal binding	1443	1443	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12491	UniProtKB	Metal binding	1625	1625	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12491	UniProtKB	Metal binding	1667	1667	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12491	UniProtKB	Metal binding	1700	1700	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q12491	UniProtKB	Site	397	398	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12491	UniProtKB	Site	578	579	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q12491	UniProtKB	Site	1232	1233	.	.	.	Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38317 1 127
+P38317	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000202513;Note=Uncharacterized protein YBR219C	
+P38317	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38317	UniProtKB	Transmembrane	101	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38322 1 136
+P38322	UniProtKB	Chain	1	136	.	.	.	ID=PRO_0000202516;Note=Putative uncharacterized protein YBR226C	
+##sequence-region P38357 1 123
+P38357	UniProtKB	Chain	1	123	.	.	.	ID=PRO_0000202535;Note=Uncharacterized protein YBR292C	
+P38357	UniProtKB	Transmembrane	25	45	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38357	UniProtKB	Transmembrane	78	98	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38350 1 133
+P38350	UniProtKB	Chain	1	133	.	.	.	ID=PRO_0000202533;Note=Putative uncharacterized protein YBR277C	
+##sequence-region P38188 1 114
+P38188	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000202452;Note=Putative uncharacterized protein YBL065W	
+##sequence-region P38184 1 103
+P38184	UniProtKB	Chain	1	103	.	.	.	ID=PRO_0000202449;Note=Putative uncharacterized protein YBL073W	
+##sequence-region Q8TGQ1 1 68
+Q8TGQ1	UniProtKB	Chain	1	68	.	.	.	ID=PRO_0000299838;Note=Putative uncharacterized protein YCR047W-A	
+##sequence-region Q96VG6 1 88
+Q96VG6	UniProtKB	Chain	1	88	.	.	.	ID=PRO_0000299840;Note=Putative uncharacterized protein YCR097W-A	
+Q96VG6	UniProtKB	Transmembrane	27	46	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q96VG6	UniProtKB	Transmembrane	61	83	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PXB0 1 110
+A0A023PXB0	UniProtKB	Chain	1	110	.	.	.	ID=PRO_0000430970;Note=Putative uncharacterized protein YAR019W-A	
+##sequence-region O42831 1 157
+O42831	UniProtKB	Chain	1	157	.	.	.	ID=PRO_0000248413;Note=Putative inosine-5'-monophosphate dehydrogenase-like protein YAR075W	
+##sequence-region A0A023PYC6 1 104
+A0A023PYC6	UniProtKB	Signal peptide	1	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+A0A023PYC6	UniProtKB	Chain	26	104	.	.	.	ID=PRO_0000430975;Note=Putative uncharacterized membrane protein YAL016C-A	
+A0A023PYC6	UniProtKB	Transmembrane	79	99	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P39548 1 234
+P39548	UniProtKB	Chain	1	234	.	.	.	ID=PRO_0000207529;Note=DUP240 protein YAR028W	
+P39548	UniProtKB	Topological domain	1	47	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39548	UniProtKB	Transmembrane	48	68	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39548	UniProtKB	Topological domain	69	76	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39548	UniProtKB	Transmembrane	77	97	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39548	UniProtKB	Topological domain	98	234	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P39548	UniProtKB	Cross-link	217	217	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047	
+##sequence-region P0CX88 1 111
+P0CX88	UniProtKB	Chain	1	111	.	.	.	ID=PRO_0000202430;Note=Putative uncharacterized protein YAR060C	
+##sequence-region P0CI66 1 198
+P0CI66	UniProtKB	Chain	1	198	.	.	.	ID=PRO_0000202432;Note=Putative uncharacterized protein YAR062W	
+P0CI66	UniProtKB	Domain	1	110	.	.	.	Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164	
+P0CI66	UniProtKB	Compositional bias	133	198	.	.	.	Note=Ser/Thr-rich	
+##sequence-region P39564 1 161
+P39564	UniProtKB	Chain	1	161	.	.	.	ID=PRO_0000202434;Note=Uncharacterized protein YAR068W	
+##sequence-region P40917 1 295
+P40917	UniProtKB	Chain	1	295	.	.	.	ID=PRO_0000076524;Note=AP-1-like transcription factor YAP4	
+P40917	UniProtKB	Domain	237	295	.	.	.	Note=bZIP	
+P40917	UniProtKB	Region	239	260	.	.	.	Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40917	UniProtKB	Region	262	271	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P40917	UniProtKB	Modified residue	85	85	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40917	UniProtKB	Modified residue	89	89	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40917	UniProtKB	Modified residue	196	196	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P39710 1 102
+P39710	UniProtKB	Chain	1	102	.	.	.	ID=PRO_0000202426;Note=Putative uncharacterized protein YAL066W	
+##sequence-region Q3E821 1 79
+Q3E821	UniProtKB	Signal peptide	1	24	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E821	UniProtKB	Chain	25	79	.	.	.	ID=PRO_0000248434;Note=Uncharacterized protein YBL008W-A	
+Q3E821	UniProtKB	Glycosylation	33	33	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q3E7Y5 1 667
+Q3E7Y5	UniProtKB	Chain	1	667	.	.	.	ID=PRO_0000248406;Note=Uncharacterized helicase-like protein YBL111C	
+Q3E7Y5	UniProtKB	Domain	375	552	.	.	.	Note=Helicase ATP-binding	
+Q3E7Y5	UniProtKB	Nucleotide binding	388	395	.	.	.	Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E7Y5	UniProtKB	Motif	498	501	.	.	.	Note=DEAH box	
+##sequence-region Q8TGU7 1 68
+Q8TGU7	UniProtKB	Chain	1	68	.	.	.	ID=PRO_0000299747;Note=Uncharacterized protein YBR126W-A	
+Q8TGU7	UniProtKB	Transmembrane	24	44	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGQ5 1 29
+Q8TGQ5	UniProtKB	Chain	1	29	.	.	.	ID=PRO_0000299794;Note=Putative uncharacterized protein YBR131C-A	
+##sequence-region P0C5L5 1 24
+P0C5L5	UniProtKB	Chain	1	24	.	.	.	ID=PRO_0000309013;Note=Putative uncharacterized protein YBR191W-A	
+##sequence-region P0C268 1 59
+P0C268	UniProtKB	Chain	1	59	.	.	.	ID=PRO_0000268624;Note=Uncharacterized protein YBL039W-B	
+##sequence-region Q3E820 1 49
+Q3E820	UniProtKB	Chain	1	49	.	.	.	ID=PRO_0000248438;Note=Uncharacterized protein YBR196C-A	
+Q3E820	UniProtKB	Transmembrane	6	28	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38190 1 124
+P38190	UniProtKB	Chain	1	124	.	.	.	ID=PRO_0000202455;Note=Putative uncharacterized protein YBL053W	
+P38190	UniProtKB	Transmembrane	27	51	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38186 1 106
+P38186	UniProtKB	Chain	1	106	.	.	.	ID=PRO_0000202451;Note=Putative uncharacterized protein YBL070C	
+P38186	UniProtKB	Transmembrane	43	63	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+P38186	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38081 1 501
+P38081	UniProtKB	Chain	1	501	.	.	.	ID=PRO_0000184055;Note=Uncharacterized glycosyl hydrolase YBR056W	
+P38081	UniProtKB	Active site	236	236	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+P38081	UniProtKB	Active site	333	333	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+##sequence-region P38252 1 199
+P38252	UniProtKB	Chain	1	199	.	.	.	ID=PRO_0000202480;Note=Putative uncharacterized protein YBR089W	
+P38252	UniProtKB	Transmembrane	21	38	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P38258 1 127
+P38258	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000202484;Note=Putative uncharacterized protein YBR099C	
+P38258	UniProtKB	Transmembrane	84	103	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region P25572 1 119
+P25572	UniProtKB	Chain	1	119	.	.	.	ID=PRO_0000202545;Note=Putative uncharacterized protein YCL042W	
+##sequence-region Q12448 1 114
+Q12448	UniProtKB	Chain	1	114	.	.	.	ID=PRO_0000299849;Note=Putative uncharacterized protein YDL034W	
+##sequence-region Q3E6R4 1 66
+Q3E6R4	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E6R4	UniProtKB	Chain	19	42	.	.	.	ID=PRO_0000253883;Note=Uncharacterized protein YDR524C-B	
+Q3E6R4	UniProtKB	Propeptide	43	66	.	.	.	ID=PRO_0000253884;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E6R4	UniProtKB	Lipidation	42	42	.	.	.	Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E6R4	UniProtKB	Glycosylation	20	20	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E6R4	UniProtKB	Glycosylation	24	24	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E6R4	UniProtKB	Glycosylation	27	27	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E6R4	UniProtKB	Glycosylation	30	30	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+Q3E6R4	UniProtKB	Glycosylation	33	33	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region A0A023PZF2 1 135
+A0A023PZF2	UniProtKB	Chain	1	135	.	.	.	ID=PRO_0000430990;Note=Uncharacterized protein YEL009C-A	
+##sequence-region Q3E7B0 1 37
+Q3E7B0	UniProtKB	Chain	1	37	.	.	.	ID=PRO_0000245370;Note=Uncharacterized protein YER053C-A	
+Q3E7B0	UniProtKB	Transmembrane	1	21	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
+##sequence-region Q8TGR4 1 48
+Q8TGR4	UniProtKB	Chain	1	48	.	.	.	ID=PRO_0000299658;Note=Putative uncharacterized protein YER088W-B	
+##sequence-region Q03612 1 1755
+Q03612	UniProtKB	Chain	1	1755	.	.	.	ID=PRO_0000279043;Note=Transposon Ty1-ER1 Gag-Pol polyprotein	
+Q03612	UniProtKB	Chain	1	401	.	.	.	ID=PRO_0000279044;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03612	UniProtKB	Chain	402	582	.	.	.	ID=PRO_0000279045;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03612	UniProtKB	Chain	583	1217	.	.	.	ID=PRO_0000279046;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03612	UniProtKB	Chain	1218	1755	.	.	.	ID=PRO_0000279047;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03612	UniProtKB	Domain	660	835	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03612	UniProtKB	Domain	1338	1476	.	.	.	Note=Reverse transcriptase Ty1/copia-type	
+Q03612	UniProtKB	Domain	1610	1752	.	.	.	Note=RNase H Ty1/copia-type	
+Q03612	UniProtKB	Region	299	401	.	.	.	Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03612	UniProtKB	Region	583	640	.	.	.	Note=Integrase-type zinc finger-like	
+Q03612	UniProtKB	Motif	1178	1212	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03612	UniProtKB	Compositional bias	64	146	.	.	.	Note=Pro-rich	
+Q03612	UniProtKB	Active site	461	461	.	.	.	Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
+Q03612	UniProtKB	Metal binding	671	671	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03612	UniProtKB	Metal binding	736	736	.	.	.	Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03612	UniProtKB	Metal binding	1346	1346	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03612	UniProtKB	Metal binding	1427	1427	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03612	UniProtKB	Metal binding	1428	1428	.	.	.	Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03612	UniProtKB	Metal binding	1610	1610	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03612	UniProtKB	Metal binding	1652	1652	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03612	UniProtKB	Metal binding	1685	1685	.	.	.	Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457	
+Q03612	UniProtKB	Site	401	402	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03612	UniProtKB	Site	582	583	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03612	UniProtKB	Site	1217	1218	.	.	.	Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250	
+Q03612	UniProtKB	Modified residue	416	416	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231	
+##sequence-region P40103 1 239
+P40103	UniProtKB	Chain	1	239	.	.	.	ID=PRO_0000202664;Note=Uncharacterized protein YER188W	
+##sequence-region P40104 1 122
+P40104	UniProtKB	Chain	1	122	.	.	.	ID=PRO_0000202665;Note=Uncharacterized protein YER189W	
+##sequence-region P32622 1 495
+P32622	UniProtKB	Chain	1	495	.	.	.	ID=PRO_0000120717;Note=ATP-NADH kinase YEF1	
+##sequence-region P40052 1 210
+P40052	UniProtKB	Chain	1	210	.	.	.	ID=PRO_0000202636;Note=Uncharacterized protein YER079W	
+P40052	UniProtKB	Modified residue	18	18	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40052	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
+P40052	UniProtKB	Modified residue	41	41	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40052	UniProtKB	Modified residue	57	57	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377	
+P40052	UniProtKB	Modified residue	60	60	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950	
+P40052	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+P40052	UniProtKB	Modified residue	189	189	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956	
+P40052	UniProtKB	Modified residue	192	192	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198	
+##sequence-region P40560 1 513
+P40560	UniProtKB	Chain	1	513	.	.	.	ID=PRO_0000067246;Note=Ankyrin repeat-containing protein YIL001W	
+P40560	UniProtKB	Repeat	8	37	.	.	.	Note=ANK 1	
+P40560	UniProtKB	Repeat	41	70	.	.	.	Note=ANK 2	
+P40560	UniProtKB	Domain	122	179	.	.	.	Note=BTB 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00037	
+P40560	UniProtKB	Domain	274	360	.	.	.	Note=BTB 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00037	
+##sequence-region P40536 1 118
+P40536	UniProtKB	Chain	1	118	.	.	.	ID=PRO_0000202995;Note=Putative uncharacterized protein YIL032C	
+##sequence-region E2QC18 1 100
+##sequence-region E9PAE8 1 55
+##sequence-region E9PAE4 1 146
+E9PAE4	UniProtKB	Transmembrane	31	55	.	.	.	Note=Helical;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:Phobius	
+##sequence-region E9PAD8 1 89
+E9PAD8	UniProtKB	Transmembrane	64	84	.	.	.	Note=Helical;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:Phobius	
+##sequence-region E9PAE3 1 403
+E9PAE3	UniProtKB	Domain	233	403	.	.	.	Note=Integrase catalytic;Ontology_term=ECO:0000259;evidence=ECO:0000259|PROSITE:PS50994	
+##sequence-region E9PAE7 1 61
+##sequence-region E9PAD6 1 88
+E9PAD6	UniProtKB	Transmembrane	6	32	.	.	.	Note=Helical;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:Phobius	
+E9PAD6	UniProtKB	Transmembrane	52	72	.	.	.	Note=Helical;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:Phobius	
+##sequence-region E9PAF1 1 94
diff --git a/test_files/yeastID.txt b/test_files/yeastID.txt
new file mode 100644
index 0000000..7bd016d
--- /dev/null
+++ b/test_files/yeastID.txt
@@ -0,0 +1,6730 @@
+Entry	Gene names  (ordered locus )	Gene names  (primary )
+P12688	YKL126W	YPK1
+P25491	YNL064C	YDJ1
+P16521	YLR249W	YEF3
+P11484	YDL229W	SSB1
+P39940	YER125W	RSP5
+Q04437	YMR106C	YKU80
+Q06224	YLR277C	YSH1
+P32795	YPR024W	YME1
+Q06102	YPR107C	YTH1
+P02829	YPL240C	HSP82
+P38801	YHR081W	LRP1
+P40009	YER005W	YND1
+P10591	YAL005C	SSA1
+P38340	YBR261C	TAE1
+P41800	YLL006W	MMM1
+P00546	YBR160W	CDC28
+P15108	YMR186W	HSC82
+P31539	YLL026W	HSP104
+P25623	YCR030C	SYP1
+P08539	YHR005C	GPA1
+P32502	YLR291C	GCD7
+P15442	YDR283C	GCN2
+P10592	YLL024C	SSA2
+P06782	YDR477W	SNF1
+P22147	YGL173C	XRN1
+P32598	YER133W	GLC7
+P53230	YGR046W	TAM41
+Q06510	YPR140W	TAZ1
+Q02457	YPL128C	TBF1
+P39078	YDL143W	CCT4
+Q3E7C1	YDR079C-A	TFB5
+Q06339	YDR362C	TFC6
+Q12308	YPL007C	TFC8
+Q06490	YPR121W	THI22
+Q04083	YDR438W	THI74
+P35202	YOR143C	THI80
+Q08231	YOL072W	THP1
+P16120	YCR053W	THR4
+P40328	YPL074W	YTA6
+P39077	YJL014W	CCT3
+P35691	YKL056C	TMA19
+P38987	YML064C	TEM1
+P53916	YNL128W	TEP1
+P29055	YPR086W	SUA7
+P29056	YGR246C	BRF1
+P38141	YBR240C	THI2
+P32318	YGR144W	THI4
+P32897	YNR017W	TIM23
+Q08144	YOL018C	TLG2
+P07273	YGL043W	DST1
+P54857	YDR058C	TGL2
+Q12052	YPL157W	TGS1
+P00927	YER086W	ILV1
+P41338	YPL028W	ERG10
+P57744	YJR135W-A	TIM8
+O74700	YEL020W-A	TIM9
+Q12218	YOR009W	TIR4
+Q04562	YDR107C	TMN2
+P53507	YNL070W	TOM7
+Q07904	YLR004C	THI73
+Q05998	YLR237W	THI7
+P40040	YER063W	THO1
+P53552	YNL139C	THO2
+O13539	YHR167W	THP2
+Q07914	YLR008C	PAM18
+P39515	YJL143W	TIM17
+Q01852	YIL022W	TIM44
+P27654	YBR067C	TIP1
+P10863	YER011W	TIR1
+P54837	YML012W	ERV25
+P32802	YLR083C	EMP70
+Q06417	YLR426W	TDA5
+Q03290	YDR460W	TFB3
+P46678	YNL039W	BDP1
+Q12415	YOR110W	TFC7
+P40308	YMR313C	TGL3
+P42883	YNL332W	THI12
+Q08224	YOL055C	THI20
+P40340	YGR270W	YTA7
+P38228	YBR044C	TCM62
+Q08921	YPL180W	TCO89
+P32776	YDR311W	TFB1
+P33339	YGR047C	TFC4
+Q08686	YOR251C	TUM1
+P42949	YJL104W	PAM16
+Q12328	YDL217C	TIM22
+P33315	YBR117C	TKL2
+Q12239	YOL107W	
+Q03525	YMR269W	TMA23
+Q04600	YDR117C	TMA64
+P36165	YKR089C	TGL4
+P47183	YJR156C	THI11
+Q07471	YDL080C	THI3
+P43534	YFL058W	THI5
+P41835	YPL214C	THI6
+P27796	YIL160C	POT1
+P87108	YHR005C-A	TIM10
+P33891	YGL145W	TIP20
+P89886	YER007C-A	TMA20
+Q12049	YPR045C	THP3
+P40462	YIL137C	TMA108
+P36142	YKR051W	
+Q12513	YDL110C	TMA17
+P53840	YNL273W	TOF1
+P40310	YJL093C	TOK1
+Q03280	YDR457W	TOM1
+P35180	YGR082W	TOM20
+P23644	YMR203W	TOM40
+P80967	YPR133W-A	TOM5
+P38825	YHR117W	TOM71
+P32830	YBR091C	TIM12
+P53299	YGR181W	TIM13
+Q08749	YOR297C	TIM18
+P53220	YGR033C	TIM21
+P33890	YOR010C	TIR2
+Q08422	YOR052C	TMC1
+P40071	YER113C	TMN3
+P32773	YOR194C	TOA1
+P04786	YOL006C	TOP1
+P06786	YNL088W	TOP2
+P35169	YJR066W	TOR1
+P53147	YGL096W	TOS8
+Q12272	YOL102C	TPT1
+Q06177	YLR327C	TMA10
+Q12116	YDR105C	TMS1
+P13099	YLR234W	TOP3
+P49334	YNL131W	TOM22
+P38288	YBR162C	TOS1
+P43637	YGL179C	TOS3
+Q03796	YMR156C	TPP1
+P53738	YNR046W	TRM112
+P12685	YJL129C	TRK1
+Q12400	YOL093W	TRM10
+Q12463	YOL124C	TRM11
+P15565	YDR120C	TRM1
+Q02648	YPL030W	TRM44
+P41814	YNL062C	GCD10
+Q08687	YOR252W	TMA16
+Q3E764	YLR262C-A	TMA7
+P32643	YER175C	TMT1
+P32600	YKL203C	TOR2
+P17536	YNL079C	TPM1
+P53099	YGL186C	TPN1
+P53283	YGR138C	TPO2
+Q12256	YOR273C	TPO4
+Q03496	YMR259C	TRM732
+Q05024	YMR233W	TRI1
+P33753	YKR056W	TRM2
+P38793	YHR070W	TRM5
+P09880	YJL087C	TRL1
+P46944	YDR108W	TRS85
+P22217	YLR043C	TRX1
+P34760	YML028W	TSA1
+P40061	YER093C	TSC11
+Q02776	YPL063W	TIM50
+P40552	YIL011W	TIR3
+Q12000	YOR091W	TMA46
+Q06266	YLR183C	TOS4
+Q07824	YLL028W	TPO1
+P47045	YJL054W	TIM54
+Q12199	YPR040W	TIP41
+P23254	YPR074C	TKL1
+Q03322	YDR468C	TLG1
+P53322	YGR260W	TNA1
+Q08919	YPL176C	TRE1
+Q03774	YDR165W	TRM82
+P38334	YBR254C	TRS20
+P32893	YGR166W	TRS65
+Q02208	YKR010C	TOF2
+P07213	YNL121C	TOM70
+P48560	YNL300W	TOS6
+P00942	YDR050C	TPI1
+P40414	YIL138C	TPM2
+Q06451	YPR156C	TPO3
+P36029	YKL174C	TPO5
+Q04183	YDR407C	TRS120
+Q03660	YMR218C	TRS130
+P38342	YBR265W	TSC10
+P38427	YML100W	TSL1
+P50078	YGR221C	TOS2
+P53257	YGR096W	TPC1
+Q00764	YBR126C	TPS1
+P35172	YBR001C	NTH2
+Q07527	YDL112W	TRM3
+Q02721	YLR329W	REC102
+P34219	YBL054W	TOD6
+P33448	YOR045W	TOM6
+P38811	YHR099W	TRA1
+Q08693	YOR256C	TRE2
+P48561	YNL299W	TRF5
+P28584	YKR050W	TRK2
+Q12383	YOL125W	TRM13
+P25040	YOL022C	TSR4
+P36164	YKR088C	TVP38
+P33122	YOR344C	TYE7
+P06785	YOR074C	CDC21
+P0CF16	YML003W	
+P21734	YDR177W	UBC1
+P33296	YER100W	UBC6
+P36026	YKR098C	UBP11
+P38237	YBR058C	UBP14
+P32571	YDR069C	DOA4
+P40453	YIL156W	UBP7
+P19812	YGR184C	UBR1
+Q07963	YLR024C	UBR2
+Q04228	YML013W	UBX2
+Q06682	YDR330W	UBX5
+Q03337	YDR472W	TRS31
+Q07381	YDL060W	TSR1
+P20049	YBR166C	TYR1
+P07285	YDR354W	TRP4
+Q03784	YDR246W	TRS23
+P25372	YCR083W	TRX3
+P29509	YDR353W	TRR1
+P47168	YJR136C	TTI2
+P38962	YDR084C	TVP23
+P22803	YGR209C	TRX2
+P38254	YBR094W	PBY1
+P29340	YGR133W	PEX4
+Q12094	YOR006C	TSR3
+Q08747	YOR295W	UAF30
+P14682	YDR054C	CDC34
+P40032	YER049W	TPA1
+P31688	YDR074W	TPS2
+P38426	YMR261C	TPS3
+P46959	YJL125C	GCD14
+P38238	YBR061C	TRM7
+P49957	YML014W	TRM9
+Q12009	YDL201W	TRM8
+P00912	YDR007W	TRP1
+Q03860	YDR100W	TVP15
+P53250	YGR080W	TWF1
+P00899	YER090W	TRP2
+P00937	YKL211C	TRP3
+P00931	YGL026C	TRP5
+Q3E790	YBR058C-A	TSC3
+Q04767	YMR071C	TVP18
+Q99394	YOR115C	TRS33
+Q04120	YDR453C	TSA2
+Q06672	YLR435W	TSR2
+P36097	YKL033W	TTI1
+P16649	YCR084C	TUP1
+P32356	YDR001C	NTH1
+P38816	YHR106W	TRR2
+P53044	YGR048W	UFD1
+P33202	YKL010C	UFD4
+P26370	YDL170W	UGA3
+P36137	YKR044W	UIP5
+Q02724	YPL020C	ULP1
+Q05776	YLR193C	UPS1
+P28274	YBL039C	URA7
+P38627	YJR103W	URA8
+Q05946	YLR222C	UTP13
+Q04305	YMR093W	UTP15
+P40362	YJL069C	UTP18
+P35194	YBL004W	UTP20
+P40498	YIL091C	UTP25
+Q02354	YDR449C	UTP6
+Q08474	YOR068C	VAM10
+P16140	YBR127C	VMA2
+P38358	YBR293W	VBA2
+Q04602	YDR119W	VBA4
+P39538	YJL197W	UBP12
+Q01477	YER151C	UBP3
+P39967	YER098W	UBP9
+Q12229	YDL091C	UBX3
+P47049	YJL048C	UBX6
+P40554	YIL008W	URM1
+Q04500	YML093W	UTP14
+Q12339	YOR004W	UTP23
+P43123	YDL103C	QRI1
+P52490	YDR092W	UBC13
+Q02159	YMR022W	UBC7
+Q12059	YPL003W	ULA1
+Q08562	YOR191W	ULS1
+Q03010	YPL139C	UME1
+P25386	YDL058W	USO1
+P42945	YJL109C	UTP10
+Q06078	YLR409C	UTP21
+P53254	YGR090W	UTP22
+Q04177	YDR398W	UTP5
+P53276	YGR128C	UTP8
+P21373	YJR049C	UTR1
+P35127	YJR099W	YUH1
+Q01476	YOR124C	UBP2
+P43593	YFR010W	UBP6
+P50102	YMR223W	UBP8
+P54730	YMR067C	UBX4
+P36135	YKR042W	UTH1
+Q12220	YLR129W	DIP2
+Q06679	YDR324C	UTP4
+P38882	YHR196W	UTP9
+P25591	YCL063W	VAC17
+Q07468	YDL077C	VAM6
+P17255	YDL185W	VMA1
+P38152	YBR291C	CTP1
+Q04235	YML005W	TRM12
+P06104	YGL058W	RAD6
+P39944	YER144C	UBP5
+P38349	YBR273C	UBX7
+P47108	YJR041C	URB2
+P53146	YGL098W	USE1
+P53177	YGL050W	TYW3
+P22515	YKL210W	UBA1
+Q99344	YPR066W	UBA3
+P52492	YOR339C	UBC11
+P52491	YLR306W	UBC12
+P15732	YDR059C	UBC5
+P38187	YBL067C	UBP13
+P25037	YDL122W	UBP1
+P38290	YBR165W	UBS1
+P32861	YKL035W	UGP1
+P38709	YHL012W	
+P38293	YBR173C	UMP1
+Q08960	YPL207W	TYW1
+Q08282	YOL141W	PPM2
+P38820	YHR111W	UBA4
+P15731	YBR082C	UBC4
+P28263	YEL012W	UBC8
+P34223	YBL058W	SHP1
+Q04511	YML088W	UFO1
+P40537	YIL031W	ULP2
+Q12151	YDR213W	UPC2
+P36096	YKL034W	TUL1
+Q06412	YLR425W	TUS1
+P38319	YBR223C	TDP1
+P53874	YNL186W	UBP10
+P08067	YEL024W	RIP1
+P41834	YOR075W	UFE1
+P0CF17	YML002W	
+P52488	YDR390C	UBA2
+P50623	YDL064W	UBC9
+P0CG63	YLL039C	UBI4
+P50101	YMR304W	UBP15
+Q02863	YPL072W	UBP16
+P32837	YDL210W	UGA4
+Q03327	YDR470C	UGO1
+P39547	YAR027W	UIP3
+Q04006	YDR185C	UPS3
+P12887	YML021C	UNG1
+P18562	YHR128W	FUR1
+Q04411	YDR520C	URC2
+P27515	YNR012W	URK1
+P32366	YLR447C	VMA6
+P40003	YEL005C	VAB2
+Q06708	YLR386W	VAC14
+Q99385	YDL128W	VCX1
+P53058	YGL258W	VEL1
+P54860	YDL190C	UFD2
+P32772	YDL169C	UGX2
+Q08926	YPL186C	UIP4
+P43604	YFR026C	ULI1
+P39001	YDR207C	UME6
+P48412	YGR072W	UPF3
+P35200	YLR168C	UPS2
+Q12208	YLR132C	USB1
+P34247	YKL099C	UTP11
+Q02931	YPL126W	NAN1
+P40055	YER082C	UTP7
+P32630	YEL035C	UTR5
+P39111	YGR020C	VMA7
+Q12063	YDL193W	NUS1
+P34241	YKL014C	URB1
+P23202	YNL229C	URE2
+Q03714	YML029W	USA1
+P41807	YPR036W	VMA13
+P25515	YEL027W	VMA3
+P36172	YKR105C	VBA5
+P04840	YNL055C	POR1
+P40157	YNL212W	VID27
+Q06685	YLR410W	VIP1
+Q04311	YDR049W	VMS1
+P38067	YBR006W	UGA2
+Q04179	YDR400W	URH1
+Q3E7B6	YCL005W-A	VMA9
+P39968	YEL013W	VAC8
+P32912	YGL212W	VAM7
+Q05934	YLR373C	VID22
+Q12241	YOR106W	VAM3
+P23642	YML115C	VAN1
+P32610	YEL051W	VMA8
+P48836	YHR039C-A	VMA10
+P32319	YBL017C	PEP1
+P32913	YOR132W	VPS17
+Q04272	YMR077C	VPS20
+Q05919	YLR360W	VPS38
+P39702	YAL002W	VPS8
+P32842	YPL234C	VMA11
+P38329	YBR235W	VHC1
+P40522	YIL056W	VHR1
+Q08438	YOR054C	VHS3
+P53285	YGR141W	VPS62
+P53142	YGL104C	VPS73
+Q06525	YPR152C	URN1
+Q12132	YPL230W	USV1
+P53950	YNL054W	VAC7
+P40041	YER064C	VHR2
+P23968	YHR026W	VMA16
+P40478	YIL114C	POR2
+O13549	YLR261C	VPS63
+P47161	YJR126C	VPS70
+P37370	YLR337C	VRP1
+Q03631	YML076C	WAR1
+P31412	YKL080W	VMA5
+P22203	YOR332W	VMA4
+Q04301	YMR088C	VBA1
+P25594	YCL069W	VBA3
+Q03785	YDR247W	VHS1
+P53262	YGR106C	VOA1
+P32563	YOR270C	VPH1
+P47142	YJR102C	VPS25
+P38959	YDR080W	VPS41
+P38932	YGL095C	VPS45
+Q12071	YDR027C	VPS54
+P47111	YJR044C	VPS55
+Q12016	YOL129W	VPS68
+Q06385	YDR372C	VPS74
+Q07655	YDL224C	WHI4
+P40080	YER128W	VFA1
+P41806	YGR105W	VMA21
+P42839	YNL321W	VNX1
+P39904	YDR484W	VPS52
+Q03913	YDR136C	VPS61
+Q03433	YML041C	VPS71
+P54787	YML097C	VPS9
+Q06263	YLR181C	VTA1
+P47165	YJR133W	XPT1
+P53076	YGL227W	VID30
+P22219	YBR097W	VPS15
+P21576	YKR001C	VPS1
+Q02767	YPL065W	VPS28
+P22543	YLR240W	VPS34
+Q06696	YLR417W	VPS36
+Q92331	YOR069W	VPS5
+Q04338	YMR197C	VTI1
+P40151	YNL218W	MGS1
+P39102	YLR090W	XDJ1
+P38759	YHR012W	VPS29
+O13584	YPR087W	VPS69
+P40438	YIL173W	VTH1
+P40890	YJL222W	VTH2
+Q08831	YOR359W	VTS1
+P12611	YOR043W	WHI2
+P34761	YNL197C	WHI3
+P40463	YIL135C	VHS2
+Q12045	YPL253C	VIK1
+P32341	YKL119C	VPH2
+Q07878	YLL040C	VPS13
+Q03390	YDR486C	VPS60
+P53853	YNL246W	VPS75
+Q12215	YOL105C	WSC3
+Q03944	YDR200C	VPS64
+Q08924	YPL183C	RTT10
+P38739	YHL028W	WSC4
+P43582	YFL010C	WWM1
+P40489	YIL101C	XBP1
+Q07993	YLR070C	XYL2
+P53241	YGR065C	VHT1
+P40547	YIL017C	VID28
+P38784	YHR060W	VMA22
+P38735	YHL035C	VMR1
+P20795	YLR396C	VPS33
+P34110	YJL154C	VPS35
+P23643	YDR495C	VPS3
+P52917	YPR173C	VPS4
+Q02725	YPL019C	VTC3
+P47075	YJL012C	VTC4
+Q12416	YOR083W	WHI5
+P38838	YHR134W	WSS1
+Q12363	YOR230W	WTM1
+P36095	YKL041W	VPS24
+P40343	YNR006W	VPS27
+P36116	YKR020W	VPS51
+P47061	YJL029C	VPS53
+O13554	YLR322W	VPS65
+Q03388	YDR485C	VPS72
+P40046	YER072W	VTC1
+P43585	YFL004W	VTC2
+P53832	YNL283C	WSC2
+P33418	YKL205W	LOS1
+Q12206	YOR229W	WTM2
+P42826	YGR194C	XKS1
+P33301	YDR369C	XRS2
+Q02792	YOR048C	RAT1
+P30822	YGR218W	CRM1
+Q03308	YPL045W	VPS16
+P36017	YOR089C	VPS21
+Q03897	YDR128W	MTC5
+P38189	YBL062W	
+P38216	YBR016W	
+P38239	YBR062C	
+P38243	YBR071W	
+P32386	YLL048C	YBT1
+P38109	YBR139W	
+Q96VG8	YCR038W-A	
+P25383	YCL020W	TY2A-C
+P25349	YCR004C	YCP4
+P25617	YCR016W	
+P25351	YCR023C	
+P25361	YCR043C	
+P25639	YCR061W	
+Q12489	YDL012C	
+Q03205	YDR042C	
+Q07438	YDL071C	
+Q03193	YDR090C	
+Q07589	YDL144C	
+P0C2I2	YDR316W-B	TY1B-DR5
+Q12307	YDL162C	
+Q12257	YDL177C	
+P48569	YDL183C	
+Q03482	YDR210W	
+Q12472	YDR034C-D	TY2B-DR1
+Q03780	YDR239C	
+P0C5L8	YDL240C-A	
+Q03788	YDR250C	
+Q8TGP6	YDR354C-A	
+Q04069	YDR431W	
+P87273	YDR521W	
+A0A023PZE8	YDR157W	
+Q2V2P8	YDR374W-A	
+Q02217	YEL034C-A	
+P40102	YER187W	
+P40001	YEL008W	
+P34225	YBL060W	YEL1
+P40062	YER097W	
+Q04210	YMR040W	YET2
+A0A023PZD0	YFR036W-A	
+P43576	YFL019C	
+P43539	YFL065C	
+P43537	YFL067W	
+P43590	YFR006W	
+P43591	YFR007W	YFH7
+Q03186	YFL012W-A	
+Q8TGP0	YGL063C-A	
+Q3E816	YGR121W-A	
+Q3E744	YGR161W-C	
+P0CX96	YGR296C-B	
+P53265	YGR111W	
+P53270	YGR117C	
+P53273	YGR125W	
+P48236	YGR149W	
+P42942	YGR210C	
+P53321	YGR259C	
+P53340	YGR291C	
+Q8TGT4	YHR213W-A	
+P0CX91	YHR212W-A	
+P0C5N4	YHR073C-B	
+P38750	YHL008C	
+P38726	YHL045W	
+P38708	YHR020W	
+P38763	YHR022C	
+P38780	YHR054C	
+P38808	YHR095W	
+P38716	YHR112C	
+P38835	YHR131C	
+P38864	YHR173C	
+P40514	YIL067C	
+P40500	YIL089W	
+P40490	YIL100W	
+P40461	YIL141W	
+P40588	YIR044C	
+Q3E827	YJR005C-A	
+Q8TGN2	YJL020W-A	
+Q3E737	YJL047C-A	
+P47106	YJR038C	
+Q3E743	YJR112W-A	
+Q3E7A3	YJL133C-A	
+P47131	YJR085C	
+P47059	YJL032W	
+P46991	YJL175W	
+P39541	YJL195C	
+P39529	YJL206C	
+P36074	YKL111C	
+P36050	YKL169C	
+P34238	YKL177W	
+P34231	YKL187C	
+Q07978	YLR031W	
+Q07986	YLR036C	
+Q07988	YLR040C	
+Q8TGR1	YLR120W-A	
+Q12088	YLR035C-A	TY1B-LR1
+Q04501	YML090W	
+Q03675	YMR007W	
+Q03687	YMR010W	
+Q05131	YMR034C	
+Q04276	YMR082C	
+Q04299	YMR087W	
+Q03177	YMR102C	
+P53846	YNL260C	
+P53842	YNL266W	
+Q3E7A8	YNL162W-A	
+P53825	YNL324W	
+P53964	YNL033W	
+Q08216	YOL046C	
+Q08448	YOR059C	
+Q08238	YOL079W	
+Q99247	YOL087C	
+Q12496	YOL098C	
+Q92393	YOR142W-B	TY1B-OR
+Q3E7A5	YOL164W-A	
+Q08634	YOR238W	
+O14468	YOR304C-A	
+P0C5R1	YOR329W-A	
+Q12182	YOR342C	
+Q08844	YOR365C	
+P0C5R4	YOL083C-A	
+P53049	YGR281W	YOR1
+Q12486	YOR131C	
+Q12251	YPR011C	
+Q12079	YPR027C	
+Q6Q5F3	YPR053C	
+Q12194	YPL066W	
+Q02864	YPL071C	
+O13585	YPR089W	
+Q06089	YPR098C	
+Q3E751	YPL119C-A	
+O13566	YPR123C	
+O13568	YPR130C	
+P0C2J0	YPR158W-B	TY1B-PR2
+Q06537	YPR153W	
+O13575	YPR177C	
+P0C5R9	YPR170W-B	
+P18961	YMR104C	YPK2
+P32939	YML001W	YPT7
+P36036	YKL214C	YRA2
+P38079	YBR054W	YRO2
+P39703	YAL004W	
+P38215	YBR013C	
+P38223	YBR032W	
+P38277	YBR138C	
+Q96VH3	YCL021W-A	
+Q2V2Q2	YCL048W-A	
+P39109	YDR135C	YCF1
+P37264	YCL065W	
+Q12316	YGR161C-D	TY1B-GR3
+P53227	YGR042W	
+Q8TGT7	YGR204C-A	
+P53234	YGR053C	
+P0CX64	YGR161W-B	TY2B-GR2
+P48238	YGR153W	
+Q3E750	YGL041C-B	
+P53302	YGR190C	
+P50083	YGR226C	
+P53326	YGR266W	
+P53162	YGL069C	
+P53161	YGL072C	
+Q12222	YOL128C	YGK3
+P53113	YGL152C	
+P53106	YGL165C	
+P46945	YGL176C	
+P53098	YGL188C	
+P53087	YGL214W	
+P53069	YGL239C	
+P53056	YGL260W	
+Q8TGT6	YHR022C-A	
+A0A023PZH9	YHL034W-A	
+Q3E746	YHR086W-A	
+P38893	YHR210C	
+Q8TGN6	YHR137C-A	
+P38898	YHR217C	
+P38900	YHR219W	
+A0A023PXF5	YHR218W-A	
+P38752	YHL005C	
+P38733	YHL037C	
+A0A023PYH8	YIL047C-A	
+Q8TGN4	YIL021C-A	
+A0A023PZK4	YIR030W-A	
+Q99219	YIL082W	TY3A-I
+P53845	YNL263C	YIF1
+P40440	YIL171W	
+P40570	YIR014W	
+P40575	YIR020C	
+P40579	YIR035C	
+P40584	YIR040C	
+P47101	YJR030C	
+Q8TGJ8	YJL026C-A	
+Q3E837	YJL052C-A	
+P0CT86	YJR107C-A	
+P47098	YJR027W	TY1B-JR1
+P47137	YJR096W	
+Q8TGT3	YJL077W-B	
+P47173	YJR142W	
+P47080	YJL007C	
+P47073	YJL015C	
+P47072	YJL016W	
+P47048	YJL049W	
+P47044	YJL055W	
+P47004	YJL150W	
+P36127	YKR032W	
+P0C5P5	YKL165C-A	
+P36158	YKR078W	
+P36103	YKL023W	
+P35733	YKL053W	
+P36089	YKL066W	
+P36081	YKL077W	
+P34245	YKL097C	
+P36067	YKL131W	
+P36015	YKL196C	YKT6
+P36111	YKR015C	
+P0CF00	YLR157W-E	
+P0CY01	YLL067W-A	
+P0C5Q2	YMR013W-A	
+Q6Q572	YMR031W-A	
+A0A023PZG9	YML047W-A	
+Q6B0Y6	YMR052C-A	
+Q12744	YML094C-A	
+Q3E7B5	YMR230W-A	
+Q04909	YMR324C	
+Q04526	YML083C	
+P0CL35	YML133W-B	
+P03881	Q0255	
+Q04674	YMR057C	
+Q8TGL7	YNR003W-A	
+Q3E7Z2	YNL042W-B	
+Q8TGQ9	YNL103W-A	
+Q8TGL9	YNL144W-A	
+P53737	YNR042W	
+P53748	YNR062C	
+P53976	YNL018C	
+P53963	YNL034W	
+P53952	YNL050C	
+P0CL36	YNL339W-B	
+P53925	YNL115C	
+P53908	YNL143C	
+P53880	YNL179C	
+P53856	YNL235C	
+Q3E807	YOR011W-A	
+Q08205	YOL037C	
+P36025	YOR062C	
+Q08234	YOL075C	
+Q3E7B9	YOR008C-A	
+Q12275	YOR093C	
+P0C272	YOL013W-A	
+Q3E7Y8	YOL155W-A	
+P0CF19	YOL162W	
+Q8TGS2	YOL019W-A	
+Q12282	YOR214C	
+Q12225	YOR225W	
+Q08681	YOR248W	
+Q08736	YOR277C	
+Q12040	YOR283W	
+Q12261	YOR325W	
+Q99326	YOR338W	
+Q08872	YOR366W	
+Q08903	YOR379C	
+Q06328	YDR352W	YPQ2
+P40583	YIR039C	YPS6
+P48559	YNL304W	YPT11
+P51996	YGL210W	YPT32
+P40517	YIL063C	YRB2
+P38374	YBR162W-A	YSY6
+P50111	YMR273C	ZDS1
+P25620	YCR022C	
+P25352	YCR025C	
+P25640	YCR064C	
+Q12264	YDL023C	
+Q07355	YDL050C	
+Q12298	YDR061W	
+Q8TGP8	YDL086C-A	
+Q03864	YDR102C	
+Q07535	YDL118W	
+Q07555	YDL129W	
+Q03900	YDR132C	
+P0CX65	YDR316W-A	TY1A-DR5
+Q3E774	YDL159W-A	
+Q12135	YDL172C	
+Q12301	YDL180W	
+Q8TGR6	YDR524C-A	
+Q6Q5X2	YDR034W-B	
+Q04170	YDR391C	
+P87269	YDR433W	
+Q04100	YDR445C	
+Q04434	YDR535C	
+Q03051	YDR543C	
+Q04585	YDR109C	
+Q3E7X8	YEL077C	
+P0C5M8	YER090C-A	
+A0A023PZG5	YER137W-A	
+A0A023PXK2	YER148W-A	
+P39992	YEL023C	
+P32616	YEL045C	
+Q07804	YLL012W	YEH1
+P0CX61	YFL002W-B	TY2A-F
+Q45U48	YGR035W-A	
+Q2V2P6	YGL194C-A	
+P53225	YGR039W	
+P0C2J2	YGR038C-E	TY2A-GR1
+Q3E786	YGR240C-A	
+P53242	YGR066C	
+P53268	YGR114C	
+Q99315	YGR109W-B	TY3B-G
+P53278	YGR130C	
+P0C5N3	YGL041W-A	
+P42936	YGR201C	
+P53310	YGR242W	
+P40326	YGR269W	
+P53156	YGL081W	
+P53143	YGL102C	
+P53071	YGL235W	
+A0A023PXE5	YHL006W-A	
+O13535	YHR214C-B	TY1B-H
+Q05451	YHR050W-A	
+P38809	YHR097C	
+P38834	YHR130C	
+P38841	YHR138C	
+P0CI67	YHR213W	
+Q3E7Z3	YIR018C-A	
+Q3E739	YIR021W-A	
+Q03884	YIL100C-A	
+P0CL42	YJL225W-A	
+P0CL25	YIL174W	
+P40566	YIR007W	
+P40572	YIR016W	
+P40586	YIR042C	
+P47100	YJR029W	TY1B-JR2
+P0CL41	YIL177W-A	
+P47139	YJR098C	
+P47145	YJR107W	
+P47148	YJR111C	
+P47172	YJR141W	
+P47184	YJR157W	
+P47022	YJL118W	
+P47020	YJL120W	
+P47014	YJL132W	
+P47085	YJR008W	
+P47090	YJR015W	
+Q3E826	YKL068W-A	
+P36140	YKR047W	
+P36153	YKR073C	
+P36099	YKL030W	
+P36087	YKL070W	
+P36079	YKL083W	
+P36030	YKL225W	
+P36109	YKR012C	
+Q07895	YLR001C	
+Q07927	YLR012C	
+P0CF33	YLL017W	
+Q07967	YLR030W	
+Q07834	YLL032C	
+Q12110	YLR049C	
+Q12244	YLL054C	
+Q99208	YLL066C	
+P0CX68	YLR035C-B	TY1A-LR1
+Q12138	YLR125W	
+P0CE96	YLR156W	
+O13531	YLR202C	
+Q05948	YLR225C	
+A0A023PXG7	YLR230W	
+A0A023PXP4	YLR235C	
+O13574	YLR255C	
+Q06146	YLR257W	
+Q06152	YLR271W	
+O13540	YLR279W	
+Q3E810	YLR342W-A	
+Q06137	YLR345W	
+Q7LIF2	YLR365W	
+O13545	YLR374C	
+Q8TGT1	YLR406C-A	
+Q06204	YLR446W	
+O13557	YLR463C	
+P0CY00	YLL066W-A	
+P0CL39	YLR467C-A	
+Q8TGS9	YMR001C-A	
+Q6B0Y1	YML009W-B	
+A0A023PXP7	YML034C-A	
+Q6B0Y7	YMR075C-A	
+Q8TGT0	YML100W-A	
+Q04214	YMR045C	TY1B-MR1
+Q6B0R2	YMR193C-A	
+Q04304	YMR090W	
+Q3E841	YNR034W-A	
+P53837	YNL276C	
+P53729	YNR029C	
+P53751	YNR065C	
+P53754	YNR068C	
+P53757	YNR071C	
+P53977	YNL017C	
+P53962	YNL035C	
+P0CL30	YNL339W-A	
+P53921	YNL122C	
+Q08207	YOL035C	
+Q08439	YOR055W	
+Q08240	YOL099C	
+Q12322	YOL114C	
+P0CX59	YOR142W-A	TY1A-OR
+Q08272	YOL134C	
+Q03080	YPL039W	
+P0C5E1	YPR059C	
+Q02749	YPL068C	
+Q06813	YPR078C	
+Q06839	YPR097W	
+P0C2I9	YPR137C-B	TY1B-PR1
+P0C2J1	YPR158C-D	TY1B-PR3
+Q08922	YPL182C	
+Q08954	YPL199C	
+Q99401	YPL238C	
+Q12523	YPL247C	
+Q08980	YPL264C	
+Q08990	YPL278C	
+A0A023PXI5	YPR197C	
+P43587	YFR003C	YPI1
+P46951	YGR198W	YPP1
+P36019	YNL093W	YPT53
+P0CX57	YAR010C	TY1A-A
+P39557	YAR047C	
+P38749	YHL009C	YAP3
+Q03935	YDR259C	YAP6
+Q8TGQ6	YBL006W-A	
+O43137	YBR085C-A	
+P89495	YBL109W	
+Q12217	YBR012W-A	TY1A-BR
+Q12193	YBR012W-B	TY1B-BR
+Q3E762	YBR230W-A	
+P0C5K9	YBL039C-A	
+P38309	YBR206W	
+P38318	YBR220C	
+P38355	YBR287W	
+P38142	YBR241C	
+P38338	YBR259W	
+P38083	YBR063C	
+P38253	YBR090C	
+P87012	YCL001W-A	
+Q8TGQ0	YCR081C-A	
+Q96VG5	YCR102W-A	
+Q8J0M4	YCL012C	
+P25562	YCL022C	
+P25593	YCL068C	
+P25614	YCR013C	
+Q12235	YLL055W	YCT1
+P25631	YCR051W	
+P25607	YCR101C	
+Q12023	YDL011C	
+Q8TGP7	YDL025W-A	
+Q07790	YDR053W	
+Q07410	YDL062W	
+Q07454	YDL073W	
+Q12103	YDL109C	
+Q03855	YDR098C-B	TY1B-DR1
+P0C5L7	YDR118W-A	
+Q12407	YDL199C	
+Q12240	YDR215C	
+Q07649	YDL221W	
+Q03494	YDR210W-B	TY2B-DR2
+Q07746	YDL242W	
+P87281	YDR269C	
+P87280	YDR290W	
+Q05503	YDR340W	
+Q03418	YDR491C	
+A0A023PXB9	YDR199W	
+P0C5M6	YEL020C-B	
+Q8TGP4	YEL032C-A	
+A0A023PYE4	YER067C-A	
+P89888	YEL075W-A	
+Q3E7A2	YER078W-A	
+A0A023PZG0	YER084W-A	
+P0CX66	YER159C-A	TY1A-ER2
+A0A023PYF7	YER172C-A	
+P0CX94	YER190C-B	
+A0A023PXD3	YER088C-A	
+P40004	YEL004W	YEA4
+P39999	YEL014C	
+P39991	YEL025C	
+P39989	YEL028W	
+P39977	YEL068C	
+P39971	YEL076C	
+P40028	YER041W	YEN1
+P40076	YER121W	
+P0C5M9	YFR009W-A	
+Q3E817	YFL041W-A	
+Q06676	YDR319C	YFT2
+Q12141	YGR027W-B	TY1B-GR1
+Q3E772	YGR169C-A	
+P53216	YGR025W	
+P53229	YGR045C	
+Q3E740	YGL258W-A	
+P53263	YGR107W	
+P53272	YGR122W	
+P53274	YGR126W	
+P53287	YGR151C	
+P32475	YGR176W	
+P53308	YGR228W	
+P53316	YGR250C	
+P53336	YGR283C	
+P53190	YGL024W	
+P53175	YGL052W	
+P53160	YGL074C	
+P53122	YGL138C	
+P53110	YGL159W	
+P53097	YGL193C	
+P53074	YGL230C	
+Q07074	YHR007C-A	
+A0A023PXL1	YHL019W-A	
+A0A023PYG5	YHL046W-A	
+P0C5B8	YHL050W-A	
+A0A023PXF2	YHR071C-A	
+P0C2I4	YHR214C-C	TY1A-H
+A0A023PXM2	YHR131W-A	
+P32792	YHR017W	YSC83
+P38799	YHR078W	
+P38831	YHR125W	
+P38833	YHR127W	
+P38867	YHR177W	
+P38870	YHR182W	
+A0A023PZF9	YIR023C-A	
+A0A023PZE9	YIL029W-A	
+A0A023PYI5	YIR036W-A	
+A0A023PXN3	YIL068W-A	
+Q45U18	YIL134C-A	
+P40538	YIL029C	
+P40434	YIL177C	
+P0C5P1	YJL127W-A	
+P47126	YJR079W	
+P47028	YJL086C	
+P42947	YJL107C	
+P47003	YJL152W	
+P46994	YJL169W	
+P39542	YJL193W	
+P40898	YJL211C	
+P47092	YJR020W	
+Q3E7A7	YKL018C-A	
+P36133	YKR040C	
+P36134	YKR041W	
+Q86ZR7	YKL033W-A	
+P35736	YKL050C	
+P36083	YKL075C	
+P0CX72	YLR157C-A	TY1A-LR2
+P0CY04	YLR157C-C	
+P0C5P6	YLR163W-A	
+O13546	YLR232W	
+O13542	YLR282C	
+Q3E771	YLR285C-A	
+Q8TGM3	YLR299C-A	
+Q3E825	YLR307C-A	
+Q06409	YLR422W	
+O13560	YLR444C	
+Q06199	YLR456W	
+Q3E760	YMR030W-A	
+Q3E809	YML054C-A	
+P0CF18	YMR085W	
+Q6B0Z2	YML101C-A	
+P0C5Q4	YMR141W-A	
+A0A023PXH6	YMR172C-A	
+Q3E766	YMR175W-A	
+Q03703	YML037C	
+Q04502	YML089C	
+P0CL29	YML133W-A	
+Q03207	YML122C	
+Q03099	YML133C	
+Q04364	YMR018W	
+Q99337	YNL054W-B	TY1B-NL2
+P53740	YNR048W	
+P53967	YNL028W	
+P53932	YNL095C	
+P53929	YNL108C	
+P53907	YNL144C	
+P53878	YNL181W	
+P40163	YNL203C	
+P53857	YNL234W	
+Q12169	YOR015W	
+Q870I1	YOL013W-B	
+Q08540	YOR169C	
+Q08560	YOR186W	
+Q12501	YOR343W-B	TY2B-OR2
+Q3E7Y7	YOR293C-A	
+Q12506	YOR314W	
+Q08842	YOR364W	
+Q08902	YOR378W	
+Q08915	YOR392W	
+Q3E769	YOL159C-A	
+P0C5R3	YOR073W-A	
+A0A023PZ99	YDR008C	
+A0A023PZE6	YDR048C	
+Q07379	YDL057W	
+Q07509	YDL094C	
+Q12441	YDR210C-C	TY1A-DR3
+Q99231	YDR210C-D	TY1B-DR3
+Q12047	YDL158C	
+Q3E789	YDR169C-A	
+Q3E796	YDR182W-A	
+P0C5E0	YDR193W	
+P0C5L9	YDL247W-A	
+P87282	YDR271C	
+P0C5M0	YDR320W-B	
+P87285	YDR355C	
+O13522	YDR396W	
+Q04033	YDR415C	
+P87270	YDR442W	
+P87271	YDR455C	
+Q03362	YDR476C	
+Q03057	YDR544C	
+Q8TGP9	YDL159C-B	
+P0C5M3	YDR183C-A	
+A0A023PYD3	YDR094W	
+P0C5M5	YDL114W-A	
+Q04925	YDR222W	
+Q8TGR5	YEL030C-A	
+P0CX95	YEL077W-A	
+Q02590	YER091C-A	
+P0CX71	YER137C-A	TY1A-ER1
+P40097	YER181C	
+A0A023PZC3	YER133W-A	
+Q03619	YER160C	TY1B-ER2
+P40000	YEL010W	
+P40083	YER137C	
+A0A023PXK7	YFL021C-A	
+A0A023PZH4	YFR052C-A	
+P43562	YFL040W	
+P43552	YFL051C	
+P43549	YFL054C	
+P0CX99	YFL068W	
+P43625	YFR057W	
+Q8TGT8	YGR174W-A	
+P53217	YGR026W	
+P53232	YGR051C	
+Q12337	YGR038C-D/YGR038C-C	TY2B-GR1
+P53249	YGR079W	
+P53275	YGR127W	
+P53291	YGR164W	
+P53339	YGR290W	
+P53144	YGL101W	
+P53134	YGL114W	
+P38887	YHR202W	
+A0A023PXL7	YHR056W-A	
+A0A023PZI4	YHR069C-A	
+O13537	YHR145C	
+A0A023PZI9	YHR182C-A	
+Q8TGK0	YHR214C-E	
+Q8TGK1	YHR213W-B	
+P0C5N6	YHR032W-A	
+P0C2J7	YHL009W-B	TY4B-H
+P0C5N7	YHR073W-A	
+Q03888	YIR020C-B	
+A0A023PZF3	YIL071W-A	
+A0A023PZJ9	YIL115W-A	
+P0CF21	YIL168W	
+Q7LHG5	YIL082W-A	TY3B-I
+P40520	YIL059C	
+P53039	YGR172C	YIP1
+P40446	YIL165C	
+Q8TGN3	YJL077W-A	
+P47151	YJR114W	
+P47174	YJR146W	
+P47063	YJL027C	
+P40365	YJL067W	
+P0C5P2	YKL100W-A	
+P36155	YKR075C	
+P36092	YKL044W	
+P35725	YKL063C	
+P36031	YKL223W	
+Q2V2P1	YLR146W-A	
+P0C2I7	YLR256W-B/YLR256W-C	TY1B-LR4
+Q06479	YLR352W	
+O13579	YLR379W	
+Q06051	YLR400W	
+Q8TGJ4	YLR466C-B	
+P0C5Q0	YLR154W-F	
+P0CE97	YLR159W	
+P0C5Q1	YLR364C-A	
+Q8TGJ7	YLL066W-B	
+P53956	YNL046W	
+P53948	YNL057W	
+Q08465	YOR064C	YNG1
+P53926	YNL114C	
+P53922	YNL120C	
+P40162	YNL205C	
+Q99248	YOR019W	
+Q3E735	YOR034C-A	
+Q08504	YOR105W	
+Q08532	YOR139C	
+P0C5R0	YOR314W-A	
+Q08321	YOL160W	
+Q8TGJ1	YOL166W-A	
+Q08620	YOR200W	
+Q12439	YOR192C-A	TY2A-OR1
+Q12293	YOR343W-A	TY2A-OR2
+Q8TGL2	YOR231C-A	
+Q08728	YOR263C	
+Q08373	YOL166C	
+Q12402	YPR028W	YOP1
+Q02659	YPL025C	
+Q3E7B4	YPL038W-A	
+Q02781	YPL062W	
+Q02754	YPL067C	
+Q02831	YPL077C	
+O13586	YPR092W	
+O13548	YPR099C	
+O13519	YPL136W	
+Q2V2P0	YPR145C-A	
+Q6Q5H1	YPR158C-C	TY1A-PR3
+Q12042	YPL162C	
+Q08930	YPL191C	
+Q08958	YPL205C	
+Q99395	YPL229W	
+Q12179	YPL245W	
+Q08977	YPL260W	
+P38298	YBR183W	YPC1
+Q07688	YDL235C	YPD1
+P53819	YNL339C	YRF1-6
+P53584	YNL237W	YTP1
+Q3E741	YAL037C-A	
+Q3E791	YAL063C-A	
+O13588	YAL069W	
+A0A023PXA5	YAL019W-A	
+P39559	YAR053W	
+P39563	YAR064W	
+P39566	YAR070C	
+Q08182	YOL028C	YAP7
+P38294	YBR174C	
+Q8TGK4	YBR298C-A	
+P38299	YBR184W	
+P38306	YBR197C	
+I2HB52	YBR056W-A	
+P38161	YBL108W	
+P38233	YBR051W	
+P38235	YBR053C	
+P38268	YBR116C	
+P38269	YBR124W	
+Q8TGQ2	YCR045W-A	
+Q3E830	YCR075W-A	
+Q3E7Z8	YCR024C-B	
+P25384	YCL019W	TY2B-C
+P25563	YCL023C	
+P25600	YCL074W	TY5A
+P39978	YEL067C	
+P39972	YEL075C	
+P40049	YER076C	
+P0CL27	YER190C-A	
+Q07451	YDL072C	YET3
+Q8TGU2	YFR032C-B	
+P43580	YFL012W	
+P43564	YFL034W	
+P43546	YFL057C	
+P43622	YFR054C	
+P53151	YGL088W	
+P53084	YGL218W	
+P53066	YGL242C	
+O13533	YHR049C-A	
+P0CL33	YHR054W-A	
+A0A023PZE1	YHR063W-A	
+A0A023PZE4	YHR165W-A	
+P0C5N5	YHR180C-B	
+O13534	YHR214W-A	
+P0CX19	YHR214W	
+P0CX93	YHR214C-D	
+Q6Q5P6	YHL009W-A	TY4A-H
+P38745	YHL017W	
+P38740	YHL026C	
+P38775	YHR045W	
+Q04013	YMR241W	YHM2
+Q04116	YDR451C	YHP1
+Q03885	YIR017W-A	
+A0A023PZJ3	YIL030W-A	
+A0A023PXF8	YIL066W-A	
+Q2V2P5	YIL102C-A	
+Q2V2P4	YIL156W-B	
+Q03886	YIR020W-A	
+P40543	YIL024C	
+P40508	YIL077C	
+Q06596	YPR199C	ARR1
+P40017	YER024W	YAT2
+P0C269	YBL100W-C	
+P0C5L2	YBR076C-A	
+Q3E7Y4	YBL112C	
+Q12266	YBL005W-A	TY1A-BL
+Q12490	YBL005W-B	TY1B-BL
+Q3E776	YBR255C-A	
+P38201	YBL029W	
+P38194	YBL044W	
+P34224	YBL059W	
+P38180	YBL081W	
+P38220	YBR027C	
+Q96VH1	YCR018C-A	
+Q3E787	YCR095W-A	
+Q3E819	YCR108C	
+P37263	YCR087C-A	
+P42937	YGR203W	YCH1
+P25347	YCR001W	
+P25354	YCR007C	
+P25654	YCR090C	
+Q12195	YDR015C	
+P0C1Z1	YDR524W-C	
+Q04408	YDR514C	
+Q03049	YDR541C	
+Q3E7B7	YDL085C-A	
+Q12331	YDR262W	
+P43551	YFL052W	
+P43624	YFR056C	
+Q8TGU0	YGL007C-A	
+Q8TGP1	YGL123C-A	
+P0CX67	YGR161C-C	TY1A-GR3
+Q8TGU1	YGL188C-A	
+P53212	YGR021W	
+Q8TGN7	YGR270C-A	
+P53243	YGR067C	
+P53182	YGL041C	
+P53139	YGL108C	
+P53116	YGL149W	
+P53105	YGL177W	
+P53100	YGL185C	
+P53089	YGL204C	
+A0A023PYG1	YHL002C-A	
+A0A023PXE8	YHR028W-A	
+Q8TGT5	YHR032C-A	
+P38899	YHR218W	
+P38730	YHL041W	
+P38727	YHL044W	
+P38765	YHR029C	YHI9
+P38690	YHR033W	
+P38769	YHR035W	
+P38842	YHR140W	
+Q02598	YIL014C-A	
+A0A023PXN9	YIL171W-A	
+P40521	YIL058W	
+P40519	YIL060W	
+P40455	YIL152W	
+P53093	YGL198W	YIP4
+P0CX74	YJR026W	TY1A-JR1
+Q3E828	YJL127C-B	
+Q3E801	YJL136W-A	
+P0C5N9	YJL156W-A	
+P47023	YJL114W	TY4A-J
+P47121	YJR071W	
+P47024	YJL113W	TY4B-J
+P47152	YJR115W	
+P47157	YJR120W	
+P47162	YJR128W	
+P40361	YJL070C	
+P47009	YJL144W	
+P46996	YJL163C	
+P46986	YJL182C	
+P39532	YJL202C	
+P40889	YJL225C	
+P47094	YJR023C	
+Q8TGM9	YKR075W-A	
+Q8TGN0	YKL156C-A	
+P36138	YKR045C	
+P36151	YKR070W	
+P40544	YIL023C	YKE4
+P34251	YKL107W	
+P36073	YKL115C	
+P36065	YKL136W	
+P36042	YKL202W	
+Q02203	YKR005C	
+Q8TGM8	YLL019W-A	
+Q07865	YLL037W	
+Q07989	YLR041W	
+Q12253	YLR046C	
+Q12026	YLR053C	
+Q12177	YLL056C	
+P25575	YCL046W	
+P25602	YCL076W	
+P37265	YCR041W	
+P25652	YCR087W	
+Q12115	YDL016C	
+P0C5L6	YDL022C-A	
+A0A023PXH9	YDR149C	
+Q12394	YDL152W	
+P0C2I3	YDR365W-B	TY1B-DR6
+A0A023PXI4	YDR203W	
+Q03480	YDR209C	
+Q00590	YDL213W-A	
+Q12392	YDR034C-C	TY2A-DR1
+Q03483	YDR210W-A	TY2A-DR2
+Q07738	YDL241W	
+Q06640	YDR306C	
+P87287	YDR366C	
+P0C5M2	YDR406W-A	
+Q2V2P7	YDR461C-A	
+P87272	YDR509W	
+P0C5M4	YDL185C-A	
+Q12147	YDL026W	
+Q12426	YDR010C	
+A0A023PXI8	YER006C-A	
+Q8TGP2	YER023C-A	
+A0A023PZF5	YER046W-A	
+A0A023PXC7	YER068C-A	
+P0CX16	YEL076C-A	
+A0A023PZB8	YER079C-A	
+P87191	YER119C-A	
+A0A023PYF4	YER145C-A	
+Q8TGR3	YER158W-A	
+P39961	YER184C	
+P39953	YEL006W	YEA6
+P40095	YER158C	
+P0C5N0	YFR010W-A	
+A0A023PXD9	YFL015W-A	
+Q8TGU3	YFL031C-A	
+Q12085	YGR027W-A	TY1A-GR1
+Q12485	YGR038C-A	TY1A-GR2
+Q12269	YGR038C-B	TY1B-GR2
+P53209	YGR016W	
+P53211	YGR018C	
+P53231	YGR050C	
+P0CX62	YGR161W-A	TY2A-GR2
+P38722	YHL049C	
+A0A023PXG3	YIL156W-A	
+P40539	YIL028W	
+P40448	YIL163C	
+P40442	YIL169C	
+Q8TGT2	YKL096C-B	
+P36128	YKR033C	
+P36086	YKL071W	
+P34248	YKL100C	
+P36072	YKL118W	
+P36058	YKL153W	
+P36114	YKR018C	
+P35995	YKL222C	
+Q02209	YKR011C	
+Q3E814	YLL006W-A	
+P0C2I6	YLR227W-B	TY1B-LR3
+P0CY02	YLR154C-H	
+Q06235	YLR162W	
+Q06251	YLR177W	
+Q06267	YLR184W	
+Q05777	YLR194C	
+P0C2J4	YLR410W-A	TY2A-LR1
+P0C2J3	YLR410W-B	TY2B-LR1
+Q8TGR0	YLR437C-A	
+Q8TGM1	YLR399W-A	
+Q06057	YLR402W	
+Q3E742	YLR412C-A	
+Q06695	YLR416C	
+P0CX17	YLR464W	
+P0C5P8	YLR149C-A	
+P0C5P9	YLR154W-B	
+P38746	YHL014C	YLF2
+Q6B0Y8	YML012C-A	
+P0C261	YML057C-A	
+Q6B2I9	YML099W-A	
+Q8TGS8	YMR105W-A	
+P0CX76	YML040W	TY1A-ML2
+Q6B0X1	YMR135W-A	
+P0C5Q3	YMR013C-A	
+Q04223	YMR130W	
+P40207	YMR134W	
+Q3E782	YMR247W-A	
+A0A023PXH2	YML031C-A	
+Q03236	YMR187C	
+Q03695	YMR206W	
+Q04018	YMR244W	
+Q04835	YMR253C	
+Q03263	YMR279C	
+P0C5Q6	YMR194C-A	
+Q04898	YMR321C	
+Q03730	YML018C	
+Q03161	YMR099C	
+Q8TGL8	YNL097W-A	
+Q3E7Z1	YNL146C-A	
+P53828	YNL296W	
+P53826	YNL319W	
+P53736	YNR040W	
+P53749	YNR063W	
+P0C271	YNL097C-B	
+P53758	YNR077C	
+P53979	YNL013C	
+P53960	YNL040W	
+P53947	YNL058C	
+P38806	YHR090C	YNG2
+P53936	YNL089C	
+P53906	YNL146W	
+P53888	YNL170W	
+P53862	YNL228W	
+Q08187	YOL029C	
+Q08206	YOL036W	
+Q08498	YOR082C	
+Q3E7Y9	YOL097W-A	
+Q08241	YOL106W	
+Q08270	YOL131W	
+Q12243	YOR029W	
+O13521	YPL035C	
+A0A023PZM3	YPR050C	
+O13582	YPR076W	
+O13517	YPL102C	
+Q02961	YPL113C	
+P0CX73	YPL257W-A	TY1A-PL
+P0CX58	YPR137C-A	TY1A-PR1
+Q06522	YPR147C	
+Q12152	YPL150W	
+A0A023PYK2	YPR170C	
+Q06594	YPR195C	
+Q08993	YPR202W	
+P0CX98	YPR204C-A	
+Q8TGL0	YPL222C-A	
+P0C5S0	YPL250W-A	
+Q08976	YPL261C	
+P0CF36	YPL276W	
+A0A0B7P3V8	YPL060C-A	TY4B-P
+P0C5S1	YPR160W-A	
+P0C1V3	YAL016C-B	
+A0A023PXH4	YAL026C-A	
+Q8TGK6	YAL067W-A	
+Q8TGK7	YAL068W-A	
+D6VPM8	YAR023C	
+P39549	YAR029W	
+P39550	YAR030C	
+Q8TGU8	YBL071C-B	
+P0C5L3	YBR103C-A	
+Q8TGQ4	YBR141W-A	
+Q2V2Q3	YBR201C-A	
+Q3E781	YBR221W-A	
+A0A023PXH5	YBR126W-B	
+P38303	YBR190W	
+P38320	YBR224W	
+P38150	YBR284W	
+P38209	YBL012C	
+P38202	YBL028C	
+Q03904	YDR133C	
+Q8TGP3	YEL008C-A	
+A0A023PYD9	YEL018C-A	
+P0C5M7	YEL050W-A	
+Q8TGU4	YER175W-A	
+P32618	YEL043W	
+Q07950	YLR020C	YEH2
+P39974	YEL073C	
+P40058	YER085C	
+P40082	YER135C	
+P43540	YFL064C	
+P43538	YFL066C	
+P43597	YFR016C	
+P43608	YFR035C	
+P43617	YFR045W	
+Q8TGN8	YGR068W-A	
+P53205	YGR011W	
+P53213	YGR022C	
+P53240	YGR064W	
+P53245	YGR069W	
+P53282	YGR137W	
+P53288	YGR160W	
+P53307	YGR219W	
+P53329	YGR273C	
+P25338	YGL010W	
+P53186	YGL034C	
+P53181	YGL042C	
+P53138	YGL109W	
+P53132	YGL118C	
+P53126	YGL132W	
+P53120	YGL140C	
+P0CL28	YGR296C-A	
+P53085	YGL217C	
+Q3E7Z6	YHL015W-A	
+A0A023PZD5	YHL030W-A	
+Q3E758	YHL048C-A	
+P0CL32	YHR052W-A	
+A0A023PYH0	YHR070C-A	
+O13536	YHR139C-A	
+Q3E815	YHR175W-A	
+P38868	YHR180W	
+Q3E7Z5	YIL002W-A	
+Q3E7Z4	YIL046W-A	
+Q8TGN5	YIL105W-A	
+A0A023PYI2	YIL142C-A	
+P0CF22	YIL167W	SDL1
+P40551	YIL012W	
+P40542	YIL025C	
+Q08956	YPL201C	YIG1
+P25637	YCR059C	YIH1
+P40497	YIL092W	
+P40488	YIL102C	
+P40483	YIL108W	
+A0A023PXM7	YIL020C-A	
+P28626	YMR151W	YIM2
+P53108	YGL161C	YIP5
+P0CL23	YIL175W	
+Q8TGN1	YJR140W-A	
+P47159	YJR124C	
+P47188	YJR162C	
+P47078	YJL009W	
+P47021	YJL119C	
+P47012	YJL135W	
+P40895	YJL215C	
+P40892	YJL218W	
+P47086	YJR011C	
+P36119	YKR023W	
+P0CE69	YKR104W	
+P0C5P3	YKL145W-A	
+Q3E765	YKL183C-A	
+P36098	YKL031W	
+P34249	YKL102C	
+P36071	YKL123W	
+Q08018	YLR076C	
+Q12528	YLR111W	
+Q12174	YLR123C	
+Q12288	YLR126C	
+P0CY05	YLR159C-A	
+Q06070	YLR407W	
+O13578	YLR415C	
+Q06698	YLR419W	
+Q06188	YLR455W	
+Q6B0Y5	YMR046W-A	
+A0A023PZL2	YMR119W-A	
+Q04711	YML045W	TY1B-ML1
+Q03434	YML039W	TY1B-ML2
+A0A023PYJ4	YMR153C-A	
+P40218	YMR147W	
+Q04336	YMR196W	
+Q04019	YMR245W	
+Q04838	YMR254C	
+Q03508	YMR265C	
+Q03559	YMR295C	
+Q04869	YMR315W	
+Q6Q571	YMR086C-A	
+A0A023PYJ0	YML009C-A	
+P39523	YMR124W	
+Q04215	YMR046C	TY1A-MR1
+I2HB70	YMR316C-A	
+A0A023PXQ4	YMR173W-A	
+Q8TGS7	YMR182W-A	
+P40214	YMR144W	
+Q8TGS5	YMR272W-B	
+A0A023PXI0	YMR306C-A	
+Q03795	YMR155W	
+Q03648	YMR209C	
+Q05016	YMR226C	
+P38430	YMR262W	
+Q04893	YMR317W	
+Q6B0R7	YMR326C	
+P32331	YPR058W	YMC1
+Q04521	YML084W	
+Q03759	YML108W	
+P47147	YJR110W	YMR1
+P0CX09	YNR073C	
+Q12112	YNL284C-B	TY1B-NL1
+Q3E7Z0	YNL277W-A	
+P53827	YNL303W	
+Q3E767	YNL067W-B	
+P53820	YNL338W	
+P53723	YNR021W	
+Q08300	YOL159C	
+P0CF20	YOL163W	
+Q3E736	YOR192C-C	
+Q08756	YOR300W	
+Q3E806	YOR316C-A	
+Q08786	YOR331C	
+Q12484	YOR343C	
+Q08910	YOR387C	
+Q3E832	YOR072W-B	
+Q08157	YOL019W	
+P38070	YBR028C	YPK3
+Q3E7B3	YPR108W-A	
+Q6B0W0	YPR039W	
+O13572	YPR150W	
+P53057	YGL259W	YPS5
+P38815	YHR105W	YPT35
+Q99260	YLR262C	YPT6
+P31111	YDR285W	ZIP1
+P40021	YER033C	ZRG8
+Q12512	YOL154W	ZPS1
+O13518	YPL114W	
+O13571	YPR146C	
+O13583	YPR077C	
+Q06325	YDR349C	YPS7
+P38146	YBR264C	YPT10
+P38555	YER031C	YPT31
+P36018	YKR014C	YPT52
+P0CX22	YOR396W	YRF1-8
+P38280	YBR148W	YSW1
+Q12324	YOR087W	YVC1
+P53303	YGR211W	ZPR1
+P0CF34	YLL016W	SDC25
+Q07880	YLL044W	
+Q07881	YLL047W	
+Q3E798	YLR099W-A	
+P0C2I5	YLR157C-B	TY1B-LR2
+Q12077	YLR140W	
+Q3E813	YLR154C-G	
+P0CE98	YLR161W	
+A0A023PZG4	YLR236C	
+O13573	YLR252W	
+O13541	YLR280C	
+Q05867	YLR283W	
+Q05898	YLR296W	
+O94085	YLR339C	
+Q06139	YLR346C	
+Q3E795	YLR361C-A	
+Q06689	YLR413W	
+O13564	YLR428C	
+A0A023PZK9	YLR458W	
+P0CE99	YLR157W-D	
+Q04461	YMR111C	
+Q04471	YMR114C	
+A2P2R3	YMR084W	
+Q04670	YMR050C	TY1B-MR2
+Q8TGS6	YMR242W-A	
+A0A023PZL7	YMR294W-A	
+P0C5Q5	YMR307C-A	
+Q8TGS4	YMR315W-A	
+Q03823	YMR160W	
+Q03231	YMR181C	
+Q04814	YMR252C	
+Q04867	YMR310C	
+P32843	YMR302C	YME2
+Q03629	YML079W	
+Q03208	YML119W	
+Q03102	YML131W	
+Q04773	YMR074C	
+Q04436	YMR103C	
+P0C5Q7	YNR001W-A	
+Q8TGJ2	YNR075C-A	
+Q12391	YNL284C-A	TY1A-NL1
+Q12470	YNL054W-A	TY1A-NL2
+P42840	YNL320W	
+P53821	YNL337W	
+P53719	YNR014W	
+P53726	YNR025C	
+P53747	YNR061C	
+P53980	YNL011C	
+P53902	YNL150W	
+P53887	YNL171C	
+P40169	YNL194C	
+P40159	YNL208W	
+Q08110	YOL014W	
+Q8TGS1	YOR032W-A	
+Q3E7Z9	YOL038C-A	
+Q8TGL6	YOR108C-A	
+Q92392	YOL103W-A	TY1A-OL
+Q08521	YOR121C	
+Q08293	YOL150C	
+Q08621	YOR203W	
+Q12015	YOR223W	
+Q08741	YOR282W	
+Q08743	YOR292C	
+Q08789	YOR333C	
+Q08811	YOR345C	
+Q3E805	YOR376W-A	
+Q3E804	YOR381W-A	
+Q08912	YOR389W	
+Q8TGL5	YOR161W-A	
+Q8TGQ8	YOL085W-A	
+P0CL40	YOR396C-A	
+Q12219	YOR114W	
+P34161	YML027W	YOX1
+Q03083	YPL034W	
+O13520	YPL044C	
+Q12160	YPR063C	
+P40323	YPL073C	
+Q06821	YPR084W	
+O13587	YPR096C	
+Q02873	YPL107W	
+Q06116	YPR117W	
+O13567	YPR126C	
+P0CX60	YPR158W-A	TY1A-PR2
+Q06523	YPR148C	
+Q8TGR9	YPL152W-A	
+Q8TGK8	YPR160C-A	
+P0C5R8	YPR170W-A	
+Q08927	YPL185W	
+Q08953	YPL197C	
+Q08995	YPR204W	
+Q08971	YPL225W	
+Q12058	YPL251W	
+Q08984	YPL272C	
+P0CX97	YPL283W-B	
+Q12159	YDR381W	YRA1
+P53107	YGL164C	YRB30
+Q12436	YLR130C	ZRT2
+P32527	YGR285C	ZUO1
+P40523	YIL055C	
+P40445	YIL166C	
+Q3E775	YJR151W-A	
+P0C5P0	YJL197C-A	
+P47114	YJR054W	
+P47062	YJL028W	
+P0CL24	YJL222W-B	
+P46992	YJL171C	
+P40891	YJL220W	
+P47087	YJR012C	
+Q2V2P2	YKL065W-A	
+Q3E7A0	YKL106C-A	
+P0C5P4	YKL162C-A	
+P32859	YKL036C	
+P33324	YKL091C	
+P36061	YKL147C	
+Q07799	YLL007C	
+Q07811	YLL020C	
+Q07990	YLR042C	
+Q12155	YLR050C	
+Q07888	YLL067C	
+Q08027	YLR101C	
+Q12130	YLR112W	
+Q12312	YLR122C	
+P0CX75	YLR227W-A	TY1A-LR3
+Q99296	YLR149C	
+P54072	YLR152C	
+P0CY03	YLR156C-A	
+P0C2J5	YLR424C-A	TY2B-LR2
+Q3E732	YLR264C-A	
+O13550	YLR269C	
+Q05854	YLR278C	
+Q05863	YLR281C	
+Q8TGM4	YLR286W-A	
+O13544	YLR302C	
+O13553	YLR317W	
+Q8TGM2	YLR347W-A	
+Q3E747	YLR363W-A	
+O13576	YLR434C	
+P54007	YLR460C	
+Q06493	YPR125W	YLH47
+P0CD98	YLL053C	
+Q3E7A6	YML007C-A	
+Q03879	YMR122C	
+Q6B108	YML116W-A	
+Q04706	YML045W-A	TY1A-ML1
+Q3E842	YMR122W-A	
+P0CX69	YMR051C	TY1A-MR2
+Q6B0X2	YMR158W-B	
+P40211	YMR141C	
+A0A023PZH5	YMR290W-A	
+A0A023PYJ7	YMR304C-A	
+A0A023PXQ9	YMR316C-B	
+Q03829	YMR166C	
+Q03219	YMR178W	
+Q3E843	YMR158C-A	
+Q03649	YMR210W	
+Q8TGM0	YMR272W-A	
+Q04897	YMR320W	
+Q03722	YML020W	
+P38087	YBR104W	YMC2
+Q03697	YML038C	YMD8
+P53957	YNL043C	
+P53912	YNL134C	
+P40168	YNL195C	
+Q08411	YOR041C	
+Q99345	YOL085C	
+P0C5Q9	YOR008W-B	
+Q08503	YOR102W	
+Q99210	YOR111W	
+Q12273	YOL103W-B	TY1B-OL
+Q08533	YOR146W	
+Q12249	YOR218C	
+Q12113	YOR192C-B	TY2B-OR1
+Q08734	YOR268C	
+Q12012	YOR289W	
+Q99318	YOR318C	
+Q8TGL1	YOR335W-A	
+P0C5R2	YOR072W-A	
+Q08428	YOR053W	
+Q3E834	YER074W-A	YOS1
+Q12145	YPR013C	
+P0C5R5	YPR016W-A	
+Q12139	YPR022C	
+Q3E752	YPR036W-A	
+Q02826	YPL080C	
+Q06833	YPR091C	
+Q02981	YPL109C	
+Q8TGK9	YPL135C-A	
+Q8TGQ7	YPR159C-A	
+Q06616	YPR174C	
+Q12697	YOR291W	YPK9
+P38279	YBR147W	RTC2
+Q6B0W2	YPR014C	
+O13569	YPR136C	
+O13570	YPR142C	
+Q12346	YPR071W	
+Q12303	YLR121C	YPS3
+P0CD97	YER039C-A	
+P41920	YDR002W	YRB1
+Q12172	YOR162C	YRR1
+P25036	YOR003W	YSP3
+Q12024	YOR272W	YTM1
+Q08245	YOL109W	ZEO1
+P53061	YGL249W	ZIP2
+P53831	YNL285W	
+P0C5Q8	YNL067W-A	
+P53717	YNR005C	
+P53750	YNR064C	
+P53752	YNR066C	
+P53981	YNL010W	
+P53975	YNL019C	
+P53928	YNL109W	
+P53910	YNL140C	
+P53891	YNL165W	
+P53884	YNL174W	
+P53876	YNL184C	
+P53870	YNL193W	
+P40166	YNL198C	
+P40152	YNL217W	
+P53864	YNL226W	
+Q12351	YOR012W	
+Q08172	YOL024W	
+Q3E824	YOR020W-A	
+Q08222	YOL050C	
+Q08232	YOL073C	
+Q6B0V7	YPR002C-A	
+Q06104	YPR109W	
+Q12458	YDR368W	YPR1
+P32329	YLR120C	YPS1
+P01123	YFL038C	YPT1
+P40105	YER190W	YRF1-2
+P0CX15	YPL283C	YRF1-7
+Q12340	YOR172W	YRM1
+P47043	YJL056C	ZAP1
+P54786	YML109W	ZDS2
+P25650	YCR085W	
+P25657	YCR099C	
+P25606	YCR100C	
+Q12210	YDL009C	
+Q12111	YDR029W	
+Q12025	YDR056C	
+Q07435	YDL068W	
+P38966	YDR089W	
+Q07530	YDL114W	
+Q04608	YDR124W	
+Q03899	YDR131C	
+A0A023PZA4	YDR154C	
+Q07613	YDL187C	
+Q12121	YDL211C	
+Q07658	YDL228C	
+Q3E763	YDR246W-A	
+P87283	YDR274C	
+Q05530	YDR286C	
+P87288	YDR327W	
+P0C289	YDR034C-A	
+O13523	YDR401W	
+P87267	YDR417C	
+Q04093	YDR444W	
+P87264	YDR467C	
+Q8TGR7	YDR510C-A	
+P87263	YER066C-A	
+A0A023PYE9	YER087C-A	
+A0A023PXJ7	YER107W-A	
+A0A023PXD5	YER147C-A	
+A0A023PZC7	YER152W-A	
+A0A023PZH1	YER165C-A	
+P40101	YER186C	
+P0C0V2	YER188C-A	
+P0C270	YER138W-A	
+A0A023PXC2	YEL053W-A	
+A0A023PXJ3	YER076W-A	
+P39994	YEL020C	
+P39983	YEL057C	
+P39973	YEL074W	
+P40022	YER034W	
+P35723	YKL065C	YET1
+P39959	YER130C	
+P10356	YER152C	
+Q03187	YFL013W-A	
+Q8TGR2	YFR034W-A	
+P0CX63	YFL002W-A	TY2B-F
+P43578	YFL015C	
+P43566	YFL032W	
+P43599	YFR018C	
+Q3E802	YGL006W-A	
+P0C5N2	YGR122C-A	
+Q8TGT9	YGR146C-A	
+P53208	YGR015C	
+P53210	YGR017W	
+P53222	YGR035C	
+P53247	YGR073C	
+Q12173	YGR109W-A	TY3A-G
+P53269	YGR115C	
+P53284	YGR139W	
+P53293	YGR168C	
+P53300	YGR182C	
+P50089	YGR237C	
+P53325	YGR265W	
+P53342	YGR293C	
+P33199	YGL015C	
+P53183	YGL039W	
+P53155	YGL082W	
+P53133	YGL117W	
+P38616	YNL160W	YGP1
+P53103	YGL182C	
+P53092	YGL199C	
+P53054	YGL262W	
+A0A023PYH5	YHR193C-A	
+P0CX89	YHR212C	
+P0CL34	YHR219C-A	
+P0C5N8	YHR180W-A	
+P38729	YHL042W	
+P38721	YHL050C	
+P38776	YHR048W	YHK8
+P38829	YHR122W	
+P40556	YIL006W	YIA6
+P40524	YIL054W	
+P40503	YIL086C	
+P28625	YMR152W	YIM1
+P40449	YIL161W	
+P40587	YIR043C	
+P47105	YJR037W	
+P47107	YJR039W	
+P47099	YJR028W	TY1A-JR2
+P47115	YJR056C	
+P40355	YJR061W	
+P47132	YJR087W	
+P47181	YJR154W	
+P47066	YJL022W	
+P47053	YJL043W	
+P47038	YJL064W	
+P0CL26	YJL222W-A	
+P46987	YJL181W	
+P40896	YJL213W	
+P47091	YJR018W	
+Q2V2P3	YKL023C-A	
+Q12336	YLL059C	
+Q12259	YLR108C	
+Q12327	YLR124W	
+P0C2I8	YLR256W-A	TY1A-LR4
+O13561	YLR169W	
+O13562	YLR171W	
+Q06247	YLR173W	
+Q06252	YLR179C	
+O13530	YLR198C	
+O13532	YLR217W	
+P0C5P7	YLR222C-A	
+Q05947	YLR224W	
+P0C2J6	YLR424C-B	TY2A-LR2
+Q05881	YLR287C	
+O13543	YLR294C	
+Q05899	YLR297W	
+Q06158	YLR311C	
+Q06170	YLR326W	
+Q06127	YLR334C	
+O94086	YLR349W	
+O13565	YLR358C	
+Q7LIF1	YLR366W	
+O13556	YLR462W	
+P0CL38	YLR466C-A	
+Q04978	YML053C	
+Q12204	YOR022C	
+Q08419	YOR050C	
+Q08486	YOR072W	
+Q08994	YPR203W	
+Q08974	YPL257W	
+Q08989	YPL277C	
+P0CX20	YDR545W	YRF1-1
+P0CX21	YLR467W	YRF1-5
+P42844	YNL310C	ZIM17
+Q8TGS0	YOR161C-C	
+Q08543	YOR170W	
+Q08604	YOR199W	
+Q08748	YOR296W	
+Q12444	YOR309C	
+Q08816	YOR352W	
+Q08909	YOR385W	
+Q8TGJ0	YOR394C-A	
+Q8TGL4	YOR161W-B	
+Q8TGL3	YOR186C-A	
+Q08259	YOL118C	
+Q12070	YOR024W	
+Q08900	YOR376W	
+Q12274	YOR097C	
+A5Z2X5	YPR010C-A	
+Q04203	YPR012W	
+Q12531	YPR015C	
+Q02606	YPL014W	
+Q12492	YPR064W	
+P0C5R6	YPR074W-A	
+Q02872	YPL108W	
+Q06107	YPR114W	
+Q12414	YPL257W-B	TY1B-PL
+Q08916	YPL142C	
+P0C5R7	YPR169W-A	
+Q06595	YPR196W	
+Q08964	YPL216W	
+P0CL31	YPL283W-A	
+Q12010	YOL092W	YPQ1
+O13559	YLR466W	YRF1-4
+P32793	YHR016C	YSC84
+P0C074	YNL138W-A	YSF3
+P26725	YJL139C	YUR1
+P53735	YNR039C	ZRG17
+P20107	YMR243C	ZRC1
+P32804	YGL255W	ZRT1
+P34240	YKL175W	ZRT3
+P0CX14	YGR296W	YRF1-3
+Q06681	YDR326C	YSP2
+P40341	YMR089C	YTA12
+P31383	YAL016W	TPD3
+Q08361	YOL165C	AAD15
+P43547	YFL056C	AAD6
+P15891	YCR088W	ABP1
+P39970	YER045C	ACA1
+P32316	YBL015W	ACH1
+Q01574	YAL054C	ACS1
+Q00362	YGL190C	CDC55
+P47096	YJR025C	BNA1
+P42884	YNL331C	AAD14
+P32357	YBL074C	AAR2
+P47146	YJR108W	ABM1
+Q12031	YPR006C	ICL2
+P07248	YDR216W	ADR1
+P39925	YER017C	AFG3
+P38903	YOR014W	RTS1
+P47129	YJR083C	ACF4
+P14164	YKL112W	ABF1
+P40535	YIL036W	CST6
+P31787	YGR037C	ACB1
+P53930	YNL107W	YAF9
+P32317	YEL052W	AFG1
+P32323	YNR044W	AGA1
+Q12482	YPR021C	AGC1
+Q04412	YDR524C	AGE1
+P38090	YBR132C	AGP2
+P03876	Q0055	AI2
+Q12471	YOL136C	PFK27
+P53319	YGR256W	GND2
+P23542	YLR027C	AAT2
+Q07622	YDL203C	ACK1
+Q03771	YDR161W	ACL4
+Q07747	YDL243C	AAD4
+P08521	YOR302W	
+P21192	YLR131C	ACE2
+P47182	YJR155W	AAD10
+P25612	YCR107W	AAD3
+P37898	YHR047C	AAP1
+P28240	YER065C	ICL1
+P38720	YHR183W	GND1
+Q02895	YPL088W	AAD16
+Q01802	YKL106W	AAT1
+Q08641	YOR239W	ABP140
+P47177	YJR149W	
+P40433	YIL107C	PFK26
+P12904	YGL115W	SNF4
+Q02486	YMR072W	ABF2
+Q00955	YNR016C	ACC1
+P40529	YIL044C	AGE2
+P52923	YNR074C	AIF1
+P23180	YHL021C	AIM17
+P38884	YHR198C	AIM18
+P40451	YIL158W	AIM20
+P32858	YKL037W	AIM26
+Q03673	YMR003W	AIM34
+Q03798	YMR157C	AIM36
+Q12032	YOR215C	AIM41
+P38305	YBR194W	AIM4
+P46680	YMR092C	AIP1
+P52893	YLR089C	ALT1
+P47019	YJL122W	ALB1
+P40047	YER073W	ALD5
+P53178	YGL047W	ALG13
+P38179	YBL082C	ALG3
+Q06497	YPR128C	ANT1
+P38856	YHR161C	YAP1801
+Q12028	YPR029C	APL4
+P38065	YBL037W	APL3
+P53886	YNL172W	APC1
+Q12440	YLR127C	APC2
+Q12449	YDR214W	AHA1
+Q9ZZX0	Q0075	AI5_BETA
+P47015	YJL131C	AIM23
+P36154	YKR074W	AIM29
+Q08223	YOL053W	AIM39
+Q07716	YDL237W	AIM6
+P47771	YMR170C	ALD2
+P54114	YMR169C	ALD3
+P46367	YOR374W	ALD4
+P38242	YBR070C	ALG14
+P40350	YPL227C	ALG5
+P40351	YOR067C	ALG8
+P43633	YGL021W	ALK1
+P32459	YIR032C	DAL3
+Q08269	YOL130W	ALR1
+P14904	YKL103C	APE1
+P47064	YJL024C	APS3
+P60010	YFL039C	ACT1
+P25371	YCR011C	ADP1
+P25613	YCR010C	ADY2
+P33304	YDR085C	AFR1
+P22149	YGL071W	AFT1
+P87275	YER093C-A	AIM11
+P53109	YGL160W	AIM14
+P47140	YJR100C	AIM25
+P39721	YAL049C	AIM2
+Q04689	YML050W	AIM32
+P53730	YNR030W	ALG12
+P43636	YGL065C	ALG2
+P32789	YBL009W	ALK2
+P43553	YFL050C	ALR2
+P47029	YJL084C	ALY2
+P50082	YGR225W	AMA1
+P38285	YBR158W	AMN1
+P40502	YIL087C	AIM19
+P40563	YIR003W	AIM21
+P40053	YER080W	AIM9
+P25335	YIR029W	DAL2
+Q00776	YPL259C	APM1
+P35181	YLR170C	APS1
+P16550	YCL050C	APA1
+P38281	YBR151W	APD1
+P40532	YIL040W	APQ12
+P53909	YNL141W	AAH1
+Q2V2Q1	YCL058W-A	ADF1
+P00330	YOL086C	ADH1
+P00331	YMR303C	ADH2
+P10127	YGL256W	ADH4
+Q04894	YMR318C	ADH6
+P47143	YJR105W	ADO1
+Q01976	YBR111C	YSA1
+P18239	YBL030C	PET9
+P18238	YBR085W	AAC3
+Q07732	YDL239C	ADY3
+P32493	YMR064W	AEP1
+P22136	YMR282C	AEP2
+Q08957	YPL202C	AFT2
+P43548	YFL055W	AGP3
+P25649	YCR082W	AHC2
+P29589	YHR093W	AHT1
+P38266	YBR108W	AIM3
+Q99299	YPL158C	AIM44
+P38885	YHR199C	AIM46
+P53954	YNL048W	ALG11
+Q12001	YOR002W	ALG6
+P53868	YNL219C	ALG9
+P38313	YBR211C	AME1
+P39533	YJL200C	ACO2
+P52910	YLR153C	ACS2
+P48360	YDR376W	ARH1
+P25376	YCL025C	AGP1
+P10869	YER052C	HOM3
+Q08548	YOR175C	ALE1
+P36117	YKR021W	ALY1
+P22580	YDR242W	AMD2
+P38113	YBR145W	ADH5
+P04710	YMR056C	AAC1
+P47127	YJR080C	AIM24
+Q12013	YOR034C	AKR2
+P52892	YDR111C	ALT2
+P14540	YKL060C	FBA1
+P50076	YGR227W	DIE2
+P32375	YIR027C	DAL1
+P54783	YML086C	ALO1
+P38971	YNL270C	ALP1
+Q08981	YPL267W	ACM1
+P13711	YGL205W	POX1
+P32463	YKL192C	ACP1
+Q02336	YDR448W	ADA2
+P07246	YMR083W	ADH3
+P25377	YCR105W	ADH7
+Q12184	YPL252C	YAH1
+P38872	YHR185C	PFS1
+Q05955	YLR227C	ADY4
+Q12089	YPL005W	AEP3
+Q99222	YOR129C	AFI1
+P32781	YGL032C	AGA2
+P38628	YEL058W	PCM1
+P43567	YFL030W	AGX1
+Q04516	YML087C	AIM33
+Q12476	YDL175C	AIR2
+P21147	YGL055W	OLE1
+P19414	YLR304C	ACO1
+Q03233	YMR184W	ADD37
+P32794	YLR397C	AFG2
+Q12433	YOR023C	AHC1
+P38013	YLR109W	AHP1
+P03875	Q0050	AI1
+Q12156	YDR063W	AIM7
+P40507	YIL079C	AIR1
+P39010	YDR264C	AKR1
+P38207	YBL019W	APN2
+Q12354	YLR118C	
+Q08702	YOR258W	HNT3
+Q04212	YMR041C	ARA2
+P38724	YHL047C	ARN2
+P38840	YHR137W	ARO9
+Q04549	YDR106W	ARP10
+P80428	YJL081C	ARP4
+P40467	YIL130W	ASG1
+P34233	YKL185W	ASH1
+Q06834	YPR093C	ASR1
+P49435	YML022W	APT1
+P07347	YHR013C	ARD1
+P18544	YOL140W	ARG8
+P53974	YNL020C	ARK1
+P38116	YBR164C	ARL1
+P38696	YHR129C	ARP1
+Q06597	YPR200C	ARR2
+P40994	YOR094W	ARF3
+Q04728	YMR062C	ARG7
+P07249	YMR042W	ARG80
+P38731	YHL040C	ARN1
+P53090	YGL202W	ARO8
+P32449	YBR249C	ARO4
+P53946	YNL059C	ARP5
+Q12386	YOR141C	ARP8
+Q05123	YMR033W	ARP9
+P38328	YBR234C	ARC40
+P53731	YNR035C	ARC35
+P32447	YJL115W	ASF1
+P38986	YDR321W	ASP1
+P40024	YER036C	ARB1
+P11076	YDL192W	ARF1
+P00812	YPL111W	CAR1
+P08566	YDR127W	ARO1
+P15274	YML035C	AMD1
+Q08951	YPL195W	APL5
+P22108	YDR530C	APA2
+Q04601	YDR118W	APC4
+Q08683	YOR249C	APC5
+Q12107	YLR102C	APC9
+P53933	YNL094W	APP1
+P47036	YJL075C	APQ13
+P36973	YDR441C	APT2
+P25628	YCR048W	ARE1
+P53111	YGL157W	ARI1
+P36090	YKL047W	ANR2
+P46682	YGR261C	APL6
+Q12157	YDL008W	APC11
+Q04413	YDR525W	API2
+P04076	YHR018C	ARG4
+P08019	YIL099W	SGA1
+P32629	YEL036C	ANP1
+P38832	YHR126C	ANS1
+P38153	YBR288C	APM3
+P37302	YBR286W	APE3
+P53940	YNL077W	APJ1
+P38700	YHL019C	APM2
+P22936	YKL114C	APN1
+P53943	YNL065W	AQR1
+P0CD90	YLL052C	AQY2
+Q04371	YMR027W	
+Q06408	YDR380W	ARO10
+Q04052	YDR421W	ARO80
+P38080	YBR059C	AKL1
+P54115	YPL061W	ALD6
+P16661	YBR110W	ALG1
+P36000	YKL135C	APL2
+P19880	YML007W	YAP1
+P27351	YJR005W	APL1
+Q99186	YOL062C	APM4
+P53068	YGL240W	DOC1
+P0CD91	YPR192W	AQY1
+P38115	YBR149W	ARA1
+P46672	YGL105W	ARC1
+P53309	YGR241C	YAP1802
+Q00381	YJR058C	APS2
+P24813	YDR423C	CAD1
+Q8TGM5	YLR154W-E	ART3
+Q03862	YDR101C	ARX1
+P22768	YOL058W	ARG1
+P13586	YGL167C	PMR1
+Q12675	YDR093W	DNF2
+P40527	YIL048W	NEO1
+P16639	YGL017W	ATE1
+P38316	YBR217W	ATG12
+Q06628	YPR185W	ATG13
+Q06671	YLR431C	ATG23
+P46989	YJL178C	ATG27
+P01097	YDL181W	INH1
+P21306	YPL271W	ATP15
+P00830	YJR121W	ATP2
+P05626	YPL078C	ATP4
+Q07879	YLL042C	ATG10
+Q07528	YDL113C	ATG20
+Q12421	YDR022C	ATG31
+Q99325	YOR152C	ATG40
+P48016	YPR026W	ATH1
+Q12233	YPR020W	ATP20
+P38111	YBR136W	MEC1
+Q08409	YOR011W	AUS1
+Q12500	YLR114C	AVL9
+Q05933	YLR370C	ARC18
+P0CX79	YLR160C	ASP3-4
+P39945	YER101C	AST2
+P53296	YGR177C	ATF2
+Q12527	YPR049C	ATG11
+P38270	YBR128C	ATG14
+P25641	YCR068W	ATG15
+Q03818	YMR159C	ATG16
+Q06410	YLR423C	ATG17
+P35193	YOL082W	ATG19
+P53104	YGL180W	ATG1
+Q06159	YLR312C	ATG39
+P53867	YNL223W	ATG4
+Q12380	YPL149W	ATG5
+P53722	YNR020C	ATP23
+Q12092	YPL166W	ATG29
+P40458	YIL146C	ATG32
+P46983	YJL185C	ATG36
+Q12048	YPL250C	ATG41
+P38862	YHR171W	ATG7
+P38182	YBL078C	ATG8
+Q12691	YDR038C	ENA5
+P32453	YNL315C	ATP11
+P00854	Q0085	ATP6
+Q12165	YDL004W	ATP16
+Q06405	YDR377W	ATP17
+P31386	YAL020C	ATS1
+P38636	YNL259C	ATX1
+P40851	YPR122W	AXL1
+Q06541	YLR242C	ARV1
+Q06822	YPR085C	ASA1
+P46993	YJL170C	ASG7
+P54074	YMR119W	ASI1
+P48361	YGR097W	ASK10
+P32660	YER166W	DNF1
+Q12674	YMR162C	DNF3
+Q03153	YMR098C	ATP25
+P30902	YKL016C	ATP7
+P00856	Q0080	ATP8
+Q12406	YPR034W	ARP7
+P40518	YIL062C	ARC15
+Q06598	YPR201W	ARR3
+Q8TGM7	YLR154W-A	ART2
+P35734	YKL052C	ASK1
+P35183	YBL069W	AST1
+P40353	YOR377W	ATF1
+P53855	YNL242W	ATG2
+Q12292	YOL083W	ATG34
+Q05789	YLR211C	ATG38
+Q01896	YDR039C	ENA2
+P22135	YJL180C	ATP12
+P38360	YBR295W	PCA1
+P32450	YFL010W-A	AUA1
+P36107	YKL004W	AUR1
+P39981	YEL064C	AVT2
+P36062	YKL146W	AVT3
+P53629	YNR019W	ARE2
+P19146	YDL137W	ARF2
+P14843	YDR035W	ARO3
+P32448	YDL197C	ASF2
+P53895	YNL159C	ASI2
+Q04489	YML096W	
+P49089	YPR145W	ASN1
+P49090	YGR124W	ASN2
+P43601	YFR021W	ATG18
+Q02887	YPL100W	ATG21
+P25568	YCL038C	ATG22
+Q06485	YLR356W	ATG33
+P40344	YNR007C	ATG3
+P32907	YNR002C	ATO2
+Q12349	YLR295C	ATP14
+P32454	YKL157W	APE2
+P05085	YML099C	ARG81
+P32381	YDL029W	ARP2
+P47117	YJR065C	ARP3
+Q12509	YLR085C	ARP6
+P33204	YKL013C	ARC19
+P53244	YGR068C	ART5
+P53983	YNL008C	ASI3
+P0CZ17	YLR155C	ASP3-1
+P38929	YGL006W	PMC1
+P39524	YAL026C	DRS2
+P39986	YEL031W	SPF1
+Q01217	YER069W	ARG5,6
+Q02804	YPL051W	ARL3
+P28777	YGL148W	ARO2
+P18634	YLR392C	ART10
+P50275	YOR058C	ASE1
+P0CX77	YLR157C	ASP3-2
+P0CX78	YLR158C	ASP3-3
+P40416	YMR301C	ATM1
+P81450	YML081C-A	ATP18
+Q06321	YLR189C	ATG26
+Q12142	YDL149W	ATG9
+P38110	YBL088C	TEL1
+P13587	YDR040C	ENA1
+Q12359	YDR384C	ATO3
+P18496	YLR393W	ATP10
+P81451	YOL077W-A	ATP19
+P61829	Q0130	OLI1
+P22035	YKR099W	BAS1
+Q05029	YMR237W	BCH1
+P35817	YLR399C	BDF1
+P39714	YAL060W	BDH1
+P50273	YDR350C	ATP22
+P07251	YBL099W	ATP1
+P09457	YDR298C	ATP5
+P13090	YML116W	ATR1
+Q12067	YOR079C	ATX2
+Q12128	YOR134W	BAG7
+Q01389	YJL095W	BCK1
+P32839	YDR375C	BCS1
+P39713	YAL061W	BDH2
+Q08347	YOL164W	BDS1
+P38077	YBR039W	ATP3
+P81449	YDR322C-A	TIM11
+Q12226	YLL063C	AYT1
+P41815	YDR046C	BAP3
+P47068	YJL020C	BBC1
+Q08236	YOL078W	AVO1
+P47082	YJR001W	AVT1
+P38176	YBL089W	AVT5
+P50080	YGR224W	AZR1
+P38084	YBR068C	BAP2
+P39960	YER155C	BEM2
+P36149	YKR068C	BET3
+P47134	YJR089W	BIR1
+P47041	YJL058C	BIT61
+Q99177	YPR057W	BRR1
+P53062	YGL247W	BRR6
+Q08235	YOL077C	BRX1
+Q05611	YDR275W	BSC2
+Q08280	YOL137W	BSC6
+P47176	YJR148W	BAT2
+P15703	YGR282C	BGL2
+P50277	YNR058W	BIO3
+Q08965	YPL217C	BMS1
+P47039	YJL060W	BNA3
+P40450	YIL159W	BNR1
+Q07457	YDL074C	BRE1
+Q07660	YDL231C	BRE4
+Q12140	YDL037C	BSC1
+P53755	YNR069C	BSC5
+Q06604	YPR171W	BSP1
+P25627	YCR047C	BUD23
+P50944	YNL101W	AVT4
+P40501	YIL088C	AVT7
+P41696	YOR113W	AZF1
+Q12365	YPL255W	BBP1
+Q3E793	YAL044W-A	BOL1
+P38928	YIL140W	AXL2
+P36122	YKR027W	BCH2
+P33306	YER167W	BCK2
+Q07442	YDL070W	BDF2
+P53858	YNL233W	BNI4
+P53958	YNL042W	BOP3
+Q06338	YDR361C	BCP1
+P47113	YJR053W	BFA1
+P40013	YER016W	BIM1
+P38346	YBR270C	BIT2
+P35727	YKL061W	BLI1
+P40471	YIL124W	AYR1
+P29366	YBR200W	BEM1
+P39011	YPL161C	BEM4
+Q03630	YML077W	BET5
+P38813	YHR101C	BIG1
+P53744	YNR056C	BIO5
+P43583	YFL007W	BLM10
+P47040	YJL059W	YHC3
+P41695	YGR188C	BUB1
+P39988	YEL029C	BUD16
+Q04347	YMR014W	BUD22
+P85052	YER014C-A	BUD25
+P33314	YKL092C	BUD2
+P47136	YJR092W	BUD4
+P41697	YLR319C	BUD6
+P38822	YHR114W	BZZ1
+Q04749	YMR068W	AVO2
+P40074	YER119C	AVT6
+P12630	YIL015W	BAR1
+Q12186	YLR116W	MSL5
+P38891	YHR208W	BAT1
+P38772	YHR040W	BCD1
+P32873	YPL115C	BEM3
+P22804	YIL004C	BET1
+Q06631	YDR299W	BFR2
+P11709	YCL029C	BIK1
+P32451	YGR286C	BIO2
+P40493	YIL096C	BMT5
+P39724	YAL046C	BOL3
+P26449	YOR026W	BUB3
+Q08492	YOR078W	BUD21
+Q05949	YLR226W	BUR2
+P40580	YIR036C	IRC24
+P09440	YBR084W	MIS1
+P43569	YFL028C	CAF16
+P53615	YNL036W	NCE103
+P07252	YJL209W	CBP1
+P0C155	YOL153C	
+P27614	YJL172W	CPS1
+P00729	YMR297W	PRC1
+P14905	YDR197W	CBS2
+P34730	YDR099W	BMH2
+P38041	YBL085W	BOI1
+P48558	YNL305C	BXI1
+P53836	YNL278W	CAF120
+P39101	YER048C	CAJ1
+P17555	YNL138W	SRV2
+P06787	YBR109C	CMD1
+P27825	YAL058W	CNE1
+P04817	YEL063C	CAN1
+P28495	YKL007W	CAP1
+P34237	YKL179C	COY1
+P15202	YDR256C	CTA1
+P53630	YNR057C	BIO4
+Q06071	YLR408C	BLS1
+Q01532	YNL239W	LAP3
+P29311	YER177W	BMH1
+P48445	YDL141W	BPL1
+P48582	YPL084W	BRO1
+P32639	YER172C	BRR2
+O13558	YLR465C	BSC3
+Q07992	YLR062C	BUD28
+Q12064	YDL151C	BUD30
+P25558	YCL014W	BUD3
+Q12191	YDL099W	BUG1
+Q03758	YML111W	BUL2
+P12962	YOR276W	CAF20
+P03965	YJR109C	CPA2
+P38278	YBR141C	BMT2
+Q12291	YLR063W	BMT6
+P53890	YNL166C	BNI5
+P39969	YER114C	BOI2
+P43132	YLR015W	BRE2
+P53841	YNL269W	BSC4
+P38356	YBR290W	BSD2
+O94143	YJL188C	BUD19
+Q08004	YLR074C	BUD20
+Q03783	YDR241W	BUD26
+P43573	YFL023W	BUD27
+P53323	YGR262C	BUD32
+P41698	YLR353W	BUD8
+P53226	YGR041W	BUD9
+P48524	YMR275C	BUL1
+P07245	YGR204W	ADE3
+P36076	YKL088W	CAB3
+Q03941	YDR196C	CAB5
+P13517	YIL034C	CAP2
+P07258	YOR303W	CPA1
+P38995	YDR270W	CCC2
+Q02948	YPL120W	VPS30
+P38934	YOR198C	BFR1
+Q06333	YDR357C	CNL1
+Q04199	YML102W	CAC2
+Q06150	YLR267W	BOP2
+P53741	YNR051C	BRE5
+P43571	YFL025C	BST1
+P36130	YKR036C	CAF4
+P41832	YNL271C	BNI1
+P50084	YGR230W	BNS1
+P53838	YNL275W	BOR1
+P25385	YLR078C	BOS1
+P14772	YLL015W	BPT1
+P38770	YHR036W	BRL1
+P53194	YGL007W	BRP1
+P53286	YGR142W	BTN2
+P53727	YNR027W	BUD17
+P25337	YCR063W	BUD31
+P25300	YCR038C	BUD5
+Q08754	YOR299W	BUD7
+P23293	YPR161C	SGV1
+P36106	YKL005C	BYE1
+Q05791	YLR215C	CDC123
+P32797	YDL220C	CDC13
+P25656	YCR094W	CDC50
+P09119	YJL194W	CDC6
+P53197	YGL003C	CDH1
+P47112	YJR046W	TAH11
+Q12453	YOR112W	CEX1
+Q06632	YDR301W	CFT1
+P13365	YAL040C	CLN3
+P53188	YGL029W	CGR1
+P07267	YPL154C	PEP4
+P39113	YMR280C	CAT8
+P35203	YMR094W	CTF13
+P32582	YGR155W	CYS4
+P21269	YER168C	CCA1
+Q06703	YLR308W	CDA2
+P27636	YAR019C	CDC15
+P40986	YDR182W	CDC1
+P04821	YLR310C	CDC25
+P25694	YDL126C	CDC48
+P06243	YDL017W	CDC7
+P53829	YNL288W	CAF40
+P43568	YFL029C	CAK1
+P53223	YGR036C	CAX4
+P40969	YMR168C	CEP3
+P53894	YNL161W	CBK1
+P03874	YHL038C	CBP2
+P11433	YAL041W	CDC24
+P38042	YBL084C	CDC27
+Q06549	YLR245C	CDD1
+P20438	YPL256C	CLN2
+P24869	YPR119W	CLB2
+P80235	YAR035W	YAT1
+P32796	YML042W	CAT2
+P25296	YKL190W	CNB1
+P07253	YBR120C	CBP6
+P36038	YKL208W	CBT1
+P37366	YPR025C	CCL1
+P37267	YGR174C	CBP4
+P48237	YGR150C	CCM1
+P31384	YAL021C	CCR4
+Q12127	YLR110C	CCW12
+P32457	YLR314C	CDC3
+Q06697	YLR418C	CDC73
+P41733	YLR459W	GAB1
+P17106	YJR060W	CBF1
+Q03702	YKL011C	CCE1
+P38273	YBR131W	CCZ1
+Q06702	YLR307W	CDA1
+P25342	YCR002C	CDC10
+P32468	YHR107C	CDC12
+P09798	YKL022C	CDC16
+P16522	YHR166C	CDC23
+P06704	YOR257W	CDC31
+P53082	YGL220W	BOL2
+P25356	YCR032W	BPH1
+P26448	YMR055C	BUB2
+P27637	YAR014C	BUD14
+P47158	YJR122W	IBA57
+P53934	YNL092W	
+P06115	YGR088W	CTT1
+P32504	YGR140W	CBF2
+P33322	YLR175W	CBF5
+P14066	YDL069C	CBS1
+P50077	YGR217W	CCH1
+P00431	YKR066C	CCP1
+Q7LHD1	YDR134C	CCW22
+P21560	YPL215W	CBP3
+P19073	YLR229C	CDC42
+P32458	YJR076C	CDC11
+P14724	YFR036W	CDC26
+P06101	YDR168W	CDC37
+Q12018	YDL132W	CDC53
+P38910	YOR020C	HSP10
+P47818	YLR220W	CCC1
+P06182	YAL039C	CYC3
+P40202	YMR038C	CCS1
+O13547	YLR390W-A	CCW14
+Q00684	YFR028C	CDC14
+P26309	YGL116W	CDC20
+O13297	YPL228W	CET1
+P20437	YMR199W	CLN1
+P29029	YLR286C	CTS1
+P32178	YPR060C	ARO7
+Q12114	YLR330W	CHS5
+P38843	YHR142W	CHS7
+P35190	YGL215W	CLG1
+Q03654	YMR213W	CEF1
+Q12102	YLR115W	CFT2
+P24868	YGR108W	CLB1
+P24870	YDL155W	CLB3
+P30283	YPR120C	CLB5
+P43634	YLR098C	CHA4
+P22516	YPL008W	CHL1
+Q08032	YLR103C	CDC45
+P07834	YFL009W	CDC4
+P32562	YMR001C	CDC5
+P36012	YKL049C	CSE4
+Q03705	YML036W	CGI121
+P24871	YLR210W	CLB4
+P38221	YBR029C	CDS1
+P39525	YER061C	CEM1
+P40558	YIL003W	CFD1
+P32656	YER163C	GCG1
+Q05583	YDR267C	CIA1
+P53280	YGR134W	CAF130
+P32943	YGR109C	CLB6
+P08004	YNL192W	CHS1
+P14180	YBR038W	CHS2
+P38147	YBR274W	CHK1
+P38907	YDR254W	CHL4
+P40955	YJL099W	CHS6
+P20486	YBR135W	CKS1
+P53264	YGR110W	CLD1
+P38323	YBR227C	MCX1
+P33313	YBR155W	CNS1
+Q3E823	YPL189C-A	COA2
+Q3E7B2	YJL062W-A	COA3
+Q3E846	YMR244C-A	COA6
+Q12309	YLR117C	CLF1
+Q08685	YOR250C	CLP1
+P32657	YER164W	CHD1
+Q06350	YDR371W	CTS2
+P05374	YGR157W	CHO2
+P29465	YBR023C	CHS3
+P40019	YER030W	CHZ1
+P43635	YPR001W	CIT3
+Q07897	YLR003C	CMS1
+Q01649	YMR198W	CIK1
+P40987	YOR349W	CIN1
+P27895	YEL061C	CIN8
+P48562	YNL298W	CLA4
+P22137	YGL206C	CHC1
+D6W196	YNL083W	SAL1
+Q08058	YOL008W	COQ10
+P53318	YGR255C	COQ6
+Q05779	YLR201C	COQ9
+Q06156	YLR272C	YCS4
+P53079	YGL223C	COG1
+P38779	YHR052W	CIC1
+P00890	YNR001C	CIT1
+Q3E7A9	YMR194C-B	CMC4
+Q12510	YDL156W	CMR1
+Q06680	YDR325W	YCG1
+P39110	YMR138W	CIN4
+P47001	YJL158C	CIS3
+Q03690	YMR012W	CLU1
+P53865	YNL225C	CNM67
+P41810	YDR238C	SEC26
+P40509	YIL076W	SEC28
+O13525	YDR204W	COQ4
+P41735	YOR125C	CAT5
+Q01519	YLR038C	COX12
+Q03048	YLL050C	COF1
+P53622	YDL145C	COP1
+P00401	Q0045	COX1
+P32344	YLR204W	QRI5
+P38287	YBR161W	CSH1
+P43639	YGL019W	CKB1
+P46946	YGL175C	SAE2
+P32074	YNL287W	SEC21
+Q05892	YLR290C	COQ11
+P18900	YBR003W	COQ1
+P27697	YGL119W	COQ8
+P52924	YNR075W	COS10
+P43542	YFL062W	COS4
+P53344	YGR295C	COS6
+P32798	YOR316C	COT1
+P47081	YJL003W	COX16
+Q12287	YLL009C	COX17
+P04037	YGL187C	COX4
+P00424	YNL052W	COX5A
+P00425	YIL111W	COX5B
+P04039	YLR395C	COX8
+P10614	YHR007C	ERG11
+P17898	YNL130C	CPT1
+P08679	YCR005C	CIT2
+P17891	YGR167W	CLC1
+P53332	YGR277C	CAB4
+P43618	YFR046C	CNN1
+P40452	YIL157C	COA1
+Q05809	YLR218C	COA4
+P53600	YPL010W	RET3
+P53239	YGR062C	COX18
+Q3E731	YLL018C-A	COX19
+P00410	Q0250	COX2
+P00420	Q0275	COX3
+P41811	YGL137W	SEC27
+P27680	YOL096C	COQ3
+P49017	YML110C	COQ5
+P53053	YGL263W	COS12
+P0CX13	YML132W	COS3
+Q07788	YDL248W	COS7
+P39103	YML129C	COX14
+P38170	YBL097W	BRN1
+Q06096	YPR105C	COG4
+P53195	YGL005C	COG7
+Q04935	YDR231C	COX20
+Q3E7A4	YBL059C-A	CMC2
+P53951	YNL051W	COG5
+P43621	YFR051C	RET2
+P32378	YNR041C	COQ2
+P00427	YHR051W	COX6
+P21595	YDR402C	DIT2
+P38930	YOR039W	CKB2
+P40465	YIL132C	CSM2
+Q06705	YLR380W	CSR1
+P47976	YDR151C	CTH1
+Q03957	YKL139W	CTK1
+P38428	YMR264W	CUE1
+P40094	YER157W	COG3
+P53959	YNL041C	COG6
+Q06440	YLR429W	CRN1
+P53822	YNL336W	COS1
+P47187	YJR161C	COS5
+P38723	YHL048W	COS8
+P21592	YPL172C	COX10
+P40086	YER141W	COX15
+P10174	YMR256C	COX7
+Q12150	YLR087C	CSF1
+P15790	YIL035C	CKA1
+P19454	YOR061W	CKA2
+Q12748	YLR381W	CTF3
+P47977	YLR136C	TIS11
+Q08923	YPL181W	CTI6
+Q12734	YPR030W	CSR2
+Q06032	YLR394W	CST9
+Q02732	YPL018W	CTF19
+P46962	YJL006C	CTK2
+Q03220	YMR180C	CTL1
+P38818	YHR109W	CTM1
+P41817	YPL177C	CUP9
+P53333	YGR278W	CWC22
+P25603	YCL007C	CWH36
+P25618	YCR017C	CWH43
+P53271	YGR120C	COG2
+Q04632	YML071C	COG8
+P07255	YDL067C	COX9
+P36064	YKL137W	CMC1
+P38845	YHR146W	CRP1
+P41902	YOR031W	CRS5
+P33307	YGL238W	CSE1
+P43497	YKL096W-A	CWP2
+P0CX12	YBR302C	COS2
+P36034	YKL219W	COS9
+P19516	YPL132W	COX11
+P32799	YGL191W	COX13
+P38824	YHR116W	COX23
+P53314	YGR247W	CPD1
+Q12289	YOR100C	CRC1
+P38892	YHR209W	CRG1
+P53968	YNL027W	CRZ1
+Q08054	YOL007C	CSI2
+Q12348	YOL117W	RRI2
+P14306	YLR178C	TFS1
+P53301	YGR189C	CRH1
+Q06538	YLR241W	CSC1
+P35206	YBR036C	CSG2
+P25651	YCR086W	CSM1
+Q08955	YPL200W	CSM4
+P47130	YJR084W	CSN12
+Q12468	YDL216C	RRI1
+P25355	YCR054C	CTR86
+P53923	YNL119W	NCS2
+P53830	YNL286W	CUS2
+P00044	YJR048W	CYC1
+P32898	YDR430C	CYM1
+P32623	YEL040W	UTR2
+Q05790	YLR213C	CRR1
+P38308	YBR203W	COS111
+Q04368	YMR025W	CSI1
+P49573	YPR124W	CTR1
+P38865	YHR175W	CTR2
+P89105	YOL145C	CTR9
+Q04201	YML101C	CUE4
+Q08412	YOR042W	CUE5
+P47050	YJL047C	RTT101
+P28320	YKL095W	YJU2
+P53854	YNL245C	CWC25
+Q12046	YDL209C	CWC2
+P53008	YGL027C	CWH41
+P28319	YKL096W	CWP1
+Q07560	YDL142C	CRD1
+Q08226	YOL063C	CRT10
+P53859	YNL232W	CSL4
+Q03981	YDR179C	CSN9
+P38226	YBR042C	CST26
+P36075	YKL090W	CUE2
+Q06469	YPR158W	CUR1
+P21657	YIR023W	DAL81
+P47179	YJR151C	DAN4
+P22204	YGR092W	DBF2
+P36120	YKR024C	DBP7
+P24309	YKL149C	DBR1
+P32347	YDR047W	HEM12
+P36091	YKL046C	DCW1
+Q99321	YOR163W	DDP1
+P53899	YNL155W	CUZ1
+P08678	YJL005W	CYR1
+P00163	Q0105	COB
+P53206	YGR012W	
+Q00873	YKL087C	CYT2
+P43550	YFL053W	DAK2
+P47178	YJR150C	DAN1
+P18962	YHR028C	DAP2
+P47005	YJL149W	DAS1
+Q12084	YDR020C	DAS2
+Q12517	YOL149W	DCP1
+Q12123	YOR173W	DCS2
+P06773	YHR144C	DCD1
+P38877	YHR191C	CTF8
+P46963	YML112W	CTK3
+Q06686	YLR411W	CTR3
+P53088	YGL211W	NCS6
+P53137	YGL110C	CUE3
+P15315	YGL166W	CUP2
+Q03772	YDR163W	CWC15
+P46947	YGL174W	BUD13
+Q02770	YPL064C	CWC27
+P07143	YOR065W	CYT1
+P38909	YOR037W	CYC2
+P15365	YJR152W	DAL5
+P26343	YKR034W	DAL80
+Q12091	YPL170W	DAP1
+P24784	YPL119C	DBP1
+Q06218	YLR276C	DBP9
+Q04895	YIR028W	DAL4
+Q12389	YDL031W	DBP10
+P24783	YNL112W	DBP2
+P20447	YGL078C	DBP3
+P20449	YOR046C	DBP5
+P53734	YNR038W	DBP6
+P21182	YOL052C	SPE2
+P25559	YCL016C	DCC1
+P08432	YKL184W	SPE1
+Q05924	YLR361C	DCR2
+P06634	YOR204W	DED1
+P38307	YBR201W	DER1
+Q04930	YDR223W	CRF1
+Q04659	YMR048W	CSM3
+P40512	YIL071C	PCI8
+P49956	YMR078C	CTF18
+Q01454	YPR135W	CTF4
+Q03375	YDR482C	CWC21
+P53769	YLR323C	CWC24
+P00045	YEL039C	CYC7
+P47103	YJR032W	CPR7
+P35176	YDR304C	CPR5
+P14832	YDR155C	CPR1
+P31373	YAL012W	CYS3
+Q12248	YDR016C	DAD1
+P69850	YBR233W-A	DAD3
+P25334	YCR069W	CPR4
+P06106	YLR303W	MET17
+P38719	YHR169W	DBP8
+P32460	YIR030C	DCG1
+P0CH63	YFL061W	DDI2
+Q99288	YDR051C	DET1
+Q05080	YMR032W	HOF1
+P53728	YNR028W	CPR8
+P23285	YHR057C	CPR2
+P25719	YML078W	CPR3
+P21705	YNL314W	DAL82
+P20448	YJL033W	HCA4
+Q08558	YOR180C	DCI1
+P40087	YER143W	DDI1
+P69851	YDR320C-A	DAD4
+P32328	YPR111W	DBF20
+P33750	YLL011W	SOF1
+P53550	YNL118C	DCP2
+P18899	YMR173W	DDR48
+P31385	YAL013W	DEP1
+P36108	YKL002W	DID4
+P52868	YGL128C	CWC23
+P40312	YNL111C	CYB5
+P14922	YBR112C	CYC8
+Q07533	YDL117W	CYK3
+P36162	YKR083C	DAD2
+P53267	YGR113W	DAM1
+P13483	YML113W	DAT1
+P53202	YGR003W	CUL3
+Q02554	YMR240C	CUS1
+P00175	YML054C	CYB2
+P54838	YML070W	DAK1
+Q12382	YOR311C	DGK1
+Q3E808	YNL130C-A	DGR1
+P21623	YDR403W	DIT1
+P54861	YLL001W	DNM1
+P40059	YER088C	DOT6
+P47027	YJL090C	DPB11
+P32469	YLR172C	DPH5
+P38332	YBR246W	RRT2
+P32892	YLL008W	DRS1
+P23501	YKR053C	YSR3
+P53720	YNR015W	SMM1
+P07262	YOR375C	GDH1
+P37298	YDR178W	SDH4
+Q08496	YOR080W	DIA2
+Q12086	YDR263C	DIN7
+P04819	YDL164C	CDC9
+Q08387	YOR005C	DNL4
+P38821	YHR113W	APE4
+P38774	YHR044C	DOG1
+Q03921	YDR141C	DOP1
+P46957	YJR006W	POL31
+P15801	YOR330C	MIP1
+P36152	YKR071C	DRE2
+Q04792	YMR250W	GAD1
+P35732	YKL054C	DEF1
+Q99234	YOR030W	DFG16
+P32330	YKL121W	DGR2
+P39708	YAL062W	GDH3
+Q04603	YDR121W	DPB4
+Q3E840	YBL071W-A	KTI11
+P39517	YDL160C	DHH1
+Q04217	YMR128W	ECM16
+P35497	YJR159W	SOR1
+O13577	YLR437C	DIF1
+P40318	YIL030C	SSM4
+P47110	YJR043C	POL32
+P14284	YPL167C	REV3
+P53255	YGR093W	DRN1
+P32325	YDR052C	DBF4
+P47089	YJR014W	TMA22
+Q12743	YDR411C	DFM1
+Q07786	YDL246C	SOR2
+P38791	YHR068W	DYS1
+Q03373	YDR480W	DIG2
+P40366	YJL065C	DLS1
+Q06819	YPR082C	DIB1
+P40564	YIR004W	DJP1
+P39976	YEL071W	DLD3
+Q04216	YMR126C	DLT1
+Q03652	YMR211W	DML1
+P31116	YJR139C	HOM6
+Q06143	YLR348C	DIC1
+P36037	YKL213C	DOA1
+P33309	YNL001W	DOM34
+Q12395	YLR128W	DCN1
+Q06151	YLR270W	DCS1
+P0CH64	YNL335W	DDI3
+P89113	YOL052C-A	DDR2
+P54005	YMR316W	DIA1
+P69771	YKR035W-A	DID2
+P32891	YDL174C	DLD1
+P09624	YFL018C	LPD1
+Q07505	YDL086W	
+P38823	YHR115C	DMA1
+P25453	YER179W	DMC1
+P43595	YFR012W	DCV1
+Q08949	YPL194W	DDC1
+P40526	YIL049W	DFG10
+Q05031	YMR238W	DFG5
+Q08650	YOR245C	DGA1
+P13663	YDR158W	HOM2
+P33327	YDL215C	GDH2
+P36009	YKL078W	DHR2
+Q03063	YPL049C	DIG1
+P41819	YPL266W	DIM1
+P53388	YPL265W	DIP5
+P46681	YDL178W	DLD2
+P53924	YNL116W	DMA2
+P38859	YHR164C	DNA2
+P53871	YNL191W	DUG3
+Q04110	YDR446W	ECM11
+Q06011	YLR390W	ECM19
+Q03214	YMR176W	ECM5
+P33412	YGR007W	ECT1
+P40023	YER035W	EDC2
+P02994	YPR080W; YBR118W	TEF1; TEF2
+P25039	YLR069C	MEF1
+P38347	YBR271W	EFM2
+P40516	YIL064W	EFM4
+P53970	YNL024C	EFM6
+Q03653	YMR212C	EFR3
+P09032	YOR260W	GCD1
+Q05610	YDR273W	DON1
+P32461	YKL191W	DPH2
+P38121	YBL035C	POL12
+P13382	YNL102W	POL1
+Q05521	YDR284C	DPP1
+Q08729	YOR264W	DSE3
+P48510	YMR276W	DSK2
+P40568	YIR010W	DSN1
+P33413	YHL016C	DUR3
+Q06063	YLR405W	DUS4
+P47128	YJR082C	EAF6
+P36049	YKL172W	EBP2
+P48235	YGR146C	ECL1
+Q04623	YDR125C	ECM18
+P32525	YJL201W	ECM25
+Q99252	YOR092W	ECM3
+Q3E705	YGR271C-A	EFG1
+P53168	YGL061C	DUO1
+Q06053	YLR401C	DUS3
+P36041	YKL204W	EAP1
+P38195	YBL043W	ECM13
+P35195	YBL001C	ECM15
+P47144	YJR106W	ECM27
+Q02202	YKR004C	ECM9
+P38073	YBR033W	EDS1
+P42835	YNL327W	EGT2
+P47120	YJR070C	LIA1
+P27344	YBR278W	DPB3
+P40487	YIL103W	DPH1
+Q12429	YLR143W	DPH6
+Q08225	YOL057W	
+P47013	YJL134W	LCB3
+P38844	YHR143W	DSE2
+P39112	YMR287C	DSS1
+P38125	YBR180W	DTR1
+P43616	YFR044C	DUG1
+P32528	YBR208C	DUR1,2
+P33317	YBR252W	DUT1
+P36022	YKR054C	DYN1
+P53759	YML080W	DUS1
+Q06349	YDR370C	DXO1
+P53063	YGL246C	RAI1
+Q06337	YDR359C	EAF1
+P39995	YEL018W	EAF5
+P53911	YNL136W	EAF7
+Q03212	YMR171C	EAR1
+Q05871	YLR284C	ECI1
+P38167	YBL101C	ECM21
+P38737	YHL030W	ECM29
+P38246	YBR076W	ECM8
+P38732	YHL039W	EFM1
+P53235	YGR054W	
+P32497	YMR309C	NIP1
+Q12050	YOR144C	ELG1
+P25574	YCL045C	EMC1
+P47133	YJR088C	EMC2
+P53095	YGL196W	DSD1
+P40077	YER124C	DSE1
+P0CX08	YEL070W	DSF1
+Q04949	YMR299C	DYN3
+Q12432	YPR023C	EAF3
+Q03466	YDR206W	EBS1
+P32471	YAL003W	EFB1
+P29547	YPL048W	CAM1
+P32324	YOR133W; YDR385W	EFT1; EFT2
+P47163	YJR129C	EFM3
+P53200	YGR001C	EFM5
+Q05874	YLR285W	NNT1
+P54858	YDR068W	DOS2
+P40553	YIL010W	DOT5
+P24482	YPR175W	DPB2
+P25615	YCR014C	POL4
+P39985	YEL055C	POL5
+P21951	YNL262W	POL2
+P38213	YBR007C	DSF2
+P53847	YNL258C	DSL1
+Q02647	YDR424C	DYN2
+P07807	YOR236W	DFR1
+Q06673	YLR436C	ECM30
+P38728	YHL043W	ECM34
+Q05902	YLR299W	ECM38
+P38773	YHR043C	DOG2
+Q04089	YDR440W	DOT1
+P47138	YJR097W	JJJ3
+P14020	YPR183W	DPM1
+P15436	YDL102W	POL3
+P32601	YPR017C	DSS4
+Q07648	YDL219W	DTD1
+P38149	YBR281C	DUG2
+P39009	YDL101C	DUN1
+Q04067	YDR429C	TIF35
+Q03764	YDR147W	EKI1
+Q02884	YPL101W	ELP4
+Q04409	YDR516C	EMI2
+P38333	YBR247C	ENP1
+P43572	YFL024C	EPL1
+P41912	YOL110W	SHR5
+P32352	YMR202W	ERG2
+P54781	YMR015C	ERG5
+P62651	YPL096C-A	ERI1
+P43613	YFR041C	ERJ5
+P53080	YGL222C	EDC1
+P39998	YEL015W	EDC3
+P14741	YKR026C	GCN3
+P32501	YDR211W	GCD6
+Q05775	YLR192C	HCR1
+P36053	YKL160W	ELF1
+P25358	YCR034W	ELO2
+P39013	YNL084C	END3
+P32626	YEL038W	UTR4
+Q05785	YLR206W	ENT2
+P53246	YGR071C	ENV11
+Q12003	YPL236C	ENV7
+O13529	YHR021W-A	ECM12
+P39715	YAL059W	ECM1
+Q02710	YPL021W	ECM23
+P34216	YBL047C	EDE1
+P36008	YKL081W	TEF4
+P53978	YNL014W	HEF3
+P12754	YGR083C	GCD2
+P32801	YKL048C	ELM1
+P42935	YGR200C	ELP2
+P40540	YIL027C	EMC5
+Q12431	YLL014W	EMC6
+P42842	YNL313C	EMW1
+P18414	YBL040C	ERD2
+Q06551	YLR246W	ERF2
+P32476	YGR175C	ERG1
+P53199	YGL001C	ERG26
+P0CX10	YOR393W	ERR1
+P53337	YGR284C	ERV29
+Q12168	YLR144C	ACF2
+Q99382	YLR065C	ENV10
+P22140	YHR123W	EPT1
+P38819	YHR110W	ERP5
+P38312	YBR210W	ERV15
+Q08649	YOR244W	ESA1
+Q06340	YDR363W	ESC2
+Q06344	YDR365C	ESF1
+P22696	YJR017C	ESS1
+P32474	YDR518W	EUG1
+P02992	YOR187W	TUF1
+Q06706	YLR384C	IKI3
+Q02908	YPL086C	ELP3
+P00925	YHR174W	ENO2
+Q12518	YDL161W	ENT1
+P47160	YJR125C	ENT3
+Q03769	YDR153C	ENT5
+Q08651	YOR246C	ENV9
+P25340	YGL012W	ERG4
+P25087	YML008C	ERG6
+P24521	YMR220W	ERG8
+Q12450	YOR016C	ERP4
+P40456	YIL151C	ESL1
+Q03018	YGR098C	ESP1
+Q07872	YLL038C	ENT4
+P40557	YIL005W	EPS1
+P38767	YHR032W	ERC1
+P32462	YNL280C	ERG24
+P38604	YHR072W	ERG7
+P53198	YGL002W	ERP6
+P0CX11	YPL281C	ERR2
+Q04651	YML067C	ERV41
+P36168	YKR096W	ESL2
+Q03096	YIL009C-A	EST3
+P38836	YHR132C	ECM14
+Q05958	YLR228C	ECM22
+P32644	YER176W	ECM32
+P38248	YBR078W	ECM33
+Q06200	YLR443W	ECM7
+P43605	YFR027W	ECO1
+P38249	YBR079C	RPG1
+P40217	YMR146C	TIF34
+Q05050	YMR031C	EIS1
+P40319	YLR372W	ELO3
+P53861	YNL230C	ELA1
+P43555	YFL048C	EMP47
+P53753	YNR067C	DSE4
+P06103	YOR361C	PRT1
+P39540	YJL196C	ELO1
+P38874	YHR187W	IKI1
+P53073	YGL231C	EMC4
+Q12396	YLR080W	EMP46
+P00924	YGR254W	ENO1
+P32353	YLR056W	ERG3
+Q12403	YDL018C	ERP3
+Q12284	YPR037C	ERV2
+Q12480	YPR004C	AIM45
+Q03071	YPL046C	ELC1
+Q04868	YMR312W	ELP6
+P36039	YKL207W	EMC3
+Q04406	YDR512C	EMI1
+P32803	YGL200C	EMP24
+Q08299	YOL158C	ENB1
+P53938	YNL080C	EOS1
+P16151	YDR414C	ERD1
+Q12452	YLR100W	ERG27
+Q05359	YAR002C-A	ERP1
+P38748	YHL010C	ETP1
+P38071	YBR026C	ETR1
+P23776	YLR300W	EXG1
+P52911	YDR261C	EXG2
+Q04660	YMR049C	ERB1
+P05453	YDR172W	SUP35
+P42222	YMR323W	ERR3
+P38140	YBR239C	ERT1
+P27882	YGR029W	ERV1
+P39727	YAL042W	ERV46
+P19097	YPL231W	FAS2
+Q12283	YOR221C	MCT1
+P53917	YNL127W	FAR11
+P21268	YJL157C	FAR1
+P43592	YFR008W	FAR7
+P15646	YDL014W	NOP1
+Q03034	YDR539W	FDC1
+P29704	YHR190W	ERG9
+P26793	YKL113C	RAD27
+P40988	YMR319C	FET4
+P53918	YNL125C	ESBP6
+Q08119	YOL017W	ESC8
+P17214	YLR233C	EST1
+Q08822	YOR356W	CIR2
+P35731	YKL055C	OAR1
+P38913	YDL045C	FAD1
+P38224	YBR040W	FIG1
+P40020	YER032W	FIR1
+Q08906	YOR382W	FIT2
+P12385	YBR143C	SUP45
+P40030	YER044C	ERG28
+Q03103	YML130C	ERO1
+P39704	YAL007C	ERP2
+P17261	YCR075C	ERS1
+P53173	YGL054C	ERV14
+Q03661	YMR219W	ESC1
+P53743	YNR054C	ESF2
+P42940	YGR207C	CIR1
+Q08421	YOR051C	ETT1
+P39875	YOR033C	EXO1
+P38289	YBR163W	EXO5
+P38261	YBR102C	EXO84
+P09201	YLR377C	FBP1
+P34756	YFR019W	FAB1
+P32771	YDL168W	SFA1
+P32604	YJL155C	FBP26
+Q12099	YDR021W	FAL1
+Q04952	YMR306W	FKS3
+P36170	YKR102W	FLO10
+P08640	YIR019C	FLO11
+P32768	YAR050W	FLO1
+Q08023	YLR077W	FMP25
+P43557	YFL046W	FMP32
+P53233	YGR052W	FMP48
+P50264	YMR020W	FMS1
+P40546	YIL019W	FAF1
+P46671	YMR052W	FAR3
+Q05040	YMR029C	FAR8
+P38137	YBR222C	PCS60
+Q12178	YPR062W	FCY1
+P25621	YCR028C	FEN2
+Q08907	YOR383C	FIT3
+P19658	YJL085W	EXO70
+P53971	YNL023C	FAP1
+Q05498	YDR339C	FCF1
+Q03254	YMR277W	FCP1
+Q12119	YER060W-A	FCY22
+Q06001	YLR238W	FAR10
+P17064	YER056C	FCY2
+P0CF35	YPL275W	FDH2
+P39676	YGR234W	YHB1
+P07149	YKL182W	FAS1
+P40039	YER060W	FCY21
+Q08991	YPL279C	FEX2
+P25653	YCR089W	FIG2
+P42837	YNL325C	FIG4
+P38911	YML074C	FPR3
+P20081	YNL135C	FPR1
+P38631	YLR342W	FKS1
+P40068	YER109C	FLO8
+P53279	YGR131W	FHN1
+Q08645	YOR241W	MET7
+P08524	YJL167W	ERG20
+Q07825	YLL029W	FRA1
+P32791	YLR214W	FRE1
+P53746	YNR060W	FRE4
+P08417	YPL262W	FUM1
+P28003	YAL034C	FUN19
+P11412	YNL241C	ZWF1
+P04385	YBR020W	GAL1
+P04386	YPL248C	GAL4
+Q04739	YER027C	GAL83
+P39719	YAL053W	FLC2
+P32785	YBL013W	FMT1
+Q02207	YKR009C	FOX2
+P36033	YKL220C	FRE2
+Q12473	YLL051C	FRE6
+Q12333	YOL152W	FRE7
+P12709	YBR196C	PGI1
+P17649	YGR019W	UGA1
+P38225	YBR041W	FAT1
+P38993	YMR058W	FET3
+Q08913	YOR390W	FEX1
+P39521	YPR104C	FHL1
+P32472	YDR519W	FPR2
+P53121	YGL139W	FLC3
+P40491	YIL098C	FMC1
+Q12497	YDR070C	FMP16
+P40008	YER004W	FMP52
+P22007	YDL090C	RAM1
+O13329	YDR110W	FOB1
+Q08911	YOR388C	FDH1
+P40466	YIL131C	FKH1
+Q08967	YPL221W	FLC1
+P53739	YNR047W	FPK1
+P23900	YLL043W	FPS1
+Q05015	YMR222C	FSH2
+Q99369	YOR280C	FSH3
+P38310	YBR207W	FTH1
+Q12247	YLR068W	FYV7
+P32805	YGL254W	FZF1
+P00358	YJR009C	TDH2
+P00359	YGR192C	TDH3
+P40569	YIR013C	GAT4
+P38260	YBR101C	FES1
+P43561	YFL041W	FET5
+P41813	YNL068C	FKH2
+P40989	YGR032W	GSC2
+Q12676	YMR113W	FOL3
+Q08905	YOR381W	FRE3
+Q08908	YOR384W	FRE5
+Q12209	YLR047C	FRE8
+Q03002	YPL141C	FRK1
+P37261	YCL026C-A	FRM2
+P32599	YDR129C	SAC6
+Q03898	YDR130C	FIN1
+Q04433	YDR534C	FIT1
+P39712	YAL063C	FLO9
+P03870	R0010W	FLP1
+P38124	YBR008C	FLR1
+Q06179	YLR454W	FMP27
+P46998	YJL161W	FMP33
+P53889	YNL168C	FMP41
+Q07651	YDL222C	FMP45
+P31380	YAL019W	FUN30
+Q12035	YLR051C	FCF2
+Q06205	YLR449W	FPR4
+P38866	YHR176W	FMO1
+Q08968	YPL222W	FMP40
+Q04991	YMR221C	FMP42
+P29703	YKL019W	RAM2
+P53848	YNL256W	FOL1
+P38894	YHR211W	FLO5
+P40464	YIL134W	FLX1
+P38231	YBR047W	FMP23
+Q02883	YPL103C	FMP30
+A0A023PZB3	YER038W-A	FMP49
+Q12029	YOR271C	FSF1
+P25659	YCR076C	FUB1
+P16892	YBL016W	FUS3
+P38783	YHR059W	FYV4
+P53913	YNL133C	FYV6
+P45976	YJR093C	FIP1
+P40515	YIL065C	FIS1
+P40098	YER182W	FMP10
+P36141	YKR049C	FMP46
+P36001	YKL132C	RMA1
+P40099	YER183C	FAU1
+P04397	YBR019C	GAL10
+P13181	YLR081W	GAL2
+P13045	YDR009W	GAL3
+P43574	YFL021W	GAT1
+P39012	YLR088W	GAA1
+P28006	YOR178C	GAC1
+P41913	YOR355W	GDS1
+Q08622	YOR205C	GEP3
+P40056	YER083C	GET2
+P14742	YKL104C	GFA1
+P40036	YER054C	GIP2
+P39732	YAL031C	GIP4
+P53849	YNL255C	GIS2
+P25346	YCR098C	GIT1
+Q12315	YDL207W	GLE1
+P36143	YKR058W	GLG1
+P38777	YHR049W	FSH1
+P05316	YBR021W	FUR4
+Q05670	YMR232W	FUS2
+Q08559	YOR183W	FYV12
+P25585	YCL058C	FYV5
+P46949	YGR196C	FYV8
+P00360	YJL052W	TDH1
+P08431	YBR018C	GAL7
+P04387	YML051W	GAL80
+P25555	YCL011C	GBP2
+P51601	YGR267C	FOL2
+Q07928	YLR013W	GAT3
+P33893	YBL080C	PET112
+P43535	YFR009W	GCN20
+P53171	YGL057C	GEP7
+P53192	YGL020C	GET1
+Q12154	YDL100C	GET3
+Q04839	YMR255W	GFD1
+P22146	YMR307W	GAS1
+Q06135	YLR343W	GAS2
+P18851	YOR212W	STE4
+P39993	YEL022W	GEA2
+P25370	YCL036W	GFD2
+Q12051	YPL069C	BTS1
+Q06648	YDR309C	GIC2
+Q03833	YDR096W	GIS1
+P38196	YBL042C	FUI1
+P11710	YCL027W	FUS1
+P40492	YIL097W	FYV10
+Q99341	YDR024W	FYV1
+P38297	YBR179C	FZO1
+P53260	YGR102C	GTF1
+P18852	YJR086W	STE18
+P38301	YBR187W	GDT1
+P47102	YJR031C	GEA1
+P38988	YDL198C	GGC1
+Q04233	YML006C	GIS4
+Q07540	YDL120W	YFH1
+P32614	YEL047C	FRD1
+P36088	YKL069W	
+P40088	YER145C	FTR1
+P18411	YAL008W	FUN14
+P31381	YAL022C	FUN26
+P19145	YKR039W	GAP1
+P28007	YHR089C	GAR1
+Q03655	YMR215W	GAS3
+P40209	YMR136W	GAT2
+P39726	YAL044C	GCV3
+Q08271	YOL132W	GAS4
+Q08193	YOL030W	GAS5
+Q03557	YMR293C	HER2
+P38011	YMR116C	ASC1
+P07261	YPL075W	GCR1
+P14065	YOR120W	GCY1
+P32775	YEL011W	GLC3
+P17695	YDR513W	GRX2
+P37303	YEL046C	GLY1
+P32191	YIL155C	GUT2
+P38875	YHR188C	GPI16
+P46961	YPL076W	GPI2
+P40106	YER062C	GPP2
+P35197	YDL226C	GCS1
+Q12393	YLR091W	GEP5
+P25596	YCL073C	GEX1
+Q03016	YPL137C	GIP3
+Q05926	YLR364W	GRX8
+P03069	YEL009C	GCN4
+Q03330	YGR252W	GCN5
+Q01722	YNL199C	GCR2
+P32621	YEL042W	GDA1
+Q02979	YPL110C	GDE1
+Q99339	YLL065W	
+P38229	YBR045C	GIP1
+Q03768	YDR152W	GIR2
+P38068	YBR014C	GRX7
+P37291	YLR058C	SHM2
+P40107	YGL225W	VRG4
+P0CE11	YER039C	HVG1
+P43577	YFL017C	GNA1
+Q03554	YMR292W	GOT1
+P10823	YER020W	GPA2
+Q08886	YOR371C	GPB1
+P40066	YER107C	GLE2
+Q05584	YDR272W	GLO2
+P38682	YER122C	GLO3
+P32190	YHL032C	GUT1
+Q12438	YDL010W	GRX6
+P48813	YDR508C	GNP1
+P53839	YNL274C	GOR1
+Q00055	YDL022W	GPD1
+Q06636	YDR302W	GPI11
+P47088	YJR013W	GPI14
+Q04082	YDR437W	GPI19
+P32363	YPL175W	SPT14
+Q08726	YOR262W	GPN2
+P40581	YIR037W	HYR1
+P33892	YGL195W	GCN1
+P49095	YMR189W	GCV2
+P37020	YJR040W	GEF1
+P38812	YHR100C	GEP4
+Q12125	YOR164C	GET4
+P36173	YKR106W	GEX2
+Q06336	YDR358W	GGA1
+P38817	YHR108W	GGA2
+P25569	YCL039W	GID7
+P32642	YER174C	GRX4
+P38138	YBR229C	ROT2
+Q04924	YDR221W	GTB1
+P48015	YDR019C	GCV1
+Q06625	YPR184W	GDB1
+P39958	YER136W	GDI1
+Q12434	YDL135C	RDI1
+P39722	YAL048C	GEM1
+P38785	YHR061C	GIC1
+Q12418	YLR094C	GIS3
+P41818	YMR311C	GLC8
+P47011	YJL137C	GLG2
+P38263	YBR105C	VID24
+P40208	YMR135C	GID8
+Q12263	YDR507C	GIN4
+P32288	YPR035W	GLN1
+Q12320	YOR040W	GLO4
+P25373	YCL035C	GRX1
+Q12680	YDL171C	GLT1
+P37292	YBR263W	SHM1
+Q03786	YDR248C	
+P30777	YGL142C	GPI10
+Q07830	YLL031C	GPI13
+P53306	YGR216C	GPI1
+Q06543	YLR243W	GPN3
+P41277	YIL053W	GPP1
+P18494	YER040W	GLN3
+Q03835	YDR098C	GRX3
+Q02784	YPL059W	GRX5
+P32784	YBL011W	SCT1
+P07286	YBR243C	ALG7
+P36148	YKR067W	GPT2
+Q04410	YDR517W	GRH1
+Q08929	YPL189W	GUP2
+Q04322	YMR192W	GYL1
+P48365	YDL234C	GYP7
+P23337	YFR015C	GSY1
+P04911	YDR225W	HTA1
+P02294	YBL002W	HTB2
+P40857	YJL097W	PHS1
+P25333	YCR008W	SAT4
+Q04399	YDR506C	GMC1
+P38736	YHL031C	GOS1
+P39717	YAL056W	GPB2
+Q08969	YPL223C	GRE1
+P38715	YHR104W	GRE3
+P53154	YGL084C	GUP1
+P40531	YIL041W	GVP36
+Q08484	YOR070C	GYP1
+P48566	YNL293W	MSB3
+Q12753	YPR008W	HAA1
+P41546	YFL031W	HAC1
+P42950	YJL103C	GSM1
+P32835	YLR293C	GSP1
+Q07729	YDL238C	GUD1
+P53551	YPL127C	HHO1
+P14064	YKL109W	HAP4
+Q12341	YPL001W	HAT1
+P38523	YOR232W	MGE1
+P41921	YPL091W	GLR1
+P32836	YOR185C	GSP2
+Q00582	YML121W	GTR1
+P53290	YGR163W	GTR2
+P39996	YEL017W	GTT3
+P38970	YJL165C	HAL5
+P53973	YNL021W	HDA1
+P38199	YBL032W	HEK2
+Q12361	YDL035C	GPR1
+P24814	YJR090C	GRR1
+Q04697	YML048W	GSF2
+P40582	YIR038C	GTT1
+Q12390	YLL060C	GTT2
+P32806	YJL044C	GYP6
+P43570	YFL027C	GYP8
+Q96VH4	YCL026C-B	HBN1
+Q12096	YOR320C	GNT1
+P46984	YJL184W	GON7
+P53130	YGL121C	GPG1
+P23797	YMR281W	GPI12
+Q04080	YDR434W	GPI17
+P38211	YBR004C	GPI18
+P40367	YJL062W	LAS21
+P47122	YJR072C	NPA3
+P38143	YBR244W	GPX2
+Q12068	YOL151W	GRE2
+Q08220	YOL049W	GSH2
+Q04806	YMR251W	GTO3
+P40956	YGL181W	GTS1
+P38625	YMR217W	GUA1
+P46943	YLR289W	GUF1
+P42944	YJL110C	GZF3
+Q12180	YOL089C	HAL9
+Q05580	YDR266C	HEL2
+P36014	YKL026C	GPX1
+Q07845	YLL035W	GRC3
+P47026	YJL091C	GWT1
+P53258	YGR100W	MDR1
+Q12344	YPL249C	GYP5
+P27472	YLR258W	GSY2
+Q06201	YLR445W	GMC2
+P36125	YKR030W	GMH1
+P41911	YOL059W	GPD2
+P53961	YNL038W	GPI15
+P49018	YDR331W	GPI8
+P16474	YJL034W	KAR2
+P32477	YJL101C	GSH1
+P48239	YGR154C	GTO1
+P36156	YKR076W	ECM4
+P00815	YCL030C	HIS4
+P53187	YGL033W	HOP2
+Q12214	YPR068C	HOS1
+Q01448	YBR215W	HPC2
+Q05905	YLR301W	HRI1
+Q05549	YDR291W	HRQ1
+P09950	YDR232W	HEM1
+P28789	YDL205C	HEM3
+Q12276	YOR227W	HER1
+P41809	YDR420W	HKR1
+P0CY07	YCL066W	HMLALPHA1
+P54839	YML126C	ERG13
+P40480	YIL112W	HOS4
+P48570	YDL182W	LYS20
+P36078	YKL084W	HOT13
+Q99332	YOR324C	FRT1
+P17629	YDR138W	HPR1
+P47171	YJR140C	HIR3
+P48353	YMR161W	HLJ1
+Q04429	YDR528W	HLR1
+P12683	YML075C	HMG1
+P0CY13	YCR096C	HMRA2
+Q12398	YOR032C	HMS1
+P40545	YIL020C	HIS6
+P33734	YBR248C	HIS7
+P38635	YFR025C	HIS2
+Q03937	YDR014W-A	HED1
+P51979	YGL251C	HFM1
+P06633	YOR202W	HIS3
+P02293	YDR224C	HTB1
+P13434	YBL021C	HAP3
+P32769	YKR084C	HBS1
+Q07653	YDL223C	HBT1
+P25364	YCR065W	HCM1
+Q06623	YPR179C	HDA3
+Q12060	YPL254W	HFI1
+Q12373	YLL022C	HIF1
+P53834	YNL281W	HCH1
+Q03281	YDR458C	HEH2
+P36113	YKR017C	HEL1
+P06174	YOR278W	HEM4
+P46973	YJR055W	HIT1
+P0CY11	YCR097W	HMRA1
+Q06629	YDR295C	HDA2
+P05373	YGL040C	HEM2
+P11353	YDR044W	HEM13
+P04912	YBL003C	HTA2
+Q12692	YOL012C	HTZ1
+P61830	YBR010W; YNL031C	HHT1; HHT2
+P02309	YBR009C; YNL030W	HHF1; HHF2
+Q01766	YPR005C	HAL1
+P0CE41	YLR256W	HAP1
+P06774	YGL237C	HAP2
+Q02516	YOR358W	HAP5
+Q03532	YMR290C	HAS1
+P39984	YEL056W	HAT2
+P34243	YKL017C	HCS1
+P16622	YOR176W	HEM15
+P35843	YOR237W	HES1
+Q04458	YMR110C	HFD1
+P39982	YEL059W	HHY1
+P32480	YOR038C	HIR2
+P00498	YER055C	HIS1
+Q04344	YDL125C	HNT1
+P49775	YDR305C	HNT2
+P40481	YIL110W	HPM1
+Q05787	YLR207W	HRD3
+Q99383	YOL123W	HRP1
+P29295	YPL204W	HRR25
+Q06674	YDR317W	HIM1
+P32479	YBL008W	HIR1
+P07172	YIL116W	HIS5
+P40037	YER057C	HMF1
+Q03973	YDR174W	HMO1
+P19807	YGL077C	HNM1
+P47124	YJR075W	HOC1
+Q9URQ5	YCR020W-B	HTL1
+P45820	YGL168W	HUR1
+P32874	YMR207C	HFA1
+P38074	YBR034C	HMT1
+P32339	YLR205C	HMX1
+P53096	YGL194C	HOS2
+Q02959	YPL116W	HOS3
+P32478	YJL159W	HSP150
+P34244	YKL101W	HSL1
+P32590	YBR169C	SSE2
+P40985	YJR036C	HUL4
+P53982	YNL009W	IDP3
+P48362	YGR187C	HGH1
+P06775	YGR191W	HIP1
+P12684	YLR450W	HMG2
+P53389	YNR055C	HOL1
+Q05164	YOL155C	HPF1
+P38753	YHL002W	HSE1
+P10961	YGL073W	HSF1
+Q99181	YOR319W	HSH49
+P22943	YFL014W	HSP12
+P53687	YOR025W	HST3
+P32485	YLR113W	HOG1
+Q12122	YDL131W	LYS21
+Q03213	YMR172W	HOT1
+P39734	YAL028W	FRT2
+Q12347	YLR097C	HRT3
+P15992	YBR072W	HSP26
+P25619	YCR021C	HSP30
+Q08992	YPL280W	HSP32
+P40325	YGR268C	HUA1
+Q6Q546	YNR032C-A	HUB1
+Q12345	YLR052W	IES3
+P39730	YAL035W	FUN12
+Q04432	YDR533C	HSP31
+Q12329	YDR171W	HSP42
+Q05931	YLR369W	SSQ1
+P38790	YHR067W	HTD2
+P53119	YGL141W	HUL5
+P39924	YEL069C	HXT13
+P54854	YDL245C	HXT15
+P32465	YHR094C	HXT1
+P32466	YDR345C	HXT3
+P38695	YHR096C	HXT5
+P39004	YDR342C	HXT7
+P32464	YKL189W	HYM1
+P41734	YOR126C	IAH1
+P46958	YJL146W	IDS2
+P40060	YER092W	IES5
+P20459	YJR007W	SUI2
+P28817	YDR036C	EHD3
+P0CY09	YCL067C	HMLALPHA2
+Q12039	YOL095C	HMI1
+P20050	YIL072W	HOP1
+Q05827	YMR251W-A	HOR7
+Q06592	YPR193C	HPA2
+Q04178	YDR399W	HPT1
+P38922	YNL004W	HRB1
+Q08109	YOL013C	HRD1
+Q08732	YOR267C	HRK1
+P69852	YKL138C-A	HSK3
+Q08914	YOR391C	HSP33
+P50079	YGR223C	HSV2
+Q6Q5K6	YML058W-A	HUG1
+P04806	YFR053C	HXK1
+P04807	YGL253W	HXK2
+Q12134	YOR284W	HUA2
+Q12520	YPL244C	HUT1
+Q12385	YLR099C	ICT1
+P15496	YPL117C	IDI1
+P09064	YPL237W	SUI3
+P10081	YKR059W; YJL138C	TIF1; TIF2
+P39936	YGL049C	TIF4632
+P47175	YJR147W	HMS2
+P09932	YDL227C	HO
+P39979	YEL066W	HPA3
+P38348	YBR272C	HSM3
+P19882	YLR259C	HSP60
+P22202	YER103W	SSA4
+P33416	YDR258C	HSP78
+P53685	YOL068C	HST1
+P53686	YPL015C	HST2
+P54862	YOL156W	HXT11
+P42833	YNL318C	HXT14
+P47185	YJR158W	HXT16
+P40886	YJL214W	HXT8
+P53688	YDR191W	HST4
+P53892	YNL164C	IBD2
+P40499	YIL090W	ICE2
+P40051	YER078C	ICP55
+P38284	YBR157C	ICS2
+Q04329	YMR195W	ICY1
+P38274	YBR133C	HSL7
+P09435	YBL075C	SSA3
+P0CS90	YJR045C	SSC1
+P39987	YEL030W	ECM10
+P28834	YNL037C	IDH1
+P41939	YLR174W	IDP2
+P25038	YOL023W	IFM1
+P19211	YJR047C	ANB1
+Q12522	YPR016C	TIF6
+P06168	YLR355C	ILV5
+P39567	YAR073W	IMD1
+P50095	YLR432W	IMD3
+Q02888	YPL099C	INA17
+Q03824	YMR163C	INP2
+Q12271	YOR109W	INP53
+P00724	YIL162W	SUC2
+P28239	YMR267W	PPA2
+P32589	YPL106C	SSE1
+P17709	YCL040W	GLK1
+P43581	YFL011W	HXT10
+P40441	YIL170W	HXT12
+P53631	YNR072W	HXT17
+P23585	YMR011W	HXT2
+P32467	YHR092C	HXT4
+P39003	YDR343C	HXT6
+P40885	YJL219W	HXT9
+P47125	YJR078W	BNA2
+P43598	YFR017C	IGD1
+P39522	YJR016C	ILV3
+Q02821	YNL189W	SRP1
+P40069	YER110C	KAP123
+P32581	YJL106W	IME2
+P25626	YCR046C	IMG1
+P46972	YMR035W	IMP2
+P53941	YNL075W	IMP4
+Q03694	YMR204C	INP1
+Q08630	YOR235W	IRC13
+Q04772	YMR073C	IRC21
+P47046	YJL051W	IRC8
+P28241	YOR136W	IDH2
+P40154	YNL215W	IES2
+P32617	YEL044W	IES6
+P47170	YJR138W	IML1
+Q05533	YDR287W	INM2
+P53901	YNL152W	INN1
+P50942	YNL106C	INP52
+Q12072	YLR095C	IOC2
+Q04213	YMR044W	IOC4
+P07250	YDR173C	ARG82
+P38954	YDR072C	IPT1
+P47034	YJL077C	ICS3
+P07260	YOL139C	CDC33
+P39520	YLR223C	IFH1
+P25605	YCL009C	ILV6
+P07342	YMR108W	ILV2
+P21954	YDL066W	IDP1
+P43579	YFL013C	IES1
+Q08561	YOR189W	IES4
+P38912	YMR260C	TIF11
+P32481	YER025W	GCD11
+P39935	YGR162W	TIF4631
+P23301	YEL034W	HYP2
+Q9P305	YHR132W-A	IGO2
+P47042	YJL057C	IKS1
+P47155	YJR118C	ILM1
+P38217	YBR017C	KAP104
+P21190	YJR094C	IME1
+P41833	YGL192W	IME4
+P53219	YGR031W	IMO32
+P32899	YHR148W	IMP3
+P40573	YIR017C	MET28
+Q03081	YPL038W	MET31
+P47169	YJR137C	MET5
+P05694	YER091C	MET6
+P10659	YLR180W	SAM1
+Q04922	YDR219C	MFB1
+P32787	YJR144W	MGM101
+P28321	YKL094W	YJU3
+P32266	YOR211C	MGM1
+P26188	YDL200C	MGT1
+Q04472	YMR115W	MGR3
+P36046	YKL195W	MIA40
+P50945	YNL100W	MIC27
+P39943	YER028C	MIG3
+Q08176	YOL026C	MIM1
+Q04341	YDR031W	MIX14
+P38920	YMR167W	MLH1
+P40457	YIL149C	MLP2
+P53102	YGL183C	MND1
+P24720	YOR350C	MNE1
+P18408	YPR167C	MET16
+Q07684	YDL233W	MFG1
+P53152	YGL087C	MMS2
+P38888	YHR204W	MNL1
+P41821	YNL291C	MID1
+P53035	YGL209W	MIG2
+P32491	YPL140C	MKK2
+P34072	YNL076W	MKS1
+Q06580	YPR188C	MLC2
+P32047	YNL074C	MLF3
+Q12372	YLL061W	MMP1
+Q06324	YLR190W	MMR1
+P46982	YJL186W	MNN5
+P39107	YPL050C	MNN9
+P40549	YIL014W	MNT3
+P53745	YNR059W	MNT4
+P43563	YFL034C-B	MOB2
+P23641	YJR077C	MIR1
+P47083	YJR002W	MPP10
+Q03667	YMR002W	MIX17
+P38162	YBL107C	MIX23
+Q06211	YPR164W	MMS1
+Q12205	YLR057W	MNL2
+P46985	YJL183W	MNN11
+P38069	YBR015C	MNN2
+P53129	YGL124C	MON1
+P53311	YGR243W	MPC3
+P0CD99	YDL247W	MPH2
+P23748	YMR036C	MIH1
+P53379	YDR144C	MKC7
+Q06164	YLR320W	MMS22
+P40577	YIR025W	MND2
+P39106	YER001W	MNN1
+P36044	YKL201C	MNN4
+P35724	YKL064W	MNR2
+P53059	YGL257C	MNT2
+P53157	YGL080W	MPC1
+Q12411	YOL091W	SPO21
+Q01926	YOR334W	MRS2
+P47084	YJR003C	MRX12
+P53869	YNL211C	MRX7
+Q07980	YLR035C	MLH2
+P38257	YBR098W	MMS4
+P40484	YIL106W	MOB1
+P54785	YMR070W	MOT3
+P41940	YDL055C	PSA1
+P40562	YIR002C	MPH1
+P0CE00	YJR160C	MPH3
+P53725	YNR024W	MPP6
+P53159	YGL075C	MPS2
+Q08471	YOR066W	MSA1
+P08593	YPR134W	MSS18
+P40990	YDL107W	MSS2
+Q07938	YLR017W	MEU1
+Q03218	YMR177W	MMT1
+Q08970	YPL224C	MMT2
+P07884	YOR274W	MOD5
+P38191	YBL049W	MOH1
+P32333	YPL082C	MOT1
+P32829	YMR224C	MRE11
+P53166	YGL064C	MRH4
+P40185	YIL051C	MMF1
+P50108	YDR245W	MNN10
+P53163	YGL068W	MNP1
+P32906	YJR131W	MNS1
+P47123	YJR074W	MOG1
+P53583	YNL249C	MPA43
+P38857	YHR162W	MPC2
+Q12404	YOR288C	MPD1
+P35728	YKL059C	MPE1
+P40364	YJL066C	MPM1
+P54199	YDL028C	MPS1
+P47069	YJL019W	MPS3
+P39016	YGL178W	MPT5
+P25336	YCR092C	MSH3
+P53045	YGR060W	ERG25
+P22148	YOL116W	MSN1
+P52918	YDR335W	MSN5
+P33748	YMR037C	MSN2
+P40029	YER042W	MXR1
+Q03825	YMR164C	MSS11
+P36066	YKL133C	
+Q3E829	YDL160C-A	MHF2
+P38341	YBR262C	MIC12
+P36112	YKR016W	MIC60
+P40850	YNL085W	MKT1
+Q08925	YPL184C	MRN1
+P33201	YKL009W	MRT4
+Q05648	YDR282C	MRX10
+P40050	YER077C	MRX1
+P48564	YNL295W	MRX6
+P15424	YDR194C	MSS116
+Q08818	YOR354C	MSC6
+P25846	YHR120W	MSH1
+P40965	YFL003C	MSH4
+Q12175	YDL154W	MSH5
+P40567	YIR009W	MSL1
+P53604	YNR049C	MSO1
+P20676	YOR098C	NUP1
+Q02199	YGL172W	NUP49
+Q12454	YDR067C	OCA6
+P31755	YGL038C	OCH1
+Q99297	YOR222W	ODC2
+P38325	YBR230C	OM14
+Q07521	YDL096C	OPI6
+Q06593	YPR194C	OPT2
+P50874	YNL261W	ORC5
+Q06144	YLR350W	ORM2
+P21375	YJR051W	OSM1
+Q03723	YML019W	OST6
+Q02795	YMR149W	SWP1
+Q08692	YOR255W	OSW1
+P43558	YFL044C	OTU1
+P32336	YOR373W	NUD1
+P38738	YHL029C	OCA5
+P16387	YER178W	PDA1
+P16547	YIL136W	OM45
+Q06810	YPR075C	OPY2
+P54784	YML065W	ORC1
+Q99380	YDL232W	OST4
+P53136	YGL111W	NSA1
+P52891	YDL116W	NUP84
+P07991	YLR438W	CAR2
+P20967	YIL125W	KGD1
+P16451	YGR193C	PDX1
+Q06668	YDR316W	OMS1
+A0A023PZI1	YPR044C	OPI11
+P87286	YDR360W	OPI7
+P38271	YBR129C	OPY1
+Q02630	YMR047C	NUP116
+P33895	YOL069W	NUF2
+Q12255	YLR093C	NYV1
+P25366	YCR095C	OCA4
+P19262	YDR148C	KGD2
+P12695	YNL071W	LAT1
+P54790	YLL004W	ORC3
+Q12375	YOR130C	ORT1
+P48439	YOR085W	OST3
+P05150	YJL088W	ARG3
+P52593	YML103C	NUP188
+Q02803	YPL052W	OAZ1
+P21957	YHL020C	OPI1
+P54791	YPR162C	ORC4
+P33400	YHL027W	RIM101
+P38351	YBR279W	PAF1
+Q12033	YOR275C	RIM20
+P37304	YDR251W	PAM1
+P53010	YGL094C	PAN2
+P36102	YKL025C	PAN3
+Q03050	YDR542W	PAU10
+P0CE89	YIL176C	PAU14
+P0CE88	YJL223C	PAU1
+Q07987	YLR037C	PAU23
+P0CE90	YNR076W	PAU6
+P53298	YGR179C	OKP1
+P28273	YKL215C	OXP1
+P40897	YJL212C	OPT1
+P32833	YBR060C	ORC2
+P33751	YDR538W	PAD1
+P32567	YMR165C	PAH1
+P36129	YKR035C	OPI8
+P38826	YHR118C	ORC6
+Q12447	YDR071C	PAA1
+Q05518	YDR348C	PAL1
+P53179	YGL045W	RIM8
+P48565	YNL294C	RIM21
+Q04734	YMR063W	RIM9
+P36147	YKR065C	PAM17
+P32521	YIR006C	PAN1
+P40459	YIL145C	PAN6
+Q08202	YOL032W	OPI10
+O94084	YLR338W	OPI9
+P54964	YLR059C	REX2
+Q12451	YDL019C	OSH2
+Q02201	YKR003W	OSH6
+P38122	YBR176W	ECM31
+P50946	YNL099C	OCA1
+P36163	YKR087C	OMA1
+P33767	YEL002C	WBP1
+Q12202	YLR054C	OSW2
+P43611	YFR039C	OSW7
+P32263	YER023W	PRO3
+P40960	YDR488C	PAC11
+P39937	YER007W	PAC2
+P41543	YJL002C	OST1
+P46964	YOR103C	OST2
+Q08952	YPL196W	OXR1
+P41816	YPL171C	OYE3
+P38725	YHL046C	PAU13
+P0CE91	YLL064C	PAU18
+P0CE87	YPL282C	PAU22
+P25610	YCR104W	PAU3
+P40091	YER149C	PEA2
+P25625	YCR044C	PER1
+Q12144	YLR064W	PER33
+Q92316	YGL226C-A	OST5
+P40219	YMR148W	OSW5
+P39952	YER154W	OXA1
+Q03558	YHR179W	OYE2
+Q04430	YDR531W	CAB1
+P25644	YCR077C	PAT1
+P35994	YKL224C	PAU16
+P53427	YLR461W	PAU4
+P39545	YAR020C	PAU7
+Q12524	YLR151C	PCD1
+P38126	YBR186W	PCH2
+P53124	YGL134W	PCL10
+P24867	YNL289W	PCL1
+Q08966	YPL219W	PCL8
+P15873	YBR088C	POL30
+P40345	YNR008W	LRO1
+P37254	YNR033W	ABZ1
+P38794	YHR071W	PCL5
+P53259	YGR101W	PCP1
+P26263	YGR087C	PDC6
+P22434	YGL248W	PDE1
+P06776	YOR360C	PDE2
+Q03266	YMR289W	ABZ2
+P53632	YOL115W	PAP2
+P29468	YKR002W	PAP1
+Q12515	YDL173W	PAR32
+P40186	YIL050W	PCL7
+P17967	YCL043C	PDI1
+P40530	YIL042C	PKP1
+P12383	YGL013C	PDR1
+P33200	YBL005W	PDR3
+P33302	YOR153W	PDR5
+P53224	YGR038W	ORM1
+P35845	YAR042W	SWH1
+P38713	YHR073W	OSH3
+P38755	YHR001W	OSH7
+P38747	YHL013C	OTU2
+P38787	YHR063C	PAN5
+Q07362	YDL053C	PBP4
+P08018	YJL128C	PBS2
+P25693	YDL127W	PCL2
+Q12477	YDL179W	PCL9
+P13259	YGR202C	PCT1
+P32896	YDR081C	PDC2
+Q99220	YDR057W	YOS9
+P04147	YER165W	PAB1
+P53343	YGR294W	PAU12
+Q12370	YLL025W	PAU17
+Q08322	YOL161C	PAU20
+P38155	YBR301W	PAU24
+P0CE92	YAL068C	PAU8
+P25580	YCL052C	PBN1
+P10963	YKR097W	PCK1
+P40038	YER059W	PCL6
+P40550	YIL013C	PDR11
+Q04182	YDR406W	PDR15
+P53756	YNR070W	PDR18
+Q04264	YMR076C	PDS5
+P36139	YKR046C	PET10
+Q12462	YOL147C	PEX11
+P53112	YGL153W	PEX14
+P24004	YKL197C	PEX1
+Q03370	YDR479C	PEX29
+P39108	YDR142C	PEX7
+P48363	YGR078C	PAC10
+Q04493	YML094W	GIM5
+P53170	YGL059W	PKP2
+P53860	YNL231C	PDR16
+P38075	YBR035C	PDX3
+P25362	YCR020C	PET18
+P80667	YLR191W	PEX13
+P50091	YGR239C	PEX21
+P25584	YCL056C	PEX34
+P47116	YJR059W	PTK2
+P29461	YOR208W	PTP2
+P07244	YGL234W	ADE5,7
+P54113	YLR028C	ADE16
+P53294	YGR169C	PUS6
+Q12069	YDL036C	PUS9
+P09368	YLR142W	PUT1
+P03962	YEL021W	URA3
+Q9ZZX9	Q0010	
+Q9ZZW4	Q0142	
+Q9ZZW2	Q0144	
+P43122	YDL104C	QRI7
+P41903	YJR019C	TES1
+P25339	YGL014W	PUF4
+Q06991	YLR414C	PUN1
+P38972	YGR061C	ADE6
+P53167	YGL063W	PUS2
+P11154	YGL062W	PYC1
+P28272	YKL216W	URA1
+Q9ZZV8	Q0297	
+Q12355	YDR055W	PST1
+P39927	YGR156W	PTI1
+P27616	YAR015W	ADE1
+Q05911	YLR359W	ADE13
+Q35811	Q0092	
+Q9ZZW1	Q0182	
+P04046	YMR300C	ADE4
+P38009	YMR120C	ADE17
+Q06244	YLR165C	PUS5
+P25502	YKL015W	PUT3
+P08525	YJL166W	QCR8
+P38230	YBR046C	ZTA1
+P06838	YML095C	RAD10
+P32641	YER173W	RAD24
+Q00578	YIL143C	SSL2
+Q04231	YML011C	RAD33
+P14736	YER162C	RAD4
+P06778	YML032C	RAD52
+P22216	YPL153C	RAD53
+P38953	YDR076W	RAD55
+P06779	YJR052W	RAD7
+P32864	YOR370C	MRS6
+Q06891	R0030W	RAF1
+P25635	YCR057C	PWP2
+P34230	YKL188C	PXA2
+P32327	YBR218C	PYC2
+P13298	YML106W	URA5
+P37299	YHR001W-A	QCR10
+P07256	YBL045C	COR1
+P06777	YPL022W	RAD1
+P32628	YEL037C	RAD23
+P06839	YER171W	RAD3
+Q12270	YPL246C	RBD2
+P50086	YGR232W	NAS6
+P53037	YGR170W	PSD2
+P31374	YAL017W	PSK1
+Q02771	YER058W	PET117
+P32606	YOR017W	PET127
+P32522	YLR067C	PET309
+Q01329	YAL043C	PTA1
+Q04373	YDR496C	PUF6
+P80210	YNL220W	ADE12
+Q02256	YIR026C	YVH1
+P21304	YLR196W	PWP1
+P30620	YMR137C	PSO2
+P50896	YDR505C	PSP1
+P36082	YKL076C	PSY1
+Q12318	YLR376C	PSY3
+P47065	YJL023C	PET130
+Q02772	YJR034W	PET191
+P07390	YNR045W	PET494
+P34222	YBL057C	PTH2
+P04161	YDR408C	ADE8
+Q12488	YDR013W	PSF1
+P31115	YFL001W	DEG1
+Q08647	YOR243C	PUS7
+P39006	YNL169C	PSD1
+P25044	YDL230W	PTP1
+P40048	YER075C	PTP3
+P40454	YIL153W	RRD1
+P32588	YNL016W	PUB1
+Q12221	YPR042C	PUF2
+Q07807	YLL013C	PUF3
+P21264	YOR128C	ADE2
+P41909	YPL147W	PXA1
+P36166	YKR090W	PXL1
+P53335	YGR280C	PXR1
+P05737	YGL076C	RPL7A
+P17076	YHL033C	RPL8A
+P10622	YDL130W	RPP1B
+P53060	YGL250W	RMR1
+P36159	YKR079C	TRZ1
+P53118	YGL144C	ROG1
+P51862	YLR371W	ROM2
+P32529	YJR063W	RPA12
+Q01080	YNL248C	RPA49
+P27999	YGL070C	RPB9
+P47076	YJL011C	RPC17
+P05738	YGL147C	RPL9A
+Q02204	YKR006C	MRPL13
+P22354	YKR085C	MRPL20
+Q12508	YDR255C	RMD5
+P40993	YDR478W	SNM1
+Q02933	YPL123C	RNY1
+P25042	YPR065W	ROX1
+P10964	YOR341W	RPA190
+P40422	YHR143W-A	RPC10
+P07703	YPR110C	RPC40
+P38902	YOL005C	RPB11
+P16370	YIL021W	RPB3
+P34087	YDR404C	RPB7
+Q12189	YOR095C	RKI1
+P32496	YFR052W	RPN12
+Q12250	YDL147W	RPN5
+Q06103	YPR108W	RPN7
+Q04062	YDR427W	RPN9
+P38061	YBL092W	RPL32
+P51998	YML025C	YML6
+P05319	YOL039W	RPP2A
+P02400	YDR382W	RPP2B
+Q12495	YPR018W	RLF2
+Q03195	YDR091C	RLI1
+Q12224	YPL089C	RLM1
+P36520	YNL284C	MRPL10
+P23369	YGR076C	MRPL25
+P36531	YBR122C	MRPL36
+P36533	YML009C	MRPL39
+P36534	YPL173W	MRPL40
+Q06090	YPR100W	MRPL51
+P43620	YFR048W	RMD8
+P49166	YLR185W	RPL37A
+P04650	YJL189W	RPL39
+P25348	YCR003W	MRPL32
+Q04598	YDR115W	
+P32387	YDR405W	MRP20
+P32338	YGR044C	RME1
+Q02685	YPL024W	RMI1
+P40525	YIL052C	RPL34B
+P49167	YLR325C	RPL38
+P0CX87	YDL133C-A	RPL41B
+P0CX26	YJR094W-A	RPL43B
+P0CX28	YHR141C	RPL42B
+Q02326	YML073C	RPL6A
+P51401	YNL067W	RPL9B
+P05317	YLR340W	RPP0
+Q07915	YLR009W	RLP24
+P12687	YNL005C	MRP7
+P36516	YMR024W	MRPL3
+P22353	YJL063C	MRPL8
+P32388	YKL167C	MRP49
+P53724	YNR022C	MRPL50
+P38330	YBR238C	
+P25299	YGL044C	RNA15
+P11745	YMR235C	RNA1
+Q05635	YDR279W	RNH202
+P05747	YFR032C-A	RPL29
+P0CX27	YNL162W	RPL42A
+Q12213	YPL198W	RPL7B
+P38064	YBL038W	MRPL16
+P36527	YDR462W	MRPL28
+P20084	YMR286W	MRPL33
+P36532	YBR268W	MRPL37
+P35996	YKL170W	MRPL38
+P02406	YGL103W	RPL28
+P0CX85	YDL136W	RPL35B
+P14126	YOR063W	RPL3
+P0CH09	YKR094C	RPL40B
+P0CX86	YDL184C	RPL41A
+P10664	YBR031W	RPL4A
+P36517	YLR439W	MRPL4
+P36519	YDR237W	MRPL7
+P36528	YNL252C	MRPL17
+P53881	YNL177C	MRPL22
+Q12487	YOR150W	MRPL23
+P39975	YEL072W	RMD6
+P0CX42	YER117W	RPL23B
+P04456	YOL127W	RPL25
+P0C2H9	YLR406C	RPL31B
+P29453	YLL045C	RPL8B
+P05318	YDL081C	RPP1A
+O14455	YPL249C-A	RPL36B
+P0CH08	YIL148W	RPL40A
+P0CX25	YPR043W	RPL43A
+P26321	YPL131W	RPL5
+P05739	YLR448W	RPL6B
+P38144	YBR245C	ISW1
+Q08773	YOR304W	ISW2
+Q03419	YDR492W	IZH1
+Q99393	YOL101C	IZH4
+P40358	YJL073W	JEM1
+P36224	YMR294W	JNM1
+P07170	YDR226W	ADK1
+Q12055	YDL166C	FAP7
+P06245	YPL203W	TPK2
+Q04746	YMR065W	KAR5
+P39962	YER123W	YCK3
+P27466	YFR014C	CMK1
+P34167	YPR163C	TIF3
+P38431	YPR041W	TIF5
+P53897	YNL157W	IGO1
+P50094	YML056C	IMD4
+Q06704	YLR309C	IMH1
+P47031	YJL082W	IML2
+P32351	YIL154C	IMP2'
+P11986	YJL153C	INO1
+P13902	YOL108C	INO4
+P53115	YGL150C	INO80
+Q08227	YOL065C	INP54
+P40015	YER019W	ISC1
+Q12479	YOR013W	IRC11
+Q07843	YLL033W	IRC19
+Q08416	YOR044W	IRC23
+Q06683	YDR332W	IRC3
+Q07821	YLL027W	ISA1
+P32645	YER180C	ISC10
+P53193	YGL018C	JAC1
+P47156	YJR119C	JHD2
+O13555	YLR331C	JIP3
+P07278	YIL033C	BCY1
+P23292	YNL154C	YCK2
+P19158	YOL081W	IRA2
+Q12056	YOR226C	ISU2
+P47119	YJR069C	HAM1
+P30605	YDR497C	ITR1
+Q07959	YLR023C	IZH3
+P40034	YER051W	JHD1
+P53863	YNL227C	JJJ1
+P32767	YGL016W	KAP122
+P22517	YOL016C	CMK2
+Q12494	YDR017C	KCS1
+Q08295	YOL157C	IMA2
+P40884	YJL216C	IMA5
+Q06142	YLR347C	KAP95
+P32337	YMR308C	PSE1
+P53067	YGL241W	KAP114
+P25642	YCR071C	IMG2
+P38265	YBR107C	IML3
+P28627	YMR150C	IMP1
+P26798	YDR123C	INO2
+Q06098	YPR106W	ISR1
+Q04638	YML068W	ITT1
+Q06214	YPR169W	JIP5
+P40206	YMR132C	JLP2
+P47135	YJR091C	JSN1
+Q02932	YPL125W	KAP120
+P36132	YKR038C	KAE1
+P38697	YHR216W	IMD2
+P40576	YIR024C	INA22
+Q08118	YOL015W	IRC10
+Q6B0V8	YPR038W	IRC16
+P43615	YFR043C	IRC6
+Q03020	YPL135W	ISU1
+P38710	YHR046C	INM1
+P40559	YIL002C	INP51
+P01094	YMR174C	PAI3
+P38803	YHR085W	IPI1
+P53877	YNL182C	IPI3
+P18963	YBR140C	IRA1
+Q08522	YOR135C	IRC14
+P47056	YJL037W	IRC18
+Q12425	YPR067W	ISA2
+Q6Q560	YER048W-A	ISD11
+P21374	YJR050W	ISY1
+P53125	YGL133W	ITC1
+Q06667	YDR315C	IPK1
+P00817	YBR011C	IPP1
+Q12280	YPL242C	IQG1
+P40006	YEL001C	IRC22
+P32488	YMR081C	ISF1
+P53843	YNL265C	IST1
+Q07532	YDL115C	IWR1
+P33417	YKL032C	IXR1
+Q12442	YOL002C	IZH2
+P43596	YFR013W	IOC3
+P0CT04	YNL015W	PBI2
+P43610	YFR038W	IRC5
+P36115	YKR019C	IRS4
+Q99312	YOR155C	ISN1
+Q12358	YLL057C	JLP1
+P05986	YKL166C	TPK3
+P11927	YNL188W	KAR1
+P17119	YPR141C	KAR3
+P32526	YPL269W	KAR9
+P23291	YHR135C	YCK1
+P15700	YKL024C	URA6
+P43614	YFR042W	KEG1
+P35844	YPL145C	KES1
+P13134	YNL238W	KEX2
+P38692	YHR102W	KIC1
+P38991	YPL209C	IPL1
+P38250	YBR086C	IST2
+P25389	YCL024W	KCC4
+P17423	YHR025W	THR1
+P07277	YMR208W	ERG12
+P13185	YDR122W	KIN1
+P06242	YDL108W	KIN28
+P24583	YBL105C	PKC1
+P40565	YIR005W	IST3
+Q06505	YPR133C	SPN1
+Q12350	YPR061C	JID1
+Q03361	YDR475C	JIP4
+Q02196	YKL001C	MET14
+P25583	YCL055W	KAR4
+P00549	YAL038W	CDC19
+P14681	YGR040W	KSS1
+P50090	YGR238C	KEL2
+P13186	YLR096W	KIN2
+Q01919	YOR233W	KIN4
+P28743	YPL155C	KIP2
+P38063	YBL068W	PRS4
+P52489	YOR347C	PYK2
+P42846	YNL308C	KRI1
+P54070	YPL053C	KTR6
+Q02733	YPL017C	IRC15
+Q06554	YLR247C	IRC20
+A0A023PXB5	YDR112W	IRC2
+Q03036	YDR540C	IRC4
+P47010	YJL142C	IRC9
+P32361	YHR079C	IRE1
+P30606	YOL103W	ITR2
+Q04934	YDR229W	IVY1
+P36035	YKL217W	JEN1
+P46997	YJL162C	JJJ2
+P26364	YER170W	ADK2
+P06244	YJL164C	TPK1
+Q07551	YDL124W	
+Q08979	YPL263C	KEL3
+Q04066	YDR428C	BNA7
+P36005	YKL161C	KDX1
+P38853	YHR158C	KEL1
+P40309	YJL094C	KHA1
+P22209	YAR018C	KIN3
+P25341	YCR091W	KIN82
+P53086	YGL216W	KIP3
+Q8TGJ3	YNL024C-A	KSH1
+P50112	YDL049C	KNH1
+P38873	YHR186C	KOG1
+P40504	YIL085C	KTR7
+P36146	YKR063C	LAS1
+P39518	YER015W	FAA2
+P09620	YGL203C	KEX1
+P15454	YDR454C	GUK1
+P17260	YNL322C	KRE1
+P38691	YHR082C	KSP1
+P38130	YBR205W	KTR3
+P38800	YHR080C	LAM4
+P38210	YBL006C	LDB7
+P20485	YLR133W	CKI1
+P38689	YHL011C	PRS3
+Q04431	YDR532C	KRE28
+P22023	YOR336W	KRE5
+P33550	YKR061W	KTR2
+P43560	YFL042C	LAM5
+Q06346	YDR367W	KEI1
+P36004	YKL168C	KKQ8
+P32350	YLL019C	KNS1
+P32895	YKL181W	PRS1
+P53158	YGL079W	KXD1
+P40970	YDR062W	LCB2
+P39002	YIL009W	FAA3
+P40079	YER127W	LCP5
+P25587	YCL005W	LDB16
+Q02799	YPL054W	LEE1
+Q12166	YOR108W	LEU9
+P50107	YML004C	GLO1
+Q06005	YLR239C	LIP2
+P38878	YHR192W	LNP1
+Q04396	YDR503C	LPP1
+P53281	YGR136W	LSB1
+P42838	YNL323W	LEM3
+P06208	YNL104C	LEU4
+P32875	YOR196C	LIP5
+P36775	YBL022C	PIM1
+P38131	YBR199W	KTR4
+Q08218	YOL047C	LDS2
+P28742	YBL063W	KIP1
+P38169	YBL098W	BNA4
+P38620	YER099C	PRS2
+Q12265	YOL061W	PRS5
+P34253	YKL110C	KTI12
+P27810	YOR099W	KTR1
+Q92325	YOL025W	LAG2
+Q12446	YOR181W	LAS17
+P00572	YJR057W	CDC8
+P31379	YAL018C	LDS1
+P04173	YCL018W	LEU2
+P38702	YHR002W	LEU5
+P07264	YGL009C	LEU1
+Q02796	YPL055C	LGE1
+P53966	YNL029C	KTR5
+P32807	YMR284W	YKU70
+P25045	YMR296C	LCB1
+Q06147	YLR260W	LCB5
+P53153	YGL085W	LCL3
+Q04081	YDR435C	PPM1
+P08638	YLR451W	LEU3
+P36016	YKL073W	LHS1
+Q04005	YDR184C	ATC1
+P39946	YOR269W	PAC1
+Q10740	YNL045W	LAP2
+P40026	YER038C	KRE29
+P27809	YDR483W	KRE2
+P39005	YJL174W	KRE9
+P25586	YCL059C	KRR1
+P30624	YOR317W	FAA1
+P32486	YPR159W	KRE6
+P39526	YJL207C	LAA1
+P47912	YMR246W	FAA4
+P33399	YDL051W	LHP1
+Q03579	YMR298W	LIP1
+Q05979	YLR231C	BNA5
+P28496	YKL008C	LAC1
+P38703	YHL003C	LAG1
+P38851	YHR155W	LAM1
+Q08001	YLR072W	LAM6
+Q04377	YDR499W	LCD1
+Q02786	YPL056C	LCL1
+Q08045	YLR104W	LCL2
+Q07887	YLL049W	LDB18
+P38139	YBR204C	LDH1
+P38439	YOR123C	LEO1
+P38852	YHR156C	LIN1
+Q12342	YDL146W	LDB17
+P53150	YGL090W	LIF1
+P47055	YJL038C	LOH1
+P25579	YCL051W	LRE1
+P53237	YGR057C	LST7
+Q06508	YPR139C	LOA1
+P43586	YFR001W	LOC1
+P34234	YKL183W	LOT5
+Q12405	YOR084W	LPX1
+P35688	YDL240W	LRG1
+P47093	YJR022W	LSM8
+P40495	YIL094C	LYS12
+P47051	YJL046W	AIM22
+Q04087	YDR439W	LRS4
+P43603	YFR024C-A	LSB3
+P47017	YJL124C	LSM1
+Q12230	YPL004C	LSP1
+Q04781	YMR247C	RKR1
+P22134	YER142C	MAG1
+Q12176	YDR060W	MAK21
+P53341	YGR292W	MAL12
+Q12246	YOR171C	LCB4
+Q12502	YOR322C	LDB19
+Q02783	YPL060W	MFM1
+P40070	YER112W	LSM4
+P40089	YER146W	LSM5
+P53905	YNL147W	LSM7
+P32487	YNL268W	LYP1
+P40971	YDR034C	LYS14
+P38828	YHR121W	LSM12
+P10962	YAL025C	MAK16
+P23060	YCR019W	MAK32
+P53048	YGR289C	MAL11
+P38157	YBR297W	MAL33
+P0CW40	YIL172C	IMA3
+P53051	YGR287C	IMA1
+P40065	YER106W	MAM1
+Q01662	YLR244C	MAP1
+P38174	YBL091C	MAP2
+Q9ZZW7	Q0115	BI3
+P42951	YJL100W	LSB6
+P38203	YBL026W	LSM2
+P34239	YKL176C	LST4
+P41318	YNL006W	LST8
+P07866	YAL024C	LTE1
+Q07508	YDL087C	LUC7
+P35192	YMR021C	MAC1
+Q06436	YLR427W	MAG2
+P0CW41	YJL221C	IMA4
+P30952	YNL117W	MLS1
+P21826	YIR031C	DAL7
+P50113	YGL154C	LYS5
+P47074	YJL013C	MAD3
+P41910	YDR005C	MAF1
+P39534	YJL199C	MBB1
+Q07376	YDL054C	MCH1
+P36032	YKL221W	MCH2
+Q08777	YOR306C	MCH5
+Q12262	YPR046W	MCM16
+Q06675	YDR318W	MCM21
+P11746	YMR043W	MCM1
+P17505	YKL085W	MDH1
+Q07923	YLR011W	LOT6
+P25369	YCL034W	LSB5
+P53145	YGL099W	LSG1
+P34078	YKL143W	LTV1
+P40957	YGL086W	MAD1
+P40958	YJL030W	MAD2
+P20484	YKL021C	MAK11
+P38112	YBR142W	MAK5
+P57743	YLR438C-A	LSM3
+Q06406	YDR378C	LSM6
+P36007	YKL218C	SRY1
+P38156	YBR298C	MAL31
+P22855	YGL156W	AMS1
+Q92328	YOL009C	MDM12
+P38295	YBR177C	EHT1
+P47167	YJR135C	MCM22
+P29469	YBL023C	MCM2
+P30665	YPR019W	MCM4
+P53091	YGL201C	MCM6
+P38132	YBR202W	MCM7
+P32419	YDL078C	MDH3
+Q05930	YLR368W	MDM30
+Q12285	YOL111C	MDY2
+P32259	YNL236W	SIN4
+Q08278	YOL135C	MED7
+P38304	YBR193C	MED8
+P24719	YOR351C	MEK1
+Q12198	YLL058W	
+Q99257	YPL169C	MEX67
+P34166	YNL145W	MFA2
+P40578	YIR033W	MGA2
+P43638	YJL042W	MHP1
+Q12525	YLL062C	MHT1
+P38880	YHR194W	MDM31
+P53083	YGL219C	MDM34
+Q12019	YLR106C	MDN1
+Q06213	YPR168W	NUT2
+P32585	YGR104C	SRB5
+P25046	YBL093C	ROX3
+P34162	YHR041C	SRB2
+P40469	YIL128W	MET18
+P32179	YOL064C	MET22
+P34165	YDR461W	MFA1
+P32435	YGL089C	MF(ALPHA)2
+P40002	YEL007W	MIT1
+P38286	YBR159W	IFA38
+P32490	YOR231W	MKK1
+P53141	YGL106W	MLC1
+Q12083	YPL164C	MLH3
+P38998	YIR034C	LYS1
+P07702	YBR115C	LYS2
+P49367	YDR234W	LYS4
+P38999	YNR050C	LYS9
+O14467	YOR298C-A	MBF1
+Q08601	YOR197W	MCA1
+Q12106	YOR228C	MCP1
+P35191	YFL016C	MDJ1
+P19659	YOL051W	GAL11
+P47822	YDR308C	SRB7
+Q02205	YKR007W	MEH1
+P33441	YML062C	MFT1
+P25573	YCL044C	MGR1
+Q96VH5	YCL057C-A	MIC10
+P50087	YGR235C	MIC26
+P35201	YKL089W	MIF2
+P27705	YGL035C	MIG1
+Q06820	YPR083W	MDM36
+Q08179	YOL027C	MDM38
+Q02574	YLR288C	MEC3
+Q12321	YPR070W	MED1
+P32570	YBR253W	SRB6
+Q12041	YDR253C	MET32
+P43623	YFR055W	IRC7
+Q04533	YML082W	
+P01149	YPL187W	MF(ALPHA)1
+P53050	YGR249W	MGA1
+P40081	YER134C	
+Q06630	YDR296W	MHR1
+P43594	YFR011C	MIC19
+P36027	YLR332W	MID2
+P38760	YHR015W	MIP6
+Q02455	YKR095W	MLP1
+P38300	YBR185C	MBA1
+P32354	YIL150C	MCM10
+P22133	YOL126C	MDH2
+O60200	YKL053C-A	MDM35
+P53094	YGL197W	MDS3
+P47025	YJL112W	MDV1
+P19263	YLR071C	RGR1
+P29467	YER044C-A	MEI4
+P39692	YFR030W	MET10
+P39014	YIL046W	MET30
+P08536	YJR010W	MET3
+P47164	YJR130C	STR2
+P19358	YDR502C	SAM2
+Q02889	YPL098C	MGR2
+Q3E835	YOL086W-A	MHF1
+P36051	YKL165C	MCD4
+P21965	YNL307C	MCK1
+P24279	YEL032W	MCM3
+Q12171	YOR147W	MDM32
+Q99278	YMR112C	MED11
+Q12343	YOR174W	MED4
+P33308	YNR010W	CSE2
+P08465	YNL277W	MET2
+P53338	YGR288W	MAL13
+P38158	YBR299W	MAL32
+P40513	YIL070C	MAM33
+Q12296	YOL060C	MAM3
+P03879	Q0120	BI4
+P39678	YDL056W	MBP1
+P23493	YKL093W	MBR1
+Q01159	YGL130W	CEG1
+P32783	YBR236C	ABD1
+Q02891	YPL095C	EEB1
+P42834	YNL328C	MDJ2
+P33310	YLR188W	MDL1
+P33311	YPL270W	MDL2
+P32489	YPL121C	MEI5
+P29496	YLR274W	MCM5
+Q06567	YLR253W	MCP2
+P36060	YKL150W	MCR1
+P53885	YNL173C	MDG1
+P32569	YER022W	SRB4
+Q12124	YDL005C	MED2
+P38633	YGL127C	SOH1
+P40260	YGR121C	MEP1
+P16523	YNL210W	MER1
+P32389	YNL103W	MET4
+P15807	YBR213W	MET8
+P36013	YKL029C	MAE1
+P03873	Q0110	BI2
+Q08268	YOL119C	MCH4
+P18409	YAL010C	MDM10
+Q01846	YML104C	MDM1
+P40356	YGL025C	PGD1
+P53114	YGL151W	NUT1
+P38782	YHR058C	MED6
+P41948	YNL142W	MEP2
+P53390	YPR138C	MEP3
+P32559	YMR023C	MSS1
+P0CY06	YCR040W	MATALPHA1
+P38849	YHR151C	MTC6
+P0CX81	YHR055C	CUP1-2
+Q02046	YKR080W	MTD1
+Q03151	YMR097C	MTG1
+P47095	YJR024C	MDE1
+Q04149	YDR386W	MUS81
+P40959	YMR004W	MVP1
+P36006	YKL129C	MYO3
+P47018	YJL123C	MTC1
+P53077	YGL226W	MTC3
+P53320	YGR257C	MTM1
+P32377	YNR043W	MVD1
+P23059	YCR020C-A	MAK31
+P32505	YGL122C	NAB2
+P40314	YDR252W	BTT1
+P43619	YFR047C	BNA6
+Q03455	YDR205W	MSC2
+P25847	YOL090W	MSH2
+P28737	YGR028W	MSP1
+P53176	YGL051W	MST27
+Q03920	YDR140W	MTQ2
+P48240	YGR158C	MTR3
+Q12093	YDL033C	SLM3
+P36084	YKL074C	MUD2
+P32335	YLR203C	MSS51
+P39552	YAR033W	MST28
+P0CY08	YCR039C	MATALPHA2
+P34246	YKL098W	MTC2
+P38335	YBR255W	MTC4
+P32633	YEL033W	MTC7
+P46151	YPL023C	MET12
+P53128	YGL125W	MET13
+Q06489	YPR118W	MRI1
+Q06106	YPR112C	MRD1
+Q12117	YDR033W	MRH1
+P50873	YDL079C	MRK1
+P35719	YKL142W	MRP8
+P47007	YJL147C	MRX5
+Q07349	YDL027C	MRX9
+P13712	YBR195C	MSI1
+Q03162	YMR100W	MUB1
+P50276	YGR055W	MUP1
+P38994	YDR208W	MSS4
+Q03429	YDR493W	MZM1
+Q02642	YPL037C	EGD1
+Q99316	YOL088C	MPD2
+Q06390	YDR374C	PHO92
+P25588	YCL061C	MRC1
+Q06815	YPR079W	MRL1
+P25270	YOR201C	MRM1
+P53123	YGL136C	MRM2
+O75012	YDL045W-A	MRP10
+P10566	YJL133W	MRS3
+Q03079	YPL041C	MRX11
+P38172	YBL095W	MRX3
+P36157	YKR077W	MSA2
+P32334	YGR014W	MSB2
+P38694	YHR039C	MSC7
+P10849	YDL044C	MTF2
+P38860	YHR168W	MTG2
+P35198	YDR277C	MTH1
+Q03677	YMR009W	ADI1
+P53070	YGL236C	MTO1
+P53944	YNL063W	MTQ1
+P34232	YKL186C	MTR2
+P48563	YNL297C	MON2
+Q05812	YLR219W	MSC3
+P53214	YGR023W	MTL1
+Q08550	YOR177C	MPC54
+P29952	YER003C	PMI40
+P11914	YHR024C	MAS2
+P10507	YLR163C	MAS1
+P07266	YIR021W	MRS1
+P23500	YKR052C	MRS4
+Q12467	YPL168W	MRX4
+Q05473	YDR336W	MRX8
+P21339	YOR188W	MSB1
+Q12317	YOL112W	MSB4
+Q03104	YML128C	MSC1
+P38590	YNL053W	MSG5
+Q03834	YDR097C	MSH6
+P33749	YKL062W	MSN4
+Q99189	YOR160W	MTR10
+P47047	YJL050W	MTR4
+P39731	YAL034W-A	MTW1
+Q08750	YOR298W	MUM3
+P19524	YOR326W	MYO2
+P32492	YAL029C	MYO4
+P37293	YGR147C	NAT2
+Q06504	YPR131C	NAT3
+Q08689	YOR253W	NAT5
+Q08920	YPL178W	CBC2
+P16603	YHR042W	NCP1
+Q06389	YDR373W	FRQ1
+Q12366	YOL104C	NDJ1
+P38757	YHR004C	NEM1
+Q03264	YMR285C	NGL2
+P0CX80	YHR053C	CUP1-1
+P14908	YMR228W	MTF1
+P08964	YHR023W	MYO1
+Q04439	YMR109W	MYO5
+Q12387	YOL076W	MDM20
+P38795	YHR074W	QNS1
+P12945	YDL040C	NAT1
+P52919	YLR457C	NBP1
+Q12163	YDR162C	NBP2
+Q12374	YPR155C	NCA2
+Q02866	YPL070W	MUK1
+Q02197	YEL053C	MAK10
+Q8TGN9	YGR031C-A	NAG1
+P27929	YNL137C	NAM9
+P25293	YKR048C	NAP1
+Q02820	YJL205C	NCE101
+Q06568	YLR254C	NDL1
+P38236	YBR057C	MUM2
+P38734	YHL036W	MUP3
+P42939	YGR206W	MVB12
+P25566	YCL033C	MXR2
+Q04751	YMR069W	NAT4
+Q03735	YML117W	NAB6
+P53919	YNL124W	NAF1
+P40360	YJL071W	ARG2
+P30771	YMR080C	NAM7
+Q08229	YOL070C	NBA1
+P52920	YGL091C	NBP35
+P46955	YJL116C	NCA3
+P34160	YMR125W	STO1
+P38205	YBL024W	NCL1
+Q07500	YDL085W	NDE2
+Q03503	YPR051W	MAK3
+P38996	YPL190C	NAB3
+P38879	YHR193C	EGD2
+P23503	YNL240C	NAR1
+Q3E7Y6	YHR199C-A	NBL1
+Q12207	YPR149W	NCE102
+Q08887	YOR372C	NDD1
+P36010	YKL067W	YNK1
+P25374	YCL017C	NFS1
+Q99271	YLR138W	NHA1
+Q00539	YHR086W	NAM8
+P53914	YNL132W	KRE33
+P40096	YER159C	BUR6
+P32500	YML031W	NDC1
+P40460	YIL144W	NDC80
+P32831	YBR212W	NGR1
+P32340	YML120C	NDI1
+P39744	YOR206W	NOC2
+P25353	YCR026C	NPP1
+P53718	YNR009W	NRM1
+Q08485	YOR071C	NRT1
+P38632	YEL019C	MMS21
+Q05541	YDR288W	NSE3
+P53898	YNL156C	NSG2
+Q12457	YDR026C	NSI1
+P36052	YKL162C	
+Q06148	YLR265C	NEJ1
+P25382	YCR072C	RSA4
+P38798	YHR077C	NMD2
+P47149	YJR112W	NNF1
+P36059	YKL151C	
+P40165	YNL200C	
+Q06162	YLR315W	NKP2
+P48234	YGR145W	ENP2
+Q07623	YDL213C	NOP6
+P38082	YBR066C	NRG2
+P27476	YGR159C	NSR1
+Q08214	YOL043C	NTG2
+P40215	YMR145C	NDE1
+Q03210	YML118W	NGL3
+P32495	YDL208W	NHP2
+Q04121	YDR456W	NHX1
+P34077	YFR002W	NIC96
+P32770	YDL167C	NRP1
+Q12181	YPR048W	TAH18
+P53317	YGR251W	NOP19
+P37838	YPL043W	NOP4
+Q12080	YPL146C	NOP53
+P33755	YBR170C	NPL4
+P22211	YNL183C	NPR1
+P39683	YOR209C	NPT1
+P53915	YNL129W	NRK1
+P53935	YNL091W	NST1
+Q12311	YPR031W	NTO1
+Q02629	YKL068W	NUP100
+Q92317	YDR397C	NCB2
+P38626	YIL043C	CBR1
+P38830	YHR124W	NDT80
+P33420	YPL174C	NIP100
+P40447	YIL164C	NIT1
+P49954	YLR351C	NIT3
+Q06178	YLR328W	NMA1
+P38861	YHR170W	NMD3
+P46970	YJR132W	NMD5
+Q08213	YOL042W	NGL1
+P53939	YNL078W	NIS1
+P34909	YER068W	MOT2
+P32494	YDR176W	NGG1
+P11633	YBR089C-A	NHP6B
+P47016	YJL126W	NIT2
+Q6Q547	YHR072W-A	NOP10
+Q99207	YDL148C	NOP14
+Q01560	YDR432W	NPL3
+Q12499	YOR310C	NOP58
+P47077	YJL010C	NOP9
+P39923	YEL062W	NPR2
+P53164	YGL067W	NPY1
+Q08972	YPL226W	NEW1
+P0CE68	YKR103W	NFT1
+P32860	YKL040C	NFU1
+Q03435	YDL002C	NHP10
+P53081	YGL221C	NIF3
+P53920	YNL123W	NMA111
+Q12129	YLR363C	NMD4
+P53253	YGR089W	NNF2
+Q08444	YOR056C	NOB1
+Q06512	YPR144C	NOC4
+Q08208	YOL041C	NOP12
+Q12460	YLR197W	NOP56
+Q12408	YDL046W	NPC2
+Q06287	YLR186W	EMG1
+P47035	YJL076W	NET1
+P11632	YPR052C	NHP6A
+Q07896	YLR002C	NOC3
+Q03790	YMR153W	NUP53
+P46673	YJR042W	NUP85
+P36023	YKR064W	OAF3
+Q03028	YPL134C	ODC1
+P32473	YBR221C	PDB1
+P53397	YML060W	OGG1
+Q08962	YPL211W	NIP7
+Q12493	YDR383C	NKP1
+P14743	YLR195C	NMT1
+P36003	YKL171W	NNK1
+Q02892	YPL093W	NOG1
+P06100	YDL165W	CDC36
+Q12514	YPR072W	NOT5
+P38742	YHL023C	NPR3
+Q03718	YML023C	NSE5
+P32499	YLR335W	NUP2
+P49686	YDR192C	NUP42
+P48837	YGR119C	NUP57
+Q05166	YDL088C	ASM4
+Q12066	YDL089W	NUR1
+P32332	YKL120W	OAC1
+P39720	YAL051W	OAF1
+P53949	YNL056W	OCA2
+Q07913	YLR007W	NSE1
+P38837	YHR133C	NSG1
+Q12143	YPL233W	NSL1
+P14907	YJL041W	NSP1
+P35729	YKL057C	NUP120
+P40064	YER105C	NUP157
+P40477	YIL115C	NUP159
+P08466	YJL208C	NUC1
+P40010	YER006W	NUG1
+Q00402	YDR150W	NUM1
+P39705	YAR002W	NUP60
+P40368	YJL061W	NUP82
+P38881	YHR195W	NVJ1
+P40354	YJR062C	NTA1
+P38302	YBR188C	NTC20
+P31378	YAL015C	NTG1
+P49687	YGL092W	NUP145
+P38219	YBR025C	OLA1
+P53204	YGR010W	NMA2
+P53883	YNL175C	NOP13
+P53927	YNL110C	NOP15
+P25655	YCR093W	CDC39
+P06102	YIL038C	NOT3
+P39997	YEL016C	NPP2
+P53617	YNL251C	NRD1
+P40007	YER002W	NOP16
+P40991	YNL061W	NOP2
+Q08287	YOL144W	NOP8
+P40078	YER126C	NSA2
+P43124	YDL105W	NSE4
+Q04958	YML059C	NTE1
+P33331	YER009W	NTF2
+P36118	YKR022C	NTR2
+P36161	YKR082W	NUP133
+P38181	YBL079W	NUP170
+P47054	YJL039C	NUP192
+P53742	YNR053C	NOG2
+Q12200	YPL006W	NCR1
+Q03125	YDR043C	NRG1
+P39081	YDR228C	PCF11
+P51533	YOR328W	PDR10
+Q02785	YPL058C	PDR12
+P38855	YHR160C	PEX18
+Q07418	YDL065C	PEX19
+Q06169	YLR324W	PEX30
+P40005	YEL003W	GIM4
+Q08959	YPL206C	PGC1
+Q05637	YDR281C	PHM6
+P07269	YDL106C	PHO2
+P17442	YGR233C	PHO81
+P25360	YCR037C	PHO87
+Q06216	YLR273C	PIG1
+P38768	YHR034C	PIH1
+Q12057	YOR104W	PIN2
+P46999	YJL160C	PIR5
+Q03407	YDR490C	PKH1
+P39105	YMR008C	PLB1
+Q03674	YMR006C	PLB2
+P32383	YPL268W	PLC1
+Q12511	YOR090C	PTC5
+P25646	YCR079W	PTC6
+P53844	YNL264C	PDR17
+P27801	YLR148W	PEP3
+P40335	YJL053W	PEP8
+Q99373	YPL159C	PET20
+Q04370	YMR026C	PEX12
+Q08215	YOL044W	PEX15
+P53203	YGR004W	PEX31
+P33760	YNL329C	PEX6
+P42836	YNL326C	PFA3
+Q12006	YOL003C	PFA4
+Q03289	YDR459C	PFA5
+P46988	YJL179W	PFD1
+P52553	YLR200W	YKE2
+P32452	YNL316C	PHA2
+P07270	YFR034C	PHO4
+P20052	YOL001W	PHO80
+P38361	YBR296C	PHO89
+P06738	YPR160W	GPH1
+P40187	YIL045W	PIG2
+Q06149	YLR266C	PDR8
+Q06608	YPR172W	
+P12868	YMR231W	PEP5
+P39684	YFR023W	PES4
+Q12252	YOL084W	PHM7
+P53297	YGR178C	PBP1
+P38151	YBR233W	PBP2
+P06169	YLR044C	PDC1
+P38848	YHR150W	PEX28
+P32800	YJL210W	PEX2
+P38292	YBR168W	PEX32
+P28795	YDR329C	PEX3
+P35056	YDR244W	PEX5
+P53900	YNL153C	GIM3
+P53872	YNL190W	
+P53896	YNL158W	PGA1
+Q12746	YML125C	PGA3
+P25578	YCL004W	PGS1
+P18898	YGL155W	CDC43
+P39535	YJL198W	PHO90
+P05066	YOR386W	PHR1
+P32854	YOR036W	PEP12
+P38921	YNL003C	PET8
+P40155	YNL214W	PEX17
+Q02969	YPL112C	PEX25
+Q08580	YOR193W	PEX27
+P53248	YGR077C	PEX8
+P53903	YNL149C	PGA2
+P40025	YER037W	PHM8
+Q06651	YDR313C	PIB1
+P07271	YML061C	PIF1
+P19657	YPL036W	PMA2
+P87284	YDR276C	PMP3
+P14242	YNL082W	PMS1
+P47190	YOR321W	PMT3
+P52867	YDL093W	PMT5
+P42934	YGR199W	PMT6
+Q05788	YLR209C	PNP1
+P47180	YJR153W	PGU1
+P37012	YMR105C	PGM2
+Q03262	YMR278W	PRM15
+P40961	YGR132C	PHB1
+P50085	YGR231C	PHB2
+P36093	YKL043W	PHD1
+P50947	YNL097C	PHO23
+P25297	YML123C	PHO84
+P46956	YJL117W	PHO86
+P38264	YBR106W	PHO88
+P27514	YNR013C	PHO91
+Q03306	YDR466W	PKH3
+P33333	YDL052C	SLC1
+P05030	YGL008C	PMA1
+P53238	YGR058W	PEF1
+P32609	YDR323C	PEP7
+P53261	YGR103W	NOP7
+P39718	YAL055W	PEX22
+P16861	YGR240C	PFK1
+P16862	YMR205C	PFK2
+P00560	YCR012W	PGK1
+P33401	YKL127W	PGM1
+P0CE93	YGL261C	PAU11
+P40585	YIR041W	PAU15
+P0CE85	YMR325W	PAU19
+P0CE86	YOR394W	PAU21
+P32612	YEL049W	PAU2
+P43575	YFL020C	PAU5
+Q3E770	YBL108C-A	PAU9
+Q3E833	YKR095W-A	PCC1
+P16467	YLR134W	PDC5
+P10834	YGR222W	PET54
+Q05568	YDR265W	PEX10
+P38244	YBR074W	PFF1
+P42841	YNL317W	PFS2
+Q00618	YJL031C	BET4
+P20133	YPR176C	BET2
+P38744	YHL018W	
+P39104	YNL267W	PIK1
+P53252	YGR086C	PIL1
+Q03178	YKL164C	PIR1
+Q03180	YKL163W	PIR3
+P06197	YPR113W	PIS1
+Q12236	YOL100W	PKH2
+Q03880	YMR123W	PKR1
+P52960	YOR363C	PIP2
+Q04383	YDR501W	PLM2
+P38197	YBL036C	
+Q07930	YLR016C	PML1
+Q12412	YOR161C	PNS1
+Q07951	YLR021W	IRC25
+P25576	YCL047C	POF1
+Q04049	YDR419W	RAD30
+Q12445	YLR018C	POM34
+P28005	YAL033W	POP5
+P23287	YLR433C	CNA1
+P39966	YER089C	PTC2
+P53691	YLR216C	CPR6
+Q12326	YOL056W	GPM3
+Q02890	YPL096W	PNG1
+P53833	YNL282W	POP3
+P38208	YBL018C	POP8
+P20604	YDL047W	SIT4
+P32345	YDR075W	PPH3
+P11491	YDR481C	PHO8
+Q04004	YDR183W	PLP1
+P32634	YER132C	PMD1
+P35999	YKL134C	OCT1
+P32903	YCR024C-A	PMP1
+Q06644	YDR307W	PMT7
+P53184	YGL037C	PNC1
+Q99216	YOR145C	PNO1
+P19881	YDL236W	PHO13
+P36040	YKL206C	ADD66
+Q12164	YLL023C	POM33
+P32838	YNR032W	PPG1
+P38693	YHR215W	PHO12
+Q08108	YOL011W	PLB3
+P05375	YJR073C	OPI3
+P41812	YNL221C	POP1
+Q06494	YPR127W	
+P00950	YKL152C	GPM1
+P33775	YDL095W	PMT1
+P31382	YAL023C	PMT2
+P46971	YJR143C	PMT4
+P39685	YMR129W	POM152
+Q05778	YLR199C	PBA1
+Q12245	YPL144W	POC4
+P23594	YDL134C	PPH21
+P38797	YHR076W	PTC7
+P00635	YBR093C	PHO5
+P40035	YER053C	PIC2
+P38969	YOR266W	PNT1
+P40473	YIL122W	POG1
+P39008	YNR052C	POP2
+P17157	YPL031C	PHO85
+P53191	YGL023C	PIB2
+Q03760	YML107C	PML39
+P07283	YFL045C	SEC53
+P40975	YEL017C-A	PMP2
+P36069	YKL128C	PMU1
+P38218	YBR022W	POA1
+Q04636	YML069W	POB3
+P38336	YBR257W	POP4
+P53218	YGR030C	POP6
+P38291	YBR167C	POP7
+P23595	YDL188C	PPH22
+P35182	YDL006W	PTC1
+P34221	YBL056W	PTC3
+P40164	YNL201C	PSY2
+P35842	YAR071W	PHO11
+Q04705	YML047C	PRM6
+P39551	YAR031W	PRM9
+P32264	YDR300C	PRO1
+P53549	YOR259C	RPT4
+Q01939	YGL048C	RPT6
+P25375	YCL057W	PRD1
+P47032	YJL079C	PRY1
+Q06892	YPL188W	POS5
+P40506	YIL083C	CAB2
+P38796	YHR075C	PPE1
+Q04119	YDR452W	PPN1
+P42946	YJL108C	PRM10
+Q12498	YPL156C	PRM4
+P32524	YJL203W	PRP21
+P20053	YPR178W	PRP4
+Q06449	YPR154W	PIN3
+P34217	YBL051C	PIN4
+Q12017	YOR281C	PLP2
+Q12008	YDL021W	GPM2
+P36110	YKR013W	PRY2
+P30657	YFR050C	PRE4
+Q12161	YOL054W	PSH1
+P40555	YIL007C	NAS2
+P08456	YER026C	CHO1
+P36002	YKL198C	PTK1
+P40100	YER185W	PUG1
+P28708	YKL116C	PRR1
+P23639	YML092C	PRE8
+P50109	YML017W	PSP2
+Q07949	YLR019W	PSR2
+Q12335	YDR032C	PST2
+P38958	YDR079W	PET100
+P08468	YMR257C	PET111
+P10355	YER153C	PET122
+Q12461	YPL152W	RRD2
+P32901	YKR093W	PTR2
+P43606	YFR029W	PTR3
+P38089	YBR125C	PTC4
+P38193	YBL046W	PSY4
+P38698	YHR201C	PPX1
+P20457	YKL045W	PRI2
+Q12459	YDL039C	PRM7
+P38876	YHR189W	PTH1
+P32857	YKL039W	PTM1
+Q07350	YDL043C	PRP11
+P40968	YDR364C	CDC40
+P23394	YDR243C	PRP28
+P25043	YOR157C	PUP1
+P22141	YER012W	PRE1
+P30656	YPR103W	PRE2
+P23724	YBL041W	PRE7
+P53043	YGR123C	PPT1
+P33329	YDR436W	PPZ2
+P10363	YIR008C	PRI1
+P40494	YIL095W	PRK1
+P53835	YNL279W	PRM1
+P49704	YGR091W	PRP31
+P28004	YAL032C	PRP45
+P19735	YBR055C	PRP6
+P33334	YHR165C	PRP8
+P21243	YGL011C	SCL1
+P21242	YOR362C	PRE10
+P07272	YLR014C	PPR1
+P38148	YBR276C	PPS1
+P26570	YML016C	PPZ1
+P49960	YMR268C	PRP24
+P39682	YML046W	PRP39
+P33203	YKL012W	PRP40
+P40303	YOL038W	PRE6
+P38624	YJL001W	PRE3
+P25451	YER094C	PUP3
+P40359	YJL072C	PSF2
+Q08217	YOL045W	PSK2
+P14747	YML057W	CMP2
+P24031	YBR092C	PHO3
+P52290	YDL024C	DIA3
+P40347	YPR073C	LTP1
+P40012	YER014W	HEM14
+P32945	YPL179W	PPQ1
+Q12036	YPL148C	PPT2
+P40534	YIL037C	PRM2
+Q08931	YPL192C	PRM3
+P40476	YIL117C	PRM5
+P53174	YGL053W	PRM8
+P07274	YOR122C	PFY1
+P15938	YKR086W	PRP16
+P33411	YGR006W	PRP18
+Q00723	YGR075C	PRP38
+Q03776	YDR235W	PRP42
+P53131	YGL120C	PRP43
+P21372	YBR237W	PRP5
+P19736	YDL030W	PRP9
+Q12310	YDL214C	PRR2
+P40327	YDL007W	RPT2
+P33297	YOR117W	RPT5
+P33298	YDR394W	RPT3
+P09232	YEL060C	PRB1
+P23638	YGR135W	PRE9
+P53633	YNL044W	YIP3
+P54885	YOR323C	PRO2
+P32523	YLL036C	PRP19
+P24384	YER013W	PRP22
+P20095	YNR011C	PRP2
+Q03338	YDR473C	PRP3
+Q12417	YPL151C	PRP46
+Q12428	YPR002W	PDH1
+P33299	YKL145W	RPT1
+P34227	YBL064C	PRX1
+P47033	YJL078C	PRY3
+P32379	YGR253C	PUP2
+P40302	YMR314W	PRE5
+Q12146	YOL146W	PSF3
+Q07800	YLL010C	PSR1
+Q12211	YPL212C	PUS1
+P48567	YNL292W	PUS4
+P07275	YHR037W	PUT2
+P15380	YOR348C	PUT4
+P07259	YJL130C	URA2
+Q9ZZX8	Q0017	
+P22289	YGR183C	QCR9
+P32849	YLR032W	RAD5
+P14737	YDR217C	RAD9
+P20051	YLR420W	URA4
+P07257	YPR191W	QCR2
+P00128	YDR529C	QCR7
+P40475	YIL120W	QDR1
+P40474	YIL121W	QDR2
+P38227	YBR043C	QDR3
+P48581	YOR368W	RAD17
+P40352	YJR035W	RAD26
+Q12223	YDL059C	RAD59
+P21827	YGL097W	SRM1
+P53972	YNL022C	RCM1
+P30402	YMR271C	URA10
+Q9ZZX7	Q0032	
+Q9ZZW3	Q0143	
+P00127	YFR033C	QCR6
+P07276	YGR258C	RAD2
+Q12465	YLR084C	RAX2
+A0A0B7P221	YCL054W-A	RDT1
+P21651	YJR021C	REC107
+P31244	YBR114W	RAD16
+P25301	YDR004W	RAD57
+Q99359	YDR014W	RAD61
+P11938	YNL216W	RAP1
+P53295	YGR173W	RBG2
+Q06835	YPR094W	RDS3
+Q08096	YOL010W	RCL1
+Q03446	YDR003W	RCR2
+P39531	YJL204C	RCY1
+Q08904	YOR380W	RDR1
+P03872	R0040C	REP2
+P25560	YCL001W	RER1
+P43556	YFL047W	RGD2
+P06780	YPR165W	RHO1
+Q06665	YDR314C	RAD34
+P25454	YER095W	RAD51
+Q03956	YDR202C	RAV2
+Q05672	YDL189W	RBS1
+P25332	YCR036W	RBK1
+Q08273	YOL133W	HRT1
+Q03530	YMR274C	RCE1
+P38622	YGL158W	RCK1
+P32841	YMR133W	REC114
+P21538	YBR049C	REB1
+P42073	YDR195W	REF2
+P28519	YMR201C	RAD14
+P10862	YCR066W	RAD18
+Q12021	YDR030C	RAD28
+P12753	YNL250W	RAD50
+P32863	YGL163C	RAD54
+Q08760	YOR301W	RAX1
+Q03713	YML030W	RCF1
+Q12044	YOR220W	RCN2
+Q04779	YMR075W	RCO1
+P38212	YBR005W	RCR1
+P25611	YCR106W	RDS1
+P19541	YPL133C	RDS2
+P14291	YLR263W	RED1
+P40893	YJL217W	REE1
+Q00816	YDR028C	REG1
+Q06709	YLR387C	REH1
+P38344	YBR267W	REI1
+Q12090	YLR107W	REX3
+Q04418	YDR527W	RBA50
+P39729	YAL036C	RBG1
+P53721	YNR018W	RCF2
+P38623	YLR248W	RCK2
+P36054	YKL159C	RCN1
+P38086	YBR073W	RDH54
+Q08742	YOR286W	RDL2
+P33323	YHR157W	REC104
+Q12188	YPR007C	REC8
+P38232	YBR050C	REG2
+P01119	YOR101W	RAS1
+P01120	YNL098C	RAS2
+P47104	YJR033C	RAV1
+Q12192	YOR279C	RFM1
+P40043	YER067W	RGI1
+P32862	YKL038W	RGT1
+P25378	YCR027C	RHB1
+Q12305	YOR285W	RDL1
+P53331	YGR276C	RNH70
+Q08237	YOL080C	REX4
+P38630	YOR217W	RFC1
+P38629	YNL290W	RFC3
+Q99188	YOR107W	RGS2
+Q06624	YPR180W	AOS1
+P40395	YLR039C	RIC1
+P43565	YFL033C	RIM15
+Q08003	YLR073C	RFU1
+P39083	YOR127W	RGA1
+Q06108	YPR115W	RGC1
+P16664	YDR137W	RGP1
+Q12300	YDL138W	RGT2
+P21524	YER070W	RNR1
+Q07844	YLL034C	RIX7
+P26785	YNL069C	RPL16B
+P46990	YJL177W	RPL17B
+P38222	YBR030W	RKM3
+P36105	YKL006W	RPL14A
+P0CX49	YOL120C	RPL18A
+P0CX24	YOR312C	RPL20B
+Q12672	YPL079W	RPL21B
+P0CX41	YBL087C	RPL23A
+P35196	YBR002C	RER2
+P30775	YGL143C	MRF1
+P53893	YNL163C	RIA1
+Q06208	YLR453C	RIF2
+Q03778	YDR236C	FMN1
+Q03792	YMR154C	RIM13
+Q08961	YPL208W	RKM1
+P22336	YAR007C	RFA1
+P26754	YNL312W	RFA2
+P26755	YJL173C	RFA3
+P40348	YJR068W	RFC2
+P40339	YOL094C	RFC4
+P38251	YBR087W	RFC5
+P06781	YNL090W	RHO2
+Q12362	YOL066C	RIB2
+Q3E757	YGR085C	RPL11B
+P03871	R0020C	REP1
+P12689	YOR346W	REV1
+P38206	YBL020W	RFT1
+Q00453	YMR182C	RGM1
+P50861	YOL143C	RIB4
+P38234	YBR052C	RFS1
+P48743	YLR176C	RFX1
+Q06407	YDR379W	RGA2
+P38339	YBR260C	RGD1
+P40160	YNL207W	RIO2
+P49723	YGR180C	RNR4
+P38145	YBR256C	RIB5
+P40188	YIL057C	RGI2
+Q00245	YIL118W	RHO3
+P53879	YNL180C	RHO5
+P09938	YJL026W	RNR2
+P21672	YIL066C	RNR3
+P26784	YIL133C	RPL16A
+P38066	YBL033C	RIB1
+Q99258	YDR487C	RIB3
+P29539	YBR275C	RIF1
+P38127	YBR192W	RIM2
+P23796	YMR283C	RIT1
+P38883	YHR197W	RIX1
+P0CX53	YEL054C	RPL12A
+Q12690	YDL082W	RPL13A
+P05748	YLR029C	RPL15A
+P38927	YIL139C	REV7
+Q00246	YKR055W	RHO4
+P33312	YBR153W	RIB7
+P38615	YMR139W	RIM11
+P32445	YCR028C-A	RIM1
+Q12196	YOR119C	RIO1
+Q12504	YDR257C	RKM4
+Q12367	YLR137W	RKM5
+P41805	YLR075W	RPL10
+P38741	YHL024W	RIM4
+P0C0W9	YPR102C	RPL11A
+P0CX54	YDR418W	RPL12B
+P54780	YMR121C	RPL15B
+P0CX44	YGL135W	RPL1B
+P0CX23	YMR242C	RPL20A
+P05749	YLR061W	RPL22A
+P24000	YGR148C	RPL24B
+P0C2H6	YHR010W	RPL27A
+P0CX46	YIL018W	RPL2B
+P0C2H8	YDL075W	RPL31A
+P51402	YDR500C	RPL37B
+P0CX45	YFR031C-A	RPL2A
+P14120	YGL030W	RPL30
+P05744	YPL143W	RPL33A
+P87262	YER056C-A	RPL34A
+P0CX84	YDL191W	RPL35A
+P05745	YMR194W	RPL36A
+P49626	YDR012W	RPL4B
+Q02753	YBR191W	RPL21A
+P0CX82	YBR084C-A	RPL19A
+P56628	YFL034C-A	RPL22B
+P0CX83	YBL027W	RPL19B
+P36144	YKR060W	UTP30
+P05743	YLR344W	RPL26A
+Q03942	YDR198C	RKM2
+P40212	YMR142C	RPL13B
+P38754	YHL001W	RPL14B
+P05740	YKL180W	RPL17A
+P0CX50	YNL301C	RPL18B
+P0CX43	YPL220W	RPL1A
+P04449	YGL031C	RPL24A
+P53221	YGR034W	RPL26B
+P0C2H7	YDR471W	RPL27B
+P41056	YOR234C	RPL33B
+Q12338	YLR154C	RNH203
+P32385	YLL046C	RNP1
+P25367	YCL028W	RNQ1
+Q02555	YMR239C	RNT1
+P39956	YER169W	RPH1
+P23250	YIL119C	RPI1
+P38886	YHR200W	RPN10
+P53196	YGL004C	RPN14
+P40011	YER010C	
+P35178	YDR087C	RRP1
+Q08285	YOL142W	RRP40
+Q05636	YDR280W	RRP45
+Q05022	YMR229C	RRP5
+P25368	YCL031C	RRP7
+P25381	YCR045C	RRT12
+P32611	YEL050C	RML2
+P53942	YNL072W	RNH201
+P45818	YGL171W	ROK1
+P36121	YKR025W	RPC37
+P32565	YIL075C	RPN2
+P36523	YLR312W-A	MRPL15
+P36526	YBR282W	MRPL27
+P14063	YKL138C	MRPL31
+P02381	Q0140	VAR1
+Q03441	YDL001W	RMD1
+P53140	YGL107C	RMD9
+Q12530	YLR145W	RMP1
+Q03305	YDR465C	RMT2
+Q04740	YMR234W	RNH1
+P22138	YPR010C	RPA135
+P20435	YPR187W	RPO26
+P28000	YNL113W	RPC19
+P04050	YDL140C	RPO21
+P20433	YJL140W	RPB4
+Q02773	YML091C	RPM2
+Q04847	YMR258C	ROY1
+P50106	YDR156W	RPA14
+P04051	YOR116C	RPO31
+P32349	YPR190C	RPC82
+P17890	YNL151C	RPC31
+P35718	YKL144C	RPC25
+P46969	YJL121C	RPE1
+Q03465	YDL020C	RPN4
+Q12377	YDL097C	RPN6
+Q06506	YPR137W	RRP9
+P40042	YER066W	RRT13
+Q07829	YLL030C	RRT7
+Q08745	YOR293W	RPS10A
+P46784	YMR230W	RPS10B
+P0CX48	YBR048W	RPS11B
+P40693	YNL002C	RLP7
+Q04599	YDR116C	MRPL1
+P32904	YHR147C	MRPL6
+P31334	YGR220C	MRPL9
+P36521	YDL202W	MRPL11
+P53875	YNL185C	MRPL19
+P36525	YMR193W	MRPL24
+Q06678	YDR322W	MRPL35
+P19956	YMR225C	MRPL44
+P40858	YJL096W	MRPL49
+P25298	YMR061W	RNA14
+Q02805	YOR018W	ROD1
+P43602	YFR022W	ROG3
+P53046	YGR070W	ROM1
+Q03691	YMR200W	ROT1
+P47006	YJL148W	RPA34
+P46669	YOR340C	RPA43
+P20434	YBR154C	RPB5
+P20436	YOR224C	RPB8
+P22139	YOR210W	RPB10
+Q04307	YDR045C	RPC11
+P25441	YDL150W	RPC53
+Q12167	YDR065W	RRG1
+Q12754	YPL012W	RRP12
+Q06511	YPR143W	RRP15
+P32786	YBL014C	RRN6
+P25359	YCR035C	RRP43
+P50943	YNL105W	RRT16
+P53117	YGL146C	RRT6
+Q01855	YOL040C	RPS15
+P38701	YHL015W	RPS20
+P0C0V8	YKR057W	RPS21A
+P08518	YOR151C	RPB2
+P32561	YNL330C	RPD3
+P38805	YHR088W	RPF1
+P43588	YFR004W	RPN11
+P38764	YHR027C	RPN1
+P40016	YER021W	RPN3
+P13433	YFL036W	RPO41
+Q06109	YPR116W	RRG8
+Q02983	YLR141W	RRN5
+P38204	YBL025W	RRN10
+P40992	YJL025W	RRN7
+P0CX47	YDR025W	RPS11A
+P22276	YOR207C	RET1
+P32910	YNR003C	RPC34
+P36160	YKR081C	RPF2
+O13563	YLR421C	RPN13
+Q08723	YOR261C	RPN8
+Q12532	YPL009C	RQC2
+P53437	YMR270C	RRN9
+Q04031	YDR412W	RRP17
+P38961	YDR083W	RRP8
+P40571	YIR015W	RPR2
+P39677	YJL102W	MEF2
+Q08774	YOR305W	RRG7
+Q04712	YML043C	RRN11
+P36080	YKL082C	RRP14
+P46948	YGR195W	SKI6
+Q12277	YDL111C	RRP42
+P53256	YGR095C	RRP46
+P40470	YIL127C	RRT14
+P43607	YFR032C	RRT5
+Q08219	YOL048C	RRT8
+P07281	YNL302C	RPS19B
+Q3E792	YGR027C	RPS25A
+P39939	YER131W	RPS26B
+P41058	YDL061C	RPS29B
+P26783	YJR123W	RPS5
+P48164	YNL096C	RPS7B
+Q06488	YLR357W	RSC2
+P43609	YFR037C	RSC8
+Q03246	YMR188C	MRPS17
+P36056	YKL155C	RSM22
+Q03976	YDR175C	RSM24
+Q02950	YPL118W	MRP51
+Q03919	YDR139C	RUB1
+Q12464	YPL235W	RVB2
+Q3E754	YJL136C	RPS21B
+P0CX31	YER074W	RPS24A
+Q08932	YPL193W	RSA1
+P38781	YHR056C	RSC30
+Q05043	YMR030W	RSF1
+Q03430	YDR494W	RSM28
+Q03201	YDR041W	RSM10
+P38175	YBL090W	MRP21
+P21771	YDR337W	MRPS28
+P38786	YHR062C	RPP1
+Q05468	YDR333C	RQC1
+Q04225	YMR131C	RRB1
+P38771	YHR038W	RRF1
+P40156	YNL213C	RRG9
+P38766	YHR031C	RRM3
+P36070	YKL125W	RRN3
+P38712	YHR065C	RRP3
+Q08162	YOL021C	DIS3
+P48589	YOR369C	RPS12
+P07280	YOL121C	RPS19A
+P23248	YML063W	RPS1B
+P39516	YJL191W	RPS14B
+P0CX52	YDL083C	RPS16B
+P0CX56	YML026C	RPS18B
+P0CX29	YGR118W	RPS23A
+P0CX32	YIL069C	RPS24B
+P0C0T4	YLR333C	RPS25B
+P0CX35	YJR145C	RPS4A
+P32832	YMR091C	NPL6
+Q03124	YML127W	RSC9
+Q04693	YML049C	RSE1
+P38792	YHR069C	RRP4
+Q12149	YOR001W	RRP6
+Q08746	YOR294W	RRS1
+P38192	YBL048W	RRT1
+P0C0W1	YJL190C	RPS22A
+P35997	YKL156W	RPS27A
+P0C0X0	YLR264W	RPS28B
+P25443	YGL123W	RPS2
+P0CX34	YOR182C	RPS30B
+Q05942	YLR221C	RSA3
+P53236	YGR056W	RSC1
+Q02206	YKR008W	RSC4
+P33442	YLR441C	RPS1A
+P0CX37	YPL090C	RPS6A
+P0CX40	YER102W	RPS8B
+Q08417	YOR049C	RSB1
+P46974	YJR127C	RSF2
+P40033	YER050C	RSM18
+Q03516	YMR266W	RSN1
+P32905	YGR214W	RPS0A
+P38120	YBR146W	MRPS9
+P40063	YER104W	RTT105
+P40161	YNL206C	RTT106
+Q07794	YLL002W	RTT109
+P53732	YNR036C	MRPS12
+P53064	YGL244W	RTF1
+P0CX30	YPR132W	RPS23B
+P41057	YLR388W	RPS29A
+P05750	YNL178W	RPS3
+O13516	YPL081W	RPS9A
+Q07979	YLR033W	RSC58
+Q12481	YOR287C	RRP36
+Q3E811	YLR162W-A	RRT15
+P05756	YDR064W	RPS13
+P06367	YCR031C	RPS14A
+P39938	YGL189C	RPS26A
+P38711	YHR021C	RPS27B
+P05759	YLR167W	RPS31
+P0CX51	YMR143W	RPS16A
+P14127	YDR447C	RPS17B
+P0CX55	YDR450W	RPS18A
+Q3E7Y3	YLR367W	RPS22B
+Q3E7X9	YOR167C	RPS28A
+P0CX33	YLR287C-A	RPS30A
+P0CX36	YHR203C	RPS4B
+P0CX38	YBR181C	RPS6B
+P0CX39	YBL072C	RPS8A
+P05755	YBR189W	RPS9B
+P02407	YML024W	RPS17A
+Q06639	YDR303C	RSC3
+P40018	YER029C	SMB1
+O14464	YPL183W-A	RTC6
+P38165	YBL103C	RTG3
+Q12443	YDL204W	RTN2
+Q05900	YLR298C	YHC1
+P26786	YOR096W	RPS7A
+P25632	YCR052W	RSC6
+P28778	YKL003C	MRP17
+Q05543	YDR289C	RTT103
+P53305	YGR215W	RSM27
+P19955	YFR049W	YMR31
+Q12751	YMR185W	RTP1
+P17558	YOR158W	PET123
+Q12378	YDR066C	RTR2
+Q12330	YOR159C	SME1
+P38850	YHR154W	RTT107
+P42847	YNL306W	MRPS18
+Q01163	YGL129C	RSM23
+P40496	YIL093C	RSM25
+P53292	YGR165W	MRPS35
+Q08281	YOL138C	RTC1
+P40084	YER139C	RTR1
+Q00916	YIL061C	SNP1
+P32605	YBR119W	MUD1
+Q08963	YPL213W	LEA1
+P54999	YPR182W	SMX3
+P25343	YCR009C	RVS161
+P22470	YDR143C	SAN1
+P53330	YGR275W	RTT102
+Q02608	YPL013C	MRPS16
+P53047	YGR213C	RTA1
+P53850	YNL254C	RTC4
+Q12108	YOR118W	RTC5
+P32608	YGL252C	RTG2
+Q04947	YDR233C	RTN1
+P40962	YOR077W	RTS2
+P20606	YPL218W	SAR1
+P28707	YKL117W	SBA1
+P06105	YJL080C	SCP160
+P52871	YER019C-A	SBH2
+P40541	YIL026C	IRR1
+P03878	Q0065	AI4
+P03877	Q0060	AI3
+P11792	YHR205W	SCH9
+P10663	YPR166C	MRP2
+P47150	YJR113C	RSM7
+P12686	YGR084C	MRP13
+P53733	YNR037C	RSM19
+P47141	YJR101W	RSM26
+P32607	YOL067C	RTG1
+Q03940	YDR190C	RVB1
+P40204	YFL017W-A	SMX2
+P32915	YLR378C	SEC61
+P52870	YER087C-B	SBH1
+Q12158	YDL003W	MCD1
+P34758	YOR329C	SCD5
+P21801	YLL041C	SDH2
+Q07534	YDL119C	HEM25
+P43612	YFR040W	SAP155
+P17121	YDR389W	SAC7
+Q12136	YDL153C	SAS10
+Q04002	YDR180W	SCC2
+P40090	YER147C	SCC4
+P45978	YPR129W	SCD6
+P03882	Q0160	SCEI
+P32564	YGR049W	SCM4
+Q04951	YMR305C	SCW10
+Q03323	YDR469W	SDC1
+P13856	YGR152C	RSR1
+P46654	YLR048W	RPS0B
+P10662	YDR347W	MRP1
+P32902	YHL004W	MRP4
+P33759	YBR251W	MRPS5
+Q03799	YMR158W	MRPS8
+Q12100	YDL025C	RTK1
+P53289	YGR161C	RTS3
+Q12242	YOR138C	RUP1
+P39743	YDR388W	RVS167
+P38255	YBR095C	RXT2
+P50110	YMR060C	SAM37
+P40856	YJL098W	SAP185
+P89114	YHR079C-A	SAE3
+P38352	YBR280C	SAF1
+P20840	YJR004C	SAG1
+P39954	YER043C	SAH1
+Q08985	YPL273W	SAM4
+Q08873	YOR367W	SCP1
+P40075	YER120W	SCS2
+Q08230	YOL071W	SDH5
+P40357	YGR009C	SEC9
+Q01589	YDR077W	SED1
+Q01590	YLR026C	SED5
+P34228	YBL066C	SEF1
+P16658	YLR105C	SEN2
+P36123	YKR028W	SAP190
+P32368	YKL212W	SAC1
+P46674	YDR159W	SAC3
+P43589	YFR005C	SAD1
+P14693	YHR083W	SAM35
+Q08986	YPL274W	SAM3
+P53969	YNL026W	SAM50
+P38429	YMR263W	SAP30
+Q04003	YDR181C	SAS4
+P53324	YGR263C	SAY1
+P38814	YHR103W	SBE22
+P42223	YDR351W	SBE2
+P25303	YMR214W	SCJ1
+P47052	YJL045W	
+P36047	YKL193C	SDS22
+Q06245	YLR166C	SEC10
+P48415	YPL085W	SEC16
+P18759	YBR080C	SEC18
+P28791	YDR498C	SEC20
+P15303	YPR181C	SEC23
+P17065	YNL272C	SEC2
+P38968	YDL195W	SEC31
+P21825	YPL094C	SEC62
+P33754	YBR171W	SEC66
+P39742	YLR292C	SEC72
+Q04675	YMR059W	SEN15
+Q00416	YLR430W	SEN1
+P47008	YJL145W	SFH5
+Q05567	YDR294C	DPL1
+P36136	YKR043C	SHB17
+P39000	YER096W	SHC1
+Q02774	YDL212W	SHR3
+Q07657	YDL225W	SHS1
+P38751	YHL006C	SHU1
+P50263	YMR175W	SIP18
+P38717	YNL257C	SIP3
+P06700	YDL042C	SIR2
+P32900	YHR149C	SKG6
+P35207	YLR398C	SKI2
+P17883	YPR189W	SKI3
+Q08491	YOR076C	SKI7
+P42843	YNL311C	SKP2
+P53327	YGR271W	SLH1
+P38247	YBR077C	SLM4
+Q00772	YHR030C	SLT2
+P32908	YFL008W	SMC1
+P32566	YGR229C	SMI1
+Q04174	YOR149C	SMP3
+P38990	YER129W	SAK1
+P39955	YER047C	SAP1
+P53036	YGL229C	SAP4
+Q99314	YOR213C	SAS5
+Q00711	YKL148C	SDH1
+Q04491	YLR208W	SEC13
+P24280	YMR079W	SEC14
+P29478	YML105C	SEC65
+Q02825	YPL083C	SEN54
+P40510	YIL074C	SER33
+P46995	YJL168C	SET2
+Q08446	YOR057W	SGT1
+P53266	YGR112W	SHY1
+P38634	YLR079W	SIC1
+P38262	YBR103W	SIF2
+Q12216	YOR156C	NFI1
+Q06315	YLR187W	SKG3
+P38314	YBR214W	SDS24
+P38164	YBL104C	SEA4
+Q12745	YLR440C	SEC39
+P33332	YER008C	SEC3
+P89102	YDR166C	SEC5
+P38890	YHR207C	SET5
+Q12507	YOR315W	SFG1
+P40363	YJL068C	
+P47166	YJR134C	SGM1
+P32578	YDR422C	SIP1
+Q02793	YGL213C	SKI8
+P33336	YGR143W	SKN1
+Q12505	YPL026C	SKS1
+Q03656	YMR216C	SKY1
+Q03406	YDR489W	SLD5
+P38283	YBR156C	SLI15
+P38345	YBR269C	SDH8
+P38804	YHR087W	RTC3
+Q07953	YLR022C	SDO1
+P40479	YIL113W	SDP1
+P53078	YGL224C	SDT1
+P20048	YMR013C	SEC59
+P14906	YOR254C	SEC63
+Q04279	YMR086W	SEG1
+P53011	YGL100W	SEH1
+O94742	YDR363W-A	SEM1
+P53953	YNL049C	SFB2
+P43682	YKL006C-A	SFT1
+P38166	YBL102W	SFT2
+P40561	YIR001C	SGN1
+Q08490	YOR073W	SGO1
+P46954	YJL089W	SIP4
+P21691	YKR101W	SIR1
+P39980	YEL065W	SIT1
+P53965	YNL032W	SIW14
+Q04195	YDR409W	SIZ1
+Q3E784	YER180C-A	SLO1
+Q02775	YDR088C	SLU7
+P40072	YER116C	SLX8
+Q12334	YDL139C	SCM3
+P23833	YBR037C	SCO1
+P38072	YBR024W	SCO2
+P11655	YNR026C	SEC12
+P22224	YGL233W	SEC15
+P30619	YDR164C	SEC1
+P22214	YLR268W	SEC22
+P07560	YFL005W	SEC4
+P11075	YDR170C	SEC7
+P32855	YPR055W	SEC8
+P40316	YDR113C	PDS1
+P25365	YCR067C	SED4
+P39707	YAR008W	SEN34
+P40054	YER081W	SER3
+P42941	YGR208W	SER2
+P36124	YKR029C	SET3
+Q12529	YPL165C	SET6
+Q12314	YOR021C	SFM1
+P53313	YGR245C	SDA1
+P33421	YKL141W	SDH3
+P32602	YBL050W	SEC17
+P40482	YIL109C	SEC24
+P32844	YIL068C	SEC6
+P34250	YKL105C	SEG2
+P49955	YMR288W	HSH155
+Q03067	YPL047W	SGF11
+P53075	YGL228W	SHE10
+P36068	YKL130C	SHE2
+P38272	YBR130C	SHE3
+Q04172	YDR393W	SHE9
+P35179	YDR086C	SSS1
+Q6Q595	YBL091C-A	SCS22
+P53012	YGL126W	SCS3
+P53189	YGL028C	SCW11
+P53334	YGR279C	SCW4
+P53009	YGL083W	SCY1
+Q06058	YLR404W	SEI1
+P39709	YAL067C	SEO1
+P33330	YOR184W	SER1
+P38827	YHR119W	SET1
+Q12369	YLL003W	SFI1
+P35735	YKL051W	SFK1
+P20134	YOR140W	SFL1
+Q12234	YOR216C	RUD3
+Q07458	YDL076C	RXT3
+P34218	YBL052C	SAS3
+P40963	YMR127C	SAS2
+P39735	YAL027W	SAW1
+Q9ZZX1	Q0070	AI5_ALPHA
+P36048	YKL173W	SNU114
+P10870	YDL194W	SNF3
+P18888	YHL025W	SNF6
+P39929	YLR025W	SNF7
+P00445	YJR104C	SOD1
+Q05676	YEL059C-A	SOM1
+Q06411	YLR424W	SPP382
+Q03954	YDR201W	SPC19
+Q03868	YDR104C	SPO71
+Q06134	YLR341W	SPO77
+P09937	YOR313C	SPS4
+Q12455	YLR146C	SPE4
+P06843	YER161C	SPT2
+P35177	YBR081C	SPT7
+P38985	YDL092W	SRP14
+P32342	YKL122C	SRP21
+P38688	YPL210C	SRP72
+Q03529	YMR272C	SCS7
+Q3E785	YDR379C-A	SDH6
+Q04401	YDR511W	SDH7
+P40505	YIL084C	SDS3
+P15367	YIR022W	SEC11
+P38810	YHR098C	SFB3
+P33303	YJR095W	SFC1
+P51534	YOR035C	SHE4
+P38337	YBR258C	SHG1
+P40073	YER118C	SHO1
+P25294	YNL007C	SIS1
+P52286	YDR328C	SKP1
+P33338	YNL243W	SLA2
+P43321	YLR147C	SMD3
+Q12078	YLR034C	SMF3
+P48232	YNL086W	SNN1
+P53823	YNL334C	SNO2
+P25357	YCR033W	SNT1
+Q03782	YDR240C	SNU56
+Q08826	YOR357C	SNX3
+P43545	YFL059W	SNZ3
+P50278	YNR034W	SOL1
+P38858	YHR163W	SOL3
+P53165	YGL066W	SGF73
+Q12212	YOR137C	SIA1
+Q08199	YOL031C	SIL1
+P40472	YIL123W	SIM1
+P11978	YDR227W	SIR4
+P36169	YKR100C	SKG1
+P32790	YBL007C	SLA1
+P47037	YJL074C	SMC3
+Q02260	YGR074W	SMD1
+P38925	YOL122C	SMF1
+Q04007	YDR186C	SND1
+P38956	YDR073W	SNF11
+P22082	YOR290C	SNF2
+P46950	YGR197C	SNG1
+P53127	YGL131C	SNT2
+P39990	YEL026W	SNU13
+Q04053	YDR425W	SNX41
+Q03148	YMR096W	SNZ1
+P53438	YMR016C	SOK2
+P37262	YCR073W-A	SOL2
+P38128	YBR182C	SMP1
+P31109	YAL030W	SNC1
+P33328	YOR327C	SNC2
+P53628	YNR023W	SNF12
+Q12420	YOR308C	SNU66
+P40317	YDR006C	SOK1
+P25808	YFL002C	SPB4
+P46965	YJR010C-A	SPC1
+P38915	YLR055C	SPT8
+Q03707	YML034W	SRC1
+Q99176	YLR119W	SRN2
+P36057	YKL154W	SRP102
+Q06688	YLR412W	BER1
+Q03175	YMR101C	SRT1
+P39931	YLR250W	SSP120
+P38353	YBR283C	SSH1
+P53172	YGL056C	SDS23
+Q12118	YOR007C	SGT2
+P38200	YBL031W	SHE1
+P40486	YIL104C	SHQ1
+P36024	YKR072C	SIS2
+Q12469	YOL113W	SKM1
+P38889	YHR206W	SKN7
+Q02100	YNL167C	SKO1
+P34252	YKL108W	SLD2
+P53251	YGR081C	SLX9
+Q04964	YML058W	SML1
+Q12306	YDR510W	SMT3
+P32364	YKL079W	SMY1
+P32909	YBR172C	SMY2
+Q06091	YPR101W	SNT309
+P56508	YDR525W-A	SNA2
+Q03144	YMR095C	SNO1
+Q04902	YMR322C	SNO4
+Q12368	YDL098C	SNU23
+P00447	YHR008C	SOD2
+P53315	YGR248W	SOL4
+P23201	YLL021W	SPA2
+Q04969	YML055W	SPC2
+P36131	YKR037C	SPC34
+Q08204	YOL034W	SMC5
+Q12749	YLR383W	SMC6
+Q06217	YLR275W	SMD2
+P47057	YJL036W	SNX4
+P38282	YBR152W	SPP381
+P53540	YNL126W	SPC98
+P50088	YGR236C	SPG1
+P40092	YER150W	SPI1
+P53541	YNL012W	SPO1
+P40031	YER046W	SPO73
+P32572	YNL204C	SPS18
+P35209	YMR179W	SPT21
+P42948	YJL105W	SET4
+Q99287	YOR165W	SEY1
+Q06168	YLR321C	SFH1
+P32432	YLR403W	SFP1
+P25554	YCL010C	SGF29
+Q06236	YLR164W	SHH4
+P38957	YDR078C	SHU2
+P22579	YOL004W	SIN3
+P34164	YGL208W	SIP2
+P40210	YMR140W	SIP5
+P53955	YNL047C	SLM2
+Q12098	YLR135W	SLX4
+P22215	YOR307C	SLY41
+P40167	YNL196C	SLZ1
+P40548	YIL016W	SNL1
+Q12034	YDR515W	SLF1
+P54867	YOR008C	SLG1
+P40485	YIL105C	SLM1
+P39928	YIL147C	SLN1
+P42900	YLR139C	SLS1
+P38241	YBR065C	ECM2
+P38324	YBR228W	SLX1
+Q12267	YLR086W	SMC4
+P41808	YPR054W	SMK1
+P18480	YBR289W	SNF5
+Q12483	YPL002C	SNF8
+P43544	YFL060C	SNO3
+P32568	YDR011W	SNQ2
+P53207	YGR013W	SNU71
+P53824	YNL333W	SNZ2
+Q04748	YMR066W	SOV1
+Q12133	YLR066W	SPC3
+P36094	YKL042W	SPC42
+Q12074	YPR069C	SPE3
+Q04438	YMR107W	SPG4
+P17123	YHR152W	SPO12
+Q04359	YMR017W	SPO20
+Q02521	YOR148C	SPP2
+P50875	YOL148C	SPT20
+Q06132	YLR336C	SGD1
+P33335	YPR198W	SGE1
+P35187	YMR190C	SGS1
+Q04487	YMR118C	SHH3
+P06701	YLR442C	SIR3
+P34226	YBL061C	SKT5
+Q08457	YOR060C	SLD7
+P53304	YGR212W	SLI1
+Q08581	YOR195W	SLK19
+Q12232	YOR154W	SLP1
+P32380	YDR356W	SPC110
+P25582	YCL054W	SPB1
+P38863	YHR172W	SPC97
+Q04398	YDR504C	SPG3
+P33419	YPL124W	SPC29
+Q06160	YLR313C	SPH1
+P23179	YHL022C	SPO11
+P23624	YHR014W	SPO13
+Q03029	YPL130W	SPO19
+P40511	YIL073C	SPO22
+P45819	YGL170C	SPO74
+P18410	YAL009W	SPO7
+P38904	YDR464W	SPP41
+P32603	YOR190W	SPR1
+P41901	YGR059W	SPR3
+P32573	YNL202W	SPS19
+P08458	YDR523C	SPS1
+P32558	YGL207W	SPT16
+P35210	YKL020C	SPT23
+P32914	YGR063C	SPT4
+P53866	YNL224C	SQS1
+P25648	YCR081W	SRB8
+P24276	YDR293C	SSD1
+P32343	YKL124W	SSH4
+Q02794	YOR047C	STD1
+Q06010	YLR389C	STE23
+P15705	YOR027W	STI1
+P38960	YDR082W	STN1
+Q00947	YDR463W	STP1
+P38989	YFR031C	SMC2
+P14359	YJL151C	SNA3
+P38839	YHR136C	SPL2
+P35184	YIR012W	SQT1
+Q12516	YDL133W	SRF1
+Q12020	YLR082C	SRL2
+P36167	YKR091W	SRL3
+P25567	YCL037C	SRO9
+P20424	YPR088C	SRP54
+P36077	YKL086W	SRX1
+Q08646	YOR242C	SSP2
+P42845	YNL309W	STB1
+P38699	YHR178W	STB5
+P32584	YDR410C	STE14
+Q03497	YHL007C	STE20
+P06783	YKL178C	STE3
+P32917	YDR103W	STE5
+P12866	YKL209C	STE6
+P06784	YDL159W	STE7
+P39932	YDR536W	STL1
+P09959	YLR182W	SWI6
+P46655	YGL245W	GUS1
+P53277	YGR129W	SYF2
+P11972	YLR452C	SST2
+P41930	YPL092W	SSU1
+P50104	YMR019W	STB4
+P53394	YPR003C	
+P08153	YDR146C	SWI5
+Q12379	YDR260C	SWM1
+P43554	YFL049W	SWP82
+Q05471	YDR334W	SWR1
+P53852	YNL247W	
+P15179	YPL104W	MSD1
+P23615	YGR116W	SPT6
+Q08673	YOR247W	SRL1
+Q03085	YPL033C	SRL4
+P10080	YHL034C	SBP1
+P53599	YNR031C	SSK2
+Q07084	YLR006C	SSK1
+P32867	YPL232W	SSO1
+Q12427	YDR169C	STB3
+P36085	YKL072W	STB6
+D6VTK4	YFL026W	STE2
+P25344	YCL032W	STE50
+P16965	YGR008C	STF2
+P53312	YGR244C	LSC2
+Q06524	YPR151C	SUE1
+P38359	YBR294W	SUL1
+Q05515	YDR346C	SVF1
+Q03088	YPL032C	SVL3
+Q06677	YDR320C	SWA2
+Q12104	YOR166C	SWT1
+P53135	YGL113W	SLD3
+P38343	YBR266C	SLM6
+P32828	YDL013W	SLX5
+Q02651	YPL027W	SMA1
+Q04658	YML066C	SMA2
+Q08817	YOR353C	SOG2
+P39543	YJL192C	SOP4
+P53148	YGL093W	SPC105
+Q01684	YER115C	SPR6
+P06844	YDR392W	SPT3
+P38687	YPL243W	SRP68
+P32916	YDR292C	SRP101
+P12954	YJL092W	SRS2
+P13130	YHR139C	SPS100
+P39073	YPL042C	SSN3
+P47821	YNL025C	SSN8
+P22213	YDR189W	SLY1
+P38778	YHR050W	SMF2
+Q07549	YDL123W	SNA4
+Q04477	YMR117C	SPC24
+P40014	YER018C	SPC25
+P39723	YAL047C	SPC72
+P42933	YMR191W	SPG5
+P17122	YHR153C	SPO16
+Q03012	YPL138C	SPP1
+P25380	YCL048W	SPS22
+P35208	YJL127C	SPT10
+P27692	YML010W	SPT5
+P39015	YLR150W	STM1
+Q05937	YLR375W	STP3
+Q07351	YDL048C	STP4
+P38163	YBL106C	SRO77
+Q12038	YPR032W	SRO7
+P32583	YKR092C	SRP40
+P38931	YDR443C	SSN2
+P38871	YHR184W	SSP1
+P37296	YMR054W	STV1
+P31377	YAL014C	SYN8
+P53598	YOR142W	LSC1
+P36126	YKR031C	SPO14
+P33757	YBR250W	SPO23
+Q07798	YLL005C	SPO75
+Q04921	YDR218C	SPR28
+P08459	YDR522C	SPS2
+P09007	YCR018C	SRD1
+P38789	YHR066W	SSF1
+P39926	YMR183C	SSO2
+Q03770	YDR160W	SSY1
+P38788	YHR064C	SSZ1
+P25379	YCL064C	CHA1
+P33894	YOR219C	STE13
+P53538	YNL222W	SSU72
+P53101	YGL184C	STR3
+Q12325	YLR092W	SUL2
+P46676	YDR310C	SUM1
+P36150	YKR069W	MET1
+P53616	YNL066W	SUN4
+P33300	YPL057C	SUR1
+P54003	YML052W	SUR7
+P53937	YNL081C	SWS2
+Q08553	YOR179C	SYC1
+P04802	YLL018C	DPS1
+P48525	YOL033W	MSE1
+Q02875	YPL105C	SYH1
+P39965	YER087W	AIM10
+P54000	YMR039C	SUB1
+Q07478	YDL084W	SUB2
+P31376	YAL011W	SWC3
+P53201	YGR002C	SWC4
+P38326	YBR231C	SWC5
+Q06707	YLR385C	SWC7
+P36104	YKL018W	SWD2
+Q04175	YDR395W	SXM1
+P15624	YLR060W	FRS1
+Q06817	YPR081C	GRS2
+P38088	YBR121C	GRS1
+Q6WNK7	YBR111W-A	SUS1
+P38869	YHR181W	SVP26
+P39706	YAR003W	SWD1
+P38123	YBR175W	SWD3
+P09547	YPL016W	SWI1
+P32591	YJL176C	SWI3
+P40825	YOR335C	ALA1
+P40528	YIL047C	SYG1
+P47002	YJL156C	SSY5
+P46679	YMR053C	STB2
+P23561	YLR362W	STE11
+P01098	YDL130W-A	STF1
+P39007	YGL022W	STT3
+P38198	YBL034C	STU1
+P46675	YLR045C	STU2
+P32911	YNL244C	SUI1
+Q12286	YPR009W	SUT2
+P32580	YPL029W	SUV3
+Q12254	YPL163C	SVS1
+Q04629	YDR126W	SWF1
+P08425	YPR047W	MSF1
+P15180	YDR037W	KRS1
+Q04048	YDR416W	SYF1
+P07263	YPR033C	HTS1
+Q06563	YLR251W	SYM1
+Q05506	YDR341C	
+P07284	YDR023W	SES1
+P40150	YNL209W	SSB2
+Q12153	YDR312W	SSF2
+P25390	YCR073C	SSK22
+Q04673	YLR005W	SSL1
+P13574	YHR084W	STE12
+P47154	YJR117W	STE24
+P32597	YIL126W	STH1
+P25604	YCL008C	STP22
+P38704	YHR006W	STP2
+P38637	YIR011C	STS1
+P37297	YLR305C	STT4
+P32579	YGL169W	SUA5
+P53032	YGL162W	SUT1
+P32944	YJL187C	SWE1
+P25302	YER111C	SWI4
+P15625	YFL022C	FRS2
+P32048	YNL073W	MSK1
+P11325	YLR382C	NAM2
+Q07395	YDL063C	SYO1
+P07806	YGR094W	VAS1
+P41895	YGR186W	TFG1
+Q12030	YDR167W	TAF10
+P35189	YPL129W	TAF14
+P23255	YCR042C	TAF2
+Q12297	YPL011C	TAF3
+P38992	YDR297W	SUR2
+P40342	YNR004W	SWM2
+P53873	YNL187W	SWT21
+P09436	YBL076C	ILS1
+P48526	YPL040C	ISM1
+Q06836	YPR095C	SYT1
+P53040	YGL112C	TAF6
+Q05027	YMR236W	TAF9
+P25638	YCR060W	TAH1
+P15019	YLR354C	TAL1
+P25345	YCR024C	SLM5
+P13188	YOR168W	GLN4
+P32774	YKL058W	TOA2
+P36421	YGR185C	TYS1
+P36100	YKL028W	TFA1
+Q9URQ3	YLR316C	TAD3
+Q04226	YML015C	TAF11
+P38129	YBR198C	TAF5
+Q03750	YML114C	TAF8
+P09733	YML085C	TUB1
+P32613	YEL048C	TCA17
+P42943	YJL111W	CCT7
+Q6B2U8	YAL064C-A	TDA8
+Q04545	YML081W	TDA9
+P34163	YKL140W	TGL1
+Q12043	YOR081C	TGL5
+P38714	YHR091C	MSR1
+P38705	YHR011W	DIA4
+P04801	YIL078W	THS1
+Q12109	YOL097C	WRS1
+P38854	YHR159W	TDA11
+Q03533	YMR291W	TDA1
+P40045	YER071C	TDA2
+P47153	YJR116W	TDA4
+P07236	YKL194C	MST1
+P46677	YGR274C	TAF1
+P02557	YFL037W	TUB2
+P38114	YBR150C	TBS1
+Q12466	YOR086C	TCB1
+Q03640	YML072C	TCB3
+P36101	YKL027W	TCD2
+Q99190	YDL015C	TSC13
+P40533	YIL039W	TED1
+Q07921	YLR010C	TEN1
+P53065	YGL243W	TAD1
+P47058	YJL035C	TAD2
+Q03761	YDR145W	TAF12
+P50105	YMR005W	TAF4
+P53072	YGL232W	TAN1
+P39076	YIL142W	CCT2
+P40413	YJR064W	CCT5
+P39079	YDR188W	CCT6
+P42938	YGR205W	TDA10
+P38758	YHR009C	TDA3
+P53882	YNL176C	TDA7
+P39933	YPR186C	PZF1
+Q02939	YPL122C	TFB2
+Q12004	YPR056W	TFB4
+P34111	YAL001C	TFC3
+Q04372	YMR028W	TAP42
+P40085	YER140W	EMP65
+P13393	YER148W	SPT15
+P38756	YHR003C	TCD1
+Q06466	YPR157W	TDA6
+P47988	YOR337W	TEA1
+P18412	YBR083W	TEC1
+P53038	YGR099W	TEL2
+Q06163	YLR318W	EST2
+P53851	YNL253W	TEX1
+P32367	YBR123C	TFC1
+P53215	YGR024C	THG1
+Q07748	YDL244W	THI13
+Q08975	YPL258C	THI21
+Q08579	YOR192C	THI72
+P41544	YJL004C	SYS1
+P41896	YGR005C	TFG2
+Q05021	YMR227C	TAF7
+P40468	YIL129C	TAO3
+Q8TGM6	YLR154W-C	TAR1
+P38967	YOL020W	TAT2
+P47030	YJL083W	TAX4
+P26637	YPL160W	CDC60
+P00958	YGR264C	MES1
+P22438	YGR171C	MSM1
+P04803	YDR268W	MSW1
+P48527	YPL097W	MSY1
+P36145	YKR062W	TFA2
+P11747	YML098W	TAF13
+P53228	YGR043C	NQM1
+P38085	YBR069C	TAT1
+P48606	YOR265W	RBL2
+P46670	YPL241C	CIN2
+P38707	YHR019C	DED81
+P09734	YML124C	TUB3
+P53904	YNL148C	ALF1
+P53378	YLR212C	TUB4
+P48231	YNL087W	TCB2
+P12612	YDR212W	TCP1
+P47079	YJL008C	CCT8
+O13513	YAL056C-A	
+O13511	YAL065C	
+P39728	YAL037W	
+P39725	YAL045C	
+Q8TGU6	YBR182C-A	
+Q12260	YBL100W-A	TY2A-B
+Q8TGU5	YBR296C-A	
+P38311	YBR209W	
+P38321	YBR225W	
+P38331	YBR242W	
+P38178	YBL083C	
+P38168	YBL100C	
+P38240	YBR064W	
+P38276	YBR137W	
+P25565	YCL002C	
+P25561	YCL021W	
+O13527	YAR009C	TY1B-A
+P0C5L1	YBL068W-A	
+Q7M4S9	YBL113C	
+P0C5L4	YBR121C-A	
+Q8TGK5	YBL113W-A	
+Q3E755	YBR200W-A	
+Q8TGQ3	YBR223W-A	
+P38296	YBR178W	
+P38327	YBR232C	
+P38354	YBR285W	
+P38362	YBR300C	
+Q3E778	YBR196C-B	
+P32788	YBL010C	
+P38177	YBL086C	
+P38171	YBL096C	
+P38214	YBR012C	
+P38315	YBR216C	YBP1
+P38267	YBR113W	
+P38275	YBR134W	
+P34215	YBR144C	
+Q96VH2	YCL001W-B	
+P25571	YCL041C	
+P25350	YCR006C	
+Q3E7Z7	YDR003W-A	
+Q12281	YDL032W	
+Q07793	YDR261C-D	TY1B-DR4
+Q12082	YDL157C	
+Q12148	YDL163W	
+Q03983	YDR179W-A	
+P48568	YDL186W	
+Q2V2P9	YDR119W-A	
+Q03787	YDR249C	
+Q05612	YDR278C	
+Q05497	YDR338C	
+Q3E6R5	YDR381C-A	
+P87266	YDR413C	
+Q8TGP5	YDR464C-A	
+P87274	YDR526C	
+P87261	YDR537C	
+P0CL37	YDR545C-A	
+Q02896	YPL087W	YDC1
+P40057	YER084W	
+P40093	YER156C	
+Q3E838	YFR012W-A	
+P43541	YFL063W	
+P43600	YFR020W	
+P0C5N1	YGL014C-A	
+P53185	YGL036W	
+O13515	YAL034C-B	
+O13514	YAL042C-A	
+A0A023PYD0	YAL059C-A	
+P0CX18	YAR066W	
+P47118	YJR067C	YAE1
+P0CX90	YAR061W	
+P0CX92	YAR069C	
+P40574	YIR018W	YAP5
+Q3E756	YBL029C-A	
+P0C5L0	YBR056C-B	
+P34220	YBL055C	
+P38185	YBL071C	
+P38183	YBL077W	
+P38173	YBL094C	
+P53169	YGL060W	YBP2
+P38256	YBR096W	
+P25577	YCL049C	
+P25601	YCL075W	TY5B
+P25616	YCR015C	
+P25629	YCR049C	
+P25630	YCR050C	
+P25608	YCR102C	
+Q2V2Q0	YDL007C-A	
+Q12185	YDR018C	
+Q12352	YDL041W	
+Q03831	YDR095C	
+Q03856	YDR098C-A	TY1A-DR1
+Q07541	YDL121C	
+O74302	YDR261C-C	TY1A-DR4
+P0CX70	YDR365W-A	TY1A-DR6
+Q12027	YDL176W	
+Q03964	YDR170W-A	TY1A-DR2
+Q3E818	YDR194W-A	
+Q12424	YDL206W	
+Q07629	YDL218W	
+Q04923	YDR220C	
+A0A023PZA9	YDR230W	
+Q99303	YDR261W-A	TY2A-DR3
+Q07791	YDR261W-B	TY2B-DR3
+Q05510	YDR344C	
+P0C5M1	YDR371C-A	
+Q04162	YDR387C	
+P87268	YDR426C	
+A0A023PYD7	YDR187C	
+Q12187	YDL196W	
+Q04597	YDR114C	
+A0A023PZ94	YAL031W-A	
+Q8TGV0	YAR035C-A	
+A0A023PZE2	YAL047W-A	
+Q8TGR8	YAL037C-B	
+O13512	YAL064W-B	
+P39711	YAL064W	
+P14680	YJL141C	YAK1
+P46683	YPL239W	YAR1
+Q3E794	YBR072C-A	
+P90471	YBR109W-A	
+Q6B113	YBL107W-A	
+Q12491	YBL100W-B	TY2B-B
+P38317	YBR219C	
+P38322	YBR226C	
+P38357	YBR292C	
+P38350	YBR277C	
+P38188	YBL065W	
+P38184	YBL073W	
+Q8TGQ1	YCR047W-A	
+Q96VG6	YCR097W-A	
+A0A023PXB0	YAR019W-A	
+O42831	YAR075W	
+A0A023PYC6	YAL016C-A	
+P39548	YAR028W	
+P0CX88	YAR060C	
+P0CI66	YAR062W	
+P39564	YAR068W	
+P40917	YOR028C	CIN5
+P39710	YAL066W	
+Q3E821	YBL008W-A	
+Q3E7Y5	YBL111C	
+Q8TGU7	YBR126W-A	
+Q8TGQ5	YBR131C-A	
+P0C5L5	YBR191W-A	
+P0C268	YBL039W-B	
+Q3E820	YBR196C-A	
+P38190	YBL053W	
+P38186	YBL070C	
+P38081	YBR056W	
+P38252	YBR089W	
+P38258	YBR099C	
+P25572	YCL042W	
+Q12448	YDL034W	
+Q3E6R4	YDR524C-B	
+A0A023PZF2	YEL009C-A	
+Q3E7B0	YER053C-A	
+Q8TGR4	YER088W-B	
+Q03612	YER138C	TY1B-ER1
+P40103	YER188W	
+P40104	YER189W	
+P32622	YEL041W	YEF1
+P40052	YER079W	
+P40560	YIL001W	
+P40536	YIL032C	
+E2QC18		
+E9PAE8		
+E9PAE4		
+E9PAD8		
+E9PAE3		truncated TYB
+E9PAE7		
+E9PAD6		
+E9PAF1		
diff --git a/tests/tests.py b/tests/tests.py
index d6104da..730f978 100644
--- a/tests/tests.py
+++ b/tests/tests.py
@@ -1,18 +1,78 @@
+from __future__ import print_function, absolute_import, division, unicode_literals
 import unittest
-from ymap.ymap import data, ymap_proteins, ymap_genes, web
+import tempfile
+import shutil
+import os
+import time
+import filecmp
+from ymap.ymap import data, ymap_proteins, ymap_genes, web, YGtPM
 
-class PimpMyPackage(unittest.TestCase):
-	def test_data(self):
-		self.assertTrue(True)
+ref_dir = os.path.abspath('test_files')
 
-	def test_ymap_proteins(self):
-		self.assertTrue(True)
 
-	def test_ymap_genes(self):
-		self.assertTrue(True)
+class Timer:
+    def __enter__(self):
+        self.start = time.clock()
+        return self
 
-	def test_web(self):
-		self.assertTrue(True)
+    def __exit__(self, *args):
+        self.end = time.clock()
+        self.interval = self.end - self.start
+
+
+class YGtPMTest(unittest.TestCase):
+    """
+    YMap tests
+    """
+
+    def setUp(self):
+        # Create a temporary directory
+        # self.ref_dir = os.path.abspath('test_files')
+        self.test_dir = tempfile.mkdtemp()
+        os.chdir(self.test_dir)
+        self.c = YGtPM()
+        # self.store_ref = False
+        # at various places out put is compared to stored reference files. put this to true
+        # to regenerate all reference files
+
+    def tearDown(self):
+        # Remove the directory after the test
+        shutil.rmtree(self.test_dir)
+
+    def test_class_creation(self):
+        """
+        testing the creation of YGtPM
+        """
+        self.assertIsInstance(self.c, YGtPM)
+        self.c.pTMdata()
+        self.assertTrue(os.path.isfile('uniprot_mod_raw.txt'))
+
+    def test_data(self):
+        """
+        testing the steps in data()
+        """
+        shutil.copy(os.path.join(ref_dir, 'uniprot_mod_raw.txt'), '.')  # saving the reference data
+
+        self.c.clean('uniprot_mod_raw.txt')  # produces PTMs.txt
+        self.assertTrue(os.path.isfile('PTMs.txt'))
+        self.assertTrue(filecmp.cmp('PTMs.txt', os.path.join(ref_dir, 'PTMs.txt')))
+
+        self.c.iD()
+        self.assertTrue(os.path.isfile('yeastID.txt'))
+        self.assertTrue(filecmp.cmp('yeastID.txt', os.path.join(ref_dir, 'yeastID.txt')))
+
+        self.c.pmap('yeastID.txt', 'PTMs.txt')
+        self.assertTrue(os.path.isfile('PTM_id_file.txt'))
+        self.assertTrue(filecmp.cmp('PTM_id_file.txt', os.path.join(ref_dir, 'PTM_id_file.txt')))
+
+    def test_ymap_proteins(self):
+        self.assertTrue(True)
+
+    def test_ymap_genes(self):
+        self.assertTrue(True)
+
+    def test_web(self):
+        self.assertTrue(True)
 
 if __name__ == '__main__':
-	unittest.main()
+    unittest.main()
diff --git a/ymap/ymap.py b/ymap/ymap.py
index 77218f3..412680d 100644
--- a/ymap/ymap.py
+++ b/ymap/ymap.py
@@ -262,10 +262,8 @@ def pTMdata(self):
         fil = open('uniprot_mod_raw.txt','wb')
         fil.write(page)
         fil.close()
-    
-    
-    def clean(self, UniProt_file):              
-        
+
+    def clean(self, UniProt_file):
         """ cleans file uniprot_mod_raw.txt into a tab separated PTMs.txt
         """
 
@@ -280,7 +278,9 @@ def clean(self, UniProt_file):
                             ll = ll[2].split('=')
                             p = line[0]+'\t'+line[4]+'\t'+ll[1]
                             if p > str(0):
-                                out = open('PTMs.txt', 'a')
+                                # PTMs.txt is already open under out and being opened again and again...
+                                # this could cause problems check if you cannot just remove all the opens...
+                                #out = open('PTMs.txt', 'a')
                                 out.write(p+'\n')
                                 continue
                         if line[2] == 'Glycosylation':
@@ -289,7 +289,7 @@ def clean(self, UniProt_file):
                             gg =  gg[2].split('=')
                             p1 = line[0]+'\t'+line[4]+'\t'+gg[1]
                             if p1 > str(0):
-                                out = open('PTMs.txt', 'a+')
+                                #out = open('PTMs.txt', 'a+')
                                 out.write(p1+'\n')
                                 continue
                         if line[2] == 'Modified':
@@ -299,7 +299,7 @@ def clean(self, UniProt_file):
                             mm = mm[1].split(';')
                             p2 = line[0]+'\t'+line[4]+'\t'+mm[0]
                             if p2 > str(0):
-                                out = open('PTMs.txt', 'a+')
+                                #out = open('PTMs.txt', 'a+')
                                 out.write(p2+'\n')
                                 continue
                         if line[2] == 'Cross-link': #ubiquitination
@@ -308,8 +308,8 @@ def clean(self, UniProt_file):
                             cc = cc[2].split('=')
                             p3 = line[0]+'\t'+line[4]+'\t'+cc[1]
                             if p3 > str(0):
-                                with open('PTMs.txt', 'a+') as out:
-                                    out.write(p3+'\n')
+                                #with open('PTMs.txt', 'a+') as out:
+                                out.write(p3+'\n')
 
 
     def iD(self):
@@ -321,10 +321,10 @@ def iD(self):
         file_1.write(page1)
         file_1.close()
         
-            
+    # TODO: there seems to be a serious bit of optimization possible here. The second input file should be opened once
     def pmap(self, file_id, file_PTMs):          
-
-        """ if proteins ids are not SDG or uniprot or common names, this method maps the ids 
+        """
+        if proteins ids are not SDG or uniprot or common names, this method maps the ids
         """
         with open('PTM_id_file.txt', 'w') as file3:
             with open(file_id, 'r') as file_id_name:
@@ -337,7 +337,7 @@ def pmap(self, file_id, file_PTMs):
                                 if line[0] == i[0]:
                                     result3 = line[0]+'\t'+line[1]+'\t'+line[2]+'\t'+i[1]+'\t'+i[2]
                                     if result3 > str(0):
-                                        file3 = open('PTM_id_file.txt', 'a')
+                                        #  file3 = open('PTM_id_file.txt', 'a')
                                         file3.write(result3+'\n')
                                              
 
@@ -909,7 +909,11 @@ def betweenPro(fileb, mutation):
                                                 with open('ptm_between_proteins.txt', 'a+') as file1:
                                                     file1.write(take3+'\n')
 
-    
+
+# TODO: yeastID.txt is openen each line of mutation, suggestion to open it once store the di[0] and d1[2] in a
+# dictionary di[2] as keys list of di[0]'s as  values, for a given fi[1] you can then retreive all corresponging di[0]'s
+# don't open hotspot again and again it is already
+# there are many other cases where something similar hapens
 def hotspot(fileh, mutation):
 
     """ PTMs containing motifs in a close proximity are named hotspots (Beltrao et al. Cell 2012)"""
@@ -947,6 +951,10 @@ def sum_file_map():
 
 
 def resc():
+    """
+    documentation needed....
+    """
+
     try:
         r = resource_stream("ymap", "/data/PTMcode+PTMfunc_data/3DID_aceksites_interfaceRes_sc.txt").read().decode()
         with open('3DID_aceksites_interfaceRes_sc.txt','w') as h:
@@ -1019,6 +1027,7 @@ def resc():
 c = YGtPM()
 wd = os.getcwd()
 
+# TODO : remove the variables that store the resutls of the functions that don't return anything
 def data(): 
 
     """ this function will download and clean required data to run ymap methods smoothly """
@@ -1029,39 +1038,39 @@ def data():
     except IOError:
         pass
     try:
-        dat = c.pTMdata()
+        c.pTMdata()
     except IOError:
         pass
     try:
-        cl = c.clean('uniprot_mod_raw.txt')
+        c.clean('uniprot_mod_raw.txt')
     except IOError:
         pass
     try:
-        i = c.iD()
+        c.iD()  # this method does not return anything, all the rest below also don't
     except IOError:
         pass
     try:
-        m = c.pmap('yeastID.txt', 'PTMs.txt')
+        c.pmap('yeastID.txt', 'PTMs.txt')
     except IOError:
         pass
     try:
-        d = c.dclean('uniprot_mod_raw.txt')
+        c.dclean('uniprot_mod_raw.txt')
     except IOError:
         pass
     try:
-        dm = c.d_map('yeastID.txt', 'domains.txt')
+        c.d_map('yeastID.txt', 'domains.txt')
     except IOError:
         pass
     try:
-        ab = c.ab('uniprot_mod_raw.txt')
+        c.ab('uniprot_mod_raw.txt')
     except IOError:
             pass
     try:
-        ii = c.id('bact.txt', 'yeast_id.txt')
+        c.id('bact.txt', 'yeast_id.txt')
     except IOError:
             pass
     try:
-        bio=c.bioGrid()
+        c.bioGrid()
     except IOError:
             pass
     try:
@@ -1659,9 +1668,10 @@ def path():
     parser = argparse.ArgumentParser()
     
     parser.add_argument('-d', '--ydata', help='downloads required data to run yMap successfully')
-    parser.add_argument('-g','--ygenes', help='performs the yMap on genes level mutation positions')
+    parser.add_argument('-g', '--ygenes', help='performs the yMap on genes level mutation positions')
     parser.add_argument('-p', '--yproteins', help='performs the yMap on proteins level mutation positions')
-    parser.add_argument('-w', '--yweb', help='generates BioGrid web pages for interactome visualisation; paste the path to biog.txt file')
+    parser.add_argument('-w', '--yweb', help='generates BioGrid web pages for interactome visualisation; '
+                                             'paste the path to biog.txt file')
 
     args = parser.parse_args()
     if args.ydata:
@@ -1686,4 +1696,3 @@ def path():
             pass
     else:
         print ("to run a function seek help")
-